data_7H6H
# 
_entry.id   7H6H 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7H6H         pdb_00007h6h 10.2210/pdb7h6h/pdb 
WWPDB D_1001407084 ?            ?                   
# 
_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       2025-03-05 
_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.entry_id                        7H6H 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-19 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Rudolph 
_pdbx_contact_author.name_first         Markus 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.email              markus.rudolph@roche.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0447-1101 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Banner, D.W.'  1 
'Benz, J.M.'    2 
'Schlatter, D.' 3 
'Hilpert, H.'   4 
# 
_citation.id                        primary 
_citation.title                     'Crystal structures of human Chymase and Cathepsin G' 
_citation.journal_abbrev            'To be published' 
_citation.year                      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Markus, R.'    1 0000-0003-0447-1101 
primary 'Tosstorff, A.' 2 0000-0002-4969-3667 
# 
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 'Cathepsin G'                                                                                                
26801.787 1   3.4.21.20 NO ? ? 
2 non-polymer syn 'ZINC ION'                                                                                                   
65.409    1   ?         ?  ? ? 
3 non-polymer syn '1-[(7-fluoronaphthalen-1-yl)methyl]-3-{[(methoxycarbonyl)(methyl)amino]methyl}-1H-indole-2-carboxylic acid' 
420.433   1   ?         ?  ? ? 
4 non-polymer syn 'SULFATE ION'                                                                                                
96.063    2   ?         ?  ? ? 
5 water       nat water                                                                                                        
18.015    233 ?         ?  ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        CG 
# 
_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       
;IIGGRESRPHSRPYMAYLQIQSPAGQSRCGGFLVREDFVLTAAHCWGSNINVTLGAHNIQRRENTQQHITARRAIRHPQY
NQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGTLCTVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIFGSYD
PRRQICVGDRRERKAAFKGDSGGPLLCNNVAHGIVSYGKSSGVPPEVFTRVSSFLPWIRTTMRSFKLLDQMETPL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;IIGGRESRPHSRPYMAYLQIQSPAGQSRCGGFLVREDFVLTAAHCWGSNINVTLGAHNIQRRENTQQHITARRAIRHPQY
NQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGTLCTVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIFGSYD
PRRQICVGDRRERKAAFKGDSGGPLLCNNVAHGIVSYGKSSGVPPEVFTRVSSFLPWIRTTMRSFKLLDQMETPL
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                                                   ZN    
3 '1-[(7-fluoronaphthalen-1-yl)methyl]-3-{[(methoxycarbonyl)(methyl)amino]methyl}-1H-indole-2-carboxylic acid' A1AO6 
4 'SULFATE ION'                                                                                                SO4   
5 water                                                                                                        HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ILE n 
1 2   ILE n 
1 3   GLY n 
1 4   GLY n 
1 5   ARG n 
1 6   GLU n 
1 7   SER n 
1 8   ARG n 
1 9   PRO n 
1 10  HIS n 
1 11  SER n 
1 12  ARG n 
1 13  PRO n 
1 14  TYR n 
1 15  MET n 
1 16  ALA n 
1 17  TYR n 
1 18  LEU n 
1 19  GLN n 
1 20  ILE n 
1 21  GLN n 
1 22  SER n 
1 23  PRO n 
1 24  ALA n 
1 25  GLY n 
1 26  GLN n 
1 27  SER n 
1 28  ARG n 
1 29  CYS n 
1 30  GLY n 
1 31  GLY n 
1 32  PHE n 
1 33  LEU n 
1 34  VAL n 
1 35  ARG n 
1 36  GLU n 
1 37  ASP n 
1 38  PHE n 
1 39  VAL n 
1 40  LEU n 
1 41  THR n 
1 42  ALA n 
1 43  ALA n 
1 44  HIS n 
1 45  CYS n 
1 46  TRP n 
1 47  GLY n 
1 48  SER n 
1 49  ASN n 
1 50  ILE n 
1 51  ASN n 
1 52  VAL n 
1 53  THR n 
1 54  LEU n 
1 55  GLY n 
1 56  ALA n 
1 57  HIS n 
1 58  ASN n 
1 59  ILE n 
1 60  GLN n 
1 61  ARG n 
1 62  ARG n 
1 63  GLU n 
1 64  ASN n 
1 65  THR n 
1 66  GLN n 
1 67  GLN n 
1 68  HIS n 
1 69  ILE n 
1 70  THR n 
1 71  ALA n 
1 72  ARG n 
1 73  ARG n 
1 74  ALA n 
1 75  ILE n 
1 76  ARG n 
1 77  HIS n 
1 78  PRO n 
1 79  GLN n 
1 80  TYR n 
1 81  ASN n 
1 82  GLN n 
1 83  ARG n 
1 84  THR n 
1 85  ILE n 
1 86  GLN n 
1 87  ASN n 
1 88  ASP n 
1 89  ILE n 
1 90  MET n 
1 91  LEU n 
1 92  LEU n 
1 93  GLN n 
1 94  LEU n 
1 95  SER n 
1 96  ARG n 
1 97  ARG n 
1 98  VAL n 
1 99  ARG n 
1 100 ARG n 
1 101 ASN n 
1 102 ARG n 
1 103 ASN n 
1 104 VAL n 
1 105 ASN n 
1 106 PRO n 
1 107 VAL n 
1 108 ALA n 
1 109 LEU n 
1 110 PRO n 
1 111 ARG n 
1 112 ALA n 
1 113 GLN n 
1 114 GLU n 
1 115 GLY n 
1 116 LEU n 
1 117 ARG n 
1 118 PRO n 
1 119 GLY n 
1 120 THR n 
1 121 LEU n 
1 122 CYS n 
1 123 THR n 
1 124 VAL n 
1 125 ALA n 
1 126 GLY n 
1 127 TRP n 
1 128 GLY n 
1 129 ARG n 
1 130 VAL n 
1 131 SER n 
1 132 MET n 
1 133 ARG n 
1 134 ARG n 
1 135 GLY n 
1 136 THR n 
1 137 ASP n 
1 138 THR n 
1 139 LEU n 
1 140 ARG n 
1 141 GLU n 
1 142 VAL n 
1 143 GLN n 
1 144 LEU n 
1 145 ARG n 
1 146 VAL n 
1 147 GLN n 
1 148 ARG n 
1 149 ASP n 
1 150 ARG n 
1 151 GLN n 
1 152 CYS n 
1 153 LEU n 
1 154 ARG n 
1 155 ILE n 
1 156 PHE n 
1 157 GLY n 
1 158 SER n 
1 159 TYR n 
1 160 ASP n 
1 161 PRO n 
1 162 ARG n 
1 163 ARG n 
1 164 GLN n 
1 165 ILE n 
1 166 CYS n 
1 167 VAL n 
1 168 GLY n 
1 169 ASP n 
1 170 ARG n 
1 171 ARG n 
1 172 GLU n 
1 173 ARG n 
1 174 LYS n 
1 175 ALA n 
1 176 ALA n 
1 177 PHE n 
1 178 LYS n 
1 179 GLY n 
1 180 ASP n 
1 181 SER n 
1 182 GLY n 
1 183 GLY n 
1 184 PRO n 
1 185 LEU n 
1 186 LEU n 
1 187 CYS n 
1 188 ASN n 
1 189 ASN n 
1 190 VAL n 
1 191 ALA n 
1 192 HIS n 
1 193 GLY n 
1 194 ILE n 
1 195 VAL n 
1 196 SER n 
1 197 TYR n 
1 198 GLY n 
1 199 LYS n 
1 200 SER n 
1 201 SER n 
1 202 GLY n 
1 203 VAL n 
1 204 PRO n 
1 205 PRO n 
1 206 GLU n 
1 207 VAL n 
1 208 PHE n 
1 209 THR n 
1 210 ARG n 
1 211 VAL n 
1 212 SER n 
1 213 SER n 
1 214 PHE n 
1 215 LEU n 
1 216 PRO n 
1 217 TRP n 
1 218 ILE n 
1 219 ARG n 
1 220 THR n 
1 221 THR n 
1 222 MET n 
1 223 ARG n 
1 224 SER n 
1 225 PHE n 
1 226 LYS n 
1 227 LEU n 
1 228 LEU n 
1 229 ASP n 
1 230 GLN n 
1 231 MET n 
1 232 GLU n 
1 233 THR n 
1 234 PRO n 
1 235 LEU 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                   235 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CTSG 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1AO6 non-polymer         . 
'1-[(7-fluoronaphthalen-1-yl)methyl]-3-{[(methoxycarbonyl)(methyl)amino]methyl}-1H-indole-2-carboxylic acid' ? 'C24 H21 F N2 O4' 
420.433 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'    121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER ? 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'      105.093 
SO4   non-polymer         . 'SULFATE ION' ? 'O4 S -2'         96.063  
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'     117.146 
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   ILE 1   16  16  ILE ILE A . n 
A 1 2   ILE 2   17  17  ILE ILE A . n 
A 1 3   GLY 3   18  18  GLY GLY A . n 
A 1 4   GLY 4   19  19  GLY GLY A . n 
A 1 5   ARG 5   20  20  ARG ARG A . n 
A 1 6   GLU 6   21  21  GLU GLU A . n 
A 1 7   SER 7   22  22  SER SER A . n 
A 1 8   ARG 8   23  23  ARG ARG A . n 
A 1 9   PRO 9   24  24  PRO PRO A . n 
A 1 10  HIS 10  25  25  HIS HIS A . n 
A 1 11  SER 11  26  26  SER SER A . n 
A 1 12  ARG 12  27  27  ARG ARG A . n 
A 1 13  PRO 13  28  28  PRO PRO A . n 
A 1 14  TYR 14  29  29  TYR TYR A . n 
A 1 15  MET 15  30  30  MET MET A . n 
A 1 16  ALA 16  31  31  ALA ALA A . n 
A 1 17  TYR 17  32  32  TYR TYR A . n 
A 1 18  LEU 18  33  33  LEU LEU A . n 
A 1 19  GLN 19  34  34  GLN GLN A . n 
A 1 20  ILE 20  35  35  ILE ILE A . n 
A 1 21  GLN 21  36  36  GLN GLN A . n 
A 1 22  SER 22  36  36  SER SER A A n 
A 1 23  PRO 23  36  36  PRO PRO A B n 
A 1 24  ALA 24  37  37  ALA ALA A . n 
A 1 25  GLY 25  38  38  GLY GLY A . n 
A 1 26  GLN 26  39  39  GLN GLN A . n 
A 1 27  SER 27  40  40  SER SER A . n 
A 1 28  ARG 28  41  41  ARG ARG A . n 
A 1 29  CYS 29  42  42  CYS CYS A . n 
A 1 30  GLY 30  43  43  GLY GLY A . n 
A 1 31  GLY 31  44  44  GLY GLY A . n 
A 1 32  PHE 32  45  45  PHE PHE A . n 
A 1 33  LEU 33  46  46  LEU LEU A . n 
A 1 34  VAL 34  47  47  VAL VAL A . n 
A 1 35  ARG 35  48  48  ARG ARG A . n 
A 1 36  GLU 36  49  49  GLU GLU A . n 
A 1 37  ASP 37  50  50  ASP ASP A . n 
A 1 38  PHE 38  51  51  PHE PHE A . n 
A 1 39  VAL 39  52  52  VAL VAL A . n 
A 1 40  LEU 40  53  53  LEU LEU A . n 
A 1 41  THR 41  54  54  THR THR A . n 
A 1 42  ALA 42  55  55  ALA ALA A . n 
A 1 43  ALA 43  56  56  ALA ALA A . n 
A 1 44  HIS 44  57  57  HIS HIS A . n 
A 1 45  CYS 45  58  58  CYS CYS A . n 
A 1 46  TRP 46  59  59  TRP TRP A . n 
A 1 47  GLY 47  60  60  GLY GLY A . n 
A 1 48  SER 48  61  61  SER SER A . n 
A 1 49  ASN 49  63  63  ASN ASN A . n 
A 1 50  ILE 50  64  64  ILE ILE A . n 
A 1 51  ASN 51  65  65  ASN ASN A . n 
A 1 52  VAL 52  66  66  VAL VAL A . n 
A 1 53  THR 53  67  67  THR THR A . n 
A 1 54  LEU 54  68  68  LEU LEU A . n 
A 1 55  GLY 55  69  69  GLY GLY A . n 
A 1 56  ALA 56  70  70  ALA ALA A . n 
A 1 57  HIS 57  71  71  HIS HIS A . n 
A 1 58  ASN 58  72  72  ASN ASN A . n 
A 1 59  ILE 59  73  73  ILE ILE A . n 
A 1 60  GLN 60  74  74  GLN GLN A . n 
A 1 61  ARG 61  75  75  ARG ARG A . n 
A 1 62  ARG 62  76  76  ARG ARG A . n 
A 1 63  GLU 63  77  77  GLU GLU A . n 
A 1 64  ASN 64  78  78  ASN ASN A . n 
A 1 65  THR 65  79  79  THR THR A . n 
A 1 66  GLN 66  80  80  GLN GLN A . n 
A 1 67  GLN 67  81  81  GLN GLN A . n 
A 1 68  HIS 68  82  82  HIS HIS A . n 
A 1 69  ILE 69  83  83  ILE ILE A . n 
A 1 70  THR 70  84  84  THR THR A . n 
A 1 71  ALA 71  85  85  ALA ALA A . n 
A 1 72  ARG 72  86  86  ARG ARG A . n 
A 1 73  ARG 73  87  87  ARG ARG A . n 
A 1 74  ALA 74  88  88  ALA ALA A . n 
A 1 75  ILE 75  89  89  ILE ILE A . n 
A 1 76  ARG 76  90  90  ARG ARG A . n 
A 1 77  HIS 77  91  91  HIS HIS A . n 
A 1 78  PRO 78  92  92  PRO PRO A . n 
A 1 79  GLN 79  93  93  GLN GLN A . n 
A 1 80  TYR 80  94  94  TYR TYR A . n 
A 1 81  ASN 81  95  95  ASN ASN A . n 
A 1 82  GLN 82  96  96  GLN GLN A . n 
A 1 83  ARG 83  97  97  ARG ARG A . n 
A 1 84  THR 84  98  98  THR THR A . n 
A 1 85  ILE 85  99  99  ILE ILE A . n 
A 1 86  GLN 86  100 100 GLN GLN A . n 
A 1 87  ASN 87  101 101 ASN ASN A . n 
A 1 88  ASP 88  102 102 ASP ASP A . n 
A 1 89  ILE 89  103 103 ILE ILE A . n 
A 1 90  MET 90  104 104 MET MET A . n 
A 1 91  LEU 91  105 105 LEU LEU A . n 
A 1 92  LEU 92  106 106 LEU LEU A . n 
A 1 93  GLN 93  107 107 GLN GLN A . n 
A 1 94  LEU 94  108 108 LEU LEU A . n 
A 1 95  SER 95  109 109 SER SER A . n 
A 1 96  ARG 96  110 110 ARG ARG A . n 
A 1 97  ARG 97  111 111 ARG ARG A . n 
A 1 98  VAL 98  112 112 VAL VAL A . n 
A 1 99  ARG 99  113 113 ARG ARG A . n 
A 1 100 ARG 100 114 114 ARG ARG A . n 
A 1 101 ASN 101 115 115 ASN ASN A . n 
A 1 102 ARG 102 116 116 ARG ARG A . n 
A 1 103 ASN 103 117 117 ASN ASN A . n 
A 1 104 VAL 104 118 118 VAL VAL A . n 
A 1 105 ASN 105 119 119 ASN ASN A . n 
A 1 106 PRO 106 120 120 PRO PRO A . n 
A 1 107 VAL 107 121 121 VAL VAL A . n 
A 1 108 ALA 108 122 122 ALA ALA A . n 
A 1 109 LEU 109 123 123 LEU LEU A . n 
A 1 110 PRO 110 124 124 PRO PRO A . n 
A 1 111 ARG 111 125 125 ARG ARG A . n 
A 1 112 ALA 112 126 126 ALA ALA A . n 
A 1 113 GLN 113 127 127 GLN GLN A . n 
A 1 114 GLU 114 128 128 GLU GLU A . n 
A 1 115 GLY 115 129 129 GLY GLY A . n 
A 1 116 LEU 116 130 130 LEU LEU A . n 
A 1 117 ARG 117 131 131 ARG ARG A . n 
A 1 118 PRO 118 132 132 PRO PRO A . n 
A 1 119 GLY 119 133 133 GLY GLY A . n 
A 1 120 THR 120 134 134 THR THR A . n 
A 1 121 LEU 121 135 135 LEU LEU A . n 
A 1 122 CYS 122 136 136 CYS CYS A . n 
A 1 123 THR 123 137 137 THR THR A . n 
A 1 124 VAL 124 138 138 VAL VAL A . n 
A 1 125 ALA 125 139 139 ALA ALA A . n 
A 1 126 GLY 126 140 140 GLY GLY A . n 
A 1 127 TRP 127 141 141 TRP TRP A . n 
A 1 128 GLY 128 142 142 GLY GLY A . n 
A 1 129 ARG 129 143 143 ARG ARG A . n 
A 1 130 VAL 130 144 144 VAL VAL A . n 
A 1 131 SER 131 145 145 SER SER A . n 
A 1 132 MET 132 146 146 MET MET A . n 
A 1 133 ARG 133 147 147 ARG ARG A . n 
A 1 134 ARG 134 148 148 ARG ARG A . n 
A 1 135 GLY 135 151 151 GLY GLY A . n 
A 1 136 THR 136 152 152 THR THR A . n 
A 1 137 ASP 137 153 153 ASP ASP A . n 
A 1 138 THR 138 154 154 THR THR A . n 
A 1 139 LEU 139 155 155 LEU LEU A . n 
A 1 140 ARG 140 156 156 ARG ARG A . n 
A 1 141 GLU 141 157 157 GLU GLU A . n 
A 1 142 VAL 142 158 158 VAL VAL A . n 
A 1 143 GLN 143 159 159 GLN GLN A . n 
A 1 144 LEU 144 160 160 LEU LEU A . n 
A 1 145 ARG 145 161 161 ARG ARG A . n 
A 1 146 VAL 146 162 162 VAL VAL A . n 
A 1 147 GLN 147 163 163 GLN GLN A . n 
A 1 148 ARG 148 164 164 ARG ARG A . n 
A 1 149 ASP 149 165 165 ASP ASP A . n 
A 1 150 ARG 150 166 166 ARG ARG A . n 
A 1 151 GLN 151 167 167 GLN GLN A . n 
A 1 152 CYS 152 168 168 CYS CYS A . n 
A 1 153 LEU 153 169 169 LEU LEU A . n 
A 1 154 ARG 154 170 170 ARG ARG A . n 
A 1 155 ILE 155 171 171 ILE ILE A . n 
A 1 156 PHE 156 172 172 PHE PHE A . n 
A 1 157 GLY 157 173 173 GLY GLY A . n 
A 1 158 SER 158 174 174 SER SER A . n 
A 1 159 TYR 159 175 175 TYR TYR A . n 
A 1 160 ASP 160 176 176 ASP ASP A . n 
A 1 161 PRO 161 177 177 PRO PRO A . n 
A 1 162 ARG 162 178 178 ARG ARG A . n 
A 1 163 ARG 163 179 179 ARG ARG A . n 
A 1 164 GLN 164 180 180 GLN GLN A . n 
A 1 165 ILE 165 181 181 ILE ILE A . n 
A 1 166 CYS 166 182 182 CYS CYS A . n 
A 1 167 VAL 167 183 183 VAL VAL A . n 
A 1 168 GLY 168 184 184 GLY GLY A . n 
A 1 169 ASP 169 184 184 ASP ASP A A n 
A 1 170 ARG 170 185 185 ARG ARG A . n 
A 1 171 ARG 171 186 186 ARG ARG A . n 
A 1 172 GLU 172 187 187 GLU GLU A . n 
A 1 173 ARG 173 188 188 ARG ARG A . n 
A 1 174 LYS 174 188 188 LYS LYS A A n 
A 1 175 ALA 175 189 189 ALA ALA A . n 
A 1 176 ALA 176 190 190 ALA ALA A . n 
A 1 177 PHE 177 191 191 PHE PHE A . n 
A 1 178 LYS 178 192 192 LYS LYS A . n 
A 1 179 GLY 179 193 193 GLY GLY A . n 
A 1 180 ASP 180 194 194 ASP ASP A . n 
A 1 181 SER 181 195 195 SER SER A . n 
A 1 182 GLY 182 196 196 GLY GLY A . n 
A 1 183 GLY 183 197 197 GLY GLY A . n 
A 1 184 PRO 184 198 198 PRO PRO A . n 
A 1 185 LEU 185 199 199 LEU LEU A . n 
A 1 186 LEU 186 200 200 LEU LEU A . n 
A 1 187 CYS 187 201 201 CYS CYS A . n 
A 1 188 ASN 188 202 202 ASN ASN A . n 
A 1 189 ASN 189 203 203 ASN ASN A . n 
A 1 190 VAL 190 204 204 VAL VAL A . n 
A 1 191 ALA 191 209 209 ALA ALA A . n 
A 1 192 HIS 192 210 210 HIS HIS A . n 
A 1 193 GLY 193 211 211 GLY GLY A . n 
A 1 194 ILE 194 212 212 ILE ILE A . n 
A 1 195 VAL 195 213 213 VAL VAL A . n 
A 1 196 SER 196 214 214 SER SER A . n 
A 1 197 TYR 197 215 215 TYR TYR A . n 
A 1 198 GLY 198 216 216 GLY GLY A . n 
A 1 199 LYS 199 217 217 LYS LYS A . n 
A 1 200 SER 200 218 218 SER SER A . n 
A 1 201 SER 201 219 219 SER SER A . n 
A 1 202 GLY 202 220 220 GLY GLY A . n 
A 1 203 VAL 203 221 221 VAL VAL A . n 
A 1 204 PRO 204 224 224 PRO PRO A . n 
A 1 205 PRO 205 225 225 PRO PRO A . n 
A 1 206 GLU 206 226 226 GLU GLU A . n 
A 1 207 VAL 207 227 227 VAL VAL A . n 
A 1 208 PHE 208 228 228 PHE PHE A . n 
A 1 209 THR 209 229 229 THR THR A . n 
A 1 210 ARG 210 230 230 ARG ARG A . n 
A 1 211 VAL 211 231 231 VAL VAL A . n 
A 1 212 SER 212 232 232 SER SER A . n 
A 1 213 SER 213 233 233 SER SER A . n 
A 1 214 PHE 214 234 234 PHE PHE A . n 
A 1 215 LEU 215 235 235 LEU LEU A . n 
A 1 216 PRO 216 236 236 PRO PRO A . n 
A 1 217 TRP 217 237 237 TRP TRP A . n 
A 1 218 ILE 218 238 238 ILE ILE A . n 
A 1 219 ARG 219 239 239 ARG ARG A . n 
A 1 220 THR 220 240 240 THR THR A . n 
A 1 221 THR 221 241 241 THR THR A . n 
A 1 222 MET 222 242 242 MET MET A . n 
A 1 223 ARG 223 243 243 ARG ARG A . n 
A 1 224 SER 224 244 244 SER SER A . n 
A 1 225 PHE 225 245 ?   ?   ?   A . n 
A 1 226 LYS 226 246 ?   ?   ?   A . n 
A 1 227 LEU 227 247 ?   ?   ?   A . n 
A 1 228 LEU 228 248 ?   ?   ?   A . n 
A 1 229 ASP 229 249 ?   ?   ?   A . n 
A 1 230 GLN 230 250 ?   ?   ?   A . n 
A 1 231 MET 231 251 ?   ?   ?   A . n 
A 1 232 GLU 232 252 ?   ?   ?   A . n 
A 1 233 THR 233 253 ?   ?   ?   A . n 
A 1 234 PRO 234 254 ?   ?   ?   A . n 
A 1 235 LEU 235 255 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AO6 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AO6 
_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 
B 2 ZN    1   301 1000 ZN    ZN  A . 
C 3 A1AO6 1   302 1001 A1AO6 LIG A . 
D 4 SO4   1   303 1    SO4   SO4 A . 
E 4 SO4   1   304 2    SO4   SO4 A . 
F 5 HOH   1   401 499  HOH   HOH A . 
F 5 HOH   2   402 483  HOH   HOH A . 
F 5 HOH   3   403 506  HOH   HOH A . 
F 5 HOH   4   404 501  HOH   HOH A . 
F 5 HOH   5   405 255  HOH   HOH A . 
F 5 HOH   6   406 485  HOH   HOH A . 
F 5 HOH   7   407 210  HOH   HOH A . 
F 5 HOH   8   408 248  HOH   HOH A . 
F 5 HOH   9   409 40   HOH   HOH A . 
F 5 HOH   10  410 215  HOH   HOH A . 
F 5 HOH   11  411 302  HOH   HOH A . 
F 5 HOH   12  412 242  HOH   HOH A . 
F 5 HOH   13  413 216  HOH   HOH A . 
F 5 HOH   14  414 228  HOH   HOH A . 
F 5 HOH   15  415 490  HOH   HOH A . 
F 5 HOH   16  416 297  HOH   HOH A . 
F 5 HOH   17  417 237  HOH   HOH A . 
F 5 HOH   18  418 89   HOH   HOH A . 
F 5 HOH   19  419 4    HOH   HOH A . 
F 5 HOH   20  420 14   HOH   HOH A . 
F 5 HOH   21  421 466  HOH   HOH A . 
F 5 HOH   22  422 1    HOH   HOH A . 
F 5 HOH   23  423 233  HOH   HOH A . 
F 5 HOH   24  424 437  HOH   HOH A . 
F 5 HOH   25  425 474  HOH   HOH A . 
F 5 HOH   26  426 83   HOH   HOH A . 
F 5 HOH   27  427 484  HOH   HOH A . 
F 5 HOH   28  428 51   HOH   HOH A . 
F 5 HOH   29  429 88   HOH   HOH A . 
F 5 HOH   30  430 225  HOH   HOH A . 
F 5 HOH   31  431 243  HOH   HOH A . 
F 5 HOH   32  432 100  HOH   HOH A . 
F 5 HOH   33  433 11   HOH   HOH A . 
F 5 HOH   34  434 138  HOH   HOH A . 
F 5 HOH   35  435 94   HOH   HOH A . 
F 5 HOH   36  436 95   HOH   HOH A . 
F 5 HOH   37  437 127  HOH   HOH A . 
F 5 HOH   38  438 234  HOH   HOH A . 
F 5 HOH   39  439 316  HOH   HOH A . 
F 5 HOH   40  440 303  HOH   HOH A . 
F 5 HOH   41  441 103  HOH   HOH A . 
F 5 HOH   42  442 82   HOH   HOH A . 
F 5 HOH   43  443 21   HOH   HOH A . 
F 5 HOH   44  444 223  HOH   HOH A . 
F 5 HOH   45  445 507  HOH   HOH A . 
F 5 HOH   46  446 37   HOH   HOH A . 
F 5 HOH   47  447 454  HOH   HOH A . 
F 5 HOH   48  448 305  HOH   HOH A . 
F 5 HOH   49  449 96   HOH   HOH A . 
F 5 HOH   50  450 206  HOH   HOH A . 
F 5 HOH   51  451 207  HOH   HOH A . 
F 5 HOH   52  452 433  HOH   HOH A . 
F 5 HOH   53  453 267  HOH   HOH A . 
F 5 HOH   54  454 22   HOH   HOH A . 
F 5 HOH   55  455 75   HOH   HOH A . 
F 5 HOH   56  456 56   HOH   HOH A . 
F 5 HOH   57  457 117  HOH   HOH A . 
F 5 HOH   58  458 449  HOH   HOH A . 
F 5 HOH   59  459 107  HOH   HOH A . 
F 5 HOH   60  460 245  HOH   HOH A . 
F 5 HOH   61  461 62   HOH   HOH A . 
F 5 HOH   62  462 289  HOH   HOH A . 
F 5 HOH   63  463 12   HOH   HOH A . 
F 5 HOH   64  464 410  HOH   HOH A . 
F 5 HOH   65  465 39   HOH   HOH A . 
F 5 HOH   66  466 224  HOH   HOH A . 
F 5 HOH   67  467 38   HOH   HOH A . 
F 5 HOH   68  468 69   HOH   HOH A . 
F 5 HOH   69  469 409  HOH   HOH A . 
F 5 HOH   70  470 226  HOH   HOH A . 
F 5 HOH   71  471 68   HOH   HOH A . 
F 5 HOH   72  472 41   HOH   HOH A . 
F 5 HOH   73  473 291  HOH   HOH A . 
F 5 HOH   74  474 318  HOH   HOH A . 
F 5 HOH   75  475 214  HOH   HOH A . 
F 5 HOH   76  476 84   HOH   HOH A . 
F 5 HOH   77  477 116  HOH   HOH A . 
F 5 HOH   78  478 50   HOH   HOH A . 
F 5 HOH   79  479 295  HOH   HOH A . 
F 5 HOH   80  480 209  HOH   HOH A . 
F 5 HOH   81  481 270  HOH   HOH A . 
F 5 HOH   82  482 35   HOH   HOH A . 
F 5 HOH   83  483 33   HOH   HOH A . 
F 5 HOH   84  484 457  HOH   HOH A . 
F 5 HOH   85  485 436  HOH   HOH A . 
F 5 HOH   86  486 55   HOH   HOH A . 
F 5 HOH   87  487 251  HOH   HOH A . 
F 5 HOH   88  488 246  HOH   HOH A . 
F 5 HOH   89  489 113  HOH   HOH A . 
F 5 HOH   90  490 90   HOH   HOH A . 
F 5 HOH   91  491 261  HOH   HOH A . 
F 5 HOH   92  492 403  HOH   HOH A . 
F 5 HOH   93  493 78   HOH   HOH A . 
F 5 HOH   94  494 61   HOH   HOH A . 
F 5 HOH   95  495 432  HOH   HOH A . 
F 5 HOH   96  496 97   HOH   HOH A . 
F 5 HOH   97  497 49   HOH   HOH A . 
F 5 HOH   98  498 211  HOH   HOH A . 
F 5 HOH   99  499 253  HOH   HOH A . 
F 5 HOH   100 500 415  HOH   HOH A . 
F 5 HOH   101 501 262  HOH   HOH A . 
F 5 HOH   102 502 306  HOH   HOH A . 
F 5 HOH   103 503 80   HOH   HOH A . 
F 5 HOH   104 504 298  HOH   HOH A . 
F 5 HOH   105 505 119  HOH   HOH A . 
F 5 HOH   106 506 70   HOH   HOH A . 
F 5 HOH   107 507 427  HOH   HOH A . 
F 5 HOH   108 508 109  HOH   HOH A . 
F 5 HOH   109 509 259  HOH   HOH A . 
F 5 HOH   110 510 71   HOH   HOH A . 
F 5 HOH   111 511 10   HOH   HOH A . 
F 5 HOH   112 512 45   HOH   HOH A . 
F 5 HOH   113 513 434  HOH   HOH A . 
F 5 HOH   114 514 258  HOH   HOH A . 
F 5 HOH   115 515 205  HOH   HOH A . 
F 5 HOH   116 516 307  HOH   HOH A . 
F 5 HOH   117 517 406  HOH   HOH A . 
F 5 HOH   118 518 232  HOH   HOH A . 
F 5 HOH   119 519 93   HOH   HOH A . 
F 5 HOH   120 520 131  HOH   HOH A . 
F 5 HOH   121 521 408  HOH   HOH A . 
F 5 HOH   122 522 105  HOH   HOH A . 
F 5 HOH   123 523 230  HOH   HOH A . 
F 5 HOH   124 524 64   HOH   HOH A . 
F 5 HOH   125 525 424  HOH   HOH A . 
F 5 HOH   126 526 482  HOH   HOH A . 
F 5 HOH   127 527 219  HOH   HOH A . 
F 5 HOH   128 528 463  HOH   HOH A . 
F 5 HOH   129 529 99   HOH   HOH A . 
F 5 HOH   130 530 229  HOH   HOH A . 
F 5 HOH   131 531 13   HOH   HOH A . 
F 5 HOH   132 532 268  HOH   HOH A . 
F 5 HOH   133 533 72   HOH   HOH A . 
F 5 HOH   134 534 239  HOH   HOH A . 
F 5 HOH   135 535 477  HOH   HOH A . 
F 5 HOH   136 536 220  HOH   HOH A . 
F 5 HOH   137 537 3    HOH   HOH A . 
F 5 HOH   138 538 442  HOH   HOH A . 
F 5 HOH   139 539 256  HOH   HOH A . 
F 5 HOH   140 540 441  HOH   HOH A . 
F 5 HOH   141 541 292  HOH   HOH A . 
F 5 HOH   142 542 212  HOH   HOH A . 
F 5 HOH   143 543 44   HOH   HOH A . 
F 5 HOH   144 544 411  HOH   HOH A . 
F 5 HOH   145 545 244  HOH   HOH A . 
F 5 HOH   146 546 9    HOH   HOH A . 
F 5 HOH   147 547 2    HOH   HOH A . 
F 5 HOH   148 548 235  HOH   HOH A . 
F 5 HOH   149 549 496  HOH   HOH A . 
F 5 HOH   150 550 510  HOH   HOH A . 
F 5 HOH   151 551 497  HOH   HOH A . 
F 5 HOH   152 552 420  HOH   HOH A . 
F 5 HOH   153 553 444  HOH   HOH A . 
F 5 HOH   154 554 91   HOH   HOH A . 
F 5 HOH   155 555 129  HOH   HOH A . 
F 5 HOH   156 556 67   HOH   HOH A . 
F 5 HOH   157 557 448  HOH   HOH A . 
F 5 HOH   158 558 102  HOH   HOH A . 
F 5 HOH   159 559 60   HOH   HOH A . 
F 5 HOH   160 560 469  HOH   HOH A . 
F 5 HOH   161 561 429  HOH   HOH A . 
F 5 HOH   162 562 439  HOH   HOH A . 
F 5 HOH   163 563 473  HOH   HOH A . 
F 5 HOH   164 564 76   HOH   HOH A . 
F 5 HOH   165 565 16   HOH   HOH A . 
F 5 HOH   166 566 54   HOH   HOH A . 
F 5 HOH   167 567 498  HOH   HOH A . 
F 5 HOH   168 568 108  HOH   HOH A . 
F 5 HOH   169 569 63   HOH   HOH A . 
F 5 HOH   170 570 465  HOH   HOH A . 
F 5 HOH   171 571 296  HOH   HOH A . 
F 5 HOH   172 572 249  HOH   HOH A . 
F 5 HOH   173 573 459  HOH   HOH A . 
F 5 HOH   174 574 294  HOH   HOH A . 
F 5 HOH   175 575 414  HOH   HOH A . 
F 5 HOH   176 576 428  HOH   HOH A . 
F 5 HOH   177 577 276  HOH   HOH A . 
F 5 HOH   178 578 202  HOH   HOH A . 
F 5 HOH   179 579 404  HOH   HOH A . 
F 5 HOH   180 580 15   HOH   HOH A . 
F 5 HOH   181 581 425  HOH   HOH A . 
F 5 HOH   182 582 213  HOH   HOH A . 
F 5 HOH   183 583 500  HOH   HOH A . 
F 5 HOH   184 584 263  HOH   HOH A . 
F 5 HOH   185 585 300  HOH   HOH A . 
F 5 HOH   186 586 236  HOH   HOH A . 
F 5 HOH   187 587 204  HOH   HOH A . 
F 5 HOH   188 588 423  HOH   HOH A . 
F 5 HOH   189 589 430  HOH   HOH A . 
F 5 HOH   190 590 311  HOH   HOH A . 
F 5 HOH   191 591 315  HOH   HOH A . 
F 5 HOH   192 592 453  HOH   HOH A . 
F 5 HOH   193 593 503  HOH   HOH A . 
F 5 HOH   194 594 42   HOH   HOH A . 
F 5 HOH   195 595 458  HOH   HOH A . 
F 5 HOH   196 596 313  HOH   HOH A . 
F 5 HOH   197 597 285  HOH   HOH A . 
F 5 HOH   198 598 478  HOH   HOH A . 
F 5 HOH   199 599 304  HOH   HOH A . 
F 5 HOH   200 600 309  HOH   HOH A . 
F 5 HOH   201 601 247  HOH   HOH A . 
F 5 HOH   202 602 26   HOH   HOH A . 
F 5 HOH   203 603 272  HOH   HOH A . 
F 5 HOH   204 604 314  HOH   HOH A . 
F 5 HOH   205 605 24   HOH   HOH A . 
F 5 HOH   206 606 502  HOH   HOH A . 
F 5 HOH   207 607 426  HOH   HOH A . 
F 5 HOH   208 608 445  HOH   HOH A . 
F 5 HOH   209 609 440  HOH   HOH A . 
F 5 HOH   210 610 470  HOH   HOH A . 
F 5 HOH   211 611 402  HOH   HOH A . 
F 5 HOH   212 612 121  HOH   HOH A . 
F 5 HOH   213 613 416  HOH   HOH A . 
F 5 HOH   214 614 264  HOH   HOH A . 
F 5 HOH   215 615 486  HOH   HOH A . 
F 5 HOH   216 616 290  HOH   HOH A . 
F 5 HOH   217 617 452  HOH   HOH A . 
F 5 HOH   218 618 266  HOH   HOH A . 
F 5 HOH   219 619 227  HOH   HOH A . 
F 5 HOH   220 620 418  HOH   HOH A . 
F 5 HOH   221 621 467  HOH   HOH A . 
F 5 HOH   222 622 279  HOH   HOH A . 
F 5 HOH   223 623 460  HOH   HOH A . 
F 5 HOH   224 624 447  HOH   HOH A . 
F 5 HOH   225 625 443  HOH   HOH A . 
F 5 HOH   226 626 472  HOH   HOH A . 
F 5 HOH   227 627 118  HOH   HOH A . 
F 5 HOH   228 628 455  HOH   HOH A . 
F 5 HOH   229 629 417  HOH   HOH A . 
F 5 HOH   230 630 475  HOH   HOH A . 
F 5 HOH   231 631 421  HOH   HOH A . 
F 5 HOH   232 632 401  HOH   HOH A . 
F 5 HOH   233 633 461  HOH   HOH A . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC 5.8.0425 ? 1 
'data scaling'   XSCALE .        ? 2 
'data reduction' XDS    .        ? 3 
phasing          PHASER .        ? 4 
# 
_cell.entry_id           7H6H 
_cell.length_a           80.210 
_cell.length_b           44.730 
_cell.length_c           67.270 
_cell.angle_alpha        90.00 
_cell.angle_beta         107.08 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7H6H 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
# 
_exptl.entry_id          7H6H 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.26 
_exptl_crystal.density_percent_sol   45.65 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          MICROBATCH 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.pdbx_details    
;0.2 M LiSO4 (Salt), 
25 %w/v PEG3350 (Precipitant), 
0.1 M HEPES 7.5 pH (Buffer), 
Protein was at 17 mg/mL.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.type                   'MAR scanner 345 mm plate' 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.pdbx_collection_date   2006-05-18 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'SEALED TUBE' 
_diffrn_source.type                        'BRUKER IMUS MICROFOCUS' 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7H6H 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             19.51 
_reflns.d_resolution_high            1.94 
_reflns.number_obs                   15390 
_reflns.percent_possible_obs         89.9 
_reflns.pdbx_Rmerge_I_obs            0.08 
_reflns.pdbx_netI_over_sigmaI        14.83 
_reflns.pdbx_Rrim_I_all              0.091 
_reflns.pdbx_number_measured_all     65573 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_unique_obs 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_redundancy 
1 1 1.94 2.06  10601 2505 0.398 89.9 3.60  0.455 ? ? ? ? 
1 2 2.06 2.2   10173 2351 0.284 92.2 5.72  0.324 ? ? ? ? 
1 3 2.20 2.37  6498  1541 0.196 66.0 7.53  0.224 ? ? ? ? 
1 4 2.37 2.59  8850  2051 0.124 93.9 11.68 0.142 ? ? ? ? 
1 5 2.59 2.89  8206  1904 0.09  94.6 15.31 0.103 ? ? ? ? 
1 6 2.89 3.33  7268  1698 0.057 95.5 21.85 0.065 ? ? ? ? 
1 7 3.33 4.04  6142  1447 0.043 96.4 27.71 0.049 ? ? ? ? 
1 8 4.04 5.6   4942  1180 0.033 97.1 34.99 0.038 ? ? ? ? 
1 9 5.60 19.51 2893  713  0.037 94.4 31.77 0.043 ? ? ? ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7H6H 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     14611 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             19.51 
_refine.ls_d_res_high                            1.94 
_refine.ls_percent_reflns_obs                    90.02 
_refine.ls_R_factor_obs                          0.17363 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.17060 
_refine.ls_R_factor_R_free                       0.23162 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  779 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.954 
_refine.correlation_coeff_Fo_to_Fc_free          0.910 
_refine.B_iso_mean                               19.850 
_refine.aniso_B[1][1]                            -0.40 
_refine.aniso_B[2][2]                            0.49 
_refine.aniso_B[3][3]                            -0.30 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.44 
_refine.aniso_B[2][3]                            -0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.202 
_refine.pdbx_overall_ESU_R_Free                  0.179 
_refine.overall_SU_ML                            0.124 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             7.898 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1786 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         42 
_refine_hist.number_atoms_solvent             233 
_refine_hist.number_atoms_total               2061 
_refine_hist.d_res_high                       1.94 
_refine_hist.d_res_low                        19.51 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.004  0.012  ? 1887 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.016  ? 1808 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.181  1.830  ? 2554 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            0.425  1.806  ? 4101 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.701  5.000  ? 227  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       4.256  5.000  ? 35   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.662 10.000 ? 320  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.061  0.200  ? 266  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.004  0.020  ? 2397 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.001  0.020  ? 533  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  0.496  1.033  ? 905  'X-RAY DIFFRACTION' ? 
r_mcbond_other               0.494  1.033  ? 905  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 0.867  1.857  ? 1133 'X-RAY DIFFRACTION' ? 
r_mcangle_other              0.867  1.859  ? 1134 'X-RAY DIFFRACTION' ? 
r_scbond_it                  0.730  1.174  ? 982  'X-RAY DIFFRACTION' ? 
r_scbond_other               0.721  1.160  ? 975  'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              1.197  2.088  ? 1410 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       5.680  12.39  ? 2102 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         5.233  10.69  ? 2034 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.940 
_refine_ls_shell.d_res_low                        1.990 
_refine_ls_shell.number_reflns_R_work             1045 
_refine_ls_shell.R_factor_R_work                  0.254 
_refine_ls_shell.percent_reflns_obs               88.81 
_refine_ls_shell.R_factor_R_free                  0.264 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             58 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7H6H 
_struct.title                     
;THE 1.94 A CRYSTAL STRUCTURE OF HUMAN CATHEPSIN G IN COMPLEX WITH 1-[(7-fluoronaphthalen-1-yl)methyl]-3-[[methoxycarbonyl(methyl)amino]methyl]indole-2-carboxylic acid
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7H6H 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            'HUMAN CATHEPSIN G, SERINE PROTEINASE, COMPLEX (SERINE PROTEASE-INHIBITOR) complex, HYDROLASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CATG_HUMAN 
_struct_ref.pdbx_db_accession          P08311 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;IIGGRESRPHSRPYMAYLQIQSPAGQSRCGGFLVREDFVLTAAHCWGSNINVTLGAHNIQRRENTQQHITARRAIRHPQY
NQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGTLCTVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIFGSYD
PRRQICVGDRRERKAAFKGDSGGPLLCNNVAHGIVSYGKSSGVPPEVFTRVSSFLPWIRTTMRSFKLLDQMETPL
;
_struct_ref.pdbx_align_begin           21 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7H6H 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 235 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P08311 
_struct_ref_seq.db_align_beg                  21 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  255 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       16 
_struct_ref_seq.pdbx_auth_seq_align_end       255 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_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 ALA A 42  ? TRP A 46  ? ALA A 55  TRP A 59  5 ? 5  
HELX_P HELX_P2 AA2 ARG A 148 ? ARG A 154 ? ARG A 164 ARG A 170 1 ? 7  
HELX_P HELX_P3 AA3 PHE A 214 ? SER A 224 ? PHE A 234 SER A 244 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 29  SG  ? ? ? 1_555 A CYS 45  SG ? ? A CYS 42  A CYS 58  1_555 ? ? ? ? ? ? ? 2.060 ? ? 
disulf2 disulf ? ? A CYS 122 SG  ? ? ? 1_555 A CYS 187 SG ? ? A CYS 136 A CYS 201 1_555 ? ? ? ? ? ? ? 2.059 ? ? 
disulf3 disulf ? ? A CYS 152 SG  ? ? ? 1_555 A CYS 166 SG ? ? A CYS 168 A CYS 182 1_555 ? ? ? ? ? ? ? 2.054 ? ? 
metalc1 metalc ? ? A HIS 10  NE2 ? ? ? 1_555 B ZN  .   ZN ? ? A HIS 25  A ZN  301 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
metalc2 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F HOH .   O  ? ? A ZN  301 A HOH 403 1_555 ? ? ? ? ? ? ? 2.273 ? ? 
metalc3 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F HOH .   O  ? ? A ZN  301 A HOH 574 1_555 ? ? ? ? ? ? ? 2.352 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F HOH .   O  ? ? A ZN  301 A HOH 583 1_555 ? ? ? ? ? ? ? 2.134 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 10 ? A HIS 25  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 O ? F HOH . ? A HOH 403 ? 1_555 102.1 ? 
2 NE2 ? A HIS 10 ? A HIS 25  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 O ? F HOH . ? A HOH 574 ? 1_555 95.9  ? 
3 O   ? F HOH .  ? A HOH 403 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 O ? F HOH . ? A HOH 574 ? 1_555 127.9 ? 
4 NE2 ? A HIS 10 ? A HIS 25  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 O ? F HOH . ? A HOH 583 ? 1_555 117.2 ? 
5 O   ? F HOH .  ? A HOH 403 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 O ? F HOH . ? A HOH 583 ? 1_555 107.6 ? 
6 O   ? F HOH .  ? A HOH 574 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 O ? F HOH . ? A HOH 583 ? 1_555 106.5 ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 29  ? CYS A 45  ? CYS A 42  ? 1_555 CYS A 58  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 122 ? CYS A 187 ? CYS A 136 ? 1_555 CYS A 201 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS A 152 ? CYS A 166 ? CYS A 168 ? 1_555 CYS A 182 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PRO 
_struct_mon_prot_cis.label_seq_id           204 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           PRO 
_struct_mon_prot_cis.auth_seq_id            224 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    205 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     225 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -6.12 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 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 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
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 5   ? GLU A 6   ? ARG A 20  GLU A 21  
AA1 2 ARG A 140 ? ARG A 145 ? ARG A 156 ARG A 161 
AA1 3 LEU A 121 ? GLY A 126 ? LEU A 135 GLY A 140 
AA1 4 PRO A 184 ? CYS A 187 ? PRO A 198 CYS A 201 
AA1 5 VAL A 190 ? TYR A 197 ? VAL A 204 TYR A 215 
AA1 6 GLU A 206 ? ARG A 210 ? GLU A 226 ARG A 230 
AA1 7 GLN A 164 ? VAL A 167 ? GLN A 180 VAL A 183 
AA2 1 MET A 15  ? SER A 22  A MET A 30  SER A 36  
AA2 2 GLY A 25  ? ARG A 35  ? GLY A 38  ARG A 48  
AA2 3 PHE A 38  ? THR A 41  ? PHE A 51  THR A 54  
AA2 4 MET A 90  ? LEU A 94  ? MET A 104 LEU A 108 
AA2 5 GLN A 67  ? ARG A 76  ? GLN A 81  ARG A 90  
AA2 6 ASN A 49  ? LEU A 54  ? ASN A 63  LEU A 68  
AA2 7 MET A 15  ? SER A 22  A MET A 30  SER A 36  
# 
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 ARG A 5   ? N ARG A 20  O GLU A 141 ? O GLU A 157 
AA1 2 3 O LEU A 144 ? O LEU A 160 N CYS A 122 ? N CYS A 136 
AA1 3 4 N THR A 123 ? N THR A 137 O LEU A 186 ? O LEU A 200 
AA1 4 5 N CYS A 187 ? N CYS A 201 O VAL A 190 ? O VAL A 204 
AA1 5 6 N TYR A 197 ? N TYR A 215 O VAL A 207 ? O VAL A 227 
AA1 6 7 O PHE A 208 ? O PHE A 228 N ILE A 165 ? N ILE A 181 
AA2 1 2 N LEU A 18  ? N LEU A 33  O CYS A 29  ? O CYS A 42  
AA2 2 3 N PHE A 32  ? N PHE A 45  O LEU A 40  ? O LEU A 53  
AA2 3 4 N VAL A 39  ? N VAL A 52  O LEU A 92  ? O LEU A 106 
AA2 4 5 O LEU A 91  ? O LEU A 105 N ILE A 75  ? N ILE A 89  
AA2 5 6 O ILE A 69  ? O ILE A 83  N VAL A 52  ? N VAL A 66  
AA2 6 7 O ASN A 49  ? O ASN A 63  N GLN A 21  ? N GLN A 36  
# 
_pdbx_entry_details.entry_id                   7H6H 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    469 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    530 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.10 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     567 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     593 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_545 
_pdbx_validate_symm_contact.dist              1.67 
# 
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 HIS A 71  ? ? -123.50 -58.68 
2 1 SER A 214 ? ? -114.44 -75.03 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A SO4 303 ? D SO4 . 
2 1 A HOH 578 ? F HOH . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.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[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 14.9193 5.9266  21.9662 0.0842 0.1256 0.0337 0.0450 -0.0121 0.0157  1.5568 0.5913 1.5810 -0.0875 
-0.7035 -0.2572 0.1004  0.1077 0.1162  0.0536  -0.0087 0.0012  -0.1004 -0.1453 -0.0916 
'X-RAY DIFFRACTION' 2 ? refined 14.6948 -4.0846 23.9026 0.0878 0.1243 0.0408 0.0197 -0.0136 0.0136  2.0390 0.4561 1.3001 -0.2699 
-0.6332 0.1334  -0.0274 0.0330 -0.1372 0.0746  0.0043  0.0702  0.1233  -0.1200 0.0231  
'X-RAY DIFFRACTION' 3 ? refined 22.3443 3.6434  10.7108 0.0856 0.1627 0.0073 0.0320 -0.0028 0.0272  2.0889 1.4937 2.1038 -0.3391 
-0.7431 0.9254  0.0723  0.3230 0.0910  0.0929  -0.0225 0.0013  0.0095  -0.1192 -0.0497 
'X-RAY DIFFRACTION' 4 ? refined 31.5831 0.2933  9.0025  0.0780 0.1753 0.0453 0.0247 -0.0065 -0.0040 2.2420 1.7252 1.5739 -0.9942 
-1.1715 0.2083  0.1189  0.1856 0.0538  -0.1542 -0.0245 -0.1712 -0.0637 0.0596  -0.0943 
'X-RAY DIFFRACTION' 5 ? refined 22.2698 -5.5021 14.2102 0.0872 0.1458 0.0223 0.0252 -0.0288 -0.0083 1.3867 0.8401 1.8197 0.0067  
-0.8071 -0.2155 0.0017  0.2042 -0.1104 -0.0408 -0.0190 -0.0122 0.1876  -0.1153 0.0174  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 A 16  ? ? A 80  ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 A 81  ? ? A 123 ? ? ? ? 
'X-RAY DIFFRACTION' 3 3 A 124 ? ? A 155 ? ? ? ? 
'X-RAY DIFFRACTION' 4 4 A 156 ? ? A 196 ? ? ? ? 
'X-RAY DIFFRACTION' 5 5 A 197 ? ? A 244 ? ? ? ? 
# 
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 PHE 245 ? A PHE 225 
2  1 Y 1 A LYS 246 ? A LYS 226 
3  1 Y 1 A LEU 247 ? A LEU 227 
4  1 Y 1 A LEU 248 ? A LEU 228 
5  1 Y 1 A ASP 249 ? A ASP 229 
6  1 Y 1 A GLN 250 ? A GLN 230 
7  1 Y 1 A MET 251 ? A MET 231 
8  1 Y 1 A GLU 252 ? A GLU 232 
9  1 Y 1 A THR 253 ? A THR 233 
10 1 Y 1 A PRO 254 ? A PRO 234 
11 1 Y 1 A LEU 255 ? A LEU 235 
# 
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 
A1AO6 N1   N  Y N 1   
A1AO6 C4   C  Y N 2   
A1AO6 C5   C  Y N 3   
A1AO6 C6   C  N N 4   
A1AO6 C7   C  N N 5   
A1AO6 C8   C  N N 6   
A1AO6 C17  C  Y N 7   
A1AO6 C21  C  Y N 8   
A1AO6 C24  C  Y N 9   
A1AO6 C26  C  N N 10  
A1AO6 C28  C  Y N 11  
A1AO6 C2   C  Y N 12  
A1AO6 C3   C  Y N 13  
A1AO6 C9   C  N N 14  
A1AO6 N10  N  N N 15  
A1AO6 C11  C  Y N 16  
A1AO6 C12  C  Y N 17  
A1AO6 O13  O  N N 18  
A1AO6 C14  C  Y N 19  
A1AO6 O15  O  N N 20  
A1AO6 C16  C  Y N 21  
A1AO6 C18  C  Y N 22  
A1AO6 O19  O  N N 23  
A1AO6 O20  O  N N 24  
A1AO6 F22  F  N N 25  
A1AO6 C23  C  Y N 26  
A1AO6 C25  C  Y N 27  
A1AO6 C27  C  Y N 28  
A1AO6 C29  C  N N 29  
A1AO6 C30  C  Y N 30  
A1AO6 C31  C  Y N 31  
A1AO6 H32  H  N N 32  
A1AO6 H33  H  N N 33  
A1AO6 H34  H  N N 34  
A1AO6 H35  H  N N 35  
A1AO6 H37  H  N N 36  
A1AO6 H39  H  N N 37  
A1AO6 H41  H  N N 38  
A1AO6 H44  H  N N 39  
A1AO6 H45  H  N N 40  
A1AO6 H43  H  N N 41  
A1AO6 H47  H  N N 42  
A1AO6 H36  H  N N 43  
A1AO6 H38  H  N N 44  
A1AO6 H40  H  N N 45  
A1AO6 H42  H  N N 46  
A1AO6 H46  H  N N 47  
A1AO6 H48  H  N N 48  
A1AO6 H50  H  N N 49  
A1AO6 H49  H  N N 50  
A1AO6 H51  H  N N 51  
A1AO6 H52  H  N N 52  
ALA   N    N  N N 53  
ALA   CA   C  N S 54  
ALA   C    C  N N 55  
ALA   O    O  N N 56  
ALA   CB   C  N N 57  
ALA   OXT  O  N N 58  
ALA   H    H  N N 59  
ALA   H2   H  N N 60  
ALA   HA   H  N N 61  
ALA   HB1  H  N N 62  
ALA   HB2  H  N N 63  
ALA   HB3  H  N N 64  
ALA   HXT  H  N N 65  
ARG   N    N  N N 66  
ARG   CA   C  N S 67  
ARG   C    C  N N 68  
ARG   O    O  N N 69  
ARG   CB   C  N N 70  
ARG   CG   C  N N 71  
ARG   CD   C  N N 72  
ARG   NE   N  N N 73  
ARG   CZ   C  N N 74  
ARG   NH1  N  N N 75  
ARG   NH2  N  N N 76  
ARG   OXT  O  N N 77  
ARG   H    H  N N 78  
ARG   H2   H  N N 79  
ARG   HA   H  N N 80  
ARG   HB2  H  N N 81  
ARG   HB3  H  N N 82  
ARG   HG2  H  N N 83  
ARG   HG3  H  N N 84  
ARG   HD2  H  N N 85  
ARG   HD3  H  N N 86  
ARG   HE   H  N N 87  
ARG   HH11 H  N N 88  
ARG   HH12 H  N N 89  
ARG   HH21 H  N N 90  
ARG   HH22 H  N N 91  
ARG   HXT  H  N N 92  
ASN   N    N  N N 93  
ASN   CA   C  N S 94  
ASN   C    C  N N 95  
ASN   O    O  N N 96  
ASN   CB   C  N N 97  
ASN   CG   C  N N 98  
ASN   OD1  O  N N 99  
ASN   ND2  N  N N 100 
ASN   OXT  O  N N 101 
ASN   H    H  N N 102 
ASN   H2   H  N N 103 
ASN   HA   H  N N 104 
ASN   HB2  H  N N 105 
ASN   HB3  H  N N 106 
ASN   HD21 H  N N 107 
ASN   HD22 H  N N 108 
ASN   HXT  H  N N 109 
ASP   N    N  N N 110 
ASP   CA   C  N S 111 
ASP   C    C  N N 112 
ASP   O    O  N N 113 
ASP   CB   C  N N 114 
ASP   CG   C  N N 115 
ASP   OD1  O  N N 116 
ASP   OD2  O  N N 117 
ASP   OXT  O  N N 118 
ASP   H    H  N N 119 
ASP   H2   H  N N 120 
ASP   HA   H  N N 121 
ASP   HB2  H  N N 122 
ASP   HB3  H  N N 123 
ASP   HD2  H  N N 124 
ASP   HXT  H  N N 125 
CYS   N    N  N N 126 
CYS   CA   C  N R 127 
CYS   C    C  N N 128 
CYS   O    O  N N 129 
CYS   CB   C  N N 130 
CYS   SG   S  N N 131 
CYS   OXT  O  N N 132 
CYS   H    H  N N 133 
CYS   H2   H  N N 134 
CYS   HA   H  N N 135 
CYS   HB2  H  N N 136 
CYS   HB3  H  N N 137 
CYS   HG   H  N N 138 
CYS   HXT  H  N N 139 
GLN   N    N  N N 140 
GLN   CA   C  N S 141 
GLN   C    C  N N 142 
GLN   O    O  N N 143 
GLN   CB   C  N N 144 
GLN   CG   C  N N 145 
GLN   CD   C  N N 146 
GLN   OE1  O  N N 147 
GLN   NE2  N  N N 148 
GLN   OXT  O  N N 149 
GLN   H    H  N N 150 
GLN   H2   H  N N 151 
GLN   HA   H  N N 152 
GLN   HB2  H  N N 153 
GLN   HB3  H  N N 154 
GLN   HG2  H  N N 155 
GLN   HG3  H  N N 156 
GLN   HE21 H  N N 157 
GLN   HE22 H  N N 158 
GLN   HXT  H  N N 159 
GLU   N    N  N N 160 
GLU   CA   C  N S 161 
GLU   C    C  N N 162 
GLU   O    O  N N 163 
GLU   CB   C  N N 164 
GLU   CG   C  N N 165 
GLU   CD   C  N N 166 
GLU   OE1  O  N N 167 
GLU   OE2  O  N N 168 
GLU   OXT  O  N N 169 
GLU   H    H  N N 170 
GLU   H2   H  N N 171 
GLU   HA   H  N N 172 
GLU   HB2  H  N N 173 
GLU   HB3  H  N N 174 
GLU   HG2  H  N N 175 
GLU   HG3  H  N N 176 
GLU   HE2  H  N N 177 
GLU   HXT  H  N N 178 
GLY   N    N  N N 179 
GLY   CA   C  N N 180 
GLY   C    C  N N 181 
GLY   O    O  N N 182 
GLY   OXT  O  N N 183 
GLY   H    H  N N 184 
GLY   H2   H  N N 185 
GLY   HA2  H  N N 186 
GLY   HA3  H  N N 187 
GLY   HXT  H  N N 188 
HIS   N    N  N N 189 
HIS   CA   C  N S 190 
HIS   C    C  N N 191 
HIS   O    O  N N 192 
HIS   CB   C  N N 193 
HIS   CG   C  Y N 194 
HIS   ND1  N  Y N 195 
HIS   CD2  C  Y N 196 
HIS   CE1  C  Y N 197 
HIS   NE2  N  Y N 198 
HIS   OXT  O  N N 199 
HIS   H    H  N N 200 
HIS   H2   H  N N 201 
HIS   HA   H  N N 202 
HIS   HB2  H  N N 203 
HIS   HB3  H  N N 204 
HIS   HD1  H  N N 205 
HIS   HD2  H  N N 206 
HIS   HE1  H  N N 207 
HIS   HE2  H  N N 208 
HIS   HXT  H  N N 209 
HOH   O    O  N N 210 
HOH   H1   H  N N 211 
HOH   H2   H  N N 212 
ILE   N    N  N N 213 
ILE   CA   C  N S 214 
ILE   C    C  N N 215 
ILE   O    O  N N 216 
ILE   CB   C  N S 217 
ILE   CG1  C  N N 218 
ILE   CG2  C  N N 219 
ILE   CD1  C  N N 220 
ILE   OXT  O  N N 221 
ILE   H    H  N N 222 
ILE   H2   H  N N 223 
ILE   HA   H  N N 224 
ILE   HB   H  N N 225 
ILE   HG12 H  N N 226 
ILE   HG13 H  N N 227 
ILE   HG21 H  N N 228 
ILE   HG22 H  N N 229 
ILE   HG23 H  N N 230 
ILE   HD11 H  N N 231 
ILE   HD12 H  N N 232 
ILE   HD13 H  N N 233 
ILE   HXT  H  N N 234 
LEU   N    N  N N 235 
LEU   CA   C  N S 236 
LEU   C    C  N N 237 
LEU   O    O  N N 238 
LEU   CB   C  N N 239 
LEU   CG   C  N N 240 
LEU   CD1  C  N N 241 
LEU   CD2  C  N N 242 
LEU   OXT  O  N N 243 
LEU   H    H  N N 244 
LEU   H2   H  N N 245 
LEU   HA   H  N N 246 
LEU   HB2  H  N N 247 
LEU   HB3  H  N N 248 
LEU   HG   H  N N 249 
LEU   HD11 H  N N 250 
LEU   HD12 H  N N 251 
LEU   HD13 H  N N 252 
LEU   HD21 H  N N 253 
LEU   HD22 H  N N 254 
LEU   HD23 H  N N 255 
LEU   HXT  H  N N 256 
LYS   N    N  N N 257 
LYS   CA   C  N S 258 
LYS   C    C  N N 259 
LYS   O    O  N N 260 
LYS   CB   C  N N 261 
LYS   CG   C  N N 262 
LYS   CD   C  N N 263 
LYS   CE   C  N N 264 
LYS   NZ   N  N N 265 
LYS   OXT  O  N N 266 
LYS   H    H  N N 267 
LYS   H2   H  N N 268 
LYS   HA   H  N N 269 
LYS   HB2  H  N N 270 
LYS   HB3  H  N N 271 
LYS   HG2  H  N N 272 
LYS   HG3  H  N N 273 
LYS   HD2  H  N N 274 
LYS   HD3  H  N N 275 
LYS   HE2  H  N N 276 
LYS   HE3  H  N N 277 
LYS   HZ1  H  N N 278 
LYS   HZ2  H  N N 279 
LYS   HZ3  H  N N 280 
LYS   HXT  H  N N 281 
MET   N    N  N N 282 
MET   CA   C  N S 283 
MET   C    C  N N 284 
MET   O    O  N N 285 
MET   CB   C  N N 286 
MET   CG   C  N N 287 
MET   SD   S  N N 288 
MET   CE   C  N N 289 
MET   OXT  O  N N 290 
MET   H    H  N N 291 
MET   H2   H  N N 292 
MET   HA   H  N N 293 
MET   HB2  H  N N 294 
MET   HB3  H  N N 295 
MET   HG2  H  N N 296 
MET   HG3  H  N N 297 
MET   HE1  H  N N 298 
MET   HE2  H  N N 299 
MET   HE3  H  N N 300 
MET   HXT  H  N N 301 
PHE   N    N  N N 302 
PHE   CA   C  N S 303 
PHE   C    C  N N 304 
PHE   O    O  N N 305 
PHE   CB   C  N N 306 
PHE   CG   C  Y N 307 
PHE   CD1  C  Y N 308 
PHE   CD2  C  Y N 309 
PHE   CE1  C  Y N 310 
PHE   CE2  C  Y N 311 
PHE   CZ   C  Y N 312 
PHE   OXT  O  N N 313 
PHE   H    H  N N 314 
PHE   H2   H  N N 315 
PHE   HA   H  N N 316 
PHE   HB2  H  N N 317 
PHE   HB3  H  N N 318 
PHE   HD1  H  N N 319 
PHE   HD2  H  N N 320 
PHE   HE1  H  N N 321 
PHE   HE2  H  N N 322 
PHE   HZ   H  N N 323 
PHE   HXT  H  N N 324 
PRO   N    N  N N 325 
PRO   CA   C  N S 326 
PRO   C    C  N N 327 
PRO   O    O  N N 328 
PRO   CB   C  N N 329 
PRO   CG   C  N N 330 
PRO   CD   C  N N 331 
PRO   OXT  O  N N 332 
PRO   H    H  N N 333 
PRO   HA   H  N N 334 
PRO   HB2  H  N N 335 
PRO   HB3  H  N N 336 
PRO   HG2  H  N N 337 
PRO   HG3  H  N N 338 
PRO   HD2  H  N N 339 
PRO   HD3  H  N N 340 
PRO   HXT  H  N N 341 
SER   N    N  N N 342 
SER   CA   C  N S 343 
SER   C    C  N N 344 
SER   O    O  N N 345 
SER   CB   C  N N 346 
SER   OG   O  N N 347 
SER   OXT  O  N N 348 
SER   H    H  N N 349 
SER   H2   H  N N 350 
SER   HA   H  N N 351 
SER   HB2  H  N N 352 
SER   HB3  H  N N 353 
SER   HG   H  N N 354 
SER   HXT  H  N N 355 
SO4   S    S  N N 356 
SO4   O1   O  N N 357 
SO4   O2   O  N N 358 
SO4   O3   O  N N 359 
SO4   O4   O  N N 360 
THR   N    N  N N 361 
THR   CA   C  N S 362 
THR   C    C  N N 363 
THR   O    O  N N 364 
THR   CB   C  N R 365 
THR   OG1  O  N N 366 
THR   CG2  C  N N 367 
THR   OXT  O  N N 368 
THR   H    H  N N 369 
THR   H2   H  N N 370 
THR   HA   H  N N 371 
THR   HB   H  N N 372 
THR   HG1  H  N N 373 
THR   HG21 H  N N 374 
THR   HG22 H  N N 375 
THR   HG23 H  N N 376 
THR   HXT  H  N N 377 
TRP   N    N  N N 378 
TRP   CA   C  N S 379 
TRP   C    C  N N 380 
TRP   O    O  N N 381 
TRP   CB   C  N N 382 
TRP   CG   C  Y N 383 
TRP   CD1  C  Y N 384 
TRP   CD2  C  Y N 385 
TRP   NE1  N  Y N 386 
TRP   CE2  C  Y N 387 
TRP   CE3  C  Y N 388 
TRP   CZ2  C  Y N 389 
TRP   CZ3  C  Y N 390 
TRP   CH2  C  Y N 391 
TRP   OXT  O  N N 392 
TRP   H    H  N N 393 
TRP   H2   H  N N 394 
TRP   HA   H  N N 395 
TRP   HB2  H  N N 396 
TRP   HB3  H  N N 397 
TRP   HD1  H  N N 398 
TRP   HE1  H  N N 399 
TRP   HE3  H  N N 400 
TRP   HZ2  H  N N 401 
TRP   HZ3  H  N N 402 
TRP   HH2  H  N N 403 
TRP   HXT  H  N N 404 
TYR   N    N  N N 405 
TYR   CA   C  N S 406 
TYR   C    C  N N 407 
TYR   O    O  N N 408 
TYR   CB   C  N N 409 
TYR   CG   C  Y N 410 
TYR   CD1  C  Y N 411 
TYR   CD2  C  Y N 412 
TYR   CE1  C  Y N 413 
TYR   CE2  C  Y N 414 
TYR   CZ   C  Y N 415 
TYR   OH   O  N N 416 
TYR   OXT  O  N N 417 
TYR   H    H  N N 418 
TYR   H2   H  N N 419 
TYR   HA   H  N N 420 
TYR   HB2  H  N N 421 
TYR   HB3  H  N N 422 
TYR   HD1  H  N N 423 
TYR   HD2  H  N N 424 
TYR   HE1  H  N N 425 
TYR   HE2  H  N N 426 
TYR   HH   H  N N 427 
TYR   HXT  H  N N 428 
VAL   N    N  N N 429 
VAL   CA   C  N S 430 
VAL   C    C  N N 431 
VAL   O    O  N N 432 
VAL   CB   C  N N 433 
VAL   CG1  C  N N 434 
VAL   CG2  C  N N 435 
VAL   OXT  O  N N 436 
VAL   H    H  N N 437 
VAL   H2   H  N N 438 
VAL   HA   H  N N 439 
VAL   HB   H  N N 440 
VAL   HG11 H  N N 441 
VAL   HG12 H  N N 442 
VAL   HG13 H  N N 443 
VAL   HG21 H  N N 444 
VAL   HG22 H  N N 445 
VAL   HG23 H  N N 446 
VAL   HXT  H  N N 447 
ZN    ZN   ZN N N 448 
# 
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 
A1AO6 N1  C4   sing Y N 1   
A1AO6 N1  C3   sing Y N 2   
A1AO6 N1  C6   sing N N 3   
A1AO6 C2  C3   doub Y N 4   
A1AO6 C2  C5   sing Y N 5   
A1AO6 C2  C7   sing N N 6   
A1AO6 C3  C9   sing N N 7   
A1AO6 C4  C5   doub Y N 8   
A1AO6 C4  C23  sing Y N 9   
A1AO6 C5  C24  sing Y N 10  
A1AO6 C6  C11  sing N N 11  
A1AO6 C7  N10  sing N N 12  
A1AO6 C8  N10  sing N N 13  
A1AO6 C8  O19  sing N N 14  
A1AO6 C8  O13  doub N N 15  
A1AO6 C9  O20  sing N N 16  
A1AO6 C9  O15  doub N N 17  
A1AO6 N10 C26  sing N N 18  
A1AO6 C11 C25  doub Y N 19  
A1AO6 C11 C12  sing Y N 20  
A1AO6 C12 C16  doub Y N 21  
A1AO6 C12 C14  sing Y N 22  
A1AO6 C14 C18  doub Y N 23  
A1AO6 C16 C28  sing Y N 24  
A1AO6 C16 C17  sing Y N 25  
A1AO6 C17 C21  doub Y N 26  
A1AO6 C18 C21  sing Y N 27  
A1AO6 C18 F22  sing N N 28  
A1AO6 O19 C29  sing N N 29  
A1AO6 C23 C31  doub Y N 30  
A1AO6 C24 C30  doub Y N 31  
A1AO6 C25 C27  sing Y N 32  
A1AO6 C27 C28  doub Y N 33  
A1AO6 C30 C31  sing Y N 34  
A1AO6 C6  H32  sing N N 35  
A1AO6 C6  H33  sing N N 36  
A1AO6 C7  H34  sing N N 37  
A1AO6 C7  H35  sing N N 38  
A1AO6 C17 H37  sing N N 39  
A1AO6 C21 H39  sing N N 40  
A1AO6 C24 H41  sing N N 41  
A1AO6 C26 H44  sing N N 42  
A1AO6 C26 H45  sing N N 43  
A1AO6 C26 H43  sing N N 44  
A1AO6 C28 H47  sing N N 45  
A1AO6 C14 H36  sing N N 46  
A1AO6 O20 H38  sing N N 47  
A1AO6 C23 H40  sing N N 48  
A1AO6 C25 H42  sing N N 49  
A1AO6 C27 H46  sing N N 50  
A1AO6 C29 H48  sing N N 51  
A1AO6 C29 H50  sing N N 52  
A1AO6 C29 H49  sing N N 53  
A1AO6 C30 H51  sing N N 54  
A1AO6 C31 H52  sing N N 55  
ALA   N   CA   sing N N 56  
ALA   N   H    sing N N 57  
ALA   N   H2   sing N N 58  
ALA   CA  C    sing N N 59  
ALA   CA  CB   sing N N 60  
ALA   CA  HA   sing N N 61  
ALA   C   O    doub N N 62  
ALA   C   OXT  sing N N 63  
ALA   CB  HB1  sing N N 64  
ALA   CB  HB2  sing N N 65  
ALA   CB  HB3  sing N N 66  
ALA   OXT HXT  sing N N 67  
ARG   N   CA   sing N N 68  
ARG   N   H    sing N N 69  
ARG   N   H2   sing N N 70  
ARG   CA  C    sing N N 71  
ARG   CA  CB   sing N N 72  
ARG   CA  HA   sing N N 73  
ARG   C   O    doub N N 74  
ARG   C   OXT  sing N N 75  
ARG   CB  CG   sing N N 76  
ARG   CB  HB2  sing N N 77  
ARG   CB  HB3  sing N N 78  
ARG   CG  CD   sing N N 79  
ARG   CG  HG2  sing N N 80  
ARG   CG  HG3  sing N N 81  
ARG   CD  NE   sing N N 82  
ARG   CD  HD2  sing N N 83  
ARG   CD  HD3  sing N N 84  
ARG   NE  CZ   sing N N 85  
ARG   NE  HE   sing N N 86  
ARG   CZ  NH1  sing N N 87  
ARG   CZ  NH2  doub N N 88  
ARG   NH1 HH11 sing N N 89  
ARG   NH1 HH12 sing N N 90  
ARG   NH2 HH21 sing N N 91  
ARG   NH2 HH22 sing N N 92  
ARG   OXT HXT  sing N N 93  
ASN   N   CA   sing N N 94  
ASN   N   H    sing N N 95  
ASN   N   H2   sing N N 96  
ASN   CA  C    sing N N 97  
ASN   CA  CB   sing N N 98  
ASN   CA  HA   sing N N 99  
ASN   C   O    doub N N 100 
ASN   C   OXT  sing N N 101 
ASN   CB  CG   sing N N 102 
ASN   CB  HB2  sing N N 103 
ASN   CB  HB3  sing N N 104 
ASN   CG  OD1  doub N N 105 
ASN   CG  ND2  sing N N 106 
ASN   ND2 HD21 sing N N 107 
ASN   ND2 HD22 sing N N 108 
ASN   OXT HXT  sing N N 109 
ASP   N   CA   sing N N 110 
ASP   N   H    sing N N 111 
ASP   N   H2   sing N N 112 
ASP   CA  C    sing N N 113 
ASP   CA  CB   sing N N 114 
ASP   CA  HA   sing N N 115 
ASP   C   O    doub N N 116 
ASP   C   OXT  sing N N 117 
ASP   CB  CG   sing N N 118 
ASP   CB  HB2  sing N N 119 
ASP   CB  HB3  sing N N 120 
ASP   CG  OD1  doub N N 121 
ASP   CG  OD2  sing N N 122 
ASP   OD2 HD2  sing N N 123 
ASP   OXT HXT  sing N N 124 
CYS   N   CA   sing N N 125 
CYS   N   H    sing N N 126 
CYS   N   H2   sing N N 127 
CYS   CA  C    sing N N 128 
CYS   CA  CB   sing N N 129 
CYS   CA  HA   sing N N 130 
CYS   C   O    doub N N 131 
CYS   C   OXT  sing N N 132 
CYS   CB  SG   sing N N 133 
CYS   CB  HB2  sing N N 134 
CYS   CB  HB3  sing N N 135 
CYS   SG  HG   sing N N 136 
CYS   OXT HXT  sing N N 137 
GLN   N   CA   sing N N 138 
GLN   N   H    sing N N 139 
GLN   N   H2   sing N N 140 
GLN   CA  C    sing N N 141 
GLN   CA  CB   sing N N 142 
GLN   CA  HA   sing N N 143 
GLN   C   O    doub N N 144 
GLN   C   OXT  sing N N 145 
GLN   CB  CG   sing N N 146 
GLN   CB  HB2  sing N N 147 
GLN   CB  HB3  sing N N 148 
GLN   CG  CD   sing N N 149 
GLN   CG  HG2  sing N N 150 
GLN   CG  HG3  sing N N 151 
GLN   CD  OE1  doub N N 152 
GLN   CD  NE2  sing N N 153 
GLN   NE2 HE21 sing N N 154 
GLN   NE2 HE22 sing N N 155 
GLN   OXT HXT  sing N N 156 
GLU   N   CA   sing N N 157 
GLU   N   H    sing N N 158 
GLU   N   H2   sing N N 159 
GLU   CA  C    sing N N 160 
GLU   CA  CB   sing N N 161 
GLU   CA  HA   sing N N 162 
GLU   C   O    doub N N 163 
GLU   C   OXT  sing N N 164 
GLU   CB  CG   sing N N 165 
GLU   CB  HB2  sing N N 166 
GLU   CB  HB3  sing N N 167 
GLU   CG  CD   sing N N 168 
GLU   CG  HG2  sing N N 169 
GLU   CG  HG3  sing N N 170 
GLU   CD  OE1  doub N N 171 
GLU   CD  OE2  sing N N 172 
GLU   OE2 HE2  sing N N 173 
GLU   OXT HXT  sing N N 174 
GLY   N   CA   sing N N 175 
GLY   N   H    sing N N 176 
GLY   N   H2   sing N N 177 
GLY   CA  C    sing N N 178 
GLY   CA  HA2  sing N N 179 
GLY   CA  HA3  sing N N 180 
GLY   C   O    doub N N 181 
GLY   C   OXT  sing N N 182 
GLY   OXT HXT  sing N N 183 
HIS   N   CA   sing N N 184 
HIS   N   H    sing N N 185 
HIS   N   H2   sing N N 186 
HIS   CA  C    sing N N 187 
HIS   CA  CB   sing N N 188 
HIS   CA  HA   sing N N 189 
HIS   C   O    doub N N 190 
HIS   C   OXT  sing N N 191 
HIS   CB  CG   sing N N 192 
HIS   CB  HB2  sing N N 193 
HIS   CB  HB3  sing N N 194 
HIS   CG  ND1  sing Y N 195 
HIS   CG  CD2  doub Y N 196 
HIS   ND1 CE1  doub Y N 197 
HIS   ND1 HD1  sing N N 198 
HIS   CD2 NE2  sing Y N 199 
HIS   CD2 HD2  sing N N 200 
HIS   CE1 NE2  sing Y N 201 
HIS   CE1 HE1  sing N N 202 
HIS   NE2 HE2  sing N N 203 
HIS   OXT HXT  sing N N 204 
HOH   O   H1   sing N N 205 
HOH   O   H2   sing N N 206 
ILE   N   CA   sing N N 207 
ILE   N   H    sing N N 208 
ILE   N   H2   sing N N 209 
ILE   CA  C    sing N N 210 
ILE   CA  CB   sing N N 211 
ILE   CA  HA   sing N N 212 
ILE   C   O    doub N N 213 
ILE   C   OXT  sing N N 214 
ILE   CB  CG1  sing N N 215 
ILE   CB  CG2  sing N N 216 
ILE   CB  HB   sing N N 217 
ILE   CG1 CD1  sing N N 218 
ILE   CG1 HG12 sing N N 219 
ILE   CG1 HG13 sing N N 220 
ILE   CG2 HG21 sing N N 221 
ILE   CG2 HG22 sing N N 222 
ILE   CG2 HG23 sing N N 223 
ILE   CD1 HD11 sing N N 224 
ILE   CD1 HD12 sing N N 225 
ILE   CD1 HD13 sing N N 226 
ILE   OXT HXT  sing N N 227 
LEU   N   CA   sing N N 228 
LEU   N   H    sing N N 229 
LEU   N   H2   sing N N 230 
LEU   CA  C    sing N N 231 
LEU   CA  CB   sing N N 232 
LEU   CA  HA   sing N N 233 
LEU   C   O    doub N N 234 
LEU   C   OXT  sing N N 235 
LEU   CB  CG   sing N N 236 
LEU   CB  HB2  sing N N 237 
LEU   CB  HB3  sing N N 238 
LEU   CG  CD1  sing N N 239 
LEU   CG  CD2  sing N N 240 
LEU   CG  HG   sing N N 241 
LEU   CD1 HD11 sing N N 242 
LEU   CD1 HD12 sing N N 243 
LEU   CD1 HD13 sing N N 244 
LEU   CD2 HD21 sing N N 245 
LEU   CD2 HD22 sing N N 246 
LEU   CD2 HD23 sing N N 247 
LEU   OXT HXT  sing N N 248 
LYS   N   CA   sing N N 249 
LYS   N   H    sing N N 250 
LYS   N   H2   sing N N 251 
LYS   CA  C    sing N N 252 
LYS   CA  CB   sing N N 253 
LYS   CA  HA   sing N N 254 
LYS   C   O    doub N N 255 
LYS   C   OXT  sing N N 256 
LYS   CB  CG   sing N N 257 
LYS   CB  HB2  sing N N 258 
LYS   CB  HB3  sing N N 259 
LYS   CG  CD   sing N N 260 
LYS   CG  HG2  sing N N 261 
LYS   CG  HG3  sing N N 262 
LYS   CD  CE   sing N N 263 
LYS   CD  HD2  sing N N 264 
LYS   CD  HD3  sing N N 265 
LYS   CE  NZ   sing N N 266 
LYS   CE  HE2  sing N N 267 
LYS   CE  HE3  sing N N 268 
LYS   NZ  HZ1  sing N N 269 
LYS   NZ  HZ2  sing N N 270 
LYS   NZ  HZ3  sing N N 271 
LYS   OXT HXT  sing N N 272 
MET   N   CA   sing N N 273 
MET   N   H    sing N N 274 
MET   N   H2   sing N N 275 
MET   CA  C    sing N N 276 
MET   CA  CB   sing N N 277 
MET   CA  HA   sing N N 278 
MET   C   O    doub N N 279 
MET   C   OXT  sing N N 280 
MET   CB  CG   sing N N 281 
MET   CB  HB2  sing N N 282 
MET   CB  HB3  sing N N 283 
MET   CG  SD   sing N N 284 
MET   CG  HG2  sing N N 285 
MET   CG  HG3  sing N N 286 
MET   SD  CE   sing N N 287 
MET   CE  HE1  sing N N 288 
MET   CE  HE2  sing N N 289 
MET   CE  HE3  sing N N 290 
MET   OXT HXT  sing N N 291 
PHE   N   CA   sing N N 292 
PHE   N   H    sing N N 293 
PHE   N   H2   sing N N 294 
PHE   CA  C    sing N N 295 
PHE   CA  CB   sing N N 296 
PHE   CA  HA   sing N N 297 
PHE   C   O    doub N N 298 
PHE   C   OXT  sing N N 299 
PHE   CB  CG   sing N N 300 
PHE   CB  HB2  sing N N 301 
PHE   CB  HB3  sing N N 302 
PHE   CG  CD1  doub Y N 303 
PHE   CG  CD2  sing Y N 304 
PHE   CD1 CE1  sing Y N 305 
PHE   CD1 HD1  sing N N 306 
PHE   CD2 CE2  doub Y N 307 
PHE   CD2 HD2  sing N N 308 
PHE   CE1 CZ   doub Y N 309 
PHE   CE1 HE1  sing N N 310 
PHE   CE2 CZ   sing Y N 311 
PHE   CE2 HE2  sing N N 312 
PHE   CZ  HZ   sing N N 313 
PHE   OXT HXT  sing N N 314 
PRO   N   CA   sing N N 315 
PRO   N   CD   sing N N 316 
PRO   N   H    sing N N 317 
PRO   CA  C    sing N N 318 
PRO   CA  CB   sing N N 319 
PRO   CA  HA   sing N N 320 
PRO   C   O    doub N N 321 
PRO   C   OXT  sing N N 322 
PRO   CB  CG   sing N N 323 
PRO   CB  HB2  sing N N 324 
PRO   CB  HB3  sing N N 325 
PRO   CG  CD   sing N N 326 
PRO   CG  HG2  sing N N 327 
PRO   CG  HG3  sing N N 328 
PRO   CD  HD2  sing N N 329 
PRO   CD  HD3  sing N N 330 
PRO   OXT HXT  sing N N 331 
SER   N   CA   sing N N 332 
SER   N   H    sing N N 333 
SER   N   H2   sing N N 334 
SER   CA  C    sing N N 335 
SER   CA  CB   sing N N 336 
SER   CA  HA   sing N N 337 
SER   C   O    doub N N 338 
SER   C   OXT  sing N N 339 
SER   CB  OG   sing N N 340 
SER   CB  HB2  sing N N 341 
SER   CB  HB3  sing N N 342 
SER   OG  HG   sing N N 343 
SER   OXT HXT  sing N N 344 
SO4   S   O1   doub N N 345 
SO4   S   O2   doub N N 346 
SO4   S   O3   sing N N 347 
SO4   S   O4   sing N N 348 
THR   N   CA   sing N N 349 
THR   N   H    sing N N 350 
THR   N   H2   sing N N 351 
THR   CA  C    sing N N 352 
THR   CA  CB   sing N N 353 
THR   CA  HA   sing N N 354 
THR   C   O    doub N N 355 
THR   C   OXT  sing N N 356 
THR   CB  OG1  sing N N 357 
THR   CB  CG2  sing N N 358 
THR   CB  HB   sing N N 359 
THR   OG1 HG1  sing N N 360 
THR   CG2 HG21 sing N N 361 
THR   CG2 HG22 sing N N 362 
THR   CG2 HG23 sing N N 363 
THR   OXT HXT  sing N N 364 
TRP   N   CA   sing N N 365 
TRP   N   H    sing N N 366 
TRP   N   H2   sing N N 367 
TRP   CA  C    sing N N 368 
TRP   CA  CB   sing N N 369 
TRP   CA  HA   sing N N 370 
TRP   C   O    doub N N 371 
TRP   C   OXT  sing N N 372 
TRP   CB  CG   sing N N 373 
TRP   CB  HB2  sing N N 374 
TRP   CB  HB3  sing N N 375 
TRP   CG  CD1  doub Y N 376 
TRP   CG  CD2  sing Y N 377 
TRP   CD1 NE1  sing Y N 378 
TRP   CD1 HD1  sing N N 379 
TRP   CD2 CE2  doub Y N 380 
TRP   CD2 CE3  sing Y N 381 
TRP   NE1 CE2  sing Y N 382 
TRP   NE1 HE1  sing N N 383 
TRP   CE2 CZ2  sing Y N 384 
TRP   CE3 CZ3  doub Y N 385 
TRP   CE3 HE3  sing N N 386 
TRP   CZ2 CH2  doub Y N 387 
TRP   CZ2 HZ2  sing N N 388 
TRP   CZ3 CH2  sing Y N 389 
TRP   CZ3 HZ3  sing N N 390 
TRP   CH2 HH2  sing N N 391 
TRP   OXT HXT  sing N N 392 
TYR   N   CA   sing N N 393 
TYR   N   H    sing N N 394 
TYR   N   H2   sing N N 395 
TYR   CA  C    sing N N 396 
TYR   CA  CB   sing N N 397 
TYR   CA  HA   sing N N 398 
TYR   C   O    doub N N 399 
TYR   C   OXT  sing N N 400 
TYR   CB  CG   sing N N 401 
TYR   CB  HB2  sing N N 402 
TYR   CB  HB3  sing N N 403 
TYR   CG  CD1  doub Y N 404 
TYR   CG  CD2  sing Y N 405 
TYR   CD1 CE1  sing Y N 406 
TYR   CD1 HD1  sing N N 407 
TYR   CD2 CE2  doub Y N 408 
TYR   CD2 HD2  sing N N 409 
TYR   CE1 CZ   doub Y N 410 
TYR   CE1 HE1  sing N N 411 
TYR   CE2 CZ   sing Y N 412 
TYR   CE2 HE2  sing N N 413 
TYR   CZ  OH   sing N N 414 
TYR   OH  HH   sing N N 415 
TYR   OXT HXT  sing N N 416 
VAL   N   CA   sing N N 417 
VAL   N   H    sing N N 418 
VAL   N   H2   sing N N 419 
VAL   CA  C    sing N N 420 
VAL   CA  CB   sing N N 421 
VAL   CA  HA   sing N N 422 
VAL   C   O    doub N N 423 
VAL   C   OXT  sing N N 424 
VAL   CB  CG1  sing N N 425 
VAL   CB  CG2  sing N N 426 
VAL   CB  HB   sing N N 427 
VAL   CG1 HG11 sing N N 428 
VAL   CG1 HG12 sing N N 429 
VAL   CG1 HG13 sing N N 430 
VAL   CG2 HG21 sing N N 431 
VAL   CG2 HG22 sing N N 432 
VAL   CG2 HG23 sing N N 433 
VAL   OXT HXT  sing N N 434 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                Switzerland 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002292 
_pdbx_deposit_group.group_description   'A set of chymase crystal structures for D3R plus two CatG off-target structures' 
_pdbx_deposit_group.group_title         'A set of chymase crystal structures for D3R plus two CatG off-target structures' 
_pdbx_deposit_group.group_type          undefined 
# 
_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      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'apo structure' 
# 
_atom_sites.entry_id                    7H6H 
_atom_sites.fract_transf_matrix[1][1]   0.012467 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003831 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.022356 
_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]   0.015551 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
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   . ILE   A 1 1   ? 24.652 11.291  15.175 1.00 17.83 ? 16  ILE   A N   1 
ATOM   2    C  CA  . ILE   A 1 1   ? 24.871 11.050  13.716 1.00 18.24 ? 16  ILE   A CA  1 
ATOM   3    C  C   . ILE   A 1 1   ? 25.811 12.135  13.186 1.00 19.18 ? 16  ILE   A C   1 
ATOM   4    O  O   . ILE   A 1 1   ? 25.523 13.316  13.339 1.00 19.68 ? 16  ILE   A O   1 
ATOM   5    C  CB  . ILE   A 1 1   ? 23.528 11.033  12.953 1.00 18.09 ? 16  ILE   A CB  1 
ATOM   6    C  CG1 . ILE   A 1 1   ? 22.585 9.916   13.430 1.00 17.30 ? 16  ILE   A CG1 1 
ATOM   7    C  CG2 . ILE   A 1 1   ? 23.750 10.969  11.437 1.00 18.65 ? 16  ILE   A CG2 1 
ATOM   8    C  CD1 . ILE   A 1 1   ? 23.032 8.501   13.098 1.00 16.83 ? 16  ILE   A CD1 1 
ATOM   9    N  N   . ILE   A 1 2   ? 26.915 11.721  12.550 1.00 19.85 ? 17  ILE   A N   1 
ATOM   10   C  CA  . ILE   A 1 2   ? 27.841 12.635  11.895 1.00 20.83 ? 17  ILE   A CA  1 
ATOM   11   C  C   . ILE   A 1 2   ? 27.526 12.715  10.401 1.00 21.15 ? 17  ILE   A C   1 
ATOM   12   O  O   . ILE   A 1 2   ? 27.431 11.690  9.730  1.00 20.19 ? 17  ILE   A O   1 
ATOM   13   C  CB  . ILE   A 1 2   ? 29.302 12.200  12.120 1.00 21.11 ? 17  ILE   A CB  1 
ATOM   14   C  CG1 . ILE   A 1 2   ? 29.707 12.295  13.593 1.00 21.09 ? 17  ILE   A CG1 1 
ATOM   15   C  CG2 . ILE   A 1 2   ? 30.246 13.009  11.229 1.00 22.10 ? 17  ILE   A CG2 1 
ATOM   16   C  CD1 . ILE   A 1 2   ? 30.961 11.515  13.947 1.00 21.13 ? 17  ILE   A CD1 1 
ATOM   17   N  N   . GLY   A 1 3   ? 27.384 13.948  9.895  1.00 22.13 ? 18  GLY   A N   1 
ATOM   18   C  CA  . GLY   A 1 3   ? 27.298 14.209  8.462  1.00 23.00 ? 18  GLY   A CA  1 
ATOM   19   C  C   . GLY   A 1 3   ? 25.906 13.954  7.880  1.00 23.07 ? 18  GLY   A C   1 
ATOM   20   O  O   . GLY   A 1 3   ? 25.775 13.744  6.671  1.00 22.95 ? 18  GLY   A O   1 
ATOM   21   N  N   . GLY   A 1 4   ? 24.872 14.012  8.732  1.00 22.44 ? 19  GLY   A N   1 
ATOM   22   C  CA  . GLY   A 1 4   ? 23.520 13.652  8.336  1.00 22.31 ? 19  GLY   A CA  1 
ATOM   23   C  C   . GLY   A 1 4   ? 22.581 14.855  8.255  1.00 23.26 ? 19  GLY   A C   1 
ATOM   24   O  O   . GLY   A 1 4   ? 23.026 15.997  8.144  1.00 24.11 ? 19  GLY   A O   1 
ATOM   25   N  N   . ARG   A 1 5   ? 21.273 14.562  8.294  1.00 23.30 ? 20  ARG   A N   1 
ATOM   26   C  CA  . ARG   A 1 5   ? 20.215 15.560  8.258  1.00 24.40 ? 20  ARG   A CA  1 
ATOM   27   C  C   . ARG   A 1 5   ? 19.217 15.270  9.378  1.00 23.54 ? 20  ARG   A C   1 
ATOM   28   O  O   . ARG   A 1 5   ? 19.148 14.149  9.872  1.00 22.34 ? 20  ARG   A O   1 
ATOM   29   C  CB  . ARG   A 1 5   ? 19.456 15.524  6.928  1.00 26.06 ? 20  ARG   A CB  1 
ATOM   30   C  CG  . ARG   A 1 5   ? 18.994 14.133  6.506  1.00 26.67 ? 20  ARG   A CG  1 
ATOM   31   C  CD  . ARG   A 1 5   ? 17.854 14.152  5.488  1.00 28.30 ? 20  ARG   A CD  1 
ATOM   32   N  NE  . ARG   A 1 5   ? 16.590 14.598  6.091  1.00 29.29 ? 20  ARG   A NE  1 
ATOM   33   C  CZ  . ARG   A 1 5   ? 15.445 14.816  5.438  1.00 31.14 ? 20  ARG   A CZ  1 
ATOM   34   N  NH1 . ARG   A 1 5   ? 15.361 14.627  4.127  1.00 31.47 ? 20  ARG   A NH1 1 
ATOM   35   N  NH2 . ARG   A 1 5   ? 14.376 15.228  6.103  1.00 31.69 ? 20  ARG   A NH2 1 
ATOM   36   N  N   . GLU   A 1 6   ? 18.425 16.284  9.744  1.00 24.11 ? 21  GLU   A N   1 
ATOM   37   C  CA  . GLU   A 1 6   ? 17.277 16.100  10.622 1.00 23.63 ? 21  GLU   A CA  1 
ATOM   38   C  C   . GLU   A 1 6   ? 16.296 15.166  9.918  1.00 23.30 ? 21  GLU   A C   1 
ATOM   39   O  O   . GLU   A 1 6   ? 16.023 15.353  8.731  1.00 23.82 ? 21  GLU   A O   1 
ATOM   40   C  CB  . GLU   A 1 6   ? 16.609 17.447  10.915 1.00 25.11 ? 21  GLU   A CB  1 
ATOM   41   C  CG  . GLU   A 1 6   ? 15.821 17.486  12.221 1.00 25.17 ? 21  GLU   A CG  1 
ATOM   42   C  CD  . GLU   A 1 6   ? 15.029 18.757  12.482 1.00 26.59 ? 21  GLU   A CD  1 
ATOM   43   O  OE1 . GLU   A 1 6   ? 15.508 19.863  12.156 1.00 27.79 ? 21  GLU   A OE1 1 
ATOM   44   O  OE2 . GLU   A 1 6   ? 13.924 18.642  13.046 1.00 26.67 ? 21  GLU   A OE2 1 
ATOM   45   N  N   . SER   A 1 7   ? 15.795 14.152  10.640 1.00 22.35 ? 22  SER   A N   1 
ATOM   46   C  CA  . SER   A 1 7   ? 14.752 13.271  10.132 1.00 22.31 ? 22  SER   A CA  1 
ATOM   47   C  C   . SER   A 1 7   ? 13.460 14.070  9.942  1.00 23.39 ? 22  SER   A C   1 
ATOM   48   O  O   . SER   A 1 7   ? 13.234 15.056  10.638 1.00 23.12 ? 22  SER   A O   1 
ATOM   49   C  CB  . SER   A 1 7   ? 14.523 12.092  11.059 1.00 21.44 ? 22  SER   A CB  1 
ATOM   50   O  OG  . SER   A 1 7   ? 15.660 11.241  11.169 1.00 20.55 ? 22  SER   A OG  1 
ATOM   51   N  N   . ARG   A 1 8   ? 12.633 13.660  8.968  1.00 24.41 ? 23  ARG   A N   1 
ATOM   52   C  CA  . ARG   A 1 8   ? 11.255 14.119  8.895  1.00 25.40 ? 23  ARG   A CA  1 
ATOM   53   C  C   . ARG   A 1 8   ? 10.577 13.670  10.192 1.00 24.65 ? 23  ARG   A C   1 
ATOM   54   O  O   . ARG   A 1 8   ? 10.663 12.500  10.549 1.00 23.61 ? 23  ARG   A O   1 
ATOM   55   C  CB  . ARG   A 1 8   ? 10.545 13.608  7.630  1.00 26.39 ? 23  ARG   A CB  1 
ATOM   56   C  CG  . ARG   A 1 8   ? 9.029  13.787  7.627  1.00 27.72 ? 23  ARG   A CG  1 
ATOM   57   C  CD  . ARG   A 1 8   ? 8.292  13.456  6.315  1.00 29.12 ? 23  ARG   A CD  1 
ATOM   58   N  NE  . ARG   A 1 8   ? 8.373  12.046  5.913  0.50 28.65 ? 23  ARG   A NE  1 
ATOM   59   C  CZ  . ARG   A 1 8   ? 7.605  11.460  4.999  0.10 29.36 ? 23  ARG   A CZ  1 
ATOM   60   N  NH1 . ARG   A 1 8   ? 6.643  12.133  4.393  0.10 30.58 ? 23  ARG   A NH1 1 
ATOM   61   N  NH2 . ARG   A 1 8   ? 7.794  10.186  4.706  0.10 29.00 ? 23  ARG   A NH2 1 
ATOM   62   N  N   . PRO   A 1 9   ? 9.935  14.577  10.966 1.00 25.26 ? 24  PRO   A N   1 
ATOM   63   C  CA  . PRO   A 1 9   ? 9.334  14.197  12.247 1.00 24.88 ? 24  PRO   A CA  1 
ATOM   64   C  C   . PRO   A 1 9   ? 8.380  13.009  12.122 1.00 24.73 ? 24  PRO   A C   1 
ATOM   65   O  O   . PRO   A 1 9   ? 7.448  13.042  11.315 1.00 24.88 ? 24  PRO   A O   1 
ATOM   66   C  CB  . PRO   A 1 9   ? 8.610  15.475  12.732 1.00 25.77 ? 24  PRO   A CB  1 
ATOM   67   C  CG  . PRO   A 1 9   ? 9.271  16.607  11.965 1.00 26.63 ? 24  PRO   A CG  1 
ATOM   68   C  CD  . PRO   A 1 9   ? 9.752  16.005  10.655 1.00 26.57 ? 24  PRO   A CD  1 
ATOM   69   N  N   . HIS   A 1 10  ? 8.650  11.964  12.924 1.00 23.69 ? 25  HIS   A N   1 
ATOM   70   C  CA  . HIS   A 1 10  ? 7.792  10.797  13.072 1.00 23.88 ? 25  HIS   A CA  1 
ATOM   71   C  C   . HIS   A 1 10  ? 7.830  9.892   11.837 1.00 23.20 ? 25  HIS   A C   1 
ATOM   72   O  O   . HIS   A 1 10  ? 7.012  8.982   11.736 1.00 22.77 ? 25  HIS   A O   1 
ATOM   73   C  CB  . HIS   A 1 10  ? 6.350  11.178  13.451 1.00 26.04 ? 25  HIS   A CB  1 
ATOM   74   C  CG  . HIS   A 1 10  ? 6.235  12.160  14.567 1.00 27.90 ? 25  HIS   A CG  1 
ATOM   75   N  ND1 . HIS   A 1 10  ? 6.581  11.899  15.878 1.00 27.82 ? 25  HIS   A ND1 1 
ATOM   76   C  CD2 . HIS   A 1 10  ? 5.839  13.437  14.532 1.00 30.28 ? 25  HIS   A CD2 1 
ATOM   77   C  CE1 . HIS   A 1 10  ? 6.391  12.996  16.597 1.00 29.43 ? 25  HIS   A CE1 1 
ATOM   78   N  NE2 . HIS   A 1 10  ? 5.928  13.938  15.799 1.00 31.39 ? 25  HIS   A NE2 1 
ATOM   79   N  N   . SER   A 1 11  ? 8.828  10.077  10.956 1.00 22.96 ? 26  SER   A N   1 
ATOM   80   C  CA  . SER   A 1 11  ? 8.992  9.278   9.748  1.00 22.79 ? 26  SER   A CA  1 
ATOM   81   C  C   . SER   A 1 11  ? 9.588  7.900   10.051 1.00 21.98 ? 26  SER   A C   1 
ATOM   82   O  O   . SER   A 1 11  ? 9.561  7.013   9.196  1.00 21.67 ? 26  SER   A O   1 
ATOM   83   C  CB  . SER   A 1 11  ? 9.856  10.004  8.744  1.00 23.18 ? 26  SER   A CB  1 
ATOM   84   O  OG  . SER   A 1 11  ? 11.150 10.284  9.270  1.00 22.11 ? 26  SER   A OG  1 
ATOM   85   N  N   . ARG   A 1 12  ? 10.162 7.737   11.250 1.00 21.11 ? 27  ARG   A N   1 
ATOM   86   C  CA  . ARG   A 1 12  ? 10.738 6.472   11.679 1.00 20.58 ? 27  ARG   A CA  1 
ATOM   87   C  C   . ARG   A 1 12  ? 10.126 6.107   13.028 1.00 20.06 ? 27  ARG   A C   1 
ATOM   88   O  O   . ARG   A 1 12  ? 10.797 6.177   14.058 1.00 19.28 ? 27  ARG   A O   1 
ATOM   89   C  CB  . ARG   A 1 12  ? 12.262 6.593   11.742 1.00 20.41 ? 27  ARG   A CB  1 
ATOM   90   C  CG  . ARG   A 1 12  ? 12.874 6.986   10.403 1.00 21.27 ? 27  ARG   A CG  1 
ATOM   91   C  CD  . ARG   A 1 12  ? 14.395 6.995   10.424 1.00 21.24 ? 27  ARG   A CD  1 
ATOM   92   N  NE  . ARG   A 1 12  ? 14.896 7.395   9.104  1.00 22.02 ? 27  ARG   A NE  1 
ATOM   93   C  CZ  . ARG   A 1 12  ? 14.786 6.663   8.000  1.00 22.74 ? 27  ARG   A CZ  1 
ATOM   94   N  NH1 . ARG   A 1 12  ? 14.438 5.390   8.075  1.00 23.01 ? 27  ARG   A NH1 1 
ATOM   95   N  NH2 . ARG   A 1 12  ? 15.074 7.194   6.829  1.00 22.94 ? 27  ARG   A NH2 1 
ATOM   96   N  N   . PRO   A 1 13  ? 8.833  5.701   13.041 1.00 20.48 ? 28  PRO   A N   1 
ATOM   97   C  CA  . PRO   A 1 13  ? 8.066  5.552   14.283 1.00 20.04 ? 28  PRO   A CA  1 
ATOM   98   C  C   . PRO   A 1 13  ? 8.439  4.381   15.193 1.00 19.25 ? 28  PRO   A C   1 
ATOM   99   O  O   . PRO   A 1 13  ? 7.889  4.259   16.294 1.00 18.93 ? 28  PRO   A O   1 
ATOM   100  C  CB  . PRO   A 1 13  ? 6.628  5.428   13.739 1.00 21.15 ? 28  PRO   A CB  1 
ATOM   101  C  CG  . PRO   A 1 13  ? 6.795  4.740   12.398 1.00 21.84 ? 28  PRO   A CG  1 
ATOM   102  C  CD  . PRO   A 1 13  ? 8.040  5.390   11.835 1.00 21.46 ? 28  PRO   A CD  1 
ATOM   103  N  N   . TYR   A 1 14  ? 9.382  3.549   14.720 1.00 18.53 ? 29  TYR   A N   1 
ATOM   104  C  CA  . TYR   A 1 14  ? 9.954  2.440   15.468 1.00 17.96 ? 29  TYR   A CA  1 
ATOM   105  C  C   . TYR   A 1 14  ? 11.083 2.910   16.388 1.00 16.92 ? 29  TYR   A C   1 
ATOM   106  O  O   . TYR   A 1 14  ? 11.512 2.146   17.253 1.00 16.48 ? 29  TYR   A O   1 
ATOM   107  C  CB  . TYR   A 1 14  ? 10.494 1.367   14.512 1.00 18.38 ? 29  TYR   A CB  1 
ATOM   108  C  CG  . TYR   A 1 14  ? 11.239 1.951   13.317 1.00 19.10 ? 29  TYR   A CG  1 
ATOM   109  C  CD1 . TYR   A 1 14  ? 12.570 2.343   13.414 1.00 18.97 ? 29  TYR   A CD1 1 
ATOM   110  C  CD2 . TYR   A 1 14  ? 10.595 2.145   12.100 1.00 20.37 ? 29  TYR   A CD2 1 
ATOM   111  C  CE1 . TYR   A 1 14  ? 13.237 2.902   12.335 1.00 19.01 ? 29  TYR   A CE1 1 
ATOM   112  C  CE2 . TYR   A 1 14  ? 11.248 2.707   11.015 1.00 20.68 ? 29  TYR   A CE2 1 
ATOM   113  C  CZ  . TYR   A 1 14  ? 12.576 3.076   11.133 1.00 20.13 ? 29  TYR   A CZ  1 
ATOM   114  O  OH  . TYR   A 1 14  ? 13.230 3.626   10.075 1.00 20.13 ? 29  TYR   A OH  1 
ATOM   115  N  N   . MET   A 1 15  ? 11.564 4.151   16.222 1.00 16.21 ? 30  MET   A N   1 
ATOM   116  C  CA  . MET   A 1 15  ? 12.735 4.616   16.954 1.00 15.43 ? 30  MET   A CA  1 
ATOM   117  C  C   . MET   A 1 15  ? 12.411 4.768   18.446 1.00 15.14 ? 30  MET   A C   1 
ATOM   118  O  O   . MET   A 1 15  ? 11.366 5.298   18.809 1.00 15.44 ? 30  MET   A O   1 
ATOM   119  C  CB  . MET   A 1 15  ? 13.260 5.939   16.382 1.00 15.52 ? 30  MET   A CB  1 
ATOM   120  C  CG  . MET   A 1 15  ? 13.950 5.797   15.024 1.00 15.75 ? 30  MET   A CG  1 
ATOM   121  S  SD  . MET   A 1 15  ? 15.395 4.714   15.034 1.00 15.51 ? 30  MET   A SD  1 
ATOM   122  C  CE  . MET   A 1 15  ? 16.483 5.475   16.250 1.00 15.00 ? 30  MET   A CE  1 
ATOM   123  N  N   . ALA   A 1 16  ? 13.325 4.282   19.293 1.00 14.55 ? 31  ALA   A N   1 
ATOM   124  C  CA  . ALA   A 1 16  ? 13.226 4.383   20.743 1.00 14.54 ? 31  ALA   A CA  1 
ATOM   125  C  C   . ALA   A 1 16  ? 14.442 5.134   21.285 1.00 14.49 ? 31  ALA   A C   1 
ATOM   126  O  O   . ALA   A 1 16  ? 15.577 4.875   20.874 1.00 14.04 ? 31  ALA   A O   1 
ATOM   127  C  CB  . ALA   A 1 16  ? 13.143 3.000   21.347 1.00 14.44 ? 31  ALA   A CB  1 
ATOM   128  N  N   . TYR   A 1 17  ? 14.179 6.088   22.184 1.00 14.92 ? 32  TYR   A N   1 
ATOM   129  C  CA  . TYR   A 1 17  ? 15.213 6.770   22.939 1.00 15.10 ? 32  TYR   A CA  1 
ATOM   130  C  C   . TYR   A 1 17  ? 15.312 6.120   24.316 1.00 15.02 ? 32  TYR   A C   1 
ATOM   131  O  O   . TYR   A 1 17  ? 14.295 5.994   25.004 1.00 14.63 ? 32  TYR   A O   1 
ATOM   132  C  CB  . TYR   A 1 17  ? 14.887 8.264   23.035 1.00 16.04 ? 32  TYR   A CB  1 
ATOM   133  C  CG  . TYR   A 1 17  ? 15.930 9.074   23.793 1.00 16.90 ? 32  TYR   A CG  1 
ATOM   134  C  CD1 . TYR   A 1 17  ? 17.031 9.605   23.138 1.00 17.46 ? 32  TYR   A CD1 1 
ATOM   135  C  CD2 . TYR   A 1 17  ? 15.831 9.267   25.167 1.00 17.80 ? 32  TYR   A CD2 1 
ATOM   136  C  CE1 . TYR   A 1 17  ? 17.996 10.328  23.819 1.00 18.17 ? 32  TYR   A CE1 1 
ATOM   137  C  CE2 . TYR   A 1 17  ? 16.781 9.996   25.860 1.00 18.59 ? 32  TYR   A CE2 1 
ATOM   138  C  CZ  . TYR   A 1 17  ? 17.863 10.531  25.180 1.00 18.83 ? 32  TYR   A CZ  1 
ATOM   139  O  OH  . TYR   A 1 17  ? 18.811 11.249  25.846 1.00 20.48 ? 32  TYR   A OH  1 
ATOM   140  N  N   . LEU   A 1 18  ? 16.546 5.758   24.717 1.00 15.06 ? 33  LEU   A N   1 
ATOM   141  C  CA  . LEU   A 1 18  ? 16.805 5.099   25.991 1.00 15.23 ? 33  LEU   A CA  1 
ATOM   142  C  C   . LEU   A 1 18  ? 17.575 6.026   26.944 1.00 15.33 ? 33  LEU   A C   1 
ATOM   143  O  O   . LEU   A 1 18  ? 18.655 6.526   26.610 1.00 15.12 ? 33  LEU   A O   1 
ATOM   144  C  CB  . LEU   A 1 18  ? 17.555 3.778   25.798 1.00 15.28 ? 33  LEU   A CB  1 
ATOM   145  C  CG  . LEU   A 1 18  ? 17.037 2.816   24.723 1.00 15.80 ? 33  LEU   A CG  1 
ATOM   146  C  CD1 . LEU   A 1 18  ? 17.816 1.508   24.794 1.00 15.89 ? 33  LEU   A CD1 1 
ATOM   147  C  CD2 . LEU   A 1 18  ? 15.556 2.518   24.783 1.00 16.27 ? 33  LEU   A CD2 1 
ATOM   148  N  N   . GLN   A 1 19  ? 16.993 6.242   28.138 1.00 15.18 ? 34  GLN   A N   1 
ATOM   149  C  CA  . GLN   A 1 19  ? 17.647 6.902   29.260 1.00 15.68 ? 34  GLN   A CA  1 
ATOM   150  C  C   . GLN   A 1 19  ? 18.028 5.817   30.266 1.00 15.85 ? 34  GLN   A C   1 
ATOM   151  O  O   . GLN   A 1 19  ? 17.158 5.153   30.834 1.00 15.55 ? 34  GLN   A O   1 
ATOM   152  C  CB  . GLN   A 1 19  ? 16.715 7.955   29.868 1.00 16.28 ? 34  GLN   A CB  1 
ATOM   153  C  CG  . GLN   A 1 19  ? 17.213 8.599   31.159 1.00 17.30 ? 34  GLN   A CG  1 
ATOM   154  C  CD  . GLN   A 1 19  ? 16.115 9.268   31.956 0.10 17.62 ? 34  GLN   A CD  1 
ATOM   155  O  OE1 . GLN   A 1 19  ? 16.157 10.472  32.228 0.10 18.26 ? 34  GLN   A OE1 1 
ATOM   156  N  NE2 . GLN   A 1 19  ? 15.119 8.485   32.346 0.10 17.37 ? 34  GLN   A NE2 1 
ATOM   157  N  N   . ILE   A 1 20  ? 19.340 5.652   30.461 1.00 16.06 ? 35  ILE   A N   1 
ATOM   158  C  CA  . ILE   A 1 20  ? 19.912 4.525   31.180 1.00 16.21 ? 35  ILE   A CA  1 
ATOM   159  C  C   . ILE   A 1 20  ? 20.573 5.047   32.452 1.00 16.85 ? 35  ILE   A C   1 
ATOM   160  O  O   . ILE   A 1 20  ? 21.321 6.025   32.414 1.00 17.10 ? 35  ILE   A O   1 
ATOM   161  C  CB  . ILE   A 1 20  ? 20.913 3.791   30.269 1.00 16.01 ? 35  ILE   A CB  1 
ATOM   162  C  CG1 . ILE   A 1 20  ? 20.258 3.333   28.958 1.00 15.71 ? 35  ILE   A CG1 1 
ATOM   163  C  CG2 . ILE   A 1 20  ? 21.575 2.627   31.007 1.00 16.24 ? 35  ILE   A CG2 1 
ATOM   164  C  CD1 . ILE   A 1 20  ? 21.149 3.479   27.737 1.00 15.63 ? 35  ILE   A CD1 1 
ATOM   165  N  N   . GLN   A 1 21  ? 20.277 4.395   33.576 1.00 17.42 ? 36  GLN   A N   1 
ATOM   166  C  CA  . GLN   A 1 21  ? 20.900 4.731   34.850 1.00 18.61 ? 36  GLN   A CA  1 
ATOM   167  C  C   . GLN   A 1 21  ? 21.511 3.468   35.449 1.00 18.71 ? 36  GLN   A C   1 
ATOM   168  O  O   . GLN   A 1 21  ? 20.946 2.384   35.318 1.00 18.77 ? 36  GLN   A O   1 
ATOM   169  C  CB  . GLN   A 1 21  ? 19.891 5.336   35.830 1.00 19.52 ? 36  GLN   A CB  1 
ATOM   170  C  CG  . GLN   A 1 21  ? 18.871 6.254   35.164 0.50 19.73 ? 36  GLN   A CG  1 
ATOM   171  C  CD  . GLN   A 1 21  ? 18.230 7.266   36.087 0.50 20.59 ? 36  GLN   A CD  1 
ATOM   172  O  OE1 . GLN   A 1 21  ? 17.531 8.178   35.637 0.50 20.73 ? 36  GLN   A OE1 1 
ATOM   173  N  NE2 . GLN   A 1 21  ? 18.466 7.136   37.382 0.50 21.59 ? 36  GLN   A NE2 1 
ATOM   174  N  N   . SER   A 1 22  A 22.678 3.619   36.082 1.00 19.13 ? 36  SER   A N   1 
ATOM   175  C  CA  . SER   A 1 22  A 23.265 2.575   36.912 1.00 19.68 ? 36  SER   A CA  1 
ATOM   176  C  C   . SER   A 1 22  A 24.218 3.218   37.917 1.00 20.51 ? 36  SER   A C   1 
ATOM   177  O  O   . SER   A 1 22  A 24.357 4.439   37.931 1.00 20.25 ? 36  SER   A O   1 
ATOM   178  C  CB  . SER   A 1 22  A 23.966 1.527   36.073 1.00 19.57 ? 36  SER   A CB  1 
ATOM   179  O  OG  . SER   A 1 22  A 25.258 1.975   35.686 1.00 19.91 ? 36  SER   A OG  1 
ATOM   180  N  N   . PRO   A 1 23  B 24.888 2.438   38.802 1.00 21.52 ? 36  PRO   A N   1 
ATOM   181  C  CA  . PRO   A 1 23  B 25.867 3.006   39.733 1.00 22.90 ? 36  PRO   A CA  1 
ATOM   182  C  C   . PRO   A 1 23  B 26.957 3.796   39.014 1.00 23.68 ? 36  PRO   A C   1 
ATOM   183  O  O   . PRO   A 1 23  B 27.523 4.737   39.571 1.00 24.57 ? 36  PRO   A O   1 
ATOM   184  C  CB  . PRO   A 1 23  B 26.412 1.751   40.441 1.00 23.37 ? 36  PRO   A CB  1 
ATOM   185  C  CG  . PRO   A 1 23  B 25.255 0.785   40.401 1.00 22.68 ? 36  PRO   A CG  1 
ATOM   186  C  CD  . PRO   A 1 23  B 24.721 0.986   38.988 1.00 21.40 ? 36  PRO   A CD  1 
ATOM   187  N  N   . ALA   A 1 24  ? 27.223 3.395   37.764 1.00 23.78 ? 37  ALA   A N   1 
ATOM   188  C  CA  . ALA   A 1 24  ? 28.245 4.006   36.932 1.00 24.52 ? 37  ALA   A CA  1 
ATOM   189  C  C   . ALA   A 1 24  ? 27.793 5.354   36.378 1.00 24.60 ? 37  ALA   A C   1 
ATOM   190  O  O   . ALA   A 1 24  ? 28.609 6.035   35.758 1.00 25.87 ? 37  ALA   A O   1 
ATOM   191  C  CB  . ALA   A 1 24  ? 28.613 3.069   35.806 1.00 24.09 ? 37  ALA   A CB  1 
ATOM   192  N  N   . GLY   A 1 25  ? 26.511 5.708   36.566 1.00 23.84 ? 38  GLY   A N   1 
ATOM   193  C  CA  . GLY   A 1 25  ? 25.987 7.014   36.197 1.00 23.83 ? 38  GLY   A CA  1 
ATOM   194  C  C   . GLY   A 1 25  ? 24.954 6.918   35.072 1.00 23.09 ? 38  GLY   A C   1 
ATOM   195  O  O   . GLY   A 1 25  ? 24.326 5.876   34.895 1.00 22.17 ? 38  GLY   A O   1 
ATOM   196  N  N   . GLN   A 1 26  ? 24.787 8.027   34.335 1.00 23.50 ? 39  GLN   A N   1 
ATOM   197  C  CA  . GLN   A 1 26  ? 23.766 8.188   33.306 1.00 23.47 ? 39  GLN   A CA  1 
ATOM   198  C  C   . GLN   A 1 26  ? 24.350 7.926   31.917 1.00 21.31 ? 39  GLN   A C   1 
ATOM   199  O  O   . GLN   A 1 26  ? 25.448 8.378   31.624 1.00 20.79 ? 39  GLN   A O   1 
ATOM   200  C  CB  . GLN   A 1 26  ? 23.226 9.623   33.293 1.00 26.08 ? 39  GLN   A CB  1 
ATOM   201  C  CG  . GLN   A 1 26  ? 21.895 9.844   34.010 1.00 29.31 ? 39  GLN   A CG  1 
ATOM   202  C  CD  . GLN   A 1 26  ? 21.939 9.689   35.519 1.00 33.27 ? 39  GLN   A CD  1 
ATOM   203  O  OE1 . GLN   A 1 26  ? 22.770 10.280  36.222 1.00 35.77 ? 39  GLN   A OE1 1 
ATOM   204  N  NE2 . GLN   A 1 26  ? 21.011 8.898   36.044 1.00 34.69 ? 39  GLN   A NE2 1 
ATOM   205  N  N   . SER   A 1 27  ? 23.586 7.242   31.053 1.00 19.45 ? 40  SER   A N   1 
ATOM   206  C  CA  . SER   A 1 27  ? 23.951 7.059   29.655 1.00 18.67 ? 40  SER   A CA  1 
ATOM   207  C  C   . SER   A 1 27  ? 22.726 7.246   28.756 1.00 17.85 ? 40  SER   A C   1 
ATOM   208  O  O   . SER   A 1 27  ? 21.589 7.232   29.223 1.00 17.25 ? 40  SER   A O   1 
ATOM   209  C  CB  . SER   A 1 27  ? 24.569 5.698   29.404 1.00 18.37 ? 40  SER   A CB  1 
ATOM   210  O  OG  . SER   A 1 27  ? 25.596 5.399   30.338 1.00 19.23 ? 40  SER   A OG  1 
ATOM   211  N  N   . ARG   A 1 28  ? 22.993 7.368   27.454 1.00 17.69 ? 41  ARG   A N   1 
ATOM   212  C  CA  . ARG   A 1 28  ? 21.974 7.525   26.424 1.00 17.57 ? 41  ARG   A CA  1 
ATOM   213  C  C   . ARG   A 1 28  ? 22.257 6.550   25.286 1.00 16.42 ? 41  ARG   A C   1 
ATOM   214  O  O   . ARG   A 1 28  ? 23.409 6.406   24.876 1.00 16.73 ? 41  ARG   A O   1 
ATOM   215  C  CB  . ARG   A 1 28  ? 21.999 8.939   25.826 1.00 18.55 ? 41  ARG   A CB  1 
ATOM   216  C  CG  . ARG   A 1 28  ? 21.862 10.046  26.861 1.00 19.73 ? 41  ARG   A CG  1 
ATOM   217  C  CD  . ARG   A 1 28  ? 22.096 11.441  26.318 0.10 20.27 ? 41  ARG   A CD  1 
ATOM   218  N  NE  . ARG   A 1 28  ? 22.000 12.450  27.379 0.10 20.97 ? 41  ARG   A NE  1 
ATOM   219  C  CZ  . ARG   A 1 28  ? 22.134 13.755  27.195 0.10 21.67 ? 41  ARG   A CZ  1 
ATOM   220  N  NH1 . ARG   A 1 28  ? 22.372 14.233  25.987 0.10 21.74 ? 41  ARG   A NH1 1 
ATOM   221  N  NH2 . ARG   A 1 28  ? 22.029 14.578  28.222 0.10 22.44 ? 41  ARG   A NH2 1 
ATOM   222  N  N   . CYS   A 1 29  ? 21.198 5.891   24.789 1.00 15.28 ? 42  CYS   A N   1 
ATOM   223  C  CA  . CYS   A 1 29  ? 21.282 5.017   23.627 1.00 14.46 ? 42  CYS   A CA  1 
ATOM   224  C  C   . CYS   A 1 29  ? 20.022 5.159   22.771 1.00 14.13 ? 42  CYS   A C   1 
ATOM   225  O  O   . CYS   A 1 29  ? 19.003 5.696   23.220 1.00 13.76 ? 42  CYS   A O   1 
ATOM   226  C  CB  . CYS   A 1 29  ? 21.408 3.543   24.016 1.00 14.18 ? 42  CYS   A CB  1 
ATOM   227  S  SG  . CYS   A 1 29  ? 23.057 3.043   24.575 1.00 13.99 ? 42  CYS   A SG  1 
ATOM   228  N  N   . GLY   A 1 30  ? 20.117 4.634   21.541 1.00 13.79 ? 43  GLY   A N   1 
ATOM   229  C  CA  . GLY   A 1 30  ? 18.972 4.354   20.692 1.00 13.42 ? 43  GLY   A CA  1 
ATOM   230  C  C   . GLY   A 1 30  ? 18.545 2.890   20.791 1.00 13.25 ? 43  GLY   A C   1 
ATOM   231  O  O   . GLY   A 1 30  ? 19.142 2.093   21.513 1.00 12.99 ? 43  GLY   A O   1 
ATOM   232  N  N   . GLY   A 1 31  ? 17.495 2.561   20.040 1.00 13.30 ? 44  GLY   A N   1 
ATOM   233  C  CA  . GLY   A 1 31  ? 16.882 1.245   20.017 1.00 13.49 ? 44  GLY   A CA  1 
ATOM   234  C  C   . GLY   A 1 31  ? 15.713 1.266   19.036 1.00 13.81 ? 44  GLY   A C   1 
ATOM   235  O  O   . GLY   A 1 31  ? 15.408 2.312   18.480 1.00 13.79 ? 44  GLY   A O   1 
ATOM   236  N  N   . PHE   A 1 32  ? 15.047 0.128   18.829 1.00 14.37 ? 45  PHE   A N   1 
ATOM   237  C  CA  . PHE   A 1 32  ? 13.941 0.107   17.891 1.00 14.95 ? 45  PHE   A CA  1 
ATOM   238  C  C   . PHE   A 1 32  ? 12.919 -0.951  18.306 1.00 15.39 ? 45  PHE   A C   1 
ATOM   239  O  O   . PHE   A 1 32  ? 13.272 -2.056  18.708 1.00 15.08 ? 45  PHE   A O   1 
ATOM   240  C  CB  . PHE   A 1 32  ? 14.502 -0.038  16.465 1.00 15.40 ? 45  PHE   A CB  1 
ATOM   241  C  CG  . PHE   A 1 32  ? 15.503 -1.160  16.219 1.00 15.53 ? 45  PHE   A CG  1 
ATOM   242  C  CD1 . PHE   A 1 32  ? 16.837 -1.020  16.586 1.00 15.25 ? 45  PHE   A CD1 1 
ATOM   243  C  CD2 . PHE   A 1 32  ? 15.122 -2.331  15.563 1.00 16.24 ? 45  PHE   A CD2 1 
ATOM   244  C  CE1 . PHE   A 1 32  ? 17.751 -2.038  16.363 1.00 15.41 ? 45  PHE   A CE1 1 
ATOM   245  C  CE2 . PHE   A 1 32  ? 16.040 -3.340  15.323 1.00 16.37 ? 45  PHE   A CE2 1 
ATOM   246  C  CZ  . PHE   A 1 32  ? 17.355 -3.194  15.721 1.00 16.06 ? 45  PHE   A CZ  1 
ATOM   247  N  N   . LEU   A 1 33  ? 11.642 -0.576  18.166 1.00 16.08 ? 46  LEU   A N   1 
ATOM   248  C  CA  . LEU   A 1 33  ? 10.503 -1.419  18.495 1.00 16.90 ? 46  LEU   A CA  1 
ATOM   249  C  C   . LEU   A 1 33  ? 10.387 -2.551  17.477 1.00 17.58 ? 46  LEU   A C   1 
ATOM   250  O  O   . LEU   A 1 33  ? 10.321 -2.304  16.270 1.00 18.05 ? 46  LEU   A O   1 
ATOM   251  C  CB  . LEU   A 1 33  ? 9.279  -0.503  18.476 1.00 17.26 ? 46  LEU   A CB  1 
ATOM   252  C  CG  . LEU   A 1 33  ? 7.982  -1.059  19.068 1.00 17.85 ? 46  LEU   A CG  1 
ATOM   253  C  CD1 . LEU   A 1 33  ? 8.086  -1.124  20.578 1.00 17.39 ? 46  LEU   A CD1 1 
ATOM   254  C  CD2 . LEU   A 1 33  ? 6.805  -0.195  18.636 1.00 18.54 ? 46  LEU   A CD2 1 
ATOM   255  N  N   . VAL   A 1 34  ? 10.396 -3.795  17.966 1.00 17.85 ? 47  VAL   A N   1 
ATOM   256  C  CA  . VAL   A 1 34  ? 10.310 -4.949  17.082 1.00 18.74 ? 47  VAL   A CA  1 
ATOM   257  C  C   . VAL   A 1 34  ? 8.998  -5.698  17.305 1.00 19.78 ? 47  VAL   A C   1 
ATOM   258  O  O   . VAL   A 1 34  ? 8.648  -6.562  16.502 1.00 20.48 ? 47  VAL   A O   1 
ATOM   259  C  CB  . VAL   A 1 34  ? 11.536 -5.873  17.237 1.00 18.53 ? 47  VAL   A CB  1 
ATOM   260  C  CG1 . VAL   A 1 34  ? 12.790 -5.190  16.715 1.00 17.99 ? 47  VAL   A CG1 1 
ATOM   261  C  CG2 . VAL   A 1 34  ? 11.734 -6.360  18.672 1.00 18.14 ? 47  VAL   A CG2 1 
ATOM   262  N  N   . ARG   A 1 35  ? 8.315  -5.393  18.419 1.00 19.91 ? 48  ARG   A N   1 
ATOM   263  C  CA  . ARG   A 1 35  ? 6.961  -5.858  18.694 1.00 21.04 ? 48  ARG   A CA  1 
ATOM   264  C  C   . ARG   A 1 35  ? 6.340  -4.892  19.703 1.00 20.41 ? 48  ARG   A C   1 
ATOM   265  O  O   . ARG   A 1 35  ? 7.058  -4.111  20.312 1.00 19.73 ? 48  ARG   A O   1 
ATOM   266  C  CB  . ARG   A 1 35  ? 7.020  -7.297  19.220 1.00 21.94 ? 48  ARG   A CB  1 
ATOM   267  C  CG  . ARG   A 1 35  ? 5.703  -8.059  19.209 1.00 23.53 ? 48  ARG   A CG  1 
ATOM   268  C  CD  . ARG   A 1 35  ? 5.888  -9.560  19.398 1.00 24.64 ? 48  ARG   A CD  1 
ATOM   269  N  NE  . ARG   A 1 35  ? 6.128  -9.951  20.792 1.00 24.94 ? 48  ARG   A NE  1 
ATOM   270  C  CZ  . ARG   A 1 35  ? 6.377  -11.198 21.182 1.00 26.11 ? 48  ARG   A CZ  1 
ATOM   271  N  NH1 . ARG   A 1 35  ? 6.481  -12.164 20.284 1.00 27.52 ? 48  ARG   A NH1 1 
ATOM   272  N  NH2 . ARG   A 1 35  ? 6.536  -11.483 22.463 1.00 25.90 ? 48  ARG   A NH2 1 
ATOM   273  N  N   . GLU   A 1 36  ? 5.018  -4.954  19.903 1.00 21.12 ? 49  GLU   A N   1 
ATOM   274  C  CA  . GLU   A 1 36  ? 4.317  -4.023  20.783 1.00 21.11 ? 49  GLU   A CA  1 
ATOM   275  C  C   . GLU   A 1 36  ? 4.916  -4.005  22.196 1.00 20.30 ? 49  GLU   A C   1 
ATOM   276  O  O   . GLU   A 1 36  ? 4.745  -3.021  22.917 1.00 19.74 ? 49  GLU   A O   1 
ATOM   277  C  CB  . GLU   A 1 36  ? 2.822  -4.354  20.845 1.00 22.25 ? 49  GLU   A CB  1 
ATOM   278  C  CG  . GLU   A 1 36  ? 2.025  -3.832  19.650 0.50 22.97 ? 49  GLU   A CG  1 
ATOM   279  C  CD  . GLU   A 1 36  ? 2.402  -4.349  18.266 0.50 23.50 ? 49  GLU   A CD  1 
ATOM   280  O  OE1 . GLU   A 1 36  ? 3.040  -5.424  18.135 0.50 23.27 ? 49  GLU   A OE1 1 
ATOM   281  O  OE2 . GLU   A 1 36  ? 2.053  -3.635  17.295 0.50 23.99 ? 49  GLU   A OE2 1 
ATOM   282  N  N   . ASP   A 1 37  ? 5.636  -5.070  22.588 1.00 20.14 ? 50  ASP   A N   1 
ATOM   283  C  CA  . ASP   A 1 37  ? 6.159  -5.184  23.943 1.00 19.70 ? 50  ASP   A CA  1 
ATOM   284  C  C   . ASP   A 1 37  ? 7.687  -5.291  24.025 1.00 19.08 ? 50  ASP   A C   1 
ATOM   285  O  O   . ASP   A 1 37  ? 8.208  -5.471  25.133 1.00 18.44 ? 50  ASP   A O   1 
ATOM   286  C  CB  . ASP   A 1 37  ? 5.549  -6.383  24.649 1.00 20.72 ? 50  ASP   A CB  1 
ATOM   287  C  CG  . ASP   A 1 37  ? 5.744  -7.717  23.943 1.00 21.43 ? 50  ASP   A CG  1 
ATOM   288  O  OD1 . ASP   A 1 37  ? 6.072  -7.702  22.731 1.00 21.24 ? 50  ASP   A OD1 1 
ATOM   289  O  OD2 . ASP   A 1 37  ? 5.609  -8.753  24.623 1.00 22.07 ? 50  ASP   A OD2 1 
ATOM   290  N  N   . PHE   A 1 38  ? 8.411  -5.175  22.896 1.00 18.72 ? 51  PHE   A N   1 
ATOM   291  C  CA  . PHE   A 1 38  ? 9.853  -5.399  22.915 1.00 18.18 ? 51  PHE   A CA  1 
ATOM   292  C  C   . PHE   A 1 38  ? 10.600 -4.356  22.085 1.00 17.28 ? 51  PHE   A C   1 
ATOM   293  O  O   . PHE   A 1 38  ? 10.222 -4.058  20.956 1.00 17.11 ? 51  PHE   A O   1 
ATOM   294  C  CB  . PHE   A 1 38  ? 10.228 -6.793  22.399 1.00 19.09 ? 51  PHE   A CB  1 
ATOM   295  C  CG  . PHE   A 1 38  ? 10.212 -7.881  23.460 1.00 19.67 ? 51  PHE   A CG  1 
ATOM   296  C  CD1 . PHE   A 1 38  ? 11.270 -8.010  24.355 1.00 19.53 ? 51  PHE   A CD1 1 
ATOM   297  C  CD2 . PHE   A 1 38  ? 9.146  -8.769  23.559 1.00 20.72 ? 51  PHE   A CD2 1 
ATOM   298  C  CE1 . PHE   A 1 38  ? 11.250 -8.987  25.337 1.00 20.01 ? 51  PHE   A CE1 1 
ATOM   299  C  CE2 . PHE   A 1 38  ? 9.127  -9.744  24.542 1.00 21.22 ? 51  PHE   A CE2 1 
ATOM   300  C  CZ  . PHE   A 1 38  ? 10.178 -9.849  25.432 1.00 20.86 ? 51  PHE   A CZ  1 
ATOM   301  N  N   . VAL   A 1 39  ? 11.700 -3.835  22.649 1.00 16.16 ? 52  VAL   A N   1 
ATOM   302  C  CA  . VAL   A 1 39  ? 12.634 -2.993  21.912 1.00 15.42 ? 52  VAL   A CA  1 
ATOM   303  C  C   . VAL   A 1 39  ? 13.967 -3.733  21.779 1.00 14.96 ? 52  VAL   A C   1 
ATOM   304  O  O   . VAL   A 1 39  ? 14.433 -4.342  22.739 1.00 15.01 ? 52  VAL   A O   1 
ATOM   305  C  CB  . VAL   A 1 39  ? 12.791 -1.649  22.651 1.00 14.99 ? 52  VAL   A CB  1 
ATOM   306  C  CG1 . VAL   A 1 39  ? 14.011 -0.864  22.184 1.00 14.65 ? 52  VAL   A CG1 1 
ATOM   307  C  CG2 . VAL   A 1 39  ? 11.527 -0.807  22.567 1.00 15.36 ? 52  VAL   A CG2 1 
ATOM   308  N  N   . LEU   A 1 40  ? 14.589 -3.668  20.594 1.00 14.50 ? 53  LEU   A N   1 
ATOM   309  C  CA  . LEU   A 1 40  ? 15.913 -4.237  20.384 1.00 14.24 ? 53  LEU   A CA  1 
ATOM   310  C  C   . LEU   A 1 40  ? 16.961 -3.118  20.438 1.00 13.37 ? 53  LEU   A C   1 
ATOM   311  O  O   . LEU   A 1 40  ? 16.718 -1.997  19.985 1.00 13.11 ? 53  LEU   A O   1 
ATOM   312  C  CB  . LEU   A 1 40  ? 15.887 -4.990  19.052 1.00 14.81 ? 53  LEU   A CB  1 
ATOM   313  C  CG  . LEU   A 1 40  ? 17.076 -5.890  18.705 1.00 15.12 ? 53  LEU   A CG  1 
ATOM   314  C  CD1 . LEU   A 1 40  ? 17.278 -7.019  19.715 1.00 15.55 ? 53  LEU   A CD1 1 
ATOM   315  C  CD2 . LEU   A 1 40  ? 16.918 -6.477  17.299 1.00 15.66 ? 53  LEU   A CD2 1 
ATOM   316  N  N   . THR   A 1 41  ? 18.121 -3.420  21.039 1.00 12.97 ? 54  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 41  ? 19.204 -2.456  21.212 1.00 12.36 ? 54  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 41  ? 20.513 -3.223  21.428 1.00 12.17 ? 54  THR   A C   1 
ATOM   319  O  O   . THR   A 1 41  ? 20.566 -4.424  21.175 1.00 12.32 ? 54  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 41  ? 18.856 -1.523  22.376 1.00 12.33 ? 54  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 41  ? 19.812 -0.467  22.483 1.00 12.28 ? 54  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 41  ? 18.794 -2.259  23.703 1.00 12.47 ? 54  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 42  ? 21.575 -2.536  21.878 1.00 11.75 ? 55  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 42  ? 22.861 -3.185  22.130 1.00 12.06 ? 55  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 42  ? 23.031 -3.524  23.613 1.00 12.19 ? 55  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 42  ? 22.564 -2.788  24.464 1.00 11.95 ? 55  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 42  ? 23.988 -2.307  21.666 1.00 12.01 ? 55  ALA   A CB  1 
ATOM   328  N  N   . ALA   A 1 43  ? 23.777 -4.602  23.903 1.00 12.72 ? 56  ALA   A N   1 
ATOM   329  C  CA  . ALA   A 1 43  ? 23.978 -5.101  25.257 1.00 13.18 ? 56  ALA   A CA  1 
ATOM   330  C  C   . ALA   A 1 43  ? 24.826 -4.143  26.093 1.00 13.41 ? 56  ALA   A C   1 
ATOM   331  O  O   . ALA   A 1 43  ? 24.683 -4.104  27.315 1.00 13.73 ? 56  ALA   A O   1 
ATOM   332  C  CB  . ALA   A 1 43  ? 24.608 -6.482  25.223 1.00 13.67 ? 56  ALA   A CB  1 
ATOM   333  N  N   . HIS   A 1 44  ? 25.703 -3.375  25.436 1.00 13.56 ? 57  HIS   A N   1 
ATOM   334  C  CA  . HIS   A 1 44  ? 26.550 -2.411  26.124 1.00 13.75 ? 57  HIS   A CA  1 
ATOM   335  C  C   . HIS   A 1 44  ? 25.743 -1.195  26.604 1.00 13.53 ? 57  HIS   A C   1 
ATOM   336  O  O   . HIS   A 1 44  ? 26.308 -0.323  27.263 1.00 13.60 ? 57  HIS   A O   1 
ATOM   337  C  CB  . HIS   A 1 44  ? 27.755 -2.028  25.253 1.00 13.82 ? 57  HIS   A CB  1 
ATOM   338  C  CG  . HIS   A 1 44  ? 27.451 -1.037  24.181 1.00 13.38 ? 57  HIS   A CG  1 
ATOM   339  N  ND1 . HIS   A 1 44  ? 27.466 -1.360  22.843 1.00 13.25 ? 57  HIS   A ND1 1 
ATOM   340  C  CD2 . HIS   A 1 44  ? 27.174 0.269   24.247 1.00 13.22 ? 57  HIS   A CD2 1 
ATOM   341  C  CE1 . HIS   A 1 44  ? 27.173 -0.281  22.132 1.00 13.11 ? 57  HIS   A CE1 1 
ATOM   342  N  NE2 . HIS   A 1 44  ? 26.983 0.721   22.961 1.00 13.13 ? 57  HIS   A NE2 1 
ATOM   343  N  N   . CYS   A 1 45  ? 24.443 -1.133  26.256 1.00 13.23 ? 58  CYS   A N   1 
ATOM   344  C  CA  . CYS   A 1 45  ? 23.535 -0.104  26.740 1.00 13.19 ? 58  CYS   A CA  1 
ATOM   345  C  C   . CYS   A 1 45  ? 22.842 -0.537  28.039 1.00 13.56 ? 58  CYS   A C   1 
ATOM   346  O  O   . CYS   A 1 45  ? 21.963 0.176   28.523 1.00 13.58 ? 58  CYS   A O   1 
ATOM   347  C  CB  . CYS   A 1 45  ? 22.476 0.255   25.701 1.00 12.84 ? 58  CYS   A CB  1 
ATOM   348  S  SG  . CYS   A 1 45  ? 23.132 1.021   24.191 1.00 12.80 ? 58  CYS   A SG  1 
ATOM   349  N  N   . TRP   A 1 46  ? 23.236 -1.688  28.609 1.00 13.98 ? 59  TRP   A N   1 
ATOM   350  C  CA  . TRP   A 1 46  ? 22.596 -2.206  29.810 1.00 14.36 ? 59  TRP   A CA  1 
ATOM   351  C  C   . TRP   A 1 46  ? 22.782 -1.242  30.982 1.00 14.85 ? 59  TRP   A C   1 
ATOM   352  O  O   . TRP   A 1 46  ? 23.831 -0.613  31.130 1.00 15.20 ? 59  TRP   A O   1 
ATOM   353  C  CB  . TRP   A 1 46  ? 23.120 -3.602  30.176 1.00 14.79 ? 59  TRP   A CB  1 
ATOM   354  C  CG  . TRP   A 1 46  ? 22.451 -4.213  31.387 1.00 15.10 ? 59  TRP   A CG  1 
ATOM   355  C  CD1 . TRP   A 1 46  ? 21.386 -5.069  31.402 1.00 14.99 ? 59  TRP   A CD1 1 
ATOM   356  C  CD2 . TRP   A 1 46  ? 22.795 -3.987  32.774 1.00 15.48 ? 59  TRP   A CD2 1 
ATOM   357  N  NE1 . TRP   A 1 46  ? 21.045 -5.391  32.689 1.00 15.65 ? 59  TRP   A NE1 1 
ATOM   358  C  CE2 . TRP   A 1 46  ? 21.885 -4.737  33.554 1.00 15.76 ? 59  TRP   A CE2 1 
ATOM   359  C  CE3 . TRP   A 1 46  ? 23.766 -3.220  33.429 1.00 15.79 ? 59  TRP   A CE3 1 
ATOM   360  C  CZ2 . TRP   A 1 46  ? 21.935 -4.752  34.948 1.00 16.42 ? 59  TRP   A CZ2 1 
ATOM   361  C  CZ3 . TRP   A 1 46  ? 23.821 -3.246  34.807 1.00 16.41 ? 59  TRP   A CZ3 1 
ATOM   362  C  CH2 . TRP   A 1 46  ? 22.914 -3.996  35.554 1.00 16.63 ? 59  TRP   A CH2 1 
ATOM   363  N  N   . GLY   A 1 47  ? 21.729 -1.149  31.805 1.00 15.07 ? 60  GLY   A N   1 
ATOM   364  C  CA  . GLY   A 1 47  ? 21.763 -0.444  33.075 1.00 15.72 ? 60  GLY   A CA  1 
ATOM   365  C  C   . GLY   A 1 47  ? 20.742 -1.065  34.024 1.00 16.07 ? 60  GLY   A C   1 
ATOM   366  O  O   . GLY   A 1 47  ? 19.909 -1.857  33.580 1.00 15.67 ? 60  GLY   A O   1 
ATOM   367  N  N   . SER   A 1 48  ? 20.801 -0.696  35.311 1.00 16.88 ? 61  SER   A N   1 
ATOM   368  C  CA  . SER   A 1 48  ? 19.880 -1.241  36.300 1.00 17.64 ? 61  SER   A CA  1 
ATOM   369  C  C   . SER   A 1 48  ? 18.481 -0.634  36.168 1.00 17.89 ? 61  SER   A C   1 
ATOM   370  O  O   . SER   A 1 48  ? 17.526 -1.209  36.688 1.00 17.95 ? 61  SER   A O   1 
ATOM   371  C  CB  . SER   A 1 48  ? 20.414 -1.098  37.710 1.00 18.51 ? 61  SER   A CB  1 
ATOM   372  O  OG  . SER   A 1 48  ? 20.785 0.240   38.014 1.00 18.75 ? 61  SER   A OG  1 
ATOM   373  N  N   . ASN   A 1 49  ? 18.372 0.523   35.499 1.00 18.30 ? 63  ASN   A N   1 
ATOM   374  C  CA  . ASN   A 1 49  ? 17.097 1.177   35.224 1.00 19.17 ? 63  ASN   A CA  1 
ATOM   375  C  C   . ASN   A 1 49  ? 17.162 1.762   33.814 1.00 17.80 ? 63  ASN   A C   1 
ATOM   376  O  O   . ASN   A 1 49  ? 18.068 2.547   33.543 1.00 17.09 ? 63  ASN   A O   1 
ATOM   377  C  CB  . ASN   A 1 49  ? 16.801 2.248   36.275 1.00 21.67 ? 63  ASN   A CB  1 
ATOM   378  C  CG  . ASN   A 1 49  ? 15.543 3.053   36.017 1.00 24.27 ? 63  ASN   A CG  1 
ATOM   379  O  OD1 . ASN   A 1 49  ? 15.576 4.294   36.057 1.00 27.60 ? 63  ASN   A OD1 1 
ATOM   380  N  ND2 . ASN   A 1 49  ? 14.420 2.385   35.793 1.00 24.83 ? 63  ASN   A ND2 1 
ATOM   381  N  N   . ILE   A 1 50  ? 16.225 1.358   32.937 1.00 17.13 ? 64  ILE   A N   1 
ATOM   382  C  CA  . ILE   A 1 50  ? 16.115 1.908   31.584 1.00 17.04 ? 64  ILE   A CA  1 
ATOM   383  C  C   . ILE   A 1 50  ? 14.680 2.386   31.344 1.00 17.01 ? 64  ILE   A C   1 
ATOM   384  O  O   . ILE   A 1 50  ? 13.734 1.620   31.526 1.00 17.07 ? 64  ILE   A O   1 
ATOM   385  C  CB  . ILE   A 1 50  ? 16.551 0.884   30.514 1.00 16.69 ? 64  ILE   A CB  1 
ATOM   386  C  CG1 . ILE   A 1 50  ? 17.981 0.362   30.766 1.00 17.02 ? 64  ILE   A CG1 1 
ATOM   387  C  CG2 . ILE   A 1 50  ? 16.414 1.452   29.100 1.00 16.40 ? 64  ILE   A CG2 1 
ATOM   388  C  CD1 . ILE   A 1 50  ? 18.332 -0.906  30.009 1.00 16.92 ? 64  ILE   A CD1 1 
ATOM   389  N  N   . ASN   A 1 51  ? 14.529 3.661   30.954 1.00 17.30 ? 65  ASN   A N   1 
ATOM   390  C  CA  . ASN   A 1 51  ? 13.250 4.206   30.512 1.00 17.54 ? 65  ASN   A CA  1 
ATOM   391  C  C   . ASN   A 1 51  ? 13.278 4.407   28.999 1.00 16.78 ? 65  ASN   A C   1 
ATOM   392  O  O   . ASN   A 1 51  ? 14.257 4.919   28.470 1.00 16.81 ? 65  ASN   A O   1 
ATOM   393  C  CB  . ASN   A 1 51  ? 12.912 5.527   31.194 1.00 18.69 ? 65  ASN   A CB  1 
ATOM   394  C  CG  . ASN   A 1 51  ? 12.763 5.405   32.696 1.00 20.03 ? 65  ASN   A CG  1 
ATOM   395  O  OD1 . ASN   A 1 51  ? 12.973 6.390   33.412 1.00 21.88 ? 65  ASN   A OD1 1 
ATOM   396  N  ND2 . ASN   A 1 51  ? 12.448 4.225   33.211 1.00 20.01 ? 65  ASN   A ND2 1 
ATOM   397  N  N   . VAL   A 1 52  ? 12.186 4.028   28.322 1.00 16.31 ? 66  VAL   A N   1 
ATOM   398  C  CA  . VAL   A 1 52  ? 12.095 4.105   26.870 1.00 15.83 ? 66  VAL   A CA  1 
ATOM   399  C  C   . VAL   A 1 52  ? 11.094 5.193   26.477 1.00 16.11 ? 66  VAL   A C   1 
ATOM   400  O  O   . VAL   A 1 52  ? 9.997  5.270   27.037 1.00 16.52 ? 66  VAL   A O   1 
ATOM   401  C  CB  . VAL   A 1 52  ? 11.676 2.743   26.283 1.00 15.93 ? 66  VAL   A CB  1 
ATOM   402  C  CG1 . VAL   A 1 52  ? 11.720 2.755   24.761 1.00 15.97 ? 66  VAL   A CG1 1 
ATOM   403  C  CG2 . VAL   A 1 52  ? 12.518 1.590   26.815 1.00 15.84 ? 66  VAL   A CG2 1 
ATOM   404  N  N   . THR   A 1 53  ? 11.465 6.022   25.493 1.00 15.46 ? 67  THR   A N   1 
ATOM   405  C  CA  . THR   A 1 53  ? 10.524 6.958   24.898 1.00 15.91 ? 67  THR   A CA  1 
ATOM   406  C  C   . THR   A 1 53  ? 10.305 6.610   23.427 1.00 15.92 ? 67  THR   A C   1 
ATOM   407  O  O   . THR   A 1 53  ? 11.256 6.573   22.655 1.00 15.49 ? 67  THR   A O   1 
ATOM   408  C  CB  . THR   A 1 53  ? 11.016 8.395   25.042 1.00 16.15 ? 67  THR   A CB  1 
ATOM   409  O  OG1 . THR   A 1 53  ? 11.255 8.649   26.420 1.00 16.21 ? 67  THR   A OG1 1 
ATOM   410  C  CG2 . THR   A 1 53  ? 9.979  9.388   24.553 1.00 17.01 ? 67  THR   A CG2 1 
ATOM   411  N  N   . LEU   A 1 54  ? 9.042  6.346   23.072 1.00 16.34 ? 68  LEU   A N   1 
ATOM   412  C  CA  . LEU   A 1 54  ? 8.608  6.207   21.691 1.00 16.77 ? 68  LEU   A CA  1 
ATOM   413  C  C   . LEU   A 1 54  ? 7.773  7.428   21.305 1.00 17.20 ? 68  LEU   A C   1 
ATOM   414  O  O   . LEU   A 1 54  ? 7.300  8.143   22.178 1.00 17.26 ? 68  LEU   A O   1 
ATOM   415  C  CB  . LEU   A 1 54  ? 7.816  4.906   21.627 1.00 17.31 ? 68  LEU   A CB  1 
ATOM   416  C  CG  . LEU   A 1 54  ? 8.600  3.687   22.109 1.00 17.68 ? 68  LEU   A CG  1 
ATOM   417  C  CD1 . LEU   A 1 54  ? 7.719  2.686   22.808 1.00 18.31 ? 68  LEU   A CD1 1 
ATOM   418  C  CD2 . LEU   A 1 54  ? 9.331  3.062   20.959 1.00 18.14 ? 68  LEU   A CD2 1 
ATOM   419  N  N   . GLY   A 1 55  ? 7.630  7.673   19.998 1.00 17.26 ? 69  GLY   A N   1 
ATOM   420  C  CA  . GLY   A 1 55  ? 6.802  8.756   19.490 1.00 17.92 ? 69  GLY   A CA  1 
ATOM   421  C  C   . GLY   A 1 55  ? 7.497  10.120  19.499 1.00 18.00 ? 69  GLY   A C   1 
ATOM   422  O  O   . GLY   A 1 55  ? 6.840  11.143  19.295 1.00 18.71 ? 69  GLY   A O   1 
ATOM   423  N  N   . ALA   A 1 56  ? 8.823  10.144  19.673 1.00 17.27 ? 70  ALA   A N   1 
ATOM   424  C  CA  . ALA   A 1 56  ? 9.538  11.391  19.892 1.00 17.79 ? 70  ALA   A CA  1 
ATOM   425  C  C   . ALA   A 1 56  ? 10.187 11.904  18.607 1.00 18.47 ? 70  ALA   A C   1 
ATOM   426  O  O   . ALA   A 1 56  ? 10.538 11.125  17.715 1.00 18.34 ? 70  ALA   A O   1 
ATOM   427  C  CB  . ALA   A 1 56  ? 10.572 11.198  20.971 1.00 17.37 ? 70  ALA   A CB  1 
ATOM   428  N  N   . HIS   A 1 57  ? 10.342 13.236  18.531 1.00 19.33 ? 71  HIS   A N   1 
ATOM   429  C  CA  . HIS   A 1 57  ? 11.238 13.852  17.564 1.00 19.96 ? 71  HIS   A CA  1 
ATOM   430  C  C   . HIS   A 1 57  ? 12.246 14.723  18.310 1.00 20.28 ? 71  HIS   A C   1 
ATOM   431  O  O   . HIS   A 1 57  ? 13.442 14.488  18.222 1.00 20.06 ? 71  HIS   A O   1 
ATOM   432  C  CB  . HIS   A 1 57  ? 10.465 14.567  16.449 1.00 20.61 ? 71  HIS   A CB  1 
ATOM   433  C  CG  . HIS   A 1 57  ? 11.363 15.121  15.400 1.00 20.98 ? 71  HIS   A CG  1 
ATOM   434  N  ND1 . HIS   A 1 57  ? 12.147 14.310  14.607 1.00 20.41 ? 71  HIS   A ND1 1 
ATOM   435  C  CD2 . HIS   A 1 57  ? 11.645 16.382  15.040 1.00 21.74 ? 71  HIS   A CD2 1 
ATOM   436  C  CE1 . HIS   A 1 57  ? 12.857 15.063  13.785 1.00 20.72 ? 71  HIS   A CE1 1 
ATOM   437  N  NE2 . HIS   A 1 57  ? 12.561 16.326  14.023 1.00 21.67 ? 71  HIS   A NE2 1 
ATOM   438  N  N   . ASN   A 1 58  ? 11.759 15.706  19.066 1.00 21.39 ? 72  ASN   A N   1 
ATOM   439  C  CA  . ASN   A 1 58  ? 12.612 16.467  19.964 1.00 22.17 ? 72  ASN   A CA  1 
ATOM   440  C  C   . ASN   A 1 58  ? 12.477 15.896  21.375 1.00 22.08 ? 72  ASN   A C   1 
ATOM   441  O  O   . ASN   A 1 58  ? 11.495 16.179  22.061 1.00 22.08 ? 72  ASN   A O   1 
ATOM   442  C  CB  . ASN   A 1 58  ? 12.291 17.954  19.890 1.00 23.52 ? 72  ASN   A CB  1 
ATOM   443  C  CG  . ASN   A 1 58  ? 13.209 18.767  20.769 1.00 24.33 ? 72  ASN   A CG  1 
ATOM   444  O  OD1 . ASN   A 1 58  ? 13.741 18.250  21.761 1.00 24.25 ? 72  ASN   A OD1 1 
ATOM   445  N  ND2 . ASN   A 1 58  ? 13.383 20.041  20.447 1.00 25.53 ? 72  ASN   A ND2 1 
ATOM   446  N  N   A ILE   A 1 59  ? 13.476 15.111  21.812 0.50 21.82 ? 73  ILE   A N   1 
ATOM   447  N  N   B ILE   A 1 59  ? 13.488 15.123  21.804 0.50 21.51 ? 73  ILE   A N   1 
ATOM   448  C  CA  A ILE   A 1 59  ? 13.371 14.371  23.062 0.50 21.75 ? 73  ILE   A CA  1 
ATOM   449  C  CA  B ILE   A 1 59  ? 13.420 14.374  23.050 0.50 21.18 ? 73  ILE   A CA  1 
ATOM   450  C  C   A ILE   A 1 59  ? 13.609 15.278  24.270 0.50 22.63 ? 73  ILE   A C   1 
ATOM   451  C  C   B ILE   A 1 59  ? 13.517 15.306  24.258 0.50 22.35 ? 73  ILE   A C   1 
ATOM   452  O  O   A ILE   A 1 59  ? 13.473 14.813  25.399 0.50 22.38 ? 73  ILE   A O   1 
ATOM   453  O  O   B ILE   A 1 59  ? 13.201 14.888  25.367 0.50 22.21 ? 73  ILE   A O   1 
ATOM   454  C  CB  A ILE   A 1 59  ? 14.312 13.148  23.078 0.50 21.16 ? 73  ILE   A CB  1 
ATOM   455  C  CB  B ILE   A 1 59  ? 14.516 13.293  23.120 0.50 20.18 ? 73  ILE   A CB  1 
ATOM   456  C  CG1 A ILE   A 1 59  ? 15.751 13.515  22.719 0.50 21.37 ? 73  ILE   A CG1 1 
ATOM   457  C  CG1 B ILE   A 1 59  ? 14.191 12.242  24.174 0.50 19.53 ? 73  ILE   A CG1 1 
ATOM   458  C  CG2 A ILE   A 1 59  ? 13.774 12.040  22.174 0.50 20.95 ? 73  ILE   A CG2 1 
ATOM   459  C  CG2 B ILE   A 1 59  ? 15.890 13.919  23.358 0.50 20.46 ? 73  ILE   A CG2 1 
ATOM   460  C  CD1 A ILE   A 1 59  ? 16.559 14.069  23.878 0.50 21.79 ? 73  ILE   A CD1 1 
ATOM   461  C  CD1 B ILE   A 1 59  ? 12.991 11.371  23.840 0.50 19.27 ? 73  ILE   A CD1 1 
ATOM   462  N  N   . GLN   A 1 60  ? 13.959 16.552  24.047 1.00 24.03 ? 74  GLN   A N   1 
ATOM   463  C  CA  . GLN   A 1 60  ? 14.163 17.501  25.139 1.00 26.26 ? 74  GLN   A CA  1 
ATOM   464  C  C   . GLN   A 1 60  ? 12.890 18.276  25.487 1.00 26.82 ? 74  GLN   A C   1 
ATOM   465  O  O   . GLN   A 1 60  ? 12.868 18.959  26.506 1.00 28.01 ? 74  GLN   A O   1 
ATOM   466  C  CB  . GLN   A 1 60  ? 15.309 18.475  24.857 1.00 28.08 ? 74  GLN   A CB  1 
ATOM   467  C  CG  . GLN   A 1 60  ? 16.694 17.840  24.953 1.00 29.14 ? 74  GLN   A CG  1 
ATOM   468  C  CD  . GLN   A 1 60  ? 16.947 17.143  26.274 1.00 30.56 ? 74  GLN   A CD  1 
ATOM   469  O  OE1 . GLN   A 1 60  ? 17.098 15.918  26.345 1.00 32.62 ? 74  GLN   A OE1 1 
ATOM   470  N  NE2 . GLN   A 1 60  ? 16.978 17.913  27.349 1.00 32.18 ? 74  GLN   A NE2 1 
ATOM   471  N  N   . ARG   A 1 61  ? 11.841 18.167  24.662 1.00 26.81 ? 75  ARG   A N   1 
ATOM   472  C  CA  . ARG   A 1 61  ? 10.579 18.860  24.894 1.00 27.38 ? 75  ARG   A CA  1 
ATOM   473  C  C   . ARG   A 1 61  ? 9.430  17.854  24.987 1.00 25.72 ? 75  ARG   A C   1 
ATOM   474  O  O   . ARG   A 1 61  ? 9.509  16.770  24.411 1.00 24.18 ? 75  ARG   A O   1 
ATOM   475  C  CB  . ARG   A 1 61  ? 10.336 19.866  23.762 1.00 28.94 ? 75  ARG   A CB  1 
ATOM   476  C  CG  . ARG   A 1 61  ? 11.513 20.811  23.558 1.00 30.38 ? 75  ARG   A CG  1 
ATOM   477  C  CD  . ARG   A 1 61  ? 11.179 22.095  22.798 0.50 32.11 ? 75  ARG   A CD  1 
ATOM   478  N  NE  . ARG   A 1 61  ? 11.027 21.922  21.348 0.50 32.46 ? 75  ARG   A NE  1 
ATOM   479  C  CZ  . ARG   A 1 61  ? 10.975 22.932  20.486 0.50 34.01 ? 75  ARG   A CZ  1 
ATOM   480  N  NH1 . ARG   A 1 61  ? 11.086 24.175  20.920 0.50 35.48 ? 75  ARG   A NH1 1 
ATOM   481  N  NH2 . ARG   A 1 61  ? 10.817 22.704  19.194 0.50 34.31 ? 75  ARG   A NH2 1 
ATOM   482  N  N   . ARG   A 1 62  ? 8.363  18.231  25.714 1.00 25.47 ? 76  ARG   A N   1 
ATOM   483  C  CA  . ARG   A 1 62  ? 7.138  17.445  25.781 1.00 24.91 ? 76  ARG   A CA  1 
ATOM   484  C  C   . ARG   A 1 62  ? 6.450  17.448  24.420 1.00 25.58 ? 76  ARG   A C   1 
ATOM   485  O  O   . ARG   A 1 62  ? 6.346  18.491  23.782 1.00 27.12 ? 76  ARG   A O   1 
ATOM   486  C  CB  . ARG   A 1 62  ? 6.113  18.002  26.779 1.00 25.16 ? 76  ARG   A CB  1 
ATOM   487  C  CG  . ARG   A 1 62  ? 6.389  17.708  28.242 1.00 24.43 ? 76  ARG   A CG  1 
ATOM   488  C  CD  . ARG   A 1 62  ? 5.522  18.506  29.218 1.00 25.18 ? 76  ARG   A CD  1 
ATOM   489  N  NE  . ARG   A 1 62  ? 4.121  18.075  29.283 1.00 24.88 ? 76  ARG   A NE  1 
ATOM   490  C  CZ  . ARG   A 1 62  ? 3.147  18.697  29.936 1.00 25.29 ? 76  ARG   A CZ  1 
ATOM   491  N  NH1 . ARG   A 1 62  ? 3.366  19.855  30.531 1.00 26.22 ? 76  ARG   A NH1 1 
ATOM   492  N  NH2 . ARG   A 1 62  ? 1.938  18.176  29.950 1.00 25.20 ? 76  ARG   A NH2 1 
ATOM   493  N  N   . GLU   A 1 63  ? 5.963  16.280  23.984 1.00 24.96 ? 77  GLU   A N   1 
ATOM   494  C  CA  . GLU   A 1 63  ? 5.022  16.217  22.874 1.00 25.52 ? 77  GLU   A CA  1 
ATOM   495  C  C   . GLU   A 1 63  ? 4.001  15.126  23.189 1.00 24.25 ? 77  GLU   A C   1 
ATOM   496  O  O   . GLU   A 1 63  ? 4.369  14.066  23.686 1.00 22.93 ? 77  GLU   A O   1 
ATOM   497  C  CB  . GLU   A 1 63  ? 5.679  15.922  21.521 1.00 25.97 ? 77  GLU   A CB  1 
ATOM   498  C  CG  . GLU   A 1 63  ? 7.176  16.229  21.458 1.00 26.44 ? 77  GLU   A CG  1 
ATOM   499  C  CD  . GLU   A 1 63  ? 7.901  15.617  20.268 1.00 26.66 ? 77  GLU   A CD  1 
ATOM   500  O  OE1 . GLU   A 1 63  ? 8.754  14.704  20.448 1.00 24.43 ? 77  GLU   A OE1 1 
ATOM   501  O  OE2 . GLU   A 1 63  ? 7.594  16.079  19.140 1.00 28.37 ? 77  GLU   A OE2 1 
ATOM   502  N  N   . ASN   A 1 64  ? 2.728  15.384  22.862 1.00 24.34 ? 78  ASN   A N   1 
ATOM   503  C  CA  . ASN   A 1 64  ? 1.645  14.483  23.230 1.00 23.80 ? 78  ASN   A CA  1 
ATOM   504  C  C   . ASN   A 1 64  ? 1.710  13.200  22.401 1.00 22.84 ? 78  ASN   A C   1 
ATOM   505  O  O   . ASN   A 1 64  ? 0.899  12.298  22.605 1.00 22.80 ? 78  ASN   A O   1 
ATOM   506  C  CB  . ASN   A 1 64  ? 0.281  15.184  23.221 1.00 25.05 ? 78  ASN   A CB  1 
ATOM   507  C  CG  . ASN   A 1 64  ? -0.181 15.701  21.876 1.00 25.74 ? 78  ASN   A CG  1 
ATOM   508  O  OD1 . ASN   A 1 64  ? -1.175 16.438  21.810 1.00 26.86 ? 78  ASN   A OD1 1 
ATOM   509  N  ND2 . ASN   A 1 64  ? 0.500  15.346  20.800 1.00 24.98 ? 78  ASN   A ND2 1 
ATOM   510  N  N   . THR   A 1 65  ? 2.679  13.111  21.477 1.00 22.18 ? 79  THR   A N   1 
ATOM   511  C  CA  . THR   A 1 65  ? 2.897  11.899  20.702 1.00 21.36 ? 79  THR   A CA  1 
ATOM   512  C  C   . THR   A 1 65  ? 3.756  10.898  21.478 1.00 20.17 ? 79  THR   A C   1 
ATOM   513  O  O   . THR   A 1 65  ? 3.757  9.721   21.137 1.00 19.72 ? 79  THR   A O   1 
ATOM   514  C  CB  . THR   A 1 65  ? 3.529  12.245  19.348 1.00 21.43 ? 79  THR   A CB  1 
ATOM   515  O  OG1 . THR   A 1 65  ? 4.766  12.919  19.561 1.00 20.83 ? 79  THR   A OG1 1 
ATOM   516  C  CG2 . THR   A 1 65  ? 2.639  13.135  18.498 1.00 22.75 ? 79  THR   A CG2 1 
ATOM   517  N  N   . GLN   A 1 66  ? 4.476  11.351  22.520 1.00 19.90 ? 80  GLN   A N   1 
ATOM   518  C  CA  . GLN   A 1 66  ? 5.450  10.508  23.207 1.00 19.08 ? 80  GLN   A CA  1 
ATOM   519  C  C   . GLN   A 1 66  ? 4.768  9.483   24.116 1.00 19.14 ? 80  GLN   A C   1 
ATOM   520  O  O   . GLN   A 1 66  ? 3.740  9.771   24.731 1.00 19.77 ? 80  GLN   A O   1 
ATOM   521  C  CB  . GLN   A 1 66  ? 6.449  11.340  24.009 1.00 18.95 ? 80  GLN   A CB  1 
ATOM   522  C  CG  . GLN   A 1 66  ? 7.362  12.192  23.132 1.00 19.19 ? 80  GLN   A CG  1 
ATOM   523  C  CD  . GLN   A 1 66  ? 8.302  13.067  23.935 1.00 19.72 ? 80  GLN   A CD  1 
ATOM   524  O  OE1 . GLN   A 1 66  ? 8.457  12.894  25.149 1.00 19.76 ? 80  GLN   A OE1 1 
ATOM   525  N  NE2 . GLN   A 1 66  ? 8.967  13.996  23.260 1.00 20.36 ? 80  GLN   A NE2 1 
ATOM   526  N  N   . GLN   A 1 67  ? 5.349  8.277   24.163 1.00 19.11 ? 81  GLN   A N   1 
ATOM   527  C  CA  . GLN   A 1 67  ? 4.984  7.252   25.130 1.00 19.50 ? 81  GLN   A CA  1 
ATOM   528  C  C   . GLN   A 1 67  ? 6.224  6.867   25.934 1.00 18.97 ? 81  GLN   A C   1 
ATOM   529  O  O   . GLN   A 1 67  ? 7.226  6.439   25.359 1.00 18.05 ? 81  GLN   A O   1 
ATOM   530  C  CB  . GLN   A 1 67  ? 4.375  6.029   24.445 1.00 19.67 ? 81  GLN   A CB  1 
ATOM   531  C  CG  . GLN   A 1 67  ? 3.032  6.313   23.781 1.00 20.60 ? 81  GLN   A CG  1 
ATOM   532  C  CD  . GLN   A 1 67  ? 2.454  5.116   23.063 1.00 20.80 ? 81  GLN   A CD  1 
ATOM   533  O  OE1 . GLN   A 1 67  ? 2.352  4.012   23.608 1.00 20.69 ? 81  GLN   A OE1 1 
ATOM   534  N  NE2 . GLN   A 1 67  ? 2.073  5.326   21.816 1.00 21.75 ? 81  GLN   A NE2 1 
ATOM   535  N  N   . HIS   A 1 68  ? 6.127  7.018   27.264 1.00 19.44 ? 82  HIS   A N   1 
ATOM   536  C  CA  . HIS   A 1 68  ? 7.227  6.760   28.184 1.00 19.53 ? 82  HIS   A CA  1 
ATOM   537  C  C   . HIS   A 1 68  ? 6.958  5.480   28.980 1.00 19.08 ? 82  HIS   A C   1 
ATOM   538  O  O   . HIS   A 1 68  ? 6.040  5.438   29.805 1.00 19.24 ? 82  HIS   A O   1 
ATOM   539  C  CB  . HIS   A 1 68  ? 7.395  7.944   29.145 1.00 20.96 ? 82  HIS   A CB  1 
ATOM   540  C  CG  . HIS   A 1 68  ? 7.649  9.255   28.482 1.00 22.19 ? 82  HIS   A CG  1 
ATOM   541  N  ND1 . HIS   A 1 68  ? 8.888  9.613   27.985 1.00 22.52 ? 82  HIS   A ND1 1 
ATOM   542  C  CD2 . HIS   A 1 68  ? 6.828  10.295  28.216 1.00 23.28 ? 82  HIS   A CD2 1 
ATOM   543  C  CE1 . HIS   A 1 68  ? 8.805  10.831  27.452 1.00 23.13 ? 82  HIS   A CE1 1 
ATOM   544  N  NE2 . HIS   A 1 68  ? 7.567  11.261  27.584 1.00 23.39 ? 82  HIS   A NE2 1 
ATOM   545  N  N   . ILE   A 1 69  ? 7.779  4.448   28.744 1.00 18.30 ? 83  ILE   A N   1 
ATOM   546  C  CA  . ILE   A 1 69  ? 7.587  3.130   29.329 1.00 17.96 ? 83  ILE   A CA  1 
ATOM   547  C  C   . ILE   A 1 69  ? 8.911  2.658   29.927 1.00 17.41 ? 83  ILE   A C   1 
ATOM   548  O  O   . ILE   A 1 69  ? 9.931  2.673   29.249 1.00 16.49 ? 83  ILE   A O   1 
ATOM   549  C  CB  . ILE   A 1 69  ? 7.052  2.133   28.279 1.00 18.00 ? 83  ILE   A CB  1 
ATOM   550  C  CG1 . ILE   A 1 69  ? 5.840  2.702   27.514 1.00 18.56 ? 83  ILE   A CG1 1 
ATOM   551  C  CG2 . ILE   A 1 69  ? 6.736  0.786   28.940 1.00 18.10 ? 83  ILE   A CG2 1 
ATOM   552  C  CD1 . ILE   A 1 69  ? 5.371  1.864   26.334 1.00 18.68 ? 83  ILE   A CD1 1 
ATOM   553  N  N   . THR   A 1 70  ? 8.898  2.244   31.199 1.00 17.81 ? 84  THR   A N   1 
ATOM   554  C  CA  . THR   A 1 70  ? 10.095 1.679   31.811 1.00 18.10 ? 84  THR   A CA  1 
ATOM   555  C  C   . THR   A 1 70  ? 10.246 0.242   31.317 1.00 17.87 ? 84  THR   A C   1 
ATOM   556  O  O   . THR   A 1 70  ? 9.250  -0.427  31.052 1.00 18.44 ? 84  THR   A O   1 
ATOM   557  C  CB  . THR   A 1 70  ? 10.047 1.787   33.340 1.00 19.26 ? 84  THR   A CB  1 
ATOM   558  O  OG1 . THR   A 1 70  ? 8.980  0.979   33.819 1.00 21.75 ? 84  THR   A OG1 1 
ATOM   559  C  CG2 . THR   A 1 70  ? 9.763  3.188   33.841 1.00 19.43 ? 84  THR   A CG2 1 
ATOM   560  N  N   . ALA   A 1 71  ? 11.495 -0.215  31.146 1.00 17.30 ? 85  ALA   A N   1 
ATOM   561  C  CA  . ALA   A 1 71  ? 11.769 -1.602  30.791 1.00 17.04 ? 85  ALA   A CA  1 
ATOM   562  C  C   . ALA   A 1 71  ? 11.652 -2.488  32.032 1.00 17.29 ? 85  ALA   A C   1 
ATOM   563  O  O   . ALA   A 1 71  ? 12.369 -2.281  33.011 1.00 16.86 ? 85  ALA   A O   1 
ATOM   564  C  CB  . ALA   A 1 71  ? 13.147 -1.722  30.164 1.00 16.70 ? 85  ALA   A CB  1 
ATOM   565  N  N   . ARG   A 1 72  ? 10.766 -3.494  31.960 1.00 17.40 ? 86  ARG   A N   1 
ATOM   566  C  CA  . ARG   A 1 72  ? 10.567 -4.445  33.040 1.00 18.05 ? 86  ARG   A CA  1 
ATOM   567  C  C   . ARG   A 1 72  ? 11.726 -5.441  33.112 1.00 18.59 ? 86  ARG   A C   1 
ATOM   568  O  O   . ARG   A 1 72  ? 12.078 -5.886  34.200 1.00 18.97 ? 86  ARG   A O   1 
ATOM   569  C  CB  . ARG   A 1 72  ? 9.230  -5.181  32.890 1.00 18.08 ? 86  ARG   A CB  1 
ATOM   570  C  CG  . ARG   A 1 72  ? 8.945  -6.212  33.974 1.00 18.77 ? 86  ARG   A CG  1 
ATOM   571  C  CD  . ARG   A 1 72  ? 8.858  -5.633  35.390 1.00 18.86 ? 86  ARG   A CD  1 
ATOM   572  N  NE  . ARG   A 1 72  ? 8.777  -6.653  36.445 1.00 19.55 ? 86  ARG   A NE  1 
ATOM   573  C  CZ  . ARG   A 1 72  ? 9.798  -7.369  36.919 1.00 19.85 ? 86  ARG   A CZ  1 
ATOM   574  N  NH1 . ARG   A 1 72  ? 11.026 -7.201  36.447 1.00 19.05 ? 86  ARG   A NH1 1 
ATOM   575  N  NH2 . ARG   A 1 72  ? 9.593  -8.236  37.898 1.00 20.81 ? 86  ARG   A NH2 1 
ATOM   576  N  N   . ARG   A 1 73  ? 12.294 -5.796  31.955 1.00 19.18 ? 87  ARG   A N   1 
ATOM   577  C  CA  . ARG   A 1 73  ? 13.418 -6.714  31.864 1.00 20.47 ? 87  ARG   A CA  1 
ATOM   578  C  C   . ARG   A 1 73  ? 14.405 -6.204  30.810 1.00 19.01 ? 87  ARG   A C   1 
ATOM   579  O  O   . ARG   A 1 73  ? 14.003 -5.743  29.741 1.00 18.07 ? 87  ARG   A O   1 
ATOM   580  C  CB  . ARG   A 1 73  ? 12.922 -8.112  31.472 1.00 22.96 ? 87  ARG   A CB  1 
ATOM   581  C  CG  . ARG   A 1 73  ? 12.193 -8.891  32.563 1.00 26.02 ? 87  ARG   A CG  1 
ATOM   582  C  CD  . ARG   A 1 73  ? 13.006 -10.043 33.117 1.00 28.70 ? 87  ARG   A CD  1 
ATOM   583  N  NE  . ARG   A 1 73  ? 12.771 -11.271 32.347 1.00 31.95 ? 87  ARG   A NE  1 
ATOM   584  C  CZ  . ARG   A 1 73  ? 13.633 -12.271 32.168 1.00 34.97 ? 87  ARG   A CZ  1 
ATOM   585  N  NH1 . ARG   A 1 73  ? 14.890 -12.160 32.573 1.00 36.88 ? 87  ARG   A NH1 1 
ATOM   586  N  NH2 . ARG   A 1 73  ? 13.244 -13.378 31.557 1.00 36.15 ? 87  ARG   A NH2 1 
ATOM   587  N  N   . ALA   A 1 74  ? 15.703 -6.290  31.127 1.00 18.54 ? 88  ALA   A N   1 
ATOM   588  C  CA  . ALA   A 1 74  ? 16.762 -5.980  30.176 1.00 17.69 ? 88  ALA   A CA  1 
ATOM   589  C  C   . ALA   A 1 74  ? 17.595 -7.236  29.958 1.00 17.74 ? 88  ALA   A C   1 
ATOM   590  O  O   . ALA   A 1 74  ? 18.438 -7.575  30.789 1.00 18.13 ? 88  ALA   A O   1 
ATOM   591  C  CB  . ALA   A 1 74  ? 17.605 -4.821  30.662 1.00 17.58 ? 88  ALA   A CB  1 
ATOM   592  N  N   . ILE   A 1 75  ? 17.335 -7.915  28.832 1.00 17.24 ? 89  ILE   A N   1 
ATOM   593  C  CA  . ILE   A 1 75  ? 17.871 -9.240  28.571 1.00 17.44 ? 89  ILE   A CA  1 
ATOM   594  C  C   . ILE   A 1 75  ? 19.016 -9.142  27.561 1.00 17.10 ? 89  ILE   A C   1 
ATOM   595  O  O   . ILE   A 1 75  ? 18.798 -9.057  26.353 1.00 16.06 ? 89  ILE   A O   1 
ATOM   596  C  CB  . ILE   A 1 75  ? 16.755 -10.188 28.095 1.00 17.79 ? 89  ILE   A CB  1 
ATOM   597  C  CG1 . ILE   A 1 75  ? 15.536 -10.136 29.040 1.00 18.12 ? 89  ILE   A CG1 1 
ATOM   598  C  CG2 . ILE   A 1 75  ? 17.302 -11.608 27.925 1.00 18.48 ? 89  ILE   A CG2 1 
ATOM   599  C  CD1 . ILE   A 1 75  ? 14.343 -10.941 28.570 1.00 18.70 ? 89  ILE   A CD1 1 
ATOM   600  N  N   . ARG   A 1 76  ? 20.242 -9.168  28.084 1.00 17.48 ? 90  ARG   A N   1 
ATOM   601  C  CA  . ARG   A 1 76  ? 21.436 -9.235  27.267 1.00 17.91 ? 90  ARG   A CA  1 
ATOM   602  C  C   . ARG   A 1 76  ? 21.607 -10.644 26.710 1.00 18.30 ? 90  ARG   A C   1 
ATOM   603  O  O   . ARG   A 1 76  ? 21.158 -11.604 27.318 1.00 18.77 ? 90  ARG   A O   1 
ATOM   604  C  CB  . ARG   A 1 76  ? 22.651 -8.875  28.124 1.00 18.93 ? 90  ARG   A CB  1 
ATOM   605  C  CG  . ARG   A 1 76  ? 22.638 -7.435  28.604 1.00 19.43 ? 90  ARG   A CG  1 
ATOM   606  C  CD  . ARG   A 1 76  ? 23.940 -7.107  29.314 1.00 20.76 ? 90  ARG   A CD  1 
ATOM   607  N  NE  . ARG   A 1 76  ? 24.004 -7.758  30.623 1.00 22.81 ? 90  ARG   A NE  1 
ATOM   608  C  CZ  . ARG   A 1 76  ? 24.954 -7.537  31.520 1.00 25.15 ? 90  ARG   A CZ  1 
ATOM   609  N  NH1 . ARG   A 1 76  ? 26.045 -6.866  31.180 1.00 26.02 ? 90  ARG   A NH1 1 
ATOM   610  N  NH2 . ARG   A 1 76  ? 24.815 -8.012  32.748 1.00 26.40 ? 90  ARG   A NH2 1 
ATOM   611  N  N   . HIS   A 1 77  ? 22.249 -10.747 25.538 1.00 17.92 ? 91  HIS   A N   1 
ATOM   612  C  CA  . HIS   A 1 77  ? 22.679 -12.025 25.001 1.00 18.50 ? 91  HIS   A CA  1 
ATOM   613  C  C   . HIS   A 1 77  ? 23.547 -12.708 26.054 1.00 19.25 ? 91  HIS   A C   1 
ATOM   614  O  O   . HIS   A 1 77  ? 24.403 -12.044 26.643 1.00 18.58 ? 91  HIS   A O   1 
ATOM   615  C  CB  . HIS   A 1 77  ? 23.487 -11.843 23.708 1.00 18.06 ? 91  HIS   A CB  1 
ATOM   616  C  CG  . HIS   A 1 77  ? 23.641 -13.115 22.946 1.00 18.82 ? 91  HIS   A CG  1 
ATOM   617  N  ND1 . HIS   A 1 77  ? 24.541 -14.098 23.301 1.00 19.67 ? 91  HIS   A ND1 1 
ATOM   618  C  CD2 . HIS   A 1 77  ? 22.976 -13.588 21.884 1.00 19.15 ? 91  HIS   A CD2 1 
ATOM   619  C  CE1 . HIS   A 1 77  ? 24.423 -15.117 22.466 1.00 20.23 ? 91  HIS   A CE1 1 
ATOM   620  N  NE2 . HIS   A 1 77  ? 23.482 -14.827 21.600 1.00 20.02 ? 91  HIS   A NE2 1 
ATOM   621  N  N   . PRO   A 1 78  ? 23.353 -14.022 26.331 1.00 20.65 ? 92  PRO   A N   1 
ATOM   622  C  CA  . PRO   A 1 78  ? 24.145 -14.719 27.353 1.00 21.86 ? 92  PRO   A CA  1 
ATOM   623  C  C   . PRO   A 1 78  ? 25.658 -14.778 27.134 1.00 22.54 ? 92  PRO   A C   1 
ATOM   624  O  O   . PRO   A 1 78  ? 26.404 -15.019 28.084 1.00 22.83 ? 92  PRO   A O   1 
ATOM   625  C  CB  . PRO   A 1 78  ? 23.513 -16.128 27.408 1.00 22.84 ? 92  PRO   A CB  1 
ATOM   626  C  CG  . PRO   A 1 78  ? 22.813 -16.296 26.080 1.00 22.53 ? 92  PRO   A CG  1 
ATOM   627  C  CD  . PRO   A 1 78  ? 22.337 -14.894 25.716 1.00 21.19 ? 92  PRO   A CD  1 
ATOM   628  N  N   . GLN   A 1 79  ? 26.120 -14.562 25.896 1.00 22.83 ? 93  GLN   A N   1 
ATOM   629  C  CA  . GLN   A 1 79  ? 27.545 -14.612 25.598 1.00 23.68 ? 93  GLN   A CA  1 
ATOM   630  C  C   . GLN   A 1 79  ? 28.093 -13.231 25.240 1.00 21.91 ? 93  GLN   A C   1 
ATOM   631  O  O   . GLN   A 1 79  ? 29.181 -13.143 24.679 1.00 21.66 ? 93  GLN   A O   1 
ATOM   632  C  CB  . GLN   A 1 79  ? 27.857 -15.624 24.496 1.00 25.73 ? 93  GLN   A CB  1 
ATOM   633  C  CG  . GLN   A 1 79  ? 27.862 -17.071 24.978 1.00 28.48 ? 93  GLN   A CG  1 
ATOM   634  C  CD  . GLN   A 1 79  ? 26.499 -17.725 24.937 1.00 30.30 ? 93  GLN   A CD  1 
ATOM   635  O  OE1 . GLN   A 1 79  ? 25.983 -18.220 25.948 1.00 32.71 ? 93  GLN   A OE1 1 
ATOM   636  N  NE2 . GLN   A 1 79  ? 25.920 -17.770 23.747 1.00 30.74 ? 93  GLN   A NE2 1 
ATOM   637  N  N   . TYR   A 1 80  ? 27.366 -12.163 25.606 1.00 20.67 ? 94  TYR   A N   1 
ATOM   638  C  CA  . TYR   A 1 80  ? 27.853 -10.800 25.434 1.00 19.54 ? 94  TYR   A CA  1 
ATOM   639  C  C   . TYR   A 1 80  ? 29.170 -10.643 26.200 1.00 20.08 ? 94  TYR   A C   1 
ATOM   640  O  O   . TYR   A 1 80  ? 29.278 -11.016 27.371 1.00 19.89 ? 94  TYR   A O   1 
ATOM   641  C  CB  . TYR   A 1 80  ? 26.845 -9.714  25.845 1.00 18.86 ? 94  TYR   A CB  1 
ATOM   642  C  CG  . TYR   A 1 80  ? 27.496 -8.343  25.996 1.00 18.24 ? 94  TYR   A CG  1 
ATOM   643  C  CD1 . TYR   A 1 80  ? 27.952 -7.641  24.883 1.00 17.61 ? 94  TYR   A CD1 1 
ATOM   644  C  CD2 . TYR   A 1 80  ? 27.703 -7.769  27.248 1.00 18.44 ? 94  TYR   A CD2 1 
ATOM   645  C  CE1 . TYR   A 1 80  ? 28.573 -6.409  25.008 1.00 17.30 ? 94  TYR   A CE1 1 
ATOM   646  C  CE2 . TYR   A 1 80  ? 28.308 -6.526  27.381 1.00 18.02 ? 94  TYR   A CE2 1 
ATOM   647  C  CZ  . TYR   A 1 80  ? 28.758 -5.852  26.259 1.00 17.53 ? 94  TYR   A CZ  1 
ATOM   648  O  OH  . TYR   A 1 80  ? 29.366 -4.634  26.348 1.00 17.73 ? 94  TYR   A OH  1 
ATOM   649  N  N   . ASN   A 1 81  ? 30.173 -10.086 25.510 1.00 19.99 ? 95  ASN   A N   1 
ATOM   650  C  CA  . ASN   A 1 81  ? 31.523 -9.945  26.038 1.00 20.86 ? 95  ASN   A CA  1 
ATOM   651  C  C   . ASN   A 1 81  ? 31.916 -8.471  26.011 1.00 20.07 ? 95  ASN   A C   1 
ATOM   652  O  O   . ASN   A 1 81  ? 32.112 -7.916  24.934 1.00 19.34 ? 95  ASN   A O   1 
ATOM   653  C  CB  . ASN   A 1 81  ? 32.518 -10.747 25.205 1.00 21.87 ? 95  ASN   A CB  1 
ATOM   654  C  CG  . ASN   A 1 81  ? 33.896 -10.819 25.824 1.00 23.14 ? 95  ASN   A CG  1 
ATOM   655  O  OD1 . ASN   A 1 81  ? 34.530 -9.798  26.103 1.00 23.40 ? 95  ASN   A OD1 1 
ATOM   656  N  ND2 . ASN   A 1 81  ? 34.395 -12.022 26.026 1.00 24.76 ? 95  ASN   A ND2 1 
ATOM   657  N  N   . GLN   A 1 82  ? 32.067 -7.861  27.195 1.00 20.28 ? 96  GLN   A N   1 
ATOM   658  C  CA  . GLN   A 1 82  ? 32.424 -6.452  27.307 1.00 19.91 ? 96  GLN   A CA  1 
ATOM   659  C  C   . GLN   A 1 82  ? 33.771 -6.174  26.637 1.00 19.66 ? 96  GLN   A C   1 
ATOM   660  O  O   . GLN   A 1 82  ? 33.938 -5.166  25.948 1.00 18.64 ? 96  GLN   A O   1 
ATOM   661  C  CB  . GLN   A 1 82  ? 32.507 -6.024  28.772 1.00 20.90 ? 96  GLN   A CB  1 
ATOM   662  C  CG  . GLN   A 1 82  ? 32.856 -4.550  28.968 1.00 21.34 ? 96  GLN   A CG  1 
ATOM   663  C  CD  . GLN   A 1 82  ? 32.803 -4.104  30.415 1.00 22.56 ? 96  GLN   A CD  1 
ATOM   664  O  OE1 . GLN   A 1 82  ? 32.642 -4.913  31.336 1.00 23.96 ? 96  GLN   A OE1 1 
ATOM   665  N  NE2 . GLN   A 1 82  ? 32.974 -2.808  30.638 1.00 22.65 ? 96  GLN   A NE2 1 
ATOM   666  N  N   . ARG   A 1 83  ? 34.738 -7.061  26.886 1.00 19.99 ? 97  ARG   A N   1 
ATOM   667  C  CA  . ARG   A 1 83  ? 36.123 -6.847  26.495 1.00 20.53 ? 97  ARG   A CA  1 
ATOM   668  C  C   . ARG   A 1 83  ? 36.287 -6.805  24.970 1.00 19.75 ? 97  ARG   A C   1 
ATOM   669  O  O   . ARG   A 1 83  ? 37.038 -5.972  24.468 1.00 19.47 ? 97  ARG   A O   1 
ATOM   670  C  CB  . ARG   A 1 83  ? 36.955 -7.965  27.126 1.00 21.97 ? 97  ARG   A CB  1 
ATOM   671  C  CG  . ARG   A 1 83  ? 38.466 -7.877  26.960 1.00 23.12 ? 97  ARG   A CG  1 
ATOM   672  C  CD  . ARG   A 1 83  ? 39.141 -9.082  27.599 1.00 24.59 ? 97  ARG   A CD  1 
ATOM   673  N  NE  . ARG   A 1 83  ? 38.784 -9.291  29.005 1.00 25.71 ? 97  ARG   A NE  1 
ATOM   674  C  CZ  . ARG   A 1 83  ? 39.298 -10.232 29.793 0.10 26.74 ? 97  ARG   A CZ  1 
ATOM   675  N  NH1 . ARG   A 1 83  ? 40.316 -10.971 29.387 0.10 27.42 ? 97  ARG   A NH1 1 
ATOM   676  N  NH2 . ARG   A 1 83  ? 38.808 -10.413 31.005 0.10 27.33 ? 97  ARG   A NH2 1 
ATOM   677  N  N   . THR   A 1 84  ? 35.625 -7.718  24.247 1.00 19.41 ? 98  THR   A N   1 
ATOM   678  C  CA  . THR   A 1 84  ? 35.739 -7.785  22.789 1.00 19.19 ? 98  THR   A CA  1 
ATOM   679  C  C   . THR   A 1 84  ? 34.574 -7.067  22.103 1.00 18.52 ? 98  THR   A C   1 
ATOM   680  O  O   . THR   A 1 84  ? 34.645 -6.820  20.905 1.00 18.04 ? 98  THR   A O   1 
ATOM   681  C  CB  . THR   A 1 84  ? 35.823 -9.235  22.308 1.00 19.61 ? 98  THR   A CB  1 
ATOM   682  O  OG1 . THR   A 1 84  ? 34.646 -9.909  22.738 1.00 19.58 ? 98  THR   A OG1 1 
ATOM   683  C  CG2 . THR   A 1 84  ? 37.043 -9.970  22.835 1.00 20.56 ? 98  THR   A CG2 1 
ATOM   684  N  N   . ILE   A 1 85  ? 33.519 -6.746  22.862 1.00 18.32 ? 99  ILE   A N   1 
ATOM   685  C  CA  . ILE   A 1 85  ? 32.276 -6.179  22.344 1.00 18.40 ? 99  ILE   A CA  1 
ATOM   686  C  C   . ILE   A 1 85  ? 31.647 -7.140  21.331 1.00 18.69 ? 99  ILE   A C   1 
ATOM   687  O  O   . ILE   A 1 85  ? 31.119 -6.705  20.307 1.00 19.19 ? 99  ILE   A O   1 
ATOM   688  C  CB  . ILE   A 1 85  ? 32.470 -4.771  21.741 1.00 17.89 ? 99  ILE   A CB  1 
ATOM   689  C  CG1 . ILE   A 1 85  ? 33.472 -3.916  22.535 1.00 18.48 ? 99  ILE   A CG1 1 
ATOM   690  C  CG2 . ILE   A 1 85  ? 31.125 -4.058  21.594 1.00 17.36 ? 99  ILE   A CG2 1 
ATOM   691  C  CD1 . ILE   A 1 85  ? 33.678 -2.522  21.963 1.00 18.44 ? 99  ILE   A CD1 1 
ATOM   692  N  N   . GLN   A 1 86  ? 31.694 -8.442  21.626 1.00 19.35 ? 100 GLN   A N   1 
ATOM   693  C  CA  . GLN   A 1 86  ? 31.041 -9.456  20.810 1.00 19.71 ? 100 GLN   A CA  1 
ATOM   694  C  C   . GLN   A 1 86  ? 29.669 -9.794  21.393 1.00 18.77 ? 100 GLN   A C   1 
ATOM   695  O  O   . GLN   A 1 86  ? 29.433 -9.661  22.598 1.00 18.48 ? 100 GLN   A O   1 
ATOM   696  C  CB  . GLN   A 1 86  ? 31.898 -10.720 20.710 1.00 21.40 ? 100 GLN   A CB  1 
ATOM   697  C  CG  . GLN   A 1 86  ? 32.975 -10.670 19.633 1.00 22.38 ? 100 GLN   A CG  1 
ATOM   698  C  CD  . GLN   A 1 86  ? 32.408 -10.637 18.231 1.00 22.99 ? 100 GLN   A CD  1 
ATOM   699  O  OE1 . GLN   A 1 86  ? 31.217 -10.878 18.008 1.00 23.91 ? 100 GLN   A OE1 1 
ATOM   700  N  NE2 . GLN   A 1 86  ? 33.261 -10.334 17.267 1.00 23.28 ? 100 GLN   A NE2 1 
ATOM   701  N  N   . ASN   A 1 87  ? 28.772 -10.246 20.511 1.00 18.31 ? 101 ASN   A N   1 
ATOM   702  C  CA  . ASN   A 1 87  ? 27.399 -10.593 20.860 1.00 17.91 ? 101 ASN   A CA  1 
ATOM   703  C  C   . ASN   A 1 87  ? 26.694 -9.388  21.485 1.00 16.78 ? 101 ASN   A C   1 
ATOM   704  O  O   . ASN   A 1 87  ? 25.981 -9.527  22.483 1.00 16.57 ? 101 ASN   A O   1 
ATOM   705  C  CB  . ASN   A 1 87  ? 27.341 -11.848 21.726 1.00 18.91 ? 101 ASN   A CB  1 
ATOM   706  C  CG  . ASN   A 1 87  ? 27.988 -13.038 21.058 1.00 19.94 ? 101 ASN   A CG  1 
ATOM   707  O  OD1 . ASN   A 1 87  ? 27.721 -13.325 19.882 1.00 20.14 ? 101 ASN   A OD1 1 
ATOM   708  N  ND2 . ASN   A 1 87  ? 28.868 -13.722 21.776 1.00 20.76 ? 101 ASN   A ND2 1 
ATOM   709  N  N   . ASP   A 1 88  ? 26.866 -8.220  20.847 1.00 15.96 ? 102 ASP   A N   1 
ATOM   710  C  CA  . ASP   A 1 88  ? 26.379 -6.947  21.355 1.00 14.96 ? 102 ASP   A CA  1 
ATOM   711  C  C   . ASP   A 1 88  ? 24.925 -6.742  20.935 1.00 14.66 ? 102 ASP   A C   1 
ATOM   712  O  O   . ASP   A 1 88  ? 24.652 -6.084  19.934 1.00 14.24 ? 102 ASP   A O   1 
ATOM   713  C  CB  . ASP   A 1 88  ? 27.287 -5.801  20.937 1.00 14.55 ? 102 ASP   A CB  1 
ATOM   714  C  CG  . ASP   A 1 88  ? 27.076 -4.486  21.677 1.00 14.21 ? 102 ASP   A CG  1 
ATOM   715  O  OD1 . ASP   A 1 88  ? 26.413 -4.494  22.737 1.00 14.08 ? 102 ASP   A OD1 1 
ATOM   716  O  OD2 . ASP   A 1 88  ? 27.588 -3.458  21.194 1.00 14.12 ? 102 ASP   A OD2 1 
ATOM   717  N  N   . ILE   A 1 89  ? 24.003 -7.308  21.725 1.00 14.50 ? 103 ILE   A N   1 
ATOM   718  C  CA  . ILE   A 1 89  ? 22.582 -7.281  21.413 1.00 14.47 ? 103 ILE   A CA  1 
ATOM   719  C  C   . ILE   A 1 89  ? 21.797 -7.538  22.705 1.00 14.40 ? 103 ILE   A C   1 
ATOM   720  O  O   . ILE   A 1 89  ? 22.227 -8.337  23.536 1.00 14.33 ? 103 ILE   A O   1 
ATOM   721  C  CB  . ILE   A 1 89  ? 22.257 -8.286  20.288 1.00 14.85 ? 103 ILE   A CB  1 
ATOM   722  C  CG1 . ILE   A 1 89  ? 20.810 -8.163  19.813 1.00 15.04 ? 103 ILE   A CG1 1 
ATOM   723  C  CG2 . ILE   A 1 89  ? 22.594 -9.724  20.689 1.00 15.66 ? 103 ILE   A CG2 1 
ATOM   724  C  CD1 . ILE   A 1 89  ? 20.516 -8.945  18.550 1.00 15.56 ? 103 ILE   A CD1 1 
ATOM   725  N  N   . MET   A 1 90  ? 20.669 -6.827  22.870 1.00 14.20 ? 104 MET   A N   1 
ATOM   726  C  CA  . MET   A 1 90  ? 19.855 -6.891  24.080 1.00 14.55 ? 104 MET   A CA  1 
ATOM   727  C  C   . MET   A 1 90  ? 18.388 -6.606  23.754 1.00 14.60 ? 104 MET   A C   1 
ATOM   728  O  O   . MET   A 1 90  ? 18.071 -5.715  22.961 1.00 13.96 ? 104 MET   A O   1 
ATOM   729  C  CB  . MET   A 1 90  ? 20.352 -5.870  25.113 1.00 14.51 ? 104 MET   A CB  1 
ATOM   730  C  CG  . MET   A 1 90  ? 19.424 -5.642  26.304 1.00 14.96 ? 104 MET   A CG  1 
ATOM   731  S  SD  . MET   A 1 90  ? 20.250 -4.798  27.673 1.00 15.29 ? 104 MET   A SD  1 
ATOM   732  C  CE  . MET   A 1 90  ? 20.329 -3.122  27.040 1.00 14.51 ? 104 MET   A CE  1 
ATOM   733  N  N   . LEU   A 1 91  ? 17.492 -7.376  24.385 1.00 14.99 ? 105 LEU   A N   1 
ATOM   734  C  CA  . LEU   A 1 91  ? 16.065 -7.155  24.257 1.00 15.13 ? 105 LEU   A CA  1 
ATOM   735  C  C   . LEU   A 1 91  ? 15.531 -6.518  25.535 1.00 15.34 ? 105 LEU   A C   1 
ATOM   736  O  O   . LEU   A 1 91  ? 15.853 -6.959  26.640 1.00 15.72 ? 105 LEU   A O   1 
ATOM   737  C  CB  . LEU   A 1 91  ? 15.336 -8.461  23.947 1.00 15.89 ? 105 LEU   A CB  1 
ATOM   738  C  CG  . LEU   A 1 91  ? 15.346 -8.894  22.479 1.00 16.02 ? 105 LEU   A CG  1 
ATOM   739  C  CD1 . LEU   A 1 91  ? 15.009 -10.368 22.383 1.00 16.97 ? 105 LEU   A CD1 1 
ATOM   740  C  CD2 . LEU   A 1 91  ? 14.370 -8.059  21.669 1.00 15.90 ? 105 LEU   A CD2 1 
ATOM   741  N  N   . LEU   A 1 92  ? 14.706 -5.484  25.351 1.00 15.44 ? 106 LEU   A N   1 
ATOM   742  C  CA  . LEU   A 1 92  ? 13.987 -4.857  26.444 1.00 15.79 ? 106 LEU   A CA  1 
ATOM   743  C  C   . LEU   A 1 92  ? 12.525 -5.287  26.392 1.00 16.40 ? 106 LEU   A C   1 
ATOM   744  O  O   . LEU   A 1 92  ? 11.827 -5.007  25.417 1.00 16.26 ? 106 LEU   A O   1 
ATOM   745  C  CB  . LEU   A 1 92  ? 14.120 -3.339  26.339 1.00 15.40 ? 106 LEU   A CB  1 
ATOM   746  C  CG  . LEU   A 1 92  ? 15.548 -2.791  26.381 1.00 15.17 ? 106 LEU   A CG  1 
ATOM   747  C  CD1 . LEU   A 1 92  ? 15.558 -1.276  26.230 1.00 15.22 ? 106 LEU   A CD1 1 
ATOM   748  C  CD2 . LEU   A 1 92  ? 16.226 -3.199  27.667 1.00 15.37 ? 106 LEU   A CD2 1 
ATOM   749  N  N   . GLN   A 1 93  ? 12.075 -5.981  27.442 1.00 17.26 ? 107 GLN   A N   1 
ATOM   750  C  CA  . GLN   A 1 93  ? 10.651 -6.200  27.647 1.00 18.29 ? 107 GLN   A CA  1 
ATOM   751  C  C   . GLN   A 1 93  ? 10.043 -4.952  28.293 1.00 17.88 ? 107 GLN   A C   1 
ATOM   752  O  O   . GLN   A 1 93  ? 10.451 -4.527  29.380 1.00 17.85 ? 107 GLN   A O   1 
ATOM   753  C  CB  . GLN   A 1 93  ? 10.408 -7.459  28.475 1.00 19.83 ? 107 GLN   A CB  1 
ATOM   754  C  CG  . GLN   A 1 93  ? 8.940  -7.850  28.585 1.00 20.98 ? 107 GLN   A CG  1 
ATOM   755  C  CD  . GLN   A 1 93  ? 8.638  -8.633  29.840 1.00 22.73 ? 107 GLN   A CD  1 
ATOM   756  O  OE1 . GLN   A 1 93  ? 9.207  -8.387  30.906 1.00 23.60 ? 107 GLN   A OE1 1 
ATOM   757  N  NE2 . GLN   A 1 93  ? 7.754  -9.610  29.723 1.00 24.19 ? 107 GLN   A NE2 1 
ATOM   758  N  N   . LEU   A 1 94  ? 9.074  -4.349  27.592 1.00 17.84 ? 108 LEU   A N   1 
ATOM   759  C  CA  . LEU   A 1 94  ? 8.391  -3.162  28.083 1.00 17.85 ? 108 LEU   A CA  1 
ATOM   760  C  C   . LEU   A 1 94  ? 7.445  -3.573  29.209 1.00 18.76 ? 108 LEU   A C   1 
ATOM   761  O  O   . LEU   A 1 94  ? 6.841  -4.643  29.158 1.00 18.62 ? 108 LEU   A O   1 
ATOM   762  C  CB  . LEU   A 1 94  ? 7.636  -2.451  26.964 1.00 17.89 ? 108 LEU   A CB  1 
ATOM   763  C  CG  . LEU   A 1 94  ? 8.453  -2.050  25.730 1.00 17.53 ? 108 LEU   A CG  1 
ATOM   764  C  CD1 . LEU   A 1 94  ? 7.547  -1.425  24.690 1.00 17.96 ? 108 LEU   A CD1 1 
ATOM   765  C  CD2 . LEU   A 1 94  ? 9.585  -1.098  26.080 1.00 17.28 ? 108 LEU   A CD2 1 
ATOM   766  N  N   . SER   A 1 95  ? 7.317  -2.700  30.215 1.00 19.71 ? 109 SER   A N   1 
ATOM   767  C  CA  . SER   A 1 95  ? 6.473  -2.969  31.375 1.00 20.92 ? 109 SER   A CA  1 
ATOM   768  C  C   . SER   A 1 95  ? 4.988  -2.948  30.997 1.00 21.98 ? 109 SER   A C   1 
ATOM   769  O  O   . SER   A 1 95  ? 4.167  -3.547  31.679 1.00 22.73 ? 109 SER   A O   1 
ATOM   770  C  CB  . SER   A 1 95  ? 6.767  -2.002  32.481 1.00 21.11 ? 109 SER   A CB  1 
ATOM   771  O  OG  . SER   A 1 95  ? 6.383  -0.690  32.106 1.00 21.43 ? 109 SER   A OG  1 
ATOM   772  N  N   . ARG   A 1 96  ? 4.647  -2.244  29.912 1.00 22.55 ? 110 ARG   A N   1 
ATOM   773  C  CA  . ARG   A 1 96  ? 3.331  -2.340  29.298 1.00 23.46 ? 110 ARG   A CA  1 
ATOM   774  C  C   . ARG   A 1 96  ? 3.503  -2.257  27.780 1.00 22.27 ? 110 ARG   A C   1 
ATOM   775  O  O   . ARG   A 1 96  ? 4.533  -1.788  27.294 1.00 21.36 ? 110 ARG   A O   1 
ATOM   776  C  CB  . ARG   A 1 96  ? 2.419  -1.239  29.855 1.00 25.14 ? 110 ARG   A CB  1 
ATOM   777  C  CG  . ARG   A 1 96  ? 2.774  0.164   29.386 1.00 26.37 ? 110 ARG   A CG  1 
ATOM   778  C  CD  . ARG   A 1 96  ? 1.815  1.245   29.892 1.00 28.15 ? 110 ARG   A CD  1 
ATOM   779  N  NE  . ARG   A 1 96  ? 1.896  2.424   29.020 1.00 29.21 ? 110 ARG   A NE  1 
ATOM   780  C  CZ  . ARG   A 1 96  ? 2.668  3.485   29.244 1.00 29.98 ? 110 ARG   A CZ  1 
ATOM   781  N  NH1 . ARG   A 1 96  ? 3.408  3.542   30.335 1.00 30.47 ? 110 ARG   A NH1 1 
ATOM   782  N  NH2 . ARG   A 1 96  ? 2.709  4.479   28.374 1.00 30.96 ? 110 ARG   A NH2 1 
ATOM   783  N  N   A ARG   A 1 97  ? 2.497  -2.731  27.041 0.50 22.33 ? 111 ARG   A N   1 
ATOM   784  N  N   B ARG   A 1 97  ? 2.489  -2.728  27.043 0.50 22.67 ? 111 ARG   A N   1 
ATOM   785  C  CA  A ARG   A 1 97  ? 2.500  -2.643  25.590 0.50 21.85 ? 111 ARG   A CA  1 
ATOM   786  C  CA  B ARG   A 1 97  ? 2.480  -2.637  25.591 0.50 22.41 ? 111 ARG   A CA  1 
ATOM   787  C  C   A ARG   A 1 97  ? 2.293  -1.193  25.163 0.50 21.65 ? 111 ARG   A C   1 
ATOM   788  C  C   B ARG   A 1 97  ? 2.320  -1.176  25.182 0.50 21.92 ? 111 ARG   A C   1 
ATOM   789  O  O   A ARG   A 1 97  ? 1.592  -0.440  25.828 0.50 21.60 ? 111 ARG   A O   1 
ATOM   790  O  O   B ARG   A 1 97  ? 1.678  -0.400  25.879 0.50 21.82 ? 111 ARG   A O   1 
ATOM   791  C  CB  A ARG   A 1 97  ? 1.426  -3.574  25.016 0.50 22.44 ? 111 ARG   A CB  1 
ATOM   792  C  CB  B ARG   A 1 97  ? 1.347  -3.462  24.969 0.50 23.45 ? 111 ARG   A CB  1 
ATOM   793  C  CG  A ARG   A 1 97  ? 1.942  -4.988  24.792 0.50 22.48 ? 111 ARG   A CG  1 
ATOM   794  C  CG  B ARG   A 1 97  ? -0.056 -2.920  25.205 0.50 24.40 ? 111 ARG   A CG  1 
ATOM   795  C  CD  A ARG   A 1 97  ? 0.826  -5.973  24.538 0.50 23.20 ? 111 ARG   A CD  1 
ATOM   796  C  CD  B ARG   A 1 97  ? -1.107 -3.679  24.408 0.50 25.50 ? 111 ARG   A CD  1 
ATOM   797  N  NE  A ARG   A 1 97  ? 1.244  -7.013  23.594 0.50 23.32 ? 111 ARG   A NE  1 
ATOM   798  N  NE  B ARG   A 1 97  ? -2.467 -3.206  24.685 0.50 26.43 ? 111 ARG   A NE  1 
ATOM   799  C  CZ  A ARG   A 1 97  ? 0.919  -7.010  22.301 0.50 23.36 ? 111 ARG   A CZ  1 
ATOM   800  C  CZ  B ARG   A 1 97  ? -3.398 -3.931  25.297 0.50 27.64 ? 111 ARG   A CZ  1 
ATOM   801  N  NH1 A ARG   A 1 97  ? 0.258  -5.990  21.785 0.50 23.20 ? 111 ARG   A NH1 1 
ATOM   802  N  NH1 B ARG   A 1 97  ? -3.109 -5.148  25.729 0.50 27.94 ? 111 ARG   A NH1 1 
ATOM   803  N  NH2 A ARG   A 1 97  ? 1.282  -8.013  21.526 0.50 23.64 ? 111 ARG   A NH2 1 
ATOM   804  N  NH2 B ARG   A 1 97  ? -4.611 -3.438  25.481 0.50 28.34 ? 111 ARG   A NH2 1 
ATOM   805  N  N   . VAL   A 1 98  ? 2.918  -0.813  24.044 1.00 21.39 ? 112 VAL   A N   1 
ATOM   806  C  CA  . VAL   A 1 98  ? 2.687  0.490   23.440 1.00 21.90 ? 112 VAL   A CA  1 
ATOM   807  C  C   . VAL   A 1 98  ? 1.268  0.541   22.867 1.00 22.47 ? 112 VAL   A C   1 
ATOM   808  O  O   . VAL   A 1 98  ? 0.686  -0.494  22.545 1.00 22.87 ? 112 VAL   A O   1 
ATOM   809  C  CB  . VAL   A 1 98  ? 3.718  0.786   22.336 1.00 21.74 ? 112 VAL   A CB  1 
ATOM   810  C  CG1 . VAL   A 1 98  ? 5.137  0.732   22.875 1.00 21.22 ? 112 VAL   A CG1 1 
ATOM   811  C  CG2 . VAL   A 1 98  ? 3.555  -0.139  21.136 1.00 22.14 ? 112 VAL   A CG2 1 
ATOM   812  N  N   . ARG   A 1 99  ? 0.720  1.757   22.758 1.00 22.96 ? 113 ARG   A N   1 
ATOM   813  C  CA  . ARG   A 1 99  ? -0.446 2.010   21.922 1.00 24.04 ? 113 ARG   A CA  1 
ATOM   814  C  C   . ARG   A 1 99  ? 0.036  2.307   20.502 1.00 24.19 ? 113 ARG   A C   1 
ATOM   815  O  O   . ARG   A 1 99  ? 0.680  3.327   20.252 1.00 23.88 ? 113 ARG   A O   1 
ATOM   816  C  CB  . ARG   A 1 99  ? -1.306 3.151   22.475 1.00 24.46 ? 113 ARG   A CB  1 
ATOM   817  C  CG  . ARG   A 1 99  ? -1.829 2.908   23.883 1.00 24.79 ? 113 ARG   A CG  1 
ATOM   818  C  CD  . ARG   A 1 99  ? -2.609 4.089   24.441 0.10 25.18 ? 113 ARG   A CD  1 
ATOM   819  N  NE  . ARG   A 1 99  ? -1.793 5.307   24.496 0.10 24.82 ? 113 ARG   A NE  1 
ATOM   820  C  CZ  . ARG   A 1 99  ? -1.231 5.782   25.599 0.10 24.41 ? 113 ARG   A CZ  1 
ATOM   821  N  NH1 . ARG   A 1 99  ? -1.359 5.128   26.739 0.10 24.29 ? 113 ARG   A NH1 1 
ATOM   822  N  NH2 . ARG   A 1 99  ? -0.533 6.902   25.555 0.10 24.27 ? 113 ARG   A NH2 1 
ATOM   823  N  N   . ARG   A 1 100 ? -0.264 1.387   19.580 1.00 25.22 ? 114 ARG   A N   1 
ATOM   824  C  CA  . ARG   A 1 100 ? 0.220  1.471   18.212 1.00 25.74 ? 114 ARG   A CA  1 
ATOM   825  C  C   . ARG   A 1 100 ? -0.547 2.563   17.472 1.00 26.78 ? 114 ARG   A C   1 
ATOM   826  O  O   . ARG   A 1 100 ? -1.765 2.666   17.596 1.00 27.12 ? 114 ARG   A O   1 
ATOM   827  C  CB  . ARG   A 1 100 ? 0.060  0.125   17.498 1.00 26.57 ? 114 ARG   A CB  1 
ATOM   828  C  CG  . ARG   A 1 100 ? 0.766  0.072   16.151 1.00 27.40 ? 114 ARG   A CG  1 
ATOM   829  C  CD  . ARG   A 1 100 ? 0.338  -1.123  15.307 0.50 28.45 ? 114 ARG   A CD  1 
ATOM   830  N  NE  . ARG   A 1 100 ? 0.727  -0.958  13.903 0.50 29.07 ? 114 ARG   A NE  1 
ATOM   831  C  CZ  . ARG   A 1 100 ? 1.423  -1.842  13.207 0.50 29.28 ? 114 ARG   A CZ  1 
ATOM   832  N  NH1 . ARG   A 1 100 ? 1.800  -2.969  13.781 0.50 29.21 ? 114 ARG   A NH1 1 
ATOM   833  N  NH2 . ARG   A 1 100 ? 1.734  -1.598  11.945 0.50 29.48 ? 114 ARG   A NH2 1 
ATOM   834  N  N   . ASN   A 1 101 ? 0.189  3.392   16.725 1.00 26.42 ? 115 ASN   A N   1 
ATOM   835  C  CA  . ASN   A 1 101 ? -0.416 4.447   15.928 1.00 27.67 ? 115 ASN   A CA  1 
ATOM   836  C  C   . ASN   A 1 101 ? 0.585  4.902   14.865 1.00 27.72 ? 115 ASN   A C   1 
ATOM   837  O  O   . ASN   A 1 101 ? 1.644  4.298   14.720 1.00 27.30 ? 115 ASN   A O   1 
ATOM   838  C  CB  . ASN   A 1 101 ? -0.902 5.589   16.814 1.00 27.53 ? 115 ASN   A CB  1 
ATOM   839  C  CG  . ASN   A 1 101 ? 0.210  6.182   17.647 1.00 26.15 ? 115 ASN   A CG  1 
ATOM   840  O  OD1 . ASN   A 1 101 ? 1.318  6.415   17.141 1.00 25.34 ? 115 ASN   A OD1 1 
ATOM   841  N  ND2 . ASN   A 1 101 ? -0.063 6.415   18.924 1.00 25.09 ? 115 ASN   A ND2 1 
ATOM   842  N  N   . ARG   A 1 102 ? 0.241  5.984   14.154 1.00 28.89 ? 116 ARG   A N   1 
ATOM   843  C  CA  . ARG   A 1 102 ? 1.080  6.584   13.125 1.00 29.43 ? 116 ARG   A CA  1 
ATOM   844  C  C   . ARG   A 1 102 ? 2.499  6.856   13.617 1.00 27.92 ? 116 ARG   A C   1 
ATOM   845  O  O   . ARG   A 1 102 ? 3.422  6.796   12.819 1.00 27.90 ? 116 ARG   A O   1 
ATOM   846  C  CB  . ARG   A 1 102 ? 0.497  7.909   12.613 1.00 31.29 ? 116 ARG   A CB  1 
ATOM   847  C  CG  . ARG   A 1 102 ? 0.145  7.921   11.135 1.00 33.62 ? 116 ARG   A CG  1 
ATOM   848  C  CD  . ARG   A 1 102 ? -0.898 8.972   10.792 1.00 35.51 ? 116 ARG   A CD  1 
ATOM   849  N  NE  . ARG   A 1 102 ? -2.252 8.445   10.998 0.50 36.26 ? 116 ARG   A NE  1 
ATOM   850  C  CZ  . ARG   A 1 102 ? -3.122 8.166   10.034 0.50 37.63 ? 116 ARG   A CZ  1 
ATOM   851  N  NH1 . ARG   A 1 102 ? -2.810 8.393   8.774  0.50 38.09 ? 116 ARG   A NH1 1 
ATOM   852  N  NH2 . ARG   A 1 102 ? -4.308 7.666   10.341 0.50 38.40 ? 116 ARG   A NH2 1 
ATOM   853  N  N   . ASN   A 1 103 ? 2.661  7.177   14.908 1.00 26.78 ? 117 ASN   A N   1 
ATOM   854  C  CA  . ASN   A 1 103 ? 3.926  7.656   15.444 1.00 25.33 ? 117 ASN   A CA  1 
ATOM   855  C  C   . ASN   A 1 103 ? 4.680  6.572   16.219 1.00 23.56 ? 117 ASN   A C   1 
ATOM   856  O  O   . ASN   A 1 103 ? 5.842  6.791   16.542 1.00 22.29 ? 117 ASN   A O   1 
ATOM   857  C  CB  . ASN   A 1 103 ? 3.719  8.864   16.351 1.00 25.55 ? 117 ASN   A CB  1 
ATOM   858  C  CG  . ASN   A 1 103 ? 3.034  9.996   15.625 1.00 26.87 ? 117 ASN   A CG  1 
ATOM   859  O  OD1 . ASN   A 1 103 ? 3.274  10.191  14.428 1.00 27.67 ? 117 ASN   A OD1 1 
ATOM   860  N  ND2 . ASN   A 1 103 ? 2.176  10.735  16.312 1.00 26.86 ? 117 ASN   A ND2 1 
ATOM   861  N  N   . VAL   A 1 104 ? 4.012  5.446   16.536 1.00 23.25 ? 118 VAL   A N   1 
ATOM   862  C  CA  . VAL   A 1 104 ? 4.586  4.350   17.308 1.00 22.40 ? 118 VAL   A CA  1 
ATOM   863  C  C   . VAL   A 1 104 ? 4.154  3.023   16.686 1.00 23.06 ? 118 VAL   A C   1 
ATOM   864  O  O   . VAL   A 1 104 ? 3.000  2.632   16.836 1.00 23.33 ? 118 VAL   A O   1 
ATOM   865  C  CB  . VAL   A 1 104 ? 4.145  4.436   18.787 1.00 21.61 ? 118 VAL   A CB  1 
ATOM   866  C  CG1 . VAL   A 1 104 ? 4.649  3.264   19.623 1.00 20.66 ? 118 VAL   A CG1 1 
ATOM   867  C  CG2 . VAL   A 1 104 ? 4.563  5.757   19.423 1.00 21.47 ? 118 VAL   A CG2 1 
ATOM   868  N  N   . ASN   A 1 105 ? 5.072  2.333   15.987 1.00 23.34 ? 119 ASN   A N   1 
ATOM   869  C  CA  . ASN   A 1 105 ? 4.816  0.970   15.533 1.00 24.05 ? 119 ASN   A CA  1 
ATOM   870  C  C   . ASN   A 1 105 ? 6.129  0.264   15.186 1.00 22.40 ? 119 ASN   A C   1 
ATOM   871  O  O   . ASN   A 1 105 ? 7.145  0.916   14.951 1.00 20.98 ? 119 ASN   A O   1 
ATOM   872  C  CB  . ASN   A 1 105 ? 3.793  0.905   14.397 1.00 26.71 ? 119 ASN   A CB  1 
ATOM   873  C  CG  . ASN   A 1 105 ? 4.214  1.715   13.201 1.00 28.98 ? 119 ASN   A CG  1 
ATOM   874  O  OD1 . ASN   A 1 105 ? 5.207  1.380   12.550 1.00 31.04 ? 119 ASN   A OD1 1 
ATOM   875  N  ND2 . ASN   A 1 105 ? 3.488  2.783   12.901 1.00 31.16 ? 119 ASN   A ND2 1 
ATOM   876  N  N   . PRO   A 1 106 ? 6.146  -1.094  15.169 1.00 21.62 ? 120 PRO   A N   1 
ATOM   877  C  CA  . PRO   A 1 106 ? 7.387  -1.859  15.004 1.00 20.88 ? 120 PRO   A CA  1 
ATOM   878  C  C   . PRO   A 1 106 ? 7.984  -1.894  13.594 1.00 20.72 ? 120 PRO   A C   1 
ATOM   879  O  O   . PRO   A 1 106 ? 7.313  -1.583  12.610 1.00 21.40 ? 120 PRO   A O   1 
ATOM   880  C  CB  . PRO   A 1 106 ? 7.012  -3.290  15.471 1.00 21.25 ? 120 PRO   A CB  1 
ATOM   881  C  CG  . PRO   A 1 106 ? 5.575  -3.217  15.962 1.00 22.01 ? 120 PRO   A CG  1 
ATOM   882  C  CD  . PRO   A 1 106 ? 4.973  -1.968  15.352 1.00 22.25 ? 120 PRO   A CD  1 
ATOM   883  N  N   . VAL   A 1 107 ? 9.256  -2.307  13.514 1.00 20.00 ? 121 VAL   A N   1 
ATOM   884  C  CA  . VAL   A 1 107 ? 9.960  -2.475  12.246 1.00 20.16 ? 121 VAL   A CA  1 
ATOM   885  C  C   . VAL   A 1 107 ? 10.292 -3.957  12.058 1.00 20.21 ? 121 VAL   A C   1 
ATOM   886  O  O   . VAL   A 1 107 ? 10.506 -4.687  13.026 1.00 19.62 ? 121 VAL   A O   1 
ATOM   887  C  CB  . VAL   A 1 107 ? 11.217 -1.580  12.169 1.00 19.41 ? 121 VAL   A CB  1 
ATOM   888  C  CG1 . VAL   A 1 107 ? 12.255 -1.932  13.229 1.00 18.64 ? 121 VAL   A CG1 1 
ATOM   889  C  CG2 . VAL   A 1 107 ? 11.856 -1.595  10.788 1.00 20.02 ? 121 VAL   A CG2 1 
ATOM   890  N  N   . ALA   A 1 108 ? 10.314 -4.399  10.793 1.00 20.70 ? 122 ALA   A N   1 
ATOM   891  C  CA  . ALA   A 1 108 ? 10.559 -5.794  10.456 1.00 21.25 ? 122 ALA   A CA  1 
ATOM   892  C  C   . ALA   A 1 108 ? 12.039 -6.135  10.612 1.00 20.75 ? 122 ALA   A C   1 
ATOM   893  O  O   . ALA   A 1 108 ? 12.895 -5.270  10.459 1.00 19.47 ? 122 ALA   A O   1 
ATOM   894  C  CB  . ALA   A 1 108 ? 10.102 -6.071  9.035  1.00 22.30 ? 122 ALA   A CB  1 
ATOM   895  N  N   . LEU   A 1 109 ? 12.307 -7.417  10.900 1.00 21.81 ? 123 LEU   A N   1 
ATOM   896  C  CA  . LEU   A 1 109 ? 13.648 -7.974  10.944 1.00 22.41 ? 123 LEU   A CA  1 
ATOM   897  C  C   . LEU   A 1 109 ? 13.927 -8.733  9.650  1.00 24.47 ? 123 LEU   A C   1 
ATOM   898  O  O   . LEU   A 1 109 ? 13.004 -9.132  8.949  1.00 25.82 ? 123 LEU   A O   1 
ATOM   899  C  CB  . LEU   A 1 109 ? 13.760 -8.907  12.150 1.00 22.32 ? 123 LEU   A CB  1 
ATOM   900  C  CG  . LEU   A 1 109 ? 13.561 -8.271  13.530 1.00 21.67 ? 123 LEU   A CG  1 
ATOM   901  C  CD1 . LEU   A 1 109 ? 13.914 -9.254  14.641 1.00 21.47 ? 123 LEU   A CD1 1 
ATOM   902  C  CD2 . LEU   A 1 109 ? 14.378 -7.002  13.661 1.00 21.05 ? 123 LEU   A CD2 1 
ATOM   903  N  N   . PRO   A 1 110 ? 15.207 -8.987  9.297  1.00 28.11 ? 124 PRO   A N   1 
ATOM   904  C  CA  . PRO   A 1 110 ? 15.522 -9.789  8.116  1.00 29.99 ? 124 PRO   A CA  1 
ATOM   905  C  C   . PRO   A 1 110 ? 15.124 -11.250 8.291  1.00 33.30 ? 124 PRO   A C   1 
ATOM   906  O  O   . PRO   A 1 110 ? 14.757 -11.674 9.384  1.00 32.51 ? 124 PRO   A O   1 
ATOM   907  C  CB  . PRO   A 1 110 ? 17.040 -9.612  7.950  1.00 29.09 ? 124 PRO   A CB  1 
ATOM   908  C  CG  . PRO   A 1 110 ? 17.536 -9.284  9.339  1.00 28.05 ? 124 PRO   A CG  1 
ATOM   909  C  CD  . PRO   A 1 110 ? 16.409 -8.504  9.993  1.00 27.38 ? 124 PRO   A CD  1 
ATOM   910  N  N   . ARG   A 1 111 ? 15.183 -11.992 7.175  1.00 37.06 ? 125 ARG   A N   1 
ATOM   911  C  CA  . ARG   A 1 111 ? 15.063 -13.441 7.177  1.00 40.08 ? 125 ARG   A CA  1 
ATOM   912  C  C   . ARG   A 1 111 ? 16.457 -14.012 7.423  1.00 41.43 ? 125 ARG   A C   1 
ATOM   913  O  O   . ARG   A 1 111 ? 17.444 -13.292 7.286  1.00 40.78 ? 125 ARG   A O   1 
ATOM   914  C  CB  . ARG   A 1 111 ? 14.463 -13.871 5.836  1.00 42.38 ? 125 ARG   A CB  1 
ATOM   915  C  CG  . ARG   A 1 111 ? 13.197 -13.118 5.446  1.00 43.13 ? 125 ARG   A CG  1 
ATOM   916  C  CD  . ARG   A 1 111 ? 11.975 -13.594 6.203  1.00 45.24 ? 125 ARG   A CD  1 
ATOM   917  N  NE  . ARG   A 1 111 ? 11.509 -14.868 5.642  1.00 48.01 ? 125 ARG   A NE  1 
ATOM   918  C  CZ  . ARG   A 1 111 ? 11.717 -16.076 6.161  1.00 49.47 ? 125 ARG   A CZ  1 
ATOM   919  N  NH1 . ARG   A 1 111 ? 12.324 -16.214 7.328  1.00 49.27 ? 125 ARG   A NH1 1 
ATOM   920  N  NH2 . ARG   A 1 111 ? 11.309 -17.150 5.505  1.00 51.15 ? 125 ARG   A NH2 1 
ATOM   921  N  N   . ALA   A 1 112 ? 16.535 -15.304 7.770  1.00 44.16 ? 126 ALA   A N   1 
ATOM   922  C  CA  . ALA   A 1 112 ? 17.750 -15.884 8.333  1.00 44.49 ? 126 ALA   A CA  1 
ATOM   923  C  C   . ALA   A 1 112 ? 18.874 -15.977 7.301  1.00 44.29 ? 126 ALA   A C   1 
ATOM   924  O  O   . ALA   A 1 112 ? 20.016 -15.631 7.605  1.00 43.66 ? 126 ALA   A O   1 
ATOM   925  C  CB  . ALA   A 1 112 ? 17.448 -17.240 8.936  1.00 46.66 ? 126 ALA   A CB  1 
ATOM   926  N  N   . GLN   A 1 113 ? 18.560 -16.450 6.087  1.00 43.98 ? 127 GLN   A N   1 
ATOM   927  C  CA  . GLN   A 1 113 ? 19.595 -16.689 5.089  1.00 43.33 ? 127 GLN   A CA  1 
ATOM   928  C  C   . GLN   A 1 113 ? 19.527 -15.654 3.962  1.00 41.07 ? 127 GLN   A C   1 
ATOM   929  O  O   . GLN   A 1 113 ? 20.126 -15.844 2.908  1.00 41.56 ? 127 GLN   A O   1 
ATOM   930  C  CB  . GLN   A 1 113 ? 19.512 -18.143 4.622  1.00 45.23 ? 127 GLN   A CB  1 
ATOM   931  C  CG  . GLN   A 1 113 ? 19.890 -19.155 5.699  0.10 46.03 ? 127 GLN   A CG  1 
ATOM   932  C  CD  . GLN   A 1 113 ? 20.343 -20.485 5.139  0.10 47.71 ? 127 GLN   A CD  1 
ATOM   933  O  OE1 . GLN   A 1 113 ? 19.720 -21.528 5.366  0.10 49.38 ? 127 GLN   A OE1 1 
ATOM   934  N  NE2 . GLN   A 1 113 ? 21.444 -20.460 4.401  0.10 47.33 ? 127 GLN   A NE2 1 
ATOM   935  N  N   . GLU   A 1 114 ? 18.855 -14.525 4.219  1.00 39.25 ? 128 GLU   A N   1 
ATOM   936  C  CA  . GLU   A 1 114 ? 18.649 -13.474 3.229  1.00 37.45 ? 128 GLU   A CA  1 
ATOM   937  C  C   . GLU   A 1 114 ? 19.984 -12.819 2.858  1.00 34.60 ? 128 GLU   A C   1 
ATOM   938  O  O   . GLU   A 1 114 ? 20.355 -12.763 1.679  1.00 34.93 ? 128 GLU   A O   1 
ATOM   939  C  CB  . GLU   A 1 114 ? 17.572 -12.559 3.825  1.00 37.32 ? 128 GLU   A CB  1 
ATOM   940  C  CG  . GLU   A 1 114 ? 17.773 -11.061 3.619  1.00 36.15 ? 128 GLU   A CG  1 
ATOM   941  C  CD  . GLU   A 1 114 ? 16.487 -10.272 3.795  1.00 36.14 ? 128 GLU   A CD  1 
ATOM   942  O  OE1 . GLU   A 1 114 ? 15.663 -10.634 4.664  1.00 36.04 ? 128 GLU   A OE1 1 
ATOM   943  O  OE2 . GLU   A 1 114 ? 16.321 -9.276  3.061  1.00 35.92 ? 128 GLU   A OE2 1 
ATOM   944  N  N   . GLY   A 1 115 ? 20.676 -12.311 3.882  1.00 31.11 ? 129 GLY   A N   1 
ATOM   945  C  CA  . GLY   A 1 115 ? 22.016 -11.760 3.751  1.00 29.11 ? 129 GLY   A CA  1 
ATOM   946  C  C   . GLY   A 1 115 ? 21.995 -10.239 3.660  1.00 27.04 ? 129 GLY   A C   1 
ATOM   947  O  O   . GLY   A 1 115 ? 20.929 -9.633  3.555  1.00 26.21 ? 129 GLY   A O   1 
ATOM   948  N  N   . LEU   A 1 116 ? 23.194 -9.646  3.749  1.00 25.94 ? 130 LEU   A N   1 
ATOM   949  C  CA  . LEU   A 1 116 ? 23.429 -8.233  3.483  1.00 24.77 ? 130 LEU   A CA  1 
ATOM   950  C  C   . LEU   A 1 116 ? 24.852 -8.082  2.940  1.00 24.64 ? 130 LEU   A C   1 
ATOM   951  O  O   . LEU   A 1 116 ? 25.810 -8.283  3.681  1.00 23.42 ? 130 LEU   A O   1 
ATOM   952  C  CB  . LEU   A 1 116 ? 23.246 -7.418  4.762  1.00 23.84 ? 130 LEU   A CB  1 
ATOM   953  C  CG  . LEU   A 1 116 ? 23.363 -5.897  4.620  1.00 22.93 ? 130 LEU   A CG  1 
ATOM   954  C  CD1 . LEU   A 1 116 ? 22.243 -5.360  3.733  1.00 23.24 ? 130 LEU   A CD1 1 
ATOM   955  C  CD2 . LEU   A 1 116 ? 23.348 -5.205  5.962  1.00 22.30 ? 130 LEU   A CD2 1 
ATOM   956  N  N   . ARG   A 1 117 ? 24.981 -7.723  1.654  1.00 24.76 ? 131 ARG   A N   1 
ATOM   957  C  CA  . ARG   A 1 117 ? 26.253 -7.811  0.951  1.00 25.48 ? 131 ARG   A CA  1 
ATOM   958  C  C   . ARG   A 1 117 ? 26.899 -6.435  0.781  1.00 24.76 ? 131 ARG   A C   1 
ATOM   959  O  O   . ARG   A 1 117 ? 26.209 -5.420  0.700  1.00 23.84 ? 131 ARG   A O   1 
ATOM   960  C  CB  . ARG   A 1 117 ? 26.027 -8.494  -0.399 1.00 27.00 ? 131 ARG   A CB  1 
ATOM   961  C  CG  . ARG   A 1 117 ? 25.762 -9.988  -0.261 1.00 28.16 ? 131 ARG   A CG  1 
ATOM   962  C  CD  . ARG   A 1 117 ? 25.277 -10.627 -1.549 1.00 29.56 ? 131 ARG   A CD  1 
ATOM   963  N  NE  . ARG   A 1 117 ? 26.276 -10.501 -2.614 1.00 30.27 ? 131 ARG   A NE  1 
ATOM   964  C  CZ  . ARG   A 1 117 ? 26.073 -10.841 -3.885 1.00 31.91 ? 131 ARG   A CZ  1 
ATOM   965  N  NH1 . ARG   A 1 117 ? 24.941 -11.427 -4.242 1.00 32.77 ? 131 ARG   A NH1 1 
ATOM   966  N  NH2 . ARG   A 1 117 ? 27.003 -10.596 -4.795 1.00 32.07 ? 131 ARG   A NH2 1 
ATOM   967  N  N   . PRO   A 1 118 ? 28.253 -6.370  0.703  1.00 24.90 ? 132 PRO   A N   1 
ATOM   968  C  CA  . PRO   A 1 118 ? 28.967 -5.110  0.473  1.00 24.45 ? 132 PRO   A CA  1 
ATOM   969  C  C   . PRO   A 1 118 ? 28.383 -4.313  -0.689 1.00 24.90 ? 132 PRO   A C   1 
ATOM   970  O  O   . PRO   A 1 118 ? 27.962 -4.893  -1.689 1.00 25.03 ? 132 PRO   A O   1 
ATOM   971  C  CB  . PRO   A 1 118 ? 30.398 -5.578  0.170  1.00 25.30 ? 132 PRO   A CB  1 
ATOM   972  C  CG  . PRO   A 1 118 ? 30.528 -6.870  0.935  1.00 25.42 ? 132 PRO   A CG  1 
ATOM   973  C  CD  . PRO   A 1 118 ? 29.166 -7.521  0.803  1.00 25.51 ? 132 PRO   A CD  1 
ATOM   974  N  N   . GLY   A 1 119 ? 28.361 -2.986  -0.534 1.00 24.56 ? 133 GLY   A N   1 
ATOM   975  C  CA  . GLY   A 1 119 ? 27.858 -2.103  -1.570 1.00 25.28 ? 133 GLY   A CA  1 
ATOM   976  C  C   . GLY   A 1 119 ? 26.395 -1.722  -1.359 1.00 25.10 ? 133 GLY   A C   1 
ATOM   977  O  O   . GLY   A 1 119 ? 25.896 -0.838  -2.048 1.00 25.99 ? 133 GLY   A O   1 
ATOM   978  N  N   . THR   A 1 120 ? 25.697 -2.392  -0.427 1.00 24.34 ? 134 THR   A N   1 
ATOM   979  C  CA  . THR   A 1 120 ? 24.301 -2.065  -0.176 1.00 23.82 ? 134 THR   A CA  1 
ATOM   980  C  C   . THR   A 1 120 ? 24.254 -0.729  0.563  1.00 23.11 ? 134 THR   A C   1 
ATOM   981  O  O   . THR   A 1 120 ? 25.038 -0.503  1.488  1.00 21.92 ? 134 THR   A O   1 
ATOM   982  C  CB  . THR   A 1 120 ? 23.605 -3.159  0.631  1.00 23.33 ? 134 THR   A CB  1 
ATOM   983  O  OG1 . THR   A 1 120 ? 23.827 -4.393  -0.034 1.00 23.86 ? 134 THR   A OG1 1 
ATOM   984  C  CG2 . THR   A 1 120 ? 22.113 -2.920  0.776  1.00 23.32 ? 134 THR   A CG2 1 
ATOM   985  N  N   . LEU   A 1 121 ? 23.316 0.136   0.160  1.00 23.43 ? 135 LEU   A N   1 
ATOM   986  C  CA  . LEU   A 1 121 ? 23.125 1.411   0.827  1.00 23.43 ? 135 LEU   A CA  1 
ATOM   987  C  C   . LEU   A 1 121 ? 22.009 1.259   1.860  1.00 22.45 ? 135 LEU   A C   1 
ATOM   988  O  O   . LEU   A 1 121 ? 20.955 0.688   1.576  1.00 23.14 ? 135 LEU   A O   1 
ATOM   989  C  CB  . LEU   A 1 121 ? 22.840 2.543   -0.160 1.00 25.42 ? 135 LEU   A CB  1 
ATOM   990  C  CG  . LEU   A 1 121 ? 22.821 3.956   0.442  1.00 26.06 ? 135 LEU   A CG  1 
ATOM   991  C  CD1 . LEU   A 1 121 ? 24.218 4.434   0.800  1.00 25.83 ? 135 LEU   A CD1 1 
ATOM   992  C  CD2 . LEU   A 1 121 ? 22.172 4.963   -0.482 1.00 27.88 ? 135 LEU   A CD2 1 
ATOM   993  N  N   . CYS   A 1 122 ? 22.269 1.785   3.061  1.00 20.83 ? 136 CYS   A N   1 
ATOM   994  C  CA  . CYS   A 1 122 ? 21.364 1.689   4.196  1.00 19.99 ? 136 CYS   A CA  1 
ATOM   995  C  C   . CYS   A 1 122 ? 21.274 3.056   4.874  1.00 19.84 ? 136 CYS   A C   1 
ATOM   996  O  O   . CYS   A 1 122 ? 22.062 3.944   4.554  1.00 20.03 ? 136 CYS   A O   1 
ATOM   997  C  CB  . CYS   A 1 122 ? 21.876 0.666   5.209  1.00 18.97 ? 136 CYS   A CB  1 
ATOM   998  S  SG  . CYS   A 1 122 ? 22.140 -0.991  4.520  1.00 19.18 ? 136 CYS   A SG  1 
ATOM   999  N  N   . THR   A 1 123 ? 20.334 3.199   5.825  1.00 19.23 ? 137 THR   A N   1 
ATOM   1000 C  CA  . THR   A 1 123 ? 20.225 4.393   6.653  1.00 18.77 ? 137 THR   A CA  1 
ATOM   1001 C  C   . THR   A 1 123 ? 20.331 3.998   8.128  1.00 17.52 ? 137 THR   A C   1 
ATOM   1002 O  O   . THR   A 1 123 ? 19.783 2.974   8.533  1.00 17.27 ? 137 THR   A O   1 
ATOM   1003 C  CB  . THR   A 1 123 ? 18.893 5.096   6.373  1.00 19.70 ? 137 THR   A CB  1 
ATOM   1004 O  OG1 . THR   A 1 123 ? 18.873 5.456   4.999  1.00 20.63 ? 137 THR   A OG1 1 
ATOM   1005 C  CG2 . THR   A 1 123 ? 18.707 6.351   7.211  1.00 19.82 ? 137 THR   A CG2 1 
ATOM   1006 N  N   . VAL   A 1 124 ? 21.029 4.827   8.918  1.00 16.78 ? 138 VAL   A N   1 
ATOM   1007 C  CA  . VAL   A 1 124 ? 21.027 4.732   10.375 1.00 16.05 ? 138 VAL   A CA  1 
ATOM   1008 C  C   . VAL   A 1 124 ? 20.524 6.064   10.939 1.00 15.91 ? 138 VAL   A C   1 
ATOM   1009 O  O   . VAL   A 1 124 ? 20.814 7.123   10.382 1.00 15.98 ? 138 VAL   A O   1 
ATOM   1010 C  CB  . VAL   A 1 124 ? 22.404 4.348   10.963 1.00 15.90 ? 138 VAL   A CB  1 
ATOM   1011 C  CG1 . VAL   A 1 124 ? 23.526 5.275   10.506 1.00 16.26 ? 138 VAL   A CG1 1 
ATOM   1012 C  CG2 . VAL   A 1 124 ? 22.394 4.256   12.489 1.00 15.54 ? 138 VAL   A CG2 1 
ATOM   1013 N  N   . ALA   A 1 125 ? 19.780 5.990   12.057 1.00 15.51 ? 139 ALA   A N   1 
ATOM   1014 C  CA  . ALA   A 1 125 ? 19.191 7.151   12.707 1.00 15.69 ? 139 ALA   A CA  1 
ATOM   1015 C  C   . ALA   A 1 125 ? 19.434 7.111   14.221 1.00 15.14 ? 139 ALA   A C   1 
ATOM   1016 O  O   . ALA   A 1 125 ? 19.554 6.036   14.809 1.00 14.35 ? 139 ALA   A O   1 
ATOM   1017 C  CB  . ALA   A 1 125 ? 17.710 7.200   12.408 1.00 16.34 ? 139 ALA   A CB  1 
ATOM   1018 N  N   . GLY   A 1 126 ? 19.489 8.301   14.839 1.00 15.29 ? 140 GLY   A N   1 
ATOM   1019 C  CA  . GLY   A 1 126 ? 19.675 8.414   16.281 1.00 15.32 ? 140 GLY   A CA  1 
ATOM   1020 C  C   . GLY   A 1 126 ? 19.788 9.865   16.757 1.00 15.75 ? 140 GLY   A C   1 
ATOM   1021 O  O   . GLY   A 1 126 ? 19.807 10.798  15.945 1.00 16.11 ? 140 GLY   A O   1 
ATOM   1022 N  N   . TRP   A 1 127 ? 19.836 10.013  18.094 1.00 15.64 ? 141 TRP   A N   1 
ATOM   1023 C  CA  . TRP   A 1 127 ? 19.944 11.289  18.790 1.00 16.29 ? 141 TRP   A CA  1 
ATOM   1024 C  C   . TRP   A 1 127 ? 21.379 11.550  19.257 1.00 16.99 ? 141 TRP   A C   1 
ATOM   1025 O  O   . TRP   A 1 127 ? 21.591 12.394  20.133 1.00 17.46 ? 141 TRP   A O   1 
ATOM   1026 C  CB  . TRP   A 1 127 ? 19.003 11.318  20.009 1.00 16.20 ? 141 TRP   A CB  1 
ATOM   1027 C  CG  . TRP   A 1 127 ? 17.540 11.422  19.678 1.00 16.05 ? 141 TRP   A CG  1 
ATOM   1028 C  CD1 . TRP   A 1 127 ? 16.827 12.573  19.501 1.00 16.61 ? 141 TRP   A CD1 1 
ATOM   1029 C  CD2 . TRP   A 1 127 ? 16.606 10.334  19.493 1.00 15.50 ? 141 TRP   A CD2 1 
ATOM   1030 N  NE1 . TRP   A 1 127 ? 15.519 12.281  19.209 1.00 16.75 ? 141 TRP   A NE1 1 
ATOM   1031 C  CE2 . TRP   A 1 127 ? 15.350 10.920  19.203 1.00 16.04 ? 141 TRP   A CE2 1 
ATOM   1032 C  CE3 . TRP   A 1 127 ? 16.703 8.937   19.539 1.00 14.95 ? 141 TRP   A CE3 1 
ATOM   1033 C  CZ2 . TRP   A 1 127 ? 14.210 10.155  18.963 1.00 16.12 ? 141 TRP   A CZ2 1 
ATOM   1034 C  CZ3 . TRP   A 1 127 ? 15.576 8.182   19.288 1.00 15.08 ? 141 TRP   A CZ3 1 
ATOM   1035 C  CH2 . TRP   A 1 127 ? 14.344 8.783   19.016 1.00 15.73 ? 141 TRP   A CH2 1 
ATOM   1036 N  N   . GLY   A 1 128 ? 22.355 10.845  18.666 1.00 16.99 ? 142 GLY   A N   1 
ATOM   1037 C  CA  . GLY   A 1 128 ? 23.743 10.907  19.098 1.00 17.59 ? 142 GLY   A CA  1 
ATOM   1038 C  C   . GLY   A 1 128 ? 24.464 12.184  18.664 1.00 18.79 ? 142 GLY   A C   1 
ATOM   1039 O  O   . GLY   A 1 128 ? 23.879 13.080  18.048 1.00 19.41 ? 142 GLY   A O   1 
ATOM   1040 N  N   . ARG   A 1 129 ? 25.757 12.249  19.016 1.00 19.65 ? 143 ARG   A N   1 
ATOM   1041 C  CA  . ARG   A 1 129 ? 26.606 13.397  18.728 1.00 21.08 ? 143 ARG   A CA  1 
ATOM   1042 C  C   . ARG   A 1 129 ? 26.763 13.611  17.216 1.00 21.27 ? 143 ARG   A C   1 
ATOM   1043 O  O   . ARG   A 1 129 ? 26.797 12.654  16.435 1.00 20.15 ? 143 ARG   A O   1 
ATOM   1044 C  CB  . ARG   A 1 129 ? 27.978 13.220  19.391 1.00 21.71 ? 143 ARG   A CB  1 
ATOM   1045 C  CG  . ARG   A 1 129 ? 27.963 13.128  20.911 1.00 22.19 ? 143 ARG   A CG  1 
ATOM   1046 C  CD  . ARG   A 1 129 ? 29.372 13.147  21.511 1.00 23.14 ? 143 ARG   A CD  1 
ATOM   1047 N  NE  . ARG   A 1 129 ? 29.408 12.566  22.858 0.50 23.21 ? 143 ARG   A NE  1 
ATOM   1048 C  CZ  . ARG   A 1 129 ? 30.483 12.483  23.629 0.50 24.13 ? 143 ARG   A CZ  1 
ATOM   1049 N  NH1 . ARG   A 1 129 ? 31.648 12.948  23.214 0.50 24.89 ? 143 ARG   A NH1 1 
ATOM   1050 N  NH2 . ARG   A 1 129 ? 30.383 11.943  24.828 0.50 24.34 ? 143 ARG   A NH2 1 
ATOM   1051 N  N   . VAL   A 1 130 ? 26.880 14.891  16.833 1.00 22.72 ? 144 VAL   A N   1 
ATOM   1052 C  CA  . VAL   A 1 130 ? 27.012 15.311  15.444 1.00 23.65 ? 144 VAL   A CA  1 
ATOM   1053 C  C   . VAL   A 1 130 ? 28.470 15.643  15.130 1.00 25.02 ? 144 VAL   A C   1 
ATOM   1054 O  O   . VAL   A 1 130 ? 28.826 15.798  13.962 1.00 25.16 ? 144 VAL   A O   1 
ATOM   1055 C  CB  . VAL   A 1 130 ? 26.099 16.512  15.126 1.00 24.31 ? 144 VAL   A CB  1 
ATOM   1056 C  CG1 . VAL   A 1 130 ? 24.661 16.254  15.550 1.00 23.96 ? 144 VAL   A CG1 1 
ATOM   1057 C  CG2 . VAL   A 1 130 ? 26.603 17.806  15.752 1.00 25.65 ? 144 VAL   A CG2 1 
ATOM   1058 N  N   . SER   A 1 131 ? 29.282 15.809  16.183 1.00 26.53 ? 145 SER   A N   1 
ATOM   1059 C  CA  . SER   A 1 131 ? 30.729 15.932  16.063 1.00 28.57 ? 145 SER   A CA  1 
ATOM   1060 C  C   . SER   A 1 131 ? 31.365 15.316  17.306 1.00 29.72 ? 145 SER   A C   1 
ATOM   1061 O  O   . SER   A 1 131 ? 30.702 14.570  18.022 1.00 28.60 ? 145 SER   A O   1 
ATOM   1062 C  CB  . SER   A 1 131 ? 31.166 17.366  15.861 1.00 29.93 ? 145 SER   A CB  1 
ATOM   1063 O  OG  . SER   A 1 131 ? 31.115 18.105  17.073 1.00 30.61 ? 145 SER   A OG  1 
ATOM   1064 N  N   . MET   A 1 132 ? 32.644 15.617  17.554 1.00 32.19 ? 146 MET   A N   1 
ATOM   1065 C  CA  . MET   A 1 132 ? 33.348 15.022  18.679 1.00 34.09 ? 146 MET   A CA  1 
ATOM   1066 C  C   . MET   A 1 132 ? 32.679 15.392  20.006 1.00 34.50 ? 146 MET   A C   1 
ATOM   1067 O  O   . MET   A 1 132 ? 32.533 14.527  20.866 1.00 33.88 ? 146 MET   A O   1 
ATOM   1068 C  CB  . MET   A 1 132 ? 34.830 15.419  18.693 1.00 36.50 ? 146 MET   A CB  1 
ATOM   1069 C  CG  . MET   A 1 132 ? 35.665 14.797  17.578 1.00 36.98 ? 146 MET   A CG  1 
ATOM   1070 S  SD  . MET   A 1 132 ? 35.556 12.998  17.455 1.00 37.83 ? 146 MET   A SD  1 
ATOM   1071 C  CE  . MET   A 1 132 ? 34.314 12.801  16.170 1.00 36.30 ? 146 MET   A CE  1 
ATOM   1072 N  N   . ARG   A 1 133 ? 32.250 16.654  20.167 1.00 36.16 ? 147 ARG   A N   1 
ATOM   1073 C  CA  . ARG   A 1 133 ? 31.803 17.141  21.468 1.00 37.36 ? 147 ARG   A CA  1 
ATOM   1074 C  C   . ARG   A 1 133 ? 30.367 17.685  21.457 1.00 37.28 ? 147 ARG   A C   1 
ATOM   1075 O  O   . ARG   A 1 133 ? 29.833 17.969  22.528 1.00 38.63 ? 147 ARG   A O   1 
ATOM   1076 C  CB  . ARG   A 1 133 ? 32.795 18.205  21.958 0.10 39.07 ? 147 ARG   A CB  1 
ATOM   1077 C  CG  . ARG   A 1 133 ? 32.655 18.646  23.410 0.10 40.01 ? 147 ARG   A CG  1 
ATOM   1078 C  CD  . ARG   A 1 133 ? 33.091 17.588  24.414 0.10 39.88 ? 147 ARG   A CD  1 
ATOM   1079 N  NE  . ARG   A 1 133 ? 32.599 17.882  25.765 0.10 40.39 ? 147 ARG   A NE  1 
ATOM   1080 C  CZ  . ARG   A 1 133 ? 32.847 17.147  26.842 0.10 40.53 ? 147 ARG   A CZ  1 
ATOM   1081 N  NH1 . ARG   A 1 133 ? 33.604 16.068  26.748 0.10 40.17 ? 147 ARG   A NH1 1 
ATOM   1082 N  NH2 . ARG   A 1 133 ? 32.341 17.497  28.010 0.10 41.20 ? 147 ARG   A NH2 1 
ATOM   1083 N  N   . ARG   A 1 134 ? 29.713 17.827  20.292 1.00 36.13 ? 148 ARG   A N   1 
ATOM   1084 C  CA  . ARG   A 1 134 ? 28.412 18.490  20.267 1.00 36.47 ? 148 ARG   A CA  1 
ATOM   1085 C  C   . ARG   A 1 134 ? 27.306 17.514  19.854 1.00 34.76 ? 148 ARG   A C   1 
ATOM   1086 O  O   . ARG   A 1 134 ? 27.524 16.607  19.048 1.00 33.43 ? 148 ARG   A O   1 
ATOM   1087 C  CB  . ARG   A 1 134 ? 28.445 19.791  19.451 1.00 38.34 ? 148 ARG   A CB  1 
ATOM   1088 C  CG  . ARG   A 1 134 ? 28.225 19.695  17.949 1.00 38.64 ? 148 ARG   A CG  1 
ATOM   1089 C  CD  . ARG   A 1 134 ? 28.538 21.010  17.240 0.50 40.68 ? 148 ARG   A CD  1 
ATOM   1090 N  NE  . ARG   A 1 134 ? 28.629 20.822  15.788 0.50 40.94 ? 148 ARG   A NE  1 
ATOM   1091 C  CZ  . ARG   A 1 134 ? 29.739 20.975  15.079 0.50 42.42 ? 148 ARG   A CZ  1 
ATOM   1092 N  NH1 . ARG   A 1 134 ? 30.851 21.384  15.667 0.50 43.48 ? 148 ARG   A NH1 1 
ATOM   1093 N  NH2 . ARG   A 1 134 ? 29.733 20.723  13.782 0.50 42.63 ? 148 ARG   A NH2 1 
ATOM   1094 N  N   . GLY   A 1 135 ? 26.111 17.729  20.429 1.00 34.05 ? 151 GLY   A N   1 
ATOM   1095 C  CA  . GLY   A 1 135 ? 24.977 16.827  20.283 1.00 32.62 ? 151 GLY   A CA  1 
ATOM   1096 C  C   . GLY   A 1 135 ? 23.789 17.498  19.592 1.00 31.96 ? 151 GLY   A C   1 
ATOM   1097 O  O   . GLY   A 1 135 ? 23.932 18.559  18.995 1.00 34.62 ? 151 GLY   A O   1 
ATOM   1098 N  N   . THR   A 1 136 ? 22.624 16.848  19.682 1.00 29.92 ? 152 THR   A N   1 
ATOM   1099 C  CA  . THR   A 1 136 ? 21.387 17.303  19.068 1.00 29.28 ? 152 THR   A CA  1 
ATOM   1100 C  C   . THR   A 1 136 ? 20.223 16.928  19.985 1.00 28.12 ? 152 THR   A C   1 
ATOM   1101 O  O   . THR   A 1 136 ? 20.300 15.936  20.707 1.00 27.54 ? 152 THR   A O   1 
ATOM   1102 C  CB  . THR   A 1 136 ? 21.240 16.652  17.692 1.00 28.86 ? 152 THR   A CB  1 
ATOM   1103 O  OG1 . THR   A 1 136 ? 20.007 17.098  17.139 1.00 29.63 ? 152 THR   A OG1 1 
ATOM   1104 C  CG2 . THR   A 1 136 ? 21.202 15.135  17.765 1.00 27.41 ? 152 THR   A CG2 1 
ATOM   1105 N  N   . ASP   A 1 137 ? 19.150 17.718  19.919 1.00 27.79 ? 153 ASP   A N   1 
ATOM   1106 C  CA  . ASP   A 1 137 ? 17.916 17.457  20.646 1.00 27.89 ? 153 ASP   A CA  1 
ATOM   1107 C  C   . ASP   A 1 137 ? 16.959 16.619  19.802 1.00 25.99 ? 153 ASP   A C   1 
ATOM   1108 O  O   . ASP   A 1 137 ? 16.076 15.964  20.353 1.00 25.09 ? 153 ASP   A O   1 
ATOM   1109 C  CB  . ASP   A 1 137 ? 17.187 18.751  20.980 1.00 29.84 ? 153 ASP   A CB  1 
ATOM   1110 C  CG  . ASP   A 1 137 ? 17.859 19.657  22.001 1.00 31.77 ? 153 ASP   A CG  1 
ATOM   1111 O  OD1 . ASP   A 1 137 ? 18.780 19.176  22.696 1.00 31.95 ? 153 ASP   A OD1 1 
ATOM   1112 O  OD2 . ASP   A 1 137 ? 17.445 20.835  22.093 1.00 33.97 ? 153 ASP   A OD2 1 
ATOM   1113 N  N   . THR   A 1 138 ? 17.111 16.687  18.469 1.00 24.85 ? 154 THR   A N   1 
ATOM   1114 C  CA  . THR   A 1 138 ? 16.149 16.104  17.549 1.00 23.86 ? 154 THR   A CA  1 
ATOM   1115 C  C   . THR   A 1 138 ? 16.808 14.987  16.741 1.00 21.83 ? 154 THR   A C   1 
ATOM   1116 O  O   . THR   A 1 138 ? 17.997 15.035  16.441 1.00 21.25 ? 154 THR   A O   1 
ATOM   1117 C  CB  . THR   A 1 138 ? 15.561 17.189  16.646 1.00 25.48 ? 154 THR   A CB  1 
ATOM   1118 O  OG1 . THR   A 1 138 ? 16.594 17.751  15.842 1.00 26.09 ? 154 THR   A OG1 1 
ATOM   1119 C  CG2 . THR   A 1 138 ? 14.942 18.324  17.439 1.00 26.84 ? 154 THR   A CG2 1 
ATOM   1120 N  N   . LEU   A 1 139 ? 15.985 13.997  16.382 1.00 20.38 ? 155 LEU   A N   1 
ATOM   1121 C  CA  . LEU   A 1 139 ? 16.397 12.831  15.626 1.00 19.04 ? 155 LEU   A CA  1 
ATOM   1122 C  C   . LEU   A 1 139 ? 17.036 13.247  14.302 1.00 18.97 ? 155 LEU   A C   1 
ATOM   1123 O  O   . LEU   A 1 139 ? 16.542 14.139  13.617 1.00 19.69 ? 155 LEU   A O   1 
ATOM   1124 C  CB  . LEU   A 1 139 ? 15.181 11.935  15.402 1.00 18.86 ? 155 LEU   A CB  1 
ATOM   1125 C  CG  . LEU   A 1 139 ? 15.424 10.625  14.645 1.00 18.12 ? 155 LEU   A CG  1 
ATOM   1126 C  CD1 . LEU   A 1 139 ? 16.288 9.680   15.474 1.00 17.29 ? 155 LEU   A CD1 1 
ATOM   1127 C  CD2 . LEU   A 1 139 ? 14.116 9.949   14.255 1.00 18.34 ? 155 LEU   A CD2 1 
ATOM   1128 N  N   . ARG   A 1 140 ? 18.138 12.566  13.966 1.00 19.11 ? 156 ARG   A N   1 
ATOM   1129 C  CA  . ARG   A 1 140 ? 18.871 12.787  12.728 1.00 19.51 ? 156 ARG   A CA  1 
ATOM   1130 C  C   . ARG   A 1 140 ? 19.146 11.450  12.047 1.00 18.77 ? 156 ARG   A C   1 
ATOM   1131 O  O   . ARG   A 1 140 ? 18.987 10.400  12.661 1.00 17.93 ? 156 ARG   A O   1 
ATOM   1132 C  CB  . ARG   A 1 140 ? 20.184 13.518  13.019 1.00 19.74 ? 156 ARG   A CB  1 
ATOM   1133 C  CG  . ARG   A 1 140 ? 19.995 14.909  13.600 1.00 20.71 ? 156 ARG   A CG  1 
ATOM   1134 C  CD  . ARG   A 1 140 ? 21.313 15.655  13.737 1.00 21.26 ? 156 ARG   A CD  1 
ATOM   1135 N  NE  . ARG   A 1 140 ? 21.849 16.051  12.431 1.00 21.97 ? 156 ARG   A NE  1 
ATOM   1136 C  CZ  . ARG   A 1 140 ? 21.440 17.098  11.728 1.00 23.21 ? 156 ARG   A CZ  1 
ATOM   1137 N  NH1 . ARG   A 1 140 ? 20.521 17.908  12.223 1.00 23.77 ? 156 ARG   A NH1 1 
ATOM   1138 N  NH2 . ARG   A 1 140 ? 21.964 17.343  10.542 1.00 24.03 ? 156 ARG   A NH2 1 
ATOM   1139 N  N   . GLU   A 1 141 ? 19.576 11.497  10.778 1.00 19.03 ? 157 GLU   A N   1 
ATOM   1140 C  CA  . GLU   A 1 141 ? 19.826 10.280  10.021 1.00 18.82 ? 157 GLU   A CA  1 
ATOM   1141 C  C   . GLU   A 1 141 ? 20.916 10.513  8.975  1.00 19.40 ? 157 GLU   A C   1 
ATOM   1142 O  O   . GLU   A 1 141 ? 21.198 11.646  8.600  1.00 20.12 ? 157 GLU   A O   1 
ATOM   1143 C  CB  . GLU   A 1 141 ? 18.542 9.773   9.362  1.00 19.25 ? 157 GLU   A CB  1 
ATOM   1144 C  CG  . GLU   A 1 141 ? 17.906 10.768  8.394  1.00 20.40 ? 157 GLU   A CG  1 
ATOM   1145 C  CD  . GLU   A 1 141 ? 16.576 10.284  7.853  1.00 21.01 ? 157 GLU   A CD  1 
ATOM   1146 O  OE1 . GLU   A 1 141 ? 15.619 10.229  8.651  1.00 20.89 ? 157 GLU   A OE1 1 
ATOM   1147 O  OE2 . GLU   A 1 141 ? 16.499 9.936   6.655  1.00 21.57 ? 157 GLU   A OE2 1 
ATOM   1148 N  N   . VAL   A 1 142 ? 21.532 9.418   8.518  1.00 19.31 ? 158 VAL   A N   1 
ATOM   1149 C  CA  . VAL   A 1 142 ? 22.523 9.493   7.456  1.00 20.09 ? 158 VAL   A CA  1 
ATOM   1150 C  C   . VAL   A 1 142 ? 22.538 8.173   6.688  1.00 20.21 ? 158 VAL   A C   1 
ATOM   1151 O  O   . VAL   A 1 142 ? 22.283 7.111   7.264  1.00 19.33 ? 158 VAL   A O   1 
ATOM   1152 C  CB  . VAL   A 1 142 ? 23.901 9.835   8.054  1.00 19.63 ? 158 VAL   A CB  1 
ATOM   1153 C  CG1 . VAL   A 1 142 ? 24.504 8.645   8.797  1.00 18.64 ? 158 VAL   A CG1 1 
ATOM   1154 C  CG2 . VAL   A 1 142 ? 24.865 10.365  6.999  1.00 20.70 ? 158 VAL   A CG2 1 
ATOM   1155 N  N   . GLN   A 1 143 ? 22.860 8.254   5.390  1.00 21.43 ? 159 GLN   A N   1 
ATOM   1156 C  CA  . GLN   A 1 143 ? 23.007 7.067   4.561  1.00 22.06 ? 159 GLN   A CA  1 
ATOM   1157 C  C   . GLN   A 1 143 ? 24.460 6.603   4.567  1.00 21.00 ? 159 GLN   A C   1 
ATOM   1158 O  O   . GLN   A 1 143 ? 25.363 7.406   4.350  1.00 20.75 ? 159 GLN   A O   1 
ATOM   1159 C  CB  . GLN   A 1 143 ? 22.552 7.322   3.127  1.00 24.77 ? 159 GLN   A CB  1 
ATOM   1160 C  CG  . GLN   A 1 143 ? 21.057 7.588   3.024  1.00 26.74 ? 159 GLN   A CG  1 
ATOM   1161 C  CD  . GLN   A 1 143 ? 20.612 7.845   1.605  1.00 30.36 ? 159 GLN   A CD  1 
ATOM   1162 O  OE1 . GLN   A 1 143 ? 20.954 8.873   1.008  1.00 32.97 ? 159 GLN   A OE1 1 
ATOM   1163 N  NE2 . GLN   A 1 143 ? 19.856 6.904   1.053  1.00 31.52 ? 159 GLN   A NE2 1 
ATOM   1164 N  N   . LEU   A 1 144 ? 24.647 5.295   4.809  1.00 20.14 ? 160 LEU   A N   1 
ATOM   1165 C  CA  . LEU   A 1 144 ? 25.958 4.661   4.847  1.00 19.54 ? 160 LEU   A CA  1 
ATOM   1166 C  C   . LEU   A 1 144 ? 25.962 3.427   3.944  1.00 19.66 ? 160 LEU   A C   1 
ATOM   1167 O  O   . LEU   A 1 144 ? 24.961 2.716   3.845  1.00 19.56 ? 160 LEU   A O   1 
ATOM   1168 C  CB  . LEU   A 1 144 ? 26.323 4.261   6.276  1.00 18.47 ? 160 LEU   A CB  1 
ATOM   1169 C  CG  . LEU   A 1 144 ? 26.342 5.365   7.334  1.00 18.35 ? 160 LEU   A CG  1 
ATOM   1170 C  CD1 . LEU   A 1 144 ? 26.578 4.775   8.727  1.00 17.67 ? 160 LEU   A CD1 1 
ATOM   1171 C  CD2 . LEU   A 1 144 ? 27.389 6.403   6.998  1.00 19.12 ? 160 LEU   A CD2 1 
ATOM   1172 N  N   . ARG   A 1 145 ? 27.120 3.141   3.333  1.00 19.77 ? 161 ARG   A N   1 
ATOM   1173 C  CA  . ARG   A 1 145 ? 27.254 1.971   2.476  1.00 20.35 ? 161 ARG   A CA  1 
ATOM   1174 C  C   . ARG   A 1 145 ? 27.935 0.830   3.240  1.00 19.09 ? 161 ARG   A C   1 
ATOM   1175 O  O   . ARG   A 1 145 ? 28.881 1.048   3.991  1.00 18.37 ? 161 ARG   A O   1 
ATOM   1176 C  CB  . ARG   A 1 145 ? 27.992 2.369   1.187  1.00 21.88 ? 161 ARG   A CB  1 
ATOM   1177 C  CG  . ARG   A 1 145 ? 27.323 1.870   -0.089 1.00 23.46 ? 161 ARG   A CG  1 
ATOM   1178 C  CD  . ARG   A 1 145 ? 27.947 2.408   -1.370 1.00 24.85 ? 161 ARG   A CD  1 
ATOM   1179 N  NE  . ARG   A 1 145 ? 27.336 3.652   -1.857 0.50 25.80 ? 161 ARG   A NE  1 
ATOM   1180 C  CZ  . ARG   A 1 145 ? 26.251 3.729   -2.622 0.50 26.99 ? 161 ARG   A CZ  1 
ATOM   1181 N  NH1 . ARG   A 1 145 ? 25.647 2.632   -3.044 0.50 27.44 ? 161 ARG   A NH1 1 
ATOM   1182 N  NH2 . ARG   A 1 145 ? 25.784 4.910   -2.985 0.50 27.88 ? 161 ARG   A NH2 1 
ATOM   1183 N  N   . VAL   A 1 146 ? 27.446 -0.396  3.009  1.00 19.10 ? 162 VAL   A N   1 
ATOM   1184 C  CA  . VAL   A 1 146 ? 28.019 -1.612  3.564  1.00 18.49 ? 162 VAL   A CA  1 
ATOM   1185 C  C   . VAL   A 1 146 ? 29.383 -1.850  2.920  1.00 18.75 ? 162 VAL   A C   1 
ATOM   1186 O  O   . VAL   A 1 146 ? 29.508 -1.802  1.703  1.00 19.36 ? 162 VAL   A O   1 
ATOM   1187 C  CB  . VAL   A 1 146 ? 27.094 -2.833  3.370  1.00 18.90 ? 162 VAL   A CB  1 
ATOM   1188 C  CG1 . VAL   A 1 146 ? 27.691 -4.107  3.966  1.00 18.62 ? 162 VAL   A CG1 1 
ATOM   1189 C  CG2 . VAL   A 1 146 ? 25.704 -2.599  3.957  1.00 18.64 ? 162 VAL   A CG2 1 
ATOM   1190 N  N   . GLN   A 1 147 ? 30.396 -2.099  3.761  1.00 18.07 ? 163 GLN   A N   1 
ATOM   1191 C  CA  . GLN   A 1 147 ? 31.761 -2.330  3.324  1.00 18.63 ? 163 GLN   A CA  1 
ATOM   1192 C  C   . GLN   A 1 147 ? 32.038 -3.834  3.292  1.00 18.75 ? 163 GLN   A C   1 
ATOM   1193 O  O   . GLN   A 1 147 ? 31.231 -4.634  3.757  1.00 18.49 ? 163 GLN   A O   1 
ATOM   1194 C  CB  . GLN   A 1 147 ? 32.752 -1.637  4.266  1.00 18.42 ? 163 GLN   A CB  1 
ATOM   1195 C  CG  . GLN   A 1 147 ? 32.484 -0.151  4.492  1.00 18.42 ? 163 GLN   A CG  1 
ATOM   1196 C  CD  . GLN   A 1 147 ? 32.693 0.692   3.253  1.00 19.51 ? 163 GLN   A CD  1 
ATOM   1197 O  OE1 . GLN   A 1 147 ? 33.821 0.981   2.843  1.00 20.14 ? 163 GLN   A OE1 1 
ATOM   1198 N  NE2 . GLN   A 1 147 ? 31.597 1.107   2.640  1.00 19.99 ? 163 GLN   A NE2 1 
ATOM   1199 N  N   . ARG   A 1 148 ? 33.184 -4.201  2.712  1.00 19.20 ? 164 ARG   A N   1 
ATOM   1200 C  CA  . ARG   A 1 148 ? 33.646 -5.579  2.676  1.00 19.45 ? 164 ARG   A CA  1 
ATOM   1201 C  C   . ARG   A 1 148 ? 34.234 -5.979  4.032  1.00 18.80 ? 164 ARG   A C   1 
ATOM   1202 O  O   . ARG   A 1 148 ? 34.807 -5.148  4.730  1.00 18.03 ? 164 ARG   A O   1 
ATOM   1203 C  CB  . ARG   A 1 148 ? 34.739 -5.724  1.614  1.00 20.43 ? 164 ARG   A CB  1 
ATOM   1204 C  CG  . ARG   A 1 148 ? 34.321 -5.380  0.190  1.00 21.46 ? 164 ARG   A CG  1 
ATOM   1205 C  CD  . ARG   A 1 148 ? 35.495 -5.555  -0.760 1.00 22.60 ? 164 ARG   A CD  1 
ATOM   1206 N  NE  . ARG   A 1 148 ? 36.613 -4.651  -0.462 1.00 22.62 ? 164 ARG   A NE  1 
ATOM   1207 C  CZ  . ARG   A 1 148 ? 36.712 -3.382  -0.845 1.00 23.01 ? 164 ARG   A CZ  1 
ATOM   1208 N  NH1 . ARG   A 1 148 ? 35.788 -2.827  -1.612 1.00 23.45 ? 164 ARG   A NH1 1 
ATOM   1209 N  NH2 . ARG   A 1 148 ? 37.764 -2.673  -0.483 1.00 23.28 ? 164 ARG   A NH2 1 
ATOM   1210 N  N   . ASP   A 1 149 ? 34.124 -7.273  4.363  1.00 19.19 ? 165 ASP   A N   1 
ATOM   1211 C  CA  . ASP   A 1 149 ? 34.624 -7.830  5.614  1.00 19.15 ? 165 ASP   A CA  1 
ATOM   1212 C  C   . ASP   A 1 149 ? 36.059 -7.385  5.900  1.00 18.80 ? 165 ASP   A C   1 
ATOM   1213 O  O   . ASP   A 1 149 ? 36.360 -6.988  7.018  1.00 17.99 ? 165 ASP   A O   1 
ATOM   1214 C  CB  . ASP   A 1 149 ? 34.634 -9.350  5.615  1.00 20.44 ? 165 ASP   A CB  1 
ATOM   1215 C  CG  . ASP   A 1 149 ? 33.306 -10.067 5.394  1.00 21.44 ? 165 ASP   A CG  1 
ATOM   1216 O  OD1 . ASP   A 1 149 ? 32.240 -9.421  5.505  1.00 20.98 ? 165 ASP   A OD1 1 
ATOM   1217 O  OD2 . ASP   A 1 149 ? 33.362 -11.283 5.093  1.00 23.09 ? 165 ASP   A OD2 1 
ATOM   1218 N  N   . ARG   A 1 150 ? 36.950 -7.490  4.903  1.00 19.31 ? 166 ARG   A N   1 
ATOM   1219 C  CA  . ARG   A 1 150 ? 38.370 -7.231  5.117  1.00 19.55 ? 166 ARG   A CA  1 
ATOM   1220 C  C   . ARG   A 1 150 ? 38.639 -5.784  5.544  1.00 18.83 ? 166 ARG   A C   1 
ATOM   1221 O  O   . ARG   A 1 150 ? 39.647 -5.512  6.193  1.00 18.90 ? 166 ARG   A O   1 
ATOM   1222 C  CB  . ARG   A 1 150 ? 39.198 -7.597  3.879  1.00 20.90 ? 166 ARG   A CB  1 
ATOM   1223 C  CG  . ARG   A 1 150 ? 39.412 -9.091  3.682  1.00 21.81 ? 166 ARG   A CG  1 
ATOM   1224 C  CD  . ARG   A 1 150 ? 40.435 -9.370  2.584  1.00 23.22 ? 166 ARG   A CD  1 
ATOM   1225 N  NE  . ARG   A 1 150 ? 40.696 -10.802 2.391  1.00 24.30 ? 166 ARG   A NE  1 
ATOM   1226 C  CZ  . ARG   A 1 150 ? 39.905 -11.658 1.750  1.00 25.19 ? 166 ARG   A CZ  1 
ATOM   1227 N  NH1 . ARG   A 1 150 ? 38.791 -11.250 1.158  1.00 25.47 ? 166 ARG   A NH1 1 
ATOM   1228 N  NH2 . ARG   A 1 150 ? 40.243 -12.933 1.683  1.00 26.08 ? 166 ARG   A NH2 1 
ATOM   1229 N  N   . GLN   A 1 151 ? 37.755 -4.844  5.183  1.00 18.28 ? 167 GLN   A N   1 
ATOM   1230 C  CA  . GLN   A 1 151 ? 37.938 -3.446  5.549  1.00 18.08 ? 167 GLN   A CA  1 
ATOM   1231 C  C   . GLN   A 1 151 ? 37.809 -3.253  7.067  1.00 17.47 ? 167 GLN   A C   1 
ATOM   1232 O  O   . GLN   A 1 151 ? 38.433 -2.347  7.618  1.00 17.72 ? 167 GLN   A O   1 
ATOM   1233 C  CB  . GLN   A 1 151 ? 36.977 -2.555  4.760  1.00 18.22 ? 167 GLN   A CB  1 
ATOM   1234 C  CG  . GLN   A 1 151 ? 37.190 -2.625  3.250  1.00 19.20 ? 167 GLN   A CG  1 
ATOM   1235 C  CD  . GLN   A 1 151 ? 36.246 -1.755  2.456  1.00 19.64 ? 167 GLN   A CD  1 
ATOM   1236 O  OE1 . GLN   A 1 151 ? 35.264 -2.231  1.870  1.00 19.71 ? 167 GLN   A OE1 1 
ATOM   1237 N  NE2 . GLN   A 1 151 ? 36.539 -0.463  2.432  1.00 20.12 ? 167 GLN   A NE2 1 
ATOM   1238 N  N   . CYS   A 1 152 ? 37.024 -4.108  7.744  1.00 16.57 ? 168 CYS   A N   1 
ATOM   1239 C  CA  . CYS   A 1 152 ? 36.935 -4.082  9.197  1.00 16.31 ? 168 CYS   A CA  1 
ATOM   1240 C  C   . CYS   A 1 152 ? 37.926 -5.053  9.842  1.00 16.86 ? 168 CYS   A C   1 
ATOM   1241 O  O   . CYS   A 1 152 ? 38.387 -4.806  10.954 1.00 17.38 ? 168 CYS   A O   1 
ATOM   1242 C  CB  . CYS   A 1 152 ? 35.524 -4.404  9.681  1.00 15.50 ? 168 CYS   A CB  1 
ATOM   1243 S  SG  . CYS   A 1 152 ? 34.405 -2.983  9.628  1.00 14.91 ? 168 CYS   A SG  1 
ATOM   1244 N  N   . LEU   A 1 153 ? 38.232 -6.167  9.168  1.00 17.29 ? 169 LEU   A N   1 
ATOM   1245 C  CA  . LEU   A 1 153 ? 39.164 -7.152  9.702  1.00 18.17 ? 169 LEU   A CA  1 
ATOM   1246 C  C   . LEU   A 1 153 ? 40.545 -6.522  9.886  1.00 18.90 ? 169 LEU   A C   1 
ATOM   1247 O  O   . LEU   A 1 153 ? 41.248 -6.846  10.847 1.00 19.20 ? 169 LEU   A O   1 
ATOM   1248 C  CB  . LEU   A 1 153 ? 39.237 -8.395  8.813  1.00 18.69 ? 169 LEU   A CB  1 
ATOM   1249 C  CG  . LEU   A 1 153 ? 38.028 -9.341  8.879  1.00 18.51 ? 169 LEU   A CG  1 
ATOM   1250 C  CD1 . LEU   A 1 153 ? 37.983 -10.308 7.698  1.00 19.12 ? 169 LEU   A CD1 1 
ATOM   1251 C  CD2 . LEU   A 1 153 ? 38.017 -10.122 10.181 1.00 18.69 ? 169 LEU   A CD2 1 
ATOM   1252 N  N   . ARG   A 1 154 ? 40.917 -5.629  8.956  1.00 19.16 ? 170 ARG   A N   1 
ATOM   1253 C  CA  . ARG   A 1 154 ? 42.215 -4.967  8.988  1.00 20.14 ? 170 ARG   A CA  1 
ATOM   1254 C  C   . ARG   A 1 154 ? 42.360 -4.033  10.193 1.00 20.28 ? 170 ARG   A C   1 
ATOM   1255 O  O   . ARG   A 1 154 ? 43.465 -3.861  10.694 1.00 21.14 ? 170 ARG   A O   1 
ATOM   1256 C  CB  . ARG   A 1 154 ? 42.490 -4.215  7.679  1.00 20.46 ? 170 ARG   A CB  1 
ATOM   1257 C  CG  . ARG   A 1 154 ? 43.047 -5.107  6.576  1.00 21.01 ? 170 ARG   A CG  1 
ATOM   1258 C  CD  . ARG   A 1 154 ? 43.636 -4.314  5.429  1.00 21.67 ? 170 ARG   A CD  1 
ATOM   1259 N  NE  . ARG   A 1 154 ? 42.574 -3.610  4.704  1.00 21.11 ? 170 ARG   A NE  1 
ATOM   1260 C  CZ  . ARG   A 1 154 ? 41.768 -4.173  3.805  1.00 20.77 ? 170 ARG   A CZ  1 
ATOM   1261 N  NH1 . ARG   A 1 154 ? 41.987 -5.407  3.381  1.00 21.17 ? 170 ARG   A NH1 1 
ATOM   1262 N  NH2 . ARG   A 1 154 ? 40.772 -3.480  3.302  1.00 20.39 ? 170 ARG   A NH2 1 
ATOM   1263 N  N   . ILE   A 1 155 ? 41.273 -3.396  10.647 1.00 19.78 ? 171 ILE   A N   1 
ATOM   1264 C  CA  . ILE   A 1 155 ? 41.403 -2.325  11.624 1.00 20.10 ? 171 ILE   A CA  1 
ATOM   1265 C  C   . ILE   A 1 155 ? 40.788 -2.712  12.974 1.00 19.59 ? 171 ILE   A C   1 
ATOM   1266 O  O   . ILE   A 1 155 ? 41.076 -2.050  13.969 1.00 19.79 ? 171 ILE   A O   1 
ATOM   1267 C  CB  . ILE   A 1 155 ? 40.832 -1.002  11.074 1.00 20.17 ? 171 ILE   A CB  1 
ATOM   1268 C  CG1 . ILE   A 1 155 ? 39.329 -1.063  10.827 1.00 19.33 ? 171 ILE   A CG1 1 
ATOM   1269 C  CG2 . ILE   A 1 155 ? 41.578 -0.562  9.810  1.00 20.93 ? 171 ILE   A CG2 1 
ATOM   1270 C  CD1 . ILE   A 1 155 ? 38.739 0.270   10.402 1.00 19.27 ? 171 ILE   A CD1 1 
ATOM   1271 N  N   . PHE   A 1 156 ? 39.977 -3.780  13.022 1.00 19.03 ? 172 PHE   A N   1 
ATOM   1272 C  CA  . PHE   A 1 156 ? 39.358 -4.217  14.269 1.00 18.86 ? 172 PHE   A CA  1 
ATOM   1273 C  C   . PHE   A 1 156 ? 39.712 -5.676  14.556 1.00 19.11 ? 172 PHE   A C   1 
ATOM   1274 O  O   . PHE   A 1 156 ? 39.126 -6.589  13.979 1.00 18.62 ? 172 PHE   A O   1 
ATOM   1275 C  CB  . PHE   A 1 156 ? 37.840 -4.025  14.223 1.00 17.96 ? 172 PHE   A CB  1 
ATOM   1276 C  CG  . PHE   A 1 156 ? 37.361 -2.588  14.057 1.00 17.78 ? 172 PHE   A CG  1 
ATOM   1277 C  CD1 . PHE   A 1 156 ? 37.542 -1.648  15.072 1.00 18.43 ? 172 PHE   A CD1 1 
ATOM   1278 C  CD2 . PHE   A 1 156 ? 36.673 -2.196  12.909 1.00 17.48 ? 172 PHE   A CD2 1 
ATOM   1279 C  CE1 . PHE   A 1 156 ? 37.085 -0.341  14.915 1.00 18.36 ? 172 PHE   A CE1 1 
ATOM   1280 C  CE2 . PHE   A 1 156 ? 36.206 -0.898  12.762 1.00 17.24 ? 172 PHE   A CE2 1 
ATOM   1281 C  CZ  . PHE   A 1 156 ? 36.421 0.031   13.758 1.00 17.73 ? 172 PHE   A CZ  1 
ATOM   1282 N  N   . GLY   A 1 157 ? 40.643 -5.878  15.501 1.00 19.95 ? 173 GLY   A N   1 
ATOM   1283 C  CA  . GLY   A 1 157 ? 41.217 -7.181  15.800 1.00 20.71 ? 173 GLY   A CA  1 
ATOM   1284 C  C   . GLY   A 1 157 ? 40.179 -8.261  16.107 1.00 20.57 ? 173 GLY   A C   1 
ATOM   1285 O  O   . GLY   A 1 157 ? 40.375 -9.416  15.728 1.00 20.68 ? 173 GLY   A O   1 
ATOM   1286 N  N   . SER   A 1 158 ? 39.076 -7.880  16.771 1.00 20.41 ? 174 SER   A N   1 
ATOM   1287 C  CA  . SER   A 1 158 ? 38.098 -8.836  17.268 1.00 20.88 ? 174 SER   A CA  1 
ATOM   1288 C  C   . SER   A 1 158 ? 36.881 -8.952  16.349 1.00 20.44 ? 174 SER   A C   1 
ATOM   1289 O  O   . SER   A 1 158 ? 35.899 -9.593  16.719 1.00 20.64 ? 174 SER   A O   1 
ATOM   1290 C  CB  . SER   A 1 158 ? 37.669 -8.483  18.665 1.00 21.14 ? 174 SER   A CB  1 
ATOM   1291 O  OG  . SER   A 1 158 ? 38.724 -8.759  19.577 1.00 22.84 ? 174 SER   A OG  1 
ATOM   1292 N  N   . TYR   A 1 159 ? 36.945 -8.333  15.163 1.00 20.23 ? 175 TYR   A N   1 
ATOM   1293 C  CA  . TYR   A 1 159 ? 35.827 -8.333  14.234 1.00 19.47 ? 175 TYR   A CA  1 
ATOM   1294 C  C   . TYR   A 1 159 ? 35.557 -9.753  13.734 1.00 19.92 ? 175 TYR   A C   1 
ATOM   1295 O  O   . TYR   A 1 159 ? 36.491 -10.501 13.416 1.00 20.51 ? 175 TYR   A O   1 
ATOM   1296 C  CB  . TYR   A 1 159 ? 36.112 -7.373  13.073 1.00 19.43 ? 175 TYR   A CB  1 
ATOM   1297 C  CG  . TYR   A 1 159 ? 34.957 -7.262  12.090 1.00 18.84 ? 175 TYR   A CG  1 
ATOM   1298 C  CD1 . TYR   A 1 159 ? 33.871 -6.440  12.363 1.00 18.06 ? 175 TYR   A CD1 1 
ATOM   1299 C  CD2 . TYR   A 1 159 ? 34.946 -7.993  10.905 1.00 19.21 ? 175 TYR   A CD2 1 
ATOM   1300 C  CE1 . TYR   A 1 159 ? 32.808 -6.340  11.483 1.00 18.18 ? 175 TYR   A CE1 1 
ATOM   1301 C  CE2 . TYR   A 1 159 ? 33.894 -7.891  10.011 1.00 19.16 ? 175 TYR   A CE2 1 
ATOM   1302 C  CZ  . TYR   A 1 159 ? 32.821 -7.065  10.305 1.00 18.74 ? 175 TYR   A CZ  1 
ATOM   1303 O  OH  . TYR   A 1 159 ? 31.762 -6.976  9.454  1.00 18.96 ? 175 TYR   A OH  1 
ATOM   1304 N  N   . ASP   A 1 160 ? 34.261 -10.089 13.657 1.00 19.68 ? 176 ASP   A N   1 
ATOM   1305 C  CA  . ASP   A 1 160 ? 33.779 -11.366 13.155 1.00 20.44 ? 176 ASP   A CA  1 
ATOM   1306 C  C   . ASP   A 1 160 ? 32.621 -11.103 12.189 1.00 20.60 ? 176 ASP   A C   1 
ATOM   1307 O  O   . ASP   A 1 160 ? 31.538 -10.726 12.625 1.00 19.93 ? 176 ASP   A O   1 
ATOM   1308 C  CB  . ASP   A 1 160 ? 33.349 -12.281 14.295 1.00 20.95 ? 176 ASP   A CB  1 
ATOM   1309 C  CG  . ASP   A 1 160 ? 32.860 -13.670 13.894 1.00 21.78 ? 176 ASP   A CG  1 
ATOM   1310 O  OD1 . ASP   A 1 160 ? 32.849 -13.962 12.680 1.00 21.63 ? 176 ASP   A OD1 1 
ATOM   1311 O  OD2 . ASP   A 1 160 ? 32.491 -14.450 14.799 1.00 21.99 ? 176 ASP   A OD2 1 
ATOM   1312 N  N   . PRO   A 1 161 ? 32.800 -11.304 10.859 1.00 21.33 ? 177 PRO   A N   1 
ATOM   1313 C  CA  . PRO   A 1 161 ? 31.728 -11.044 9.889  1.00 21.61 ? 177 PRO   A CA  1 
ATOM   1314 C  C   . PRO   A 1 161 ? 30.541 -12.003 9.959  1.00 22.71 ? 177 PRO   A C   1 
ATOM   1315 O  O   . PRO   A 1 161 ? 29.492 -11.743 9.374  1.00 22.48 ? 177 PRO   A O   1 
ATOM   1316 C  CB  . PRO   A 1 161 ? 32.449 -11.122 8.532  1.00 22.14 ? 177 PRO   A CB  1 
ATOM   1317 C  CG  . PRO   A 1 161 ? 33.623 -12.039 8.783  1.00 22.77 ? 177 PRO   A CG  1 
ATOM   1318 C  CD  . PRO   A 1 161 ? 34.039 -11.782 10.227 1.00 22.05 ? 177 PRO   A CD  1 
ATOM   1319 N  N   . ARG   A 1 162 ? 30.703 -13.113 10.683 1.00 24.11 ? 178 ARG   A N   1 
ATOM   1320 C  CA  . ARG   A 1 162 ? 29.593 -14.012 10.959 1.00 25.46 ? 178 ARG   A CA  1 
ATOM   1321 C  C   . ARG   A 1 162 ? 28.547 -13.315 11.834 1.00 23.53 ? 178 ARG   A C   1 
ATOM   1322 O  O   . ARG   A 1 162 ? 27.364 -13.618 11.721 1.00 23.33 ? 178 ARG   A O   1 
ATOM   1323 C  CB  . ARG   A 1 162 ? 30.081 -15.293 11.642 1.00 28.12 ? 178 ARG   A CB  1 
ATOM   1324 C  CG  . ARG   A 1 162 ? 31.128 -16.088 10.870 1.00 31.34 ? 178 ARG   A CG  1 
ATOM   1325 C  CD  . ARG   A 1 162 ? 31.424 -17.451 11.496 1.00 34.84 ? 178 ARG   A CD  1 
ATOM   1326 N  NE  . ARG   A 1 162 ? 31.379 -17.378 12.963 1.00 38.03 ? 178 ARG   A NE  1 
ATOM   1327 C  CZ  . ARG   A 1 162 ? 32.385 -17.542 13.818 1.00 40.93 ? 178 ARG   A CZ  1 
ATOM   1328 N  NH1 . ARG   A 1 162 ? 33.565 -17.971 13.404 1.00 42.87 ? 178 ARG   A NH1 1 
ATOM   1329 N  NH2 . ARG   A 1 162 ? 32.191 -17.299 15.103 1.00 41.85 ? 178 ARG   A NH2 1 
ATOM   1330 N  N   . ARG   A 1 163 ? 28.991 -12.385 12.692 1.00 21.96 ? 179 ARG   A N   1 
ATOM   1331 C  CA  . ARG   A 1 163 ? 28.138 -11.800 13.721 1.00 21.22 ? 179 ARG   A CA  1 
ATOM   1332 C  C   . ARG   A 1 163 ? 28.014 -10.280 13.597 1.00 19.00 ? 179 ARG   A C   1 
ATOM   1333 O  O   . ARG   A 1 163 ? 27.141 -9.699  14.244 1.00 18.16 ? 179 ARG   A O   1 
ATOM   1334 C  CB  . ARG   A 1 163 ? 28.654 -12.166 15.119 1.00 22.12 ? 179 ARG   A CB  1 
ATOM   1335 C  CG  . ARG   A 1 163 ? 28.292 -13.572 15.572 1.00 24.26 ? 179 ARG   A CG  1 
ATOM   1336 C  CD  . ARG   A 1 163 ? 28.910 -13.940 16.918 1.00 25.81 ? 179 ARG   A CD  1 
ATOM   1337 N  NE  . ARG   A 1 163 ? 30.374 -13.946 16.845 1.00 26.76 ? 179 ARG   A NE  1 
ATOM   1338 C  CZ  . ARG   A 1 163 ? 31.201 -14.185 17.851 1.00 28.45 ? 179 ARG   A CZ  1 
ATOM   1339 N  NH1 . ARG   A 1 163 ? 30.722 -14.422 19.059 1.00 29.56 ? 179 ARG   A NH1 1 
ATOM   1340 N  NH2 . ARG   A 1 163 ? 32.512 -14.181 17.643 1.00 28.93 ? 179 ARG   A NH2 1 
ATOM   1341 N  N   . GLN   A 1 164 ? 28.872 -9.644  12.777 1.00 17.63 ? 180 GLN   A N   1 
ATOM   1342 C  CA  . GLN   A 1 164 ? 28.939 -8.194  12.680 1.00 16.36 ? 180 GLN   A CA  1 
ATOM   1343 C  C   . GLN   A 1 164 ? 28.897 -7.753  11.214 1.00 16.01 ? 180 GLN   A C   1 
ATOM   1344 O  O   . GLN   A 1 164 ? 29.164 -8.556  10.324 1.00 16.53 ? 180 GLN   A O   1 
ATOM   1345 C  CB  . GLN   A 1 164 ? 30.204 -7.707  13.386 1.00 16.00 ? 180 GLN   A CB  1 
ATOM   1346 C  CG  . GLN   A 1 164 ? 30.160 -7.871  14.903 1.00 16.13 ? 180 GLN   A CG  1 
ATOM   1347 C  CD  . GLN   A 1 164 ? 31.528 -7.804  15.548 1.00 16.30 ? 180 GLN   A CD  1 
ATOM   1348 O  OE1 . GLN   A 1 164 ? 32.505 -8.367  15.043 1.00 16.64 ? 180 GLN   A OE1 1 
ATOM   1349 N  NE2 . GLN   A 1 164 ? 31.611 -7.115  16.676 1.00 16.11 ? 180 GLN   A NE2 1 
ATOM   1350 N  N   . ILE   A 1 165 ? 28.531 -6.478  10.994 1.00 15.33 ? 181 ILE   A N   1 
ATOM   1351 C  CA  . ILE   A 1 165 ? 28.520 -5.846  9.677  1.00 15.31 ? 181 ILE   A CA  1 
ATOM   1352 C  C   . ILE   A 1 165 ? 29.537 -4.704  9.671  1.00 14.72 ? 181 ILE   A C   1 
ATOM   1353 O  O   . ILE   A 1 165 ? 29.656 -3.984  10.657 1.00 14.05 ? 181 ILE   A O   1 
ATOM   1354 C  CB  . ILE   A 1 165 ? 27.120 -5.322  9.290  1.00 15.49 ? 181 ILE   A CB  1 
ATOM   1355 C  CG1 . ILE   A 1 165 ? 26.016 -6.356  9.513  1.00 15.93 ? 181 ILE   A CG1 1 
ATOM   1356 C  CG2 . ILE   A 1 165 ? 27.101 -4.811  7.844  1.00 15.94 ? 181 ILE   A CG2 1 
ATOM   1357 C  CD1 . ILE   A 1 165 ? 24.633 -5.744  9.631  1.00 15.89 ? 181 ILE   A CD1 1 
ATOM   1358 N  N   . CYS   A 1 166 ? 30.236 -4.537  8.538  1.00 14.84 ? 182 CYS   A N   1 
ATOM   1359 C  CA  . CYS   A 1 166 ? 31.186 -3.452  8.328  1.00 14.92 ? 182 CYS   A CA  1 
ATOM   1360 C  C   . CYS   A 1 166 ? 30.524 -2.322  7.538  1.00 15.33 ? 182 CYS   A C   1 
ATOM   1361 O  O   . CYS   A 1 166 ? 30.079 -2.542  6.406  1.00 15.85 ? 182 CYS   A O   1 
ATOM   1362 C  CB  . CYS   A 1 166 ? 32.396 -3.973  7.557  1.00 15.28 ? 182 CYS   A CB  1 
ATOM   1363 S  SG  . CYS   A 1 166 ? 33.860 -2.911  7.649  1.00 15.28 ? 182 CYS   A SG  1 
ATOM   1364 N  N   . VAL   A 1 167 ? 30.502 -1.105  8.103  1.00 15.32 ? 183 VAL   A N   1 
ATOM   1365 C  CA  . VAL   A 1 167 ? 29.653 -0.043  7.576  1.00 15.70 ? 183 VAL   A CA  1 
ATOM   1366 C  C   . VAL   A 1 167 ? 30.382 1.303   7.538  1.00 15.94 ? 183 VAL   A C   1 
ATOM   1367 O  O   . VAL   A 1 167 ? 30.981 1.737   8.518  1.00 15.30 ? 183 VAL   A O   1 
ATOM   1368 C  CB  . VAL   A 1 167 ? 28.359 0.040   8.412  1.00 15.36 ? 183 VAL   A CB  1 
ATOM   1369 C  CG1 . VAL   A 1 167 ? 27.395 1.102   7.889  1.00 15.88 ? 183 VAL   A CG1 1 
ATOM   1370 C  CG2 . VAL   A 1 167 ? 27.663 -1.310  8.479  1.00 15.32 ? 183 VAL   A CG2 1 
ATOM   1371 N  N   . GLY   A 1 168 ? 30.283 1.982   6.387  1.00 16.80 ? 184 GLY   A N   1 
ATOM   1372 C  CA  . GLY   A 1 168 ? 30.712 3.366   6.265  1.00 17.52 ? 184 GLY   A CA  1 
ATOM   1373 C  C   . GLY   A 1 168 ? 31.990 3.502   5.441  1.00 18.48 ? 184 GLY   A C   1 
ATOM   1374 O  O   . GLY   A 1 168 ? 32.999 2.879   5.756  1.00 18.30 ? 184 GLY   A O   1 
ATOM   1375 N  N   . ASP   A 1 169 A 31.920 4.327   4.388  1.00 19.83 ? 184 ASP   A N   1 
ATOM   1376 C  CA  . ASP   A 1 169 A 33.047 4.641   3.520  1.00 21.28 ? 184 ASP   A CA  1 
ATOM   1377 C  C   . ASP   A 1 169 A 33.938 5.674   4.204  1.00 21.58 ? 184 ASP   A C   1 
ATOM   1378 O  O   . ASP   A 1 169 A 33.497 6.786   4.461  1.00 21.60 ? 184 ASP   A O   1 
ATOM   1379 C  CB  . ASP   A 1 169 A 32.540 5.159   2.180  1.00 22.63 ? 184 ASP   A CB  1 
ATOM   1380 C  CG  . ASP   A 1 169 A 33.570 5.476   1.102  1.00 24.36 ? 184 ASP   A CG  1 
ATOM   1381 O  OD1 . ASP   A 1 169 A 34.782 5.491   1.401  1.00 24.54 ? 184 ASP   A OD1 1 
ATOM   1382 O  OD2 . ASP   A 1 169 A 33.144 5.737   -0.045 1.00 26.11 ? 184 ASP   A OD2 1 
ATOM   1383 N  N   . ARG   A 1 170 ? 35.202 5.314   4.453  1.00 22.20 ? 185 ARG   A N   1 
ATOM   1384 C  CA  . ARG   A 1 170 ? 36.131 6.184   5.163  1.00 23.18 ? 185 ARG   A CA  1 
ATOM   1385 C  C   . ARG   A 1 170 ? 36.359 7.497   4.414  1.00 24.86 ? 185 ARG   A C   1 
ATOM   1386 O  O   . ARG   A 1 170 ? 36.890 8.444   4.988  1.00 25.30 ? 185 ARG   A O   1 
ATOM   1387 C  CB  . ARG   A 1 170 ? 37.475 5.483   5.395  1.00 23.35 ? 185 ARG   A CB  1 
ATOM   1388 C  CG  . ARG   A 1 170 ? 38.351 5.276   4.166  1.00 24.51 ? 185 ARG   A CG  1 
ATOM   1389 C  CD  . ARG   A 1 170 ? 39.595 4.464   4.510  1.00 24.71 ? 185 ARG   A CD  1 
ATOM   1390 N  NE  . ARG   A 1 170 ? 40.477 4.249   3.357  1.00 25.96 ? 185 ARG   A NE  1 
ATOM   1391 C  CZ  . ARG   A 1 170 ? 41.538 3.440   3.333  1.00 26.45 ? 185 ARG   A CZ  1 
ATOM   1392 N  NH1 . ARG   A 1 170 ? 41.886 2.743   4.399  1.00 26.05 ? 185 ARG   A NH1 1 
ATOM   1393 N  NH2 . ARG   A 1 170 ? 42.255 3.319   2.233  1.00 27.72 ? 185 ARG   A NH2 1 
ATOM   1394 N  N   . ARG   A 1 171 ? 35.968 7.543   3.133  1.00 26.23 ? 186 ARG   A N   1 
ATOM   1395 C  CA  . ARG   A 1 171 ? 36.171 8.719   2.303  1.00 28.22 ? 186 ARG   A CA  1 
ATOM   1396 C  C   . ARG   A 1 171 ? 35.185 9.831   2.652  1.00 29.03 ? 186 ARG   A C   1 
ATOM   1397 O  O   . ARG   A 1 171 ? 35.446 10.985  2.328  1.00 30.49 ? 186 ARG   A O   1 
ATOM   1398 C  CB  . ARG   A 1 171 ? 36.060 8.389   0.811  1.00 28.90 ? 186 ARG   A CB  1 
ATOM   1399 C  CG  . ARG   A 1 171 ? 37.304 7.700   0.271  1.00 29.61 ? 186 ARG   A CG  1 
ATOM   1400 C  CD  . ARG   A 1 171 ? 37.159 7.313   -1.184 1.00 30.52 ? 186 ARG   A CD  1 
ATOM   1401 N  NE  . ARG   A 1 171 ? 36.092 6.326   -1.355 1.00 29.88 ? 186 ARG   A NE  1 
ATOM   1402 C  CZ  . ARG   A 1 171 ? 35.813 5.673   -2.472 1.00 30.78 ? 186 ARG   A CZ  1 
ATOM   1403 N  NH1 . ARG   A 1 171 ? 36.505 5.901   -3.572 1.00 32.16 ? 186 ARG   A NH1 1 
ATOM   1404 N  NH2 . ARG   A 1 171 ? 34.853 4.768   -2.472 1.00 30.17 ? 186 ARG   A NH2 1 
ATOM   1405 N  N   . GLU   A 1 172 ? 34.063 9.493   3.297  1.00 29.01 ? 187 GLU   A N   1 
ATOM   1406 C  CA  . GLU   A 1 172 ? 33.042 10.478  3.607  1.00 30.15 ? 187 GLU   A CA  1 
ATOM   1407 C  C   . GLU   A 1 172 ? 32.948 10.672  5.117  1.00 29.04 ? 187 GLU   A C   1 
ATOM   1408 O  O   . GLU   A 1 172 ? 33.050 9.709   5.877  1.00 26.96 ? 187 GLU   A O   1 
ATOM   1409 C  CB  . GLU   A 1 172 ? 31.679 10.040  3.074  1.00 31.54 ? 187 GLU   A CB  1 
ATOM   1410 C  CG  . GLU   A 1 172 ? 31.675 9.729   1.581  1.00 34.07 ? 187 GLU   A CG  1 
ATOM   1411 C  CD  . GLU   A 1 172 ? 30.270 9.579   1.030  1.00 36.31 ? 187 GLU   A CD  1 
ATOM   1412 O  OE1 . GLU   A 1 172 ? 29.912 8.463   0.601  1.00 38.21 ? 187 GLU   A OE1 1 
ATOM   1413 O  OE2 . GLU   A 1 172 ? 29.526 10.582  1.041  1.00 38.04 ? 187 GLU   A OE2 1 
ATOM   1414 N  N   . ARG   A 1 173 ? 32.724 11.931  5.522  1.00 28.99 ? 188 ARG   A N   1 
ATOM   1415 C  CA  . ARG   A 1 173 ? 32.486 12.276  6.912  1.00 28.06 ? 188 ARG   A CA  1 
ATOM   1416 C  C   . ARG   A 1 173 ? 31.017 11.995  7.234  1.00 26.37 ? 188 ARG   A C   1 
ATOM   1417 O  O   . ARG   A 1 173 ? 30.206 12.912  7.375  1.00 27.01 ? 188 ARG   A O   1 
ATOM   1418 C  CB  . ARG   A 1 173 ? 32.912 13.725  7.180  1.00 29.82 ? 188 ARG   A CB  1 
ATOM   1419 C  CG  . ARG   A 1 173 ? 33.053 14.059  8.660  1.00 30.20 ? 188 ARG   A CG  1 
ATOM   1420 C  CD  . ARG   A 1 173 ? 33.213 15.547  8.930  1.00 32.18 ? 188 ARG   A CD  1 
ATOM   1421 N  NE  . ARG   A 1 173 ? 32.820 15.856  10.311 1.00 32.26 ? 188 ARG   A NE  1 
ATOM   1422 C  CZ  . ARG   A 1 173 ? 31.629 16.318  10.697 1.00 32.73 ? 188 ARG   A CZ  1 
ATOM   1423 N  NH1 . ARG   A 1 173 ? 30.704 16.642  9.804  1.00 33.08 ? 188 ARG   A NH1 1 
ATOM   1424 N  NH2 . ARG   A 1 173 ? 31.357 16.449  11.987 1.00 32.58 ? 188 ARG   A NH2 1 
ATOM   1425 N  N   . LYS   A 1 174 A 30.703 10.702  7.355  1.00 24.19 ? 188 LYS   A N   1 
ATOM   1426 C  CA  . LYS   A 1 174 A 29.361 10.215  7.621  1.00 22.46 ? 188 LYS   A CA  1 
ATOM   1427 C  C   . LYS   A 1 174 A 29.480 8.978   8.500  1.00 20.20 ? 188 LYS   A C   1 
ATOM   1428 O  O   . LYS   A 1 174 A 30.152 8.028   8.111  1.00 19.65 ? 188 LYS   A O   1 
ATOM   1429 C  CB  . LYS   A 1 174 A 28.636 9.838   6.322  1.00 22.99 ? 188 LYS   A CB  1 
ATOM   1430 C  CG  . LYS   A 1 174 A 28.121 11.010  5.494  1.00 24.64 ? 188 LYS   A CG  1 
ATOM   1431 C  CD  . LYS   A 1 174 A 27.489 10.559  4.182  1.00 25.63 ? 188 LYS   A CD  1 
ATOM   1432 C  CE  . LYS   A 1 174 A 26.909 11.694  3.418  1.00 27.42 ? 188 LYS   A CE  1 
ATOM   1433 N  NZ  . LYS   A 1 174 A 26.698 11.315  2.020  1.00 29.07 ? 188 LYS   A NZ  1 
ATOM   1434 N  N   . ALA   A 1 175 ? 28.831 9.000   9.677  1.00 18.84 ? 189 ALA   A N   1 
ATOM   1435 C  CA  . ALA   A 1 175 ? 28.928 7.890   10.615 1.00 17.49 ? 189 ALA   A CA  1 
ATOM   1436 C  C   . ALA   A 1 175 ? 27.844 7.960   11.690 1.00 16.50 ? 189 ALA   A C   1 
ATOM   1437 O  O   . ALA   A 1 175 ? 27.340 9.030   12.006 1.00 16.37 ? 189 ALA   A O   1 
ATOM   1438 C  CB  . ALA   A 1 175 ? 30.304 7.874   11.257 1.00 17.59 ? 189 ALA   A CB  1 
ATOM   1439 N  N   . ALA   A 1 176 ? 27.475 6.788   12.225 1.00 15.61 ? 190 ALA   A N   1 
ATOM   1440 C  CA  . ALA   A 1 176 ? 26.882 6.720   13.552 1.00 15.14 ? 190 ALA   A CA  1 
ATOM   1441 C  C   . ALA   A 1 176 ? 28.008 6.955   14.559 1.00 15.38 ? 190 ALA   A C   1 
ATOM   1442 O  O   . ALA   A 1 176 ? 29.168 6.678   14.265 1.00 15.82 ? 190 ALA   A O   1 
ATOM   1443 C  CB  . ALA   A 1 176 ? 26.179 5.396   13.756 1.00 14.46 ? 190 ALA   A CB  1 
ATOM   1444 N  N   . PHE   A 1 177 ? 27.686 7.553   15.704 1.00 15.48 ? 191 PHE   A N   1 
ATOM   1445 C  CA  . PHE   A 1 177 ? 28.703 7.892   16.685 1.00 15.98 ? 191 PHE   A CA  1 
ATOM   1446 C  C   . PHE   A 1 177 ? 28.088 7.728   18.075 1.00 15.84 ? 191 PHE   A C   1 
ATOM   1447 O  O   . PHE   A 1 177 ? 27.030 7.110   18.222 1.00 14.99 ? 191 PHE   A O   1 
ATOM   1448 C  CB  . PHE   A 1 177 ? 29.250 9.285   16.341 1.00 16.80 ? 191 PHE   A CB  1 
ATOM   1449 C  CG  . PHE   A 1 177 ? 30.562 9.653   17.020 1.00 17.64 ? 191 PHE   A CG  1 
ATOM   1450 C  CD1 . PHE   A 1 177 ? 31.651 8.782   17.010 1.00 17.72 ? 191 PHE   A CD1 1 
ATOM   1451 C  CD2 . PHE   A 1 177 ? 30.683 10.846  17.725 1.00 18.64 ? 191 PHE   A CD2 1 
ATOM   1452 C  CE1 . PHE   A 1 177 ? 32.834 9.110   17.661 1.00 18.65 ? 191 PHE   A CE1 1 
ATOM   1453 C  CE2 . PHE   A 1 177 ? 31.870 11.169  18.376 1.00 19.73 ? 191 PHE   A CE2 1 
ATOM   1454 C  CZ  . PHE   A 1 177 ? 32.945 10.308  18.334 1.00 19.69 ? 191 PHE   A CZ  1 
ATOM   1455 N  N   . LYS   A 1 178 ? 28.780 8.258   19.086 1.00 16.52 ? 192 LYS   A N   1 
ATOM   1456 C  CA  . LYS   A 1 178 ? 28.357 8.139   20.469 1.00 16.95 ? 192 LYS   A CA  1 
ATOM   1457 C  C   . LYS   A 1 178 ? 26.964 8.745   20.626 1.00 16.88 ? 192 LYS   A C   1 
ATOM   1458 O  O   . LYS   A 1 178 ? 26.682 9.805   20.070 1.00 17.08 ? 192 LYS   A O   1 
ATOM   1459 C  CB  . LYS   A 1 178 ? 29.368 8.845   21.378 1.00 17.99 ? 192 LYS   A CB  1 
ATOM   1460 C  CG  . LYS   A 1 178 ? 30.784 8.284   21.356 1.00 18.43 ? 192 LYS   A CG  1 
ATOM   1461 C  CD  . LYS   A 1 178 ? 31.770 9.142   22.147 1.00 19.92 ? 192 LYS   A CD  1 
ATOM   1462 C  CE  . LYS   A 1 178 ? 33.070 8.464   22.458 1.00 20.51 ? 192 LYS   A CE  1 
ATOM   1463 N  NZ  . LYS   A 1 178 ? 33.914 9.302   23.311 0.50 22.19 ? 192 LYS   A NZ  1 
ATOM   1464 N  N   . GLY   A 1 179 ? 26.115 8.066   21.409 1.00 16.88 ? 193 GLY   A N   1 
ATOM   1465 C  CA  . GLY   A 1 179 ? 24.722 8.445   21.584 1.00 16.85 ? 193 GLY   A CA  1 
ATOM   1466 C  C   . GLY   A 1 179 ? 23.787 7.704   20.622 1.00 15.98 ? 193 GLY   A C   1 
ATOM   1467 O  O   . GLY   A 1 179 ? 22.595 7.585   20.909 1.00 15.78 ? 193 GLY   A O   1 
ATOM   1468 N  N   . ASP   A 1 180 ? 24.336 7.185   19.510 1.00 15.42 ? 194 ASP   A N   1 
ATOM   1469 C  CA  . ASP   A 1 180 ? 23.564 6.438   18.526 1.00 14.82 ? 194 ASP   A CA  1 
ATOM   1470 C  C   . ASP   A 1 180 ? 23.572 4.929   18.784 1.00 14.40 ? 194 ASP   A C   1 
ATOM   1471 O  O   . ASP   A 1 180 ? 22.860 4.214   18.082 1.00 13.85 ? 194 ASP   A O   1 
ATOM   1472 C  CB  . ASP   A 1 180 ? 24.062 6.675   17.106 1.00 14.73 ? 194 ASP   A CB  1 
ATOM   1473 C  CG  . ASP   A 1 180 ? 24.028 8.115   16.625 1.00 15.40 ? 194 ASP   A CG  1 
ATOM   1474 O  OD1 . ASP   A 1 180 ? 23.029 8.805   16.911 1.00 15.54 ? 194 ASP   A OD1 1 
ATOM   1475 O  OD2 . ASP   A 1 180 ? 24.998 8.525   15.957 1.00 15.76 ? 194 ASP   A OD2 1 
ATOM   1476 N  N   . SER   A 1 181 ? 24.370 4.444   19.761 1.00 14.61 ? 195 SER   A N   1 
ATOM   1477 C  CA  . SER   A 1 181 ? 24.448 3.020   20.070 1.00 14.42 ? 195 SER   A CA  1 
ATOM   1478 C  C   . SER   A 1 181 ? 23.049 2.432   20.159 1.00 14.31 ? 195 SER   A C   1 
ATOM   1479 O  O   . SER   A 1 181 ? 22.160 3.066   20.731 1.00 14.56 ? 195 SER   A O   1 
ATOM   1480 C  CB  . SER   A 1 181 ? 25.143 2.715   21.395 1.00 15.28 ? 195 SER   A CB  1 
ATOM   1481 O  OG  . SER   A 1 181 ? 26.411 3.328   21.523 1.00 15.87 ? 195 SER   A OG  1 
ATOM   1482 N  N   . GLY   A 1 182 ? 22.885 1.200   19.661 1.00 13.96 ? 196 GLY   A N   1 
ATOM   1483 C  CA  . GLY   A 1 182 ? 21.645 0.461   19.845 1.00 14.44 ? 196 GLY   A CA  1 
ATOM   1484 C  C   . GLY   A 1 182 ? 20.619 0.729   18.744 1.00 14.64 ? 196 GLY   A C   1 
ATOM   1485 O  O   . GLY   A 1 182 ? 19.684 -0.049  18.560 1.00 15.01 ? 196 GLY   A O   1 
ATOM   1486 N  N   . GLY   A 1 183 ? 20.813 1.814   17.991 1.00 13.91 ? 197 GLY   A N   1 
ATOM   1487 C  CA  . GLY   A 1 183 ? 19.891 2.190   16.932 1.00 14.29 ? 197 GLY   A CA  1 
ATOM   1488 C  C   . GLY   A 1 183 ? 19.990 1.267   15.719 1.00 14.34 ? 197 GLY   A C   1 
ATOM   1489 O  O   . GLY   A 1 183 ? 20.942 0.490   15.582 1.00 13.65 ? 197 GLY   A O   1 
ATOM   1490 N  N   . PRO   A 1 184 ? 18.978 1.308   14.823 1.00 14.86 ? 198 PRO   A N   1 
ATOM   1491 C  CA  . PRO   A 1 184 ? 18.925 0.404   13.672 1.00 15.32 ? 198 PRO   A CA  1 
ATOM   1492 C  C   . PRO   A 1 184 ? 19.719 0.871   12.456 1.00 15.58 ? 198 PRO   A C   1 
ATOM   1493 O  O   . PRO   A 1 184 ? 19.800 2.065   12.202 1.00 15.82 ? 198 PRO   A O   1 
ATOM   1494 C  CB  . PRO   A 1 184 ? 17.408 0.400   13.387 1.00 15.90 ? 198 PRO   A CB  1 
ATOM   1495 C  CG  . PRO   A 1 184 ? 16.977 1.831   13.660 1.00 16.17 ? 198 PRO   A CG  1 
ATOM   1496 C  CD  . PRO   A 1 184 ? 17.839 2.241   14.861 1.00 15.60 ? 198 PRO   A CD  1 
ATOM   1497 N  N   . LEU   A 1 185 ? 20.283 -0.092  11.717 1.00 15.83 ? 199 LEU   A N   1 
ATOM   1498 C  CA  . LEU   A 1 185 ? 20.628 0.070   10.312 1.00 16.31 ? 199 LEU   A CA  1 
ATOM   1499 C  C   . LEU   A 1 185 ? 19.467 -0.451  9.465  1.00 16.91 ? 199 LEU   A C   1 
ATOM   1500 O  O   . LEU   A 1 185 ? 19.187 -1.653  9.489  1.00 16.76 ? 199 LEU   A O   1 
ATOM   1501 C  CB  . LEU   A 1 185 ? 21.918 -0.705  10.046 1.00 16.41 ? 199 LEU   A CB  1 
ATOM   1502 C  CG  . LEU   A 1 185 ? 22.587 -0.492  8.685  1.00 17.20 ? 199 LEU   A CG  1 
ATOM   1503 C  CD1 . LEU   A 1 185 ? 23.389 0.809   8.641  1.00 17.09 ? 199 LEU   A CD1 1 
ATOM   1504 C  CD2 . LEU   A 1 185 ? 23.469 -1.674  8.334  1.00 17.42 ? 199 LEU   A CD2 1 
ATOM   1505 N  N   . LEU   A 1 186 ? 18.794 0.462   8.739  1.00 17.50 ? 200 LEU   A N   1 
ATOM   1506 C  CA  . LEU   A 1 186 ? 17.664 0.130   7.881  1.00 18.61 ? 200 LEU   A CA  1 
ATOM   1507 C  C   . LEU   A 1 186 ? 18.160 -0.032  6.449  1.00 19.15 ? 200 LEU   A C   1 
ATOM   1508 O  O   . LEU   A 1 186 ? 18.689 0.917   5.880  1.00 18.87 ? 200 LEU   A O   1 
ATOM   1509 C  CB  . LEU   A 1 186 ? 16.548 1.179   7.863  1.00 19.29 ? 200 LEU   A CB  1 
ATOM   1510 C  CG  . LEU   A 1 186 ? 15.796 1.444   9.168  1.00 19.19 ? 200 LEU   A CG  1 
ATOM   1511 C  CD1 . LEU   A 1 186 ? 15.480 0.169   9.923  1.00 19.00 ? 200 LEU   A CD1 1 
ATOM   1512 C  CD2 . LEU   A 1 186 ? 16.582 2.412   10.022 1.00 18.76 ? 200 LEU   A CD2 1 
ATOM   1513 N  N   . CYS   A 1 187 ? 17.933 -1.217  5.870  1.00 20.02 ? 201 CYS   A N   1 
ATOM   1514 C  CA  . CYS   A 1 187 ? 18.215 -1.463  4.462  1.00 21.25 ? 201 CYS   A CA  1 
ATOM   1515 C  C   . CYS   A 1 187 ? 16.919 -1.946  3.804  1.00 22.90 ? 201 CYS   A C   1 
ATOM   1516 O  O   . CYS   A 1 187 ? 16.330 -2.939  4.231  1.00 22.52 ? 201 CYS   A O   1 
ATOM   1517 C  CB  . CYS   A 1 187 ? 19.380 -2.434  4.283  1.00 21.09 ? 201 CYS   A CB  1 
ATOM   1518 S  SG  . CYS   A 1 187 ? 20.760 -2.210  5.441  1.00 19.88 ? 201 CYS   A SG  1 
ATOM   1519 N  N   . ASN   A 1 188 ? 16.454 -1.202  2.793  1.00 25.06 ? 202 ASN   A N   1 
ATOM   1520 C  CA  . ASN   A 1 188 ? 15.199 -1.496  2.116  1.00 26.99 ? 202 ASN   A CA  1 
ATOM   1521 C  C   . ASN   A 1 188 ? 14.093 -1.706  3.155  1.00 26.93 ? 202 ASN   A C   1 
ATOM   1522 O  O   . ASN   A 1 188 ? 13.311 -2.652  3.065  1.00 27.43 ? 202 ASN   A O   1 
ATOM   1523 C  CB  . ASN   A 1 188 ? 15.362 -2.672  1.157  1.00 28.60 ? 202 ASN   A CB  1 
ATOM   1524 C  CG  . ASN   A 1 188 ? 16.205 -2.316  -0.048 1.00 30.26 ? 202 ASN   A CG  1 
ATOM   1525 O  OD1 . ASN   A 1 188 ? 15.807 -1.462  -0.850 1.00 32.19 ? 202 ASN   A OD1 1 
ATOM   1526 N  ND2 . ASN   A 1 188 ? 17.360 -2.951  -0.208 1.00 30.48 ? 202 ASN   A ND2 1 
ATOM   1527 N  N   . ASN   A 1 189 ? 14.067 -0.828  4.168  1.00 26.27 ? 203 ASN   A N   1 
ATOM   1528 C  CA  . ASN   A 1 189 ? 12.982 -0.744  5.138  1.00 26.45 ? 203 ASN   A CA  1 
ATOM   1529 C  C   . ASN   A 1 189 ? 13.016 -1.873  6.174  1.00 25.19 ? 203 ASN   A C   1 
ATOM   1530 O  O   . ASN   A 1 189 ? 12.070 -1.989  6.949  1.00 25.59 ? 203 ASN   A O   1 
ATOM   1531 C  CB  . ASN   A 1 189 ? 11.617 -0.647  4.460  1.00 28.99 ? 203 ASN   A CB  1 
ATOM   1532 C  CG  . ASN   A 1 189 ? 11.527 0.563   3.556  1.00 30.85 ? 203 ASN   A CG  1 
ATOM   1533 O  OD1 . ASN   A 1 189 ? 11.307 0.437   2.344  1.00 32.49 ? 203 ASN   A OD1 1 
ATOM   1534 N  ND2 . ASN   A 1 189 ? 11.700 1.743   4.132  1.00 31.26 ? 203 ASN   A ND2 1 
ATOM   1535 N  N   . VAL   A 1 190 ? 14.118 -2.639  6.244  1.00 23.57 ? 204 VAL   A N   1 
ATOM   1536 C  CA  . VAL   A 1 190 ? 14.277 -3.724  7.208  1.00 22.45 ? 204 VAL   A CA  1 
ATOM   1537 C  C   . VAL   A 1 190 ? 15.477 -3.427  8.111  1.00 20.72 ? 204 VAL   A C   1 
ATOM   1538 O  O   . VAL   A 1 190 ? 16.502 -2.940  7.633  1.00 20.28 ? 204 VAL   A O   1 
ATOM   1539 C  CB  . VAL   A 1 190 ? 14.460 -5.065  6.469  1.00 22.94 ? 204 VAL   A CB  1 
ATOM   1540 C  CG1 . VAL   A 1 190 ? 14.872 -6.191  7.405  1.00 22.54 ? 204 VAL   A CG1 1 
ATOM   1541 C  CG2 . VAL   A 1 190 ? 13.216 -5.454  5.676  1.00 24.33 ? 204 VAL   A CG2 1 
ATOM   1542 N  N   . ALA   A 1 191 ? 15.358 -3.759  9.403  1.00 19.29 ? 209 ALA   A N   1 
ATOM   1543 C  CA  . ALA   A 1 191 ? 16.428 -3.527  10.366 1.00 18.19 ? 209 ALA   A CA  1 
ATOM   1544 C  C   . ALA   A 1 191 ? 17.417 -4.693  10.371 1.00 17.53 ? 209 ALA   A C   1 
ATOM   1545 O  O   . ALA   A 1 191 ? 17.242 -5.650  11.120 1.00 17.58 ? 209 ALA   A O   1 
ATOM   1546 C  CB  . ALA   A 1 191 ? 15.854 -3.298  11.755 1.00 17.76 ? 209 ALA   A CB  1 
ATOM   1547 N  N   . HIS   A 1 192 ? 18.487 -4.575  9.571  1.00 17.22 ? 210 HIS   A N   1 
ATOM   1548 C  CA  . HIS   A 1 192 ? 19.489 -5.624  9.435  1.00 17.14 ? 210 HIS   A CA  1 
ATOM   1549 C  C   . HIS   A 1 192 ? 20.572 -5.535  10.513 1.00 16.06 ? 210 HIS   A C   1 
ATOM   1550 O  O   . HIS   A 1 192 ? 21.244 -6.528  10.783 1.00 16.01 ? 210 HIS   A O   1 
ATOM   1551 C  CB  . HIS   A 1 192 ? 20.181 -5.563  8.068  1.00 17.89 ? 210 HIS   A CB  1 
ATOM   1552 C  CG  . HIS   A 1 192 ? 19.366 -6.040  6.911  1.00 19.07 ? 210 HIS   A CG  1 
ATOM   1553 N  ND1 . HIS   A 1 192 ? 19.587 -7.258  6.299  1.00 19.97 ? 210 HIS   A ND1 1 
ATOM   1554 C  CD2 . HIS   A 1 192 ? 18.363 -5.456  6.231  1.00 19.88 ? 210 HIS   A CD2 1 
ATOM   1555 C  CE1 . HIS   A 1 192 ? 18.725 -7.408  5.306  1.00 20.97 ? 210 HIS   A CE1 1 
ATOM   1556 N  NE2 . HIS   A 1 192 ? 17.970 -6.322  5.243  1.00 20.81 ? 210 HIS   A NE2 1 
ATOM   1557 N  N   . GLY   A 1 193 ? 20.779 -4.353  11.105 1.00 15.38 ? 211 GLY   A N   1 
ATOM   1558 C  CA  . GLY   A 1 193 ? 21.910 -4.159  12.005 1.00 14.79 ? 211 GLY   A CA  1 
ATOM   1559 C  C   . GLY   A 1 193 ? 21.584 -3.305  13.231 1.00 14.44 ? 211 GLY   A C   1 
ATOM   1560 O  O   . GLY   A 1 193 ? 20.522 -2.673  13.303 1.00 14.53 ? 211 GLY   A O   1 
ATOM   1561 N  N   . ILE   A 1 194 ? 22.528 -3.314  14.192 1.00 13.88 ? 212 ILE   A N   1 
ATOM   1562 C  CA  . ILE   A 1 194 ? 22.456 -2.536  15.425 1.00 13.53 ? 212 ILE   A CA  1 
ATOM   1563 C  C   . ILE   A 1 194 ? 23.780 -1.783  15.604 1.00 13.26 ? 212 ILE   A C   1 
ATOM   1564 O  O   . ILE   A 1 194 ? 24.840 -2.399  15.536 1.00 13.18 ? 212 ILE   A O   1 
ATOM   1565 C  CB  . ILE   A 1 194 ? 22.171 -3.443  16.641 1.00 13.56 ? 212 ILE   A CB  1 
ATOM   1566 C  CG1 . ILE   A 1 194 ? 20.926 -4.324  16.437 1.00 13.84 ? 212 ILE   A CG1 1 
ATOM   1567 C  CG2 . ILE   A 1 194 ? 22.070 -2.617  17.928 1.00 13.44 ? 212 ILE   A CG2 1 
ATOM   1568 C  CD1 . ILE   A 1 194 ? 20.714 -5.355  17.532 1.00 13.82 ? 212 ILE   A CD1 1 
ATOM   1569 N  N   . VAL   A 1 195 ? 23.719 -0.467  15.866 1.00 13.18 ? 213 VAL   A N   1 
ATOM   1570 C  CA  . VAL   A 1 195 ? 24.913 0.349   16.079 1.00 13.15 ? 213 VAL   A CA  1 
ATOM   1571 C  C   . VAL   A 1 195 ? 25.658 -0.206  17.293 1.00 13.09 ? 213 VAL   A C   1 
ATOM   1572 O  O   . VAL   A 1 195 ? 25.097 -0.254  18.388 1.00 12.93 ? 213 VAL   A O   1 
ATOM   1573 C  CB  . VAL   A 1 195 ? 24.622 1.849   16.275 1.00 13.28 ? 213 VAL   A CB  1 
ATOM   1574 C  CG1 . VAL   A 1 195 ? 25.878 2.654   16.585 1.00 13.58 ? 213 VAL   A CG1 1 
ATOM   1575 C  CG2 . VAL   A 1 195 ? 23.905 2.475   15.090 1.00 13.50 ? 213 VAL   A CG2 1 
ATOM   1576 N  N   . SER   A 1 196 ? 26.921 -0.610  17.097 1.00 13.39 ? 214 SER   A N   1 
ATOM   1577 C  CA  . SER   A 1 196 ? 27.701 -1.205  18.174 1.00 13.44 ? 214 SER   A CA  1 
ATOM   1578 C  C   . SER   A 1 196 ? 28.889 -0.313  18.558 1.00 13.79 ? 214 SER   A C   1 
ATOM   1579 O  O   . SER   A 1 196 ? 28.851 0.327   19.611 1.00 13.47 ? 214 SER   A O   1 
ATOM   1580 C  CB  . SER   A 1 196 ? 28.102 -2.625  17.852 1.00 13.76 ? 214 SER   A CB  1 
ATOM   1581 O  OG  . SER   A 1 196 ? 28.852 -3.199  18.917 1.00 13.87 ? 214 SER   A OG  1 
ATOM   1582 N  N   . TYR   A 1 197 ? 29.957 -0.269  17.743 1.00 14.17 ? 215 TYR   A N   1 
ATOM   1583 C  CA  . TYR   A 1 197 ? 31.113 0.542   18.107 1.00 14.71 ? 215 TYR   A CA  1 
ATOM   1584 C  C   . TYR   A 1 197 ? 31.918 0.958   16.878 1.00 15.32 ? 215 TYR   A C   1 
ATOM   1585 O  O   . TYR   A 1 197 ? 31.652 0.529   15.757 1.00 14.80 ? 215 TYR   A O   1 
ATOM   1586 C  CB  . TYR   A 1 197 ? 32.014 -0.212  19.092 1.00 15.14 ? 215 TYR   A CB  1 
ATOM   1587 C  CG  . TYR   A 1 197 ? 32.768 -1.414  18.530 1.00 15.36 ? 215 TYR   A CG  1 
ATOM   1588 C  CD1 . TYR   A 1 197 ? 32.186 -2.674  18.462 1.00 15.20 ? 215 TYR   A CD1 1 
ATOM   1589 C  CD2 . TYR   A 1 197 ? 34.077 -1.295  18.086 1.00 16.12 ? 215 TYR   A CD2 1 
ATOM   1590 C  CE1 . TYR   A 1 197 ? 32.876 -3.773  17.974 1.00 15.60 ? 215 TYR   A CE1 1 
ATOM   1591 C  CE2 . TYR   A 1 197 ? 34.780 -2.382  17.593 1.00 16.44 ? 215 TYR   A CE2 1 
ATOM   1592 C  CZ  . TYR   A 1 197 ? 34.178 -3.626  17.533 1.00 16.38 ? 215 TYR   A CZ  1 
ATOM   1593 O  OH  . TYR   A 1 197 ? 34.893 -4.687  17.046 1.00 17.28 ? 215 TYR   A OH  1 
ATOM   1594 N  N   . GLY   A 1 198 ? 32.919 1.807   17.121 1.00 16.40 ? 216 GLY   A N   1 
ATOM   1595 C  CA  . GLY   A 1 198 ? 33.810 2.281   16.076 1.00 17.54 ? 216 GLY   A CA  1 
ATOM   1596 C  C   . GLY   A 1 198 ? 35.023 2.968   16.690 1.00 19.13 ? 216 GLY   A C   1 
ATOM   1597 O  O   . GLY   A 1 198 ? 35.235 2.887   17.899 1.00 19.18 ? 216 GLY   A O   1 
ATOM   1598 N  N   . LYS   A 1 199 ? 35.821 3.635   15.854 1.00 20.56 ? 217 LYS   A N   1 
ATOM   1599 C  CA  . LYS   A 1 199 ? 36.988 4.349   16.348 1.00 22.35 ? 217 LYS   A CA  1 
ATOM   1600 C  C   . LYS   A 1 199 ? 36.542 5.626   17.058 1.00 22.69 ? 217 LYS   A C   1 
ATOM   1601 O  O   . LYS   A 1 199 ? 35.562 6.256   16.657 1.00 22.33 ? 217 LYS   A O   1 
ATOM   1602 C  CB  . LYS   A 1 199 ? 37.957 4.690   15.209 1.00 23.55 ? 217 LYS   A CB  1 
ATOM   1603 C  CG  . LYS   A 1 199 ? 38.558 3.494   14.488 1.00 24.41 ? 217 LYS   A CG  1 
ATOM   1604 C  CD  . LYS   A 1 199 ? 39.405 2.581   15.367 1.00 25.93 ? 217 LYS   A CD  1 
ATOM   1605 C  CE  . LYS   A 1 199 ? 40.153 1.564   14.572 1.00 26.96 ? 217 LYS   A CE  1 
ATOM   1606 N  NZ  . LYS   A 1 199 ? 40.797 0.559   15.422 1.00 28.02 ? 217 LYS   A NZ  1 
ATOM   1607 N  N   . SER   A 1 200 ? 37.291 6.017   18.098 1.00 23.59 ? 218 SER   A N   1 
ATOM   1608 C  CA  . SER   A 1 200 ? 37.005 7.230   18.854 1.00 24.52 ? 218 SER   A CA  1 
ATOM   1609 C  C   . SER   A 1 200 ? 36.964 8.471   17.954 1.00 24.59 ? 218 SER   A C   1 
ATOM   1610 O  O   . SER   A 1 200 ? 36.286 9.443   18.276 1.00 24.32 ? 218 SER   A O   1 
ATOM   1611 C  CB  . SER   A 1 200 ? 38.008 7.425   19.970 1.00 26.16 ? 218 SER   A CB  1 
ATOM   1612 O  OG  . SER   A 1 200 ? 39.295 7.699   19.430 1.00 27.58 ? 218 SER   A OG  1 
ATOM   1613 N  N   . SER   A 1 201 ? 37.700 8.436   16.835 1.00 24.68 ? 219 SER   A N   1 
ATOM   1614 C  CA  . SER   A 1 201 ? 37.770 9.537   15.888 1.00 25.00 ? 219 SER   A CA  1 
ATOM   1615 C  C   . SER   A 1 201 ? 36.445 9.794   15.169 1.00 24.27 ? 219 SER   A C   1 
ATOM   1616 O  O   . SER   A 1 201 ? 36.261 10.868  14.592 1.00 24.99 ? 219 SER   A O   1 
ATOM   1617 C  CB  . SER   A 1 201 ? 38.838 9.266   14.862 1.00 25.58 ? 219 SER   A CB  1 
ATOM   1618 O  OG  . SER   A 1 201 ? 38.497 8.109   14.107 1.00 24.79 ? 219 SER   A OG  1 
ATOM   1619 N  N   . GLY   A 1 202 ? 35.565 8.789   15.122 1.00 23.20 ? 220 GLY   A N   1 
ATOM   1620 C  CA  . GLY   A 1 202 ? 34.327 8.889   14.358 1.00 22.69 ? 220 GLY   A CA  1 
ATOM   1621 C  C   . GLY   A 1 202 ? 34.520 8.594   12.866 1.00 22.41 ? 220 GLY   A C   1 
ATOM   1622 O  O   . GLY   A 1 202 ? 33.564 8.669   12.089 1.00 22.61 ? 220 GLY   A O   1 
ATOM   1623 N  N   . VAL   A 1 203 ? 35.745 8.239   12.462 1.00 22.00 ? 221 VAL   A N   1 
ATOM   1624 C  CA  . VAL   A 1 203 ? 36.026 7.960   11.061 1.00 21.84 ? 221 VAL   A CA  1 
ATOM   1625 C  C   . VAL   A 1 203 ? 35.687 6.493   10.774 1.00 20.63 ? 221 VAL   A C   1 
ATOM   1626 O  O   . VAL   A 1 203 ? 36.218 5.594   11.428 1.00 19.94 ? 221 VAL   A O   1 
ATOM   1627 C  CB  . VAL   A 1 203 ? 37.491 8.277   10.704 1.00 22.82 ? 221 VAL   A CB  1 
ATOM   1628 C  CG1 . VAL   A 1 203 ? 37.764 8.092   9.213  1.00 23.16 ? 221 VAL   A CG1 1 
ATOM   1629 C  CG2 . VAL   A 1 203 ? 37.891 9.680   11.137 1.00 23.87 ? 221 VAL   A CG2 1 
ATOM   1630 N  N   . PRO   A 1 204 ? 34.814 6.247   9.787  1.00 20.10 ? 224 PRO   A N   1 
ATOM   1631 C  CA  . PRO   A 1 204 ? 34.447 4.870   9.436  1.00 19.43 ? 224 PRO   A CA  1 
ATOM   1632 C  C   . PRO   A 1 204 ? 35.609 4.147   8.753  1.00 19.49 ? 224 PRO   A C   1 
ATOM   1633 O  O   . PRO   A 1 204 ? 36.636 4.767   8.486  1.00 20.34 ? 224 PRO   A O   1 
ATOM   1634 C  CB  . PRO   A 1 204 ? 33.202 5.037   8.533  1.00 19.29 ? 224 PRO   A CB  1 
ATOM   1635 C  CG  . PRO   A 1 204 ? 33.350 6.407   7.921  1.00 19.92 ? 224 PRO   A CG  1 
ATOM   1636 C  CD  . PRO   A 1 204 ? 34.138 7.227   8.921  1.00 20.17 ? 224 PRO   A CD  1 
ATOM   1637 N  N   . PRO   A 1 205 ? 35.517 2.838   8.412  1.00 18.88 ? 225 PRO   A N   1 
ATOM   1638 C  CA  . PRO   A 1 205 ? 34.384 1.969   8.768  1.00 18.03 ? 225 PRO   A CA  1 
ATOM   1639 C  C   . PRO   A 1 205 ? 34.117 1.765   10.260 1.00 17.01 ? 225 PRO   A C   1 
ATOM   1640 O  O   . PRO   A 1 205 ? 35.011 1.949   11.076 1.00 16.93 ? 225 PRO   A O   1 
ATOM   1641 C  CB  . PRO   A 1 205 ? 34.720 0.622   8.103  1.00 18.41 ? 225 PRO   A CB  1 
ATOM   1642 C  CG  . PRO   A 1 205 ? 36.184 0.704   7.736  1.00 19.45 ? 225 PRO   A CG  1 
ATOM   1643 C  CD  . PRO   A 1 205 ? 36.480 2.172   7.519  1.00 19.64 ? 225 PRO   A CD  1 
ATOM   1644 N  N   . GLU   A 1 206 ? 32.886 1.338   10.586 1.00 16.40 ? 226 GLU   A N   1 
ATOM   1645 C  CA  . GLU   A 1 206 ? 32.482 1.063   11.963 1.00 15.90 ? 226 GLU   A CA  1 
ATOM   1646 C  C   . GLU   A 1 206 ? 31.709 -0.257  11.999 1.00 15.57 ? 226 GLU   A C   1 
ATOM   1647 O  O   . GLU   A 1 206 ? 31.437 -0.853  10.948 1.00 15.43 ? 226 GLU   A O   1 
ATOM   1648 C  CB  . GLU   A 1 206 ? 31.710 2.249   12.555 1.00 15.90 ? 226 GLU   A CB  1 
ATOM   1649 C  CG  . GLU   A 1 206 ? 30.402 2.578   11.837 1.00 15.70 ? 226 GLU   A CG  1 
ATOM   1650 C  CD  . GLU   A 1 206 ? 29.723 3.867   12.288 1.00 16.14 ? 226 GLU   A CD  1 
ATOM   1651 O  OE1 . GLU   A 1 206 ? 30.169 4.489   13.295 1.00 16.39 ? 226 GLU   A OE1 1 
ATOM   1652 O  OE2 . GLU   A 1 206 ? 28.744 4.267   11.613 1.00 16.02 ? 226 GLU   A OE2 1 
ATOM   1653 N  N   . VAL   A 1 207 ? 31.355 -0.690  13.219 1.00 14.99 ? 227 VAL   A N   1 
ATOM   1654 C  CA  . VAL   A 1 207 ? 30.864 -2.038  13.474 1.00 14.83 ? 227 VAL   A CA  1 
ATOM   1655 C  C   . VAL   A 1 207 ? 29.417 -1.990  13.968 1.00 14.39 ? 227 VAL   A C   1 
ATOM   1656 O  O   . VAL   A 1 207 ? 29.094 -1.316  14.955 1.00 13.52 ? 227 VAL   A O   1 
ATOM   1657 C  CB  . VAL   A 1 207 ? 31.772 -2.788  14.469 1.00 15.03 ? 227 VAL   A CB  1 
ATOM   1658 C  CG1 . VAL   A 1 207 ? 31.246 -4.171  14.822 1.00 15.25 ? 227 VAL   A CG1 1 
ATOM   1659 C  CG2 . VAL   A 1 207 ? 33.191 -2.913  13.945 1.00 15.77 ? 227 VAL   A CG2 1 
ATOM   1660 N  N   . PHE   A 1 208 ? 28.565 -2.742  13.252 1.00 14.42 ? 228 PHE   A N   1 
ATOM   1661 C  CA  . PHE   A 1 208 ? 27.190 -3.000  13.651 1.00 14.16 ? 228 PHE   A CA  1 
ATOM   1662 C  C   . PHE   A 1 208 ? 27.034 -4.484  13.980 1.00 13.98 ? 228 PHE   A C   1 
ATOM   1663 O  O   . PHE   A 1 208 ? 27.711 -5.313  13.378 1.00 14.32 ? 228 PHE   A O   1 
ATOM   1664 C  CB  . PHE   A 1 208 ? 26.255 -2.613  12.499 1.00 14.45 ? 228 PHE   A CB  1 
ATOM   1665 C  CG  . PHE   A 1 208 ? 25.993 -1.126  12.306 1.00 14.70 ? 228 PHE   A CG  1 
ATOM   1666 C  CD1 . PHE   A 1 208 ? 27.002 -0.265  11.887 1.00 14.98 ? 228 PHE   A CD1 1 
ATOM   1667 C  CD2 . PHE   A 1 208 ? 24.717 -0.603  12.489 1.00 14.91 ? 228 PHE   A CD2 1 
ATOM   1668 C  CE1 . PHE   A 1 208 ? 26.748 1.083   11.683 1.00 15.08 ? 228 PHE   A CE1 1 
ATOM   1669 C  CE2 . PHE   A 1 208 ? 24.474 0.751   12.302 1.00 14.99 ? 228 PHE   A CE2 1 
ATOM   1670 C  CZ  . PHE   A 1 208 ? 25.489 1.590   11.899 1.00 15.03 ? 228 PHE   A CZ  1 
ATOM   1671 N  N   . THR   A 1 209 ? 26.129 -4.814  14.916 1.00 13.49 ? 229 THR   A N   1 
ATOM   1672 C  CA  . THR   A 1 209 ? 25.722 -6.193  15.136 1.00 13.57 ? 229 THR   A CA  1 
ATOM   1673 C  C   . THR   A 1 209 ? 24.867 -6.644  13.953 1.00 13.99 ? 229 THR   A C   1 
ATOM   1674 O  O   . THR   A 1 209 ? 23.994 -5.898  13.511 1.00 13.76 ? 229 THR   A O   1 
ATOM   1675 C  CB  . THR   A 1 209 ? 24.938 -6.340  16.442 1.00 13.29 ? 229 THR   A CB  1 
ATOM   1676 O  OG1 . THR   A 1 209 ? 25.690 -5.763  17.503 1.00 13.00 ? 229 THR   A OG1 1 
ATOM   1677 C  CG2 . THR   A 1 209 ? 24.647 -7.795  16.755 1.00 13.68 ? 229 THR   A CG2 1 
ATOM   1678 N  N   . ARG   A 1 210 ? 25.096 -7.879  13.483 1.00 14.80 ? 230 ARG   A N   1 
ATOM   1679 C  CA  . ARG   A 1 210 ? 24.342 -8.469  12.384 1.00 15.68 ? 230 ARG   A CA  1 
ATOM   1680 C  C   . ARG   A 1 210 ? 23.130 -9.206  12.962 1.00 16.27 ? 230 ARG   A C   1 
ATOM   1681 O  O   . ARG   A 1 210 ? 23.271 -10.260 13.573 1.00 16.67 ? 230 ARG   A O   1 
ATOM   1682 C  CB  . ARG   A 1 210 ? 25.271 -9.377  11.565 1.00 16.30 ? 230 ARG   A CB  1 
ATOM   1683 C  CG  . ARG   A 1 210 ? 24.702 -9.942  10.271 1.00 16.96 ? 230 ARG   A CG  1 
ATOM   1684 C  CD  . ARG   A 1 210 ? 25.661 -10.900 9.584  1.00 17.70 ? 230 ARG   A CD  1 
ATOM   1685 N  NE  . ARG   A 1 210 ? 26.837 -10.226 9.024  1.00 17.58 ? 230 ARG   A NE  1 
ATOM   1686 C  CZ  . ARG   A 1 210 ? 26.899 -9.577  7.860  1.00 17.79 ? 230 ARG   A CZ  1 
ATOM   1687 N  NH1 . ARG   A 1 210 ? 25.915 -9.660  6.973  1.00 18.09 ? 230 ARG   A NH1 1 
ATOM   1688 N  NH2 . ARG   A 1 210 ? 27.984 -8.877  7.569  1.00 17.69 ? 230 ARG   A NH2 1 
ATOM   1689 N  N   . VAL   A 1 211 ? 21.936 -8.625  12.782 1.00 16.68 ? 231 VAL   A N   1 
ATOM   1690 C  CA  . VAL   A 1 211 ? 20.713 -9.123  13.402 1.00 17.30 ? 231 VAL   A CA  1 
ATOM   1691 C  C   . VAL   A 1 211 ? 20.446 -10.565 12.957 1.00 18.52 ? 231 VAL   A C   1 
ATOM   1692 O  O   . VAL   A 1 211 ? 20.104 -11.413 13.782 1.00 18.85 ? 231 VAL   A O   1 
ATOM   1693 C  CB  . VAL   A 1 211 ? 19.502 -8.210  13.102 1.00 17.12 ? 231 VAL   A CB  1 
ATOM   1694 C  CG1 . VAL   A 1 211 ? 18.204 -8.808  13.622 1.00 17.66 ? 231 VAL   A CG1 1 
ATOM   1695 C  CG2 . VAL   A 1 211 ? 19.671 -6.814  13.689 1.00 16.41 ? 231 VAL   A CG2 1 
ATOM   1696 N  N   . SER   A 1 212 ? 20.601 -10.840 11.656 1.00 19.38 ? 232 SER   A N   1 
ATOM   1697 C  CA  . SER   A 1 212 ? 20.266 -12.138 11.072 1.00 20.84 ? 232 SER   A CA  1 
ATOM   1698 C  C   . SER   A 1 212 ? 20.912 -13.295 11.834 1.00 21.59 ? 232 SER   A C   1 
ATOM   1699 O  O   . SER   A 1 212 ? 20.378 -14.402 11.878 1.00 22.39 ? 232 SER   A O   1 
ATOM   1700 C  CB  . SER   A 1 212 ? 20.670 -12.199 9.612  1.00 21.49 ? 232 SER   A CB  1 
ATOM   1701 O  OG  . SER   A 1 212 ? 22.086 -12.126 9.465  1.00 21.22 ? 232 SER   A OG  1 
ATOM   1702 N  N   . SER   A 1 213 ? 22.084 -13.041 12.417 1.00 21.55 ? 233 SER   A N   1 
ATOM   1703 C  CA  . SER   A 1 213 ? 22.822 -14.067 13.129 1.00 22.07 ? 233 SER   A CA  1 
ATOM   1704 C  C   . SER   A 1 213 ? 22.159 -14.407 14.465 1.00 21.80 ? 233 SER   A C   1 
ATOM   1705 O  O   . SER   A 1 213 ? 22.372 -15.493 14.987 1.00 22.21 ? 233 SER   A O   1 
ATOM   1706 C  CB  . SER   A 1 213 ? 24.248 -13.628 13.320 1.00 22.17 ? 233 SER   A CB  1 
ATOM   1707 O  OG  . SER   A 1 213 ? 24.835 -13.321 12.062 1.00 22.61 ? 233 SER   A OG  1 
ATOM   1708 N  N   . PHE   A 1 214 ? 21.334 -13.500 15.012 1.00 21.31 ? 234 PHE   A N   1 
ATOM   1709 C  CA  . PHE   A 1 214 ? 20.797 -13.697 16.350 1.00 21.12 ? 234 PHE   A CA  1 
ATOM   1710 C  C   . PHE   A 1 214 ? 19.303 -14.018 16.324 1.00 21.53 ? 234 PHE   A C   1 
ATOM   1711 O  O   . PHE   A 1 214 ? 18.682 -14.055 17.384 1.00 21.52 ? 234 PHE   A O   1 
ATOM   1712 C  CB  . PHE   A 1 214 ? 21.127 -12.474 17.210 1.00 20.14 ? 234 PHE   A CB  1 
ATOM   1713 C  CG  . PHE   A 1 214 ? 22.629 -12.340 17.410 1.00 20.12 ? 234 PHE   A CG  1 
ATOM   1714 C  CD1 . PHE   A 1 214 ? 23.276 -13.020 18.439 1.00 20.39 ? 234 PHE   A CD1 1 
ATOM   1715 C  CD2 . PHE   A 1 214 ? 23.397 -11.599 16.518 1.00 19.73 ? 234 PHE   A CD2 1 
ATOM   1716 C  CE1 . PHE   A 1 214 ? 24.654 -12.933 18.587 1.00 20.47 ? 234 PHE   A CE1 1 
ATOM   1717 C  CE2 . PHE   A 1 214 ? 24.771 -11.517 16.666 1.00 19.84 ? 234 PHE   A CE2 1 
ATOM   1718 C  CZ  . PHE   A 1 214 ? 25.398 -12.182 17.703 1.00 20.44 ? 234 PHE   A CZ  1 
ATOM   1719 N  N   . LEU   A 1 215 ? 18.743 -14.306 15.140 1.00 22.06 ? 235 LEU   A N   1 
ATOM   1720 C  CA  . LEU   A 1 215 ? 17.296 -14.422 14.999 1.00 22.52 ? 235 LEU   A CA  1 
ATOM   1721 C  C   . LEU   A 1 215 ? 16.773 -15.543 15.897 1.00 23.10 ? 235 LEU   A C   1 
ATOM   1722 O  O   . LEU   A 1 215 ? 15.768 -15.362 16.584 1.00 22.96 ? 235 LEU   A O   1 
ATOM   1723 C  CB  . LEU   A 1 215 ? 16.877 -14.607 13.539 1.00 23.36 ? 235 LEU   A CB  1 
ATOM   1724 C  CG  . LEU   A 1 215 ? 16.796 -13.328 12.702 1.00 23.12 ? 235 LEU   A CG  1 
ATOM   1725 C  CD1 . LEU   A 1 215 ? 16.721 -13.657 11.221 0.50 23.83 ? 235 LEU   A CD1 1 
ATOM   1726 C  CD2 . LEU   A 1 215 ? 15.617 -12.450 13.113 1.00 22.91 ? 235 LEU   A CD2 1 
ATOM   1727 N  N   . PRO   A 1 216 ? 17.427 -16.728 15.938 1.00 23.78 ? 236 PRO   A N   1 
ATOM   1728 C  CA  . PRO   A 1 216 ? 17.026 -17.791 16.862 1.00 24.57 ? 236 PRO   A CA  1 
ATOM   1729 C  C   . PRO   A 1 216 ? 16.934 -17.353 18.324 1.00 23.79 ? 236 PRO   A C   1 
ATOM   1730 O  O   . PRO   A 1 216 ? 15.939 -17.630 18.990 1.00 24.10 ? 236 PRO   A O   1 
ATOM   1731 C  CB  . PRO   A 1 216 ? 18.109 -18.865 16.645 1.00 25.48 ? 236 PRO   A CB  1 
ATOM   1732 C  CG  . PRO   A 1 216 ? 18.550 -18.648 15.215 1.00 25.54 ? 236 PRO   A CG  1 
ATOM   1733 C  CD  . PRO   A 1 216 ? 18.554 -17.126 15.077 1.00 24.16 ? 236 PRO   A CD  1 
ATOM   1734 N  N   . TRP   A 1 217 ? 17.963 -16.649 18.815 1.00 22.68 ? 237 TRP   A N   1 
ATOM   1735 C  CA  . TRP   A 1 217 ? 17.953 -16.168 20.187 1.00 21.89 ? 237 TRP   A CA  1 
ATOM   1736 C  C   . TRP   A 1 217 ? 16.856 -15.116 20.379 1.00 21.60 ? 237 TRP   A C   1 
ATOM   1737 O  O   . TRP   A 1 217 ? 16.222 -15.068 21.432 1.00 21.51 ? 237 TRP   A O   1 
ATOM   1738 C  CB  . TRP   A 1 217 ? 19.331 -15.631 20.611 1.00 20.89 ? 237 TRP   A CB  1 
ATOM   1739 C  CG  . TRP   A 1 217 ? 19.294 -14.957 21.959 1.00 19.96 ? 237 TRP   A CG  1 
ATOM   1740 C  CD1 . TRP   A 1 217 ? 19.346 -15.555 23.185 1.00 20.36 ? 237 TRP   A CD1 1 
ATOM   1741 C  CD2 . TRP   A 1 217 ? 19.134 -13.543 22.215 1.00 18.74 ? 237 TRP   A CD2 1 
ATOM   1742 N  NE1 . TRP   A 1 217 ? 19.245 -14.617 24.180 1.00 19.57 ? 237 TRP   A NE1 1 
ATOM   1743 C  CE2 . TRP   A 1 217 ? 19.108 -13.377 23.617 1.00 18.51 ? 237 TRP   A CE2 1 
ATOM   1744 C  CE3 . TRP   A 1 217 ? 19.001 -12.413 21.403 1.00 17.74 ? 237 TRP   A CE3 1 
ATOM   1745 C  CZ2 . TRP   A 1 217 ? 18.966 -12.125 24.216 1.00 17.74 ? 237 TRP   A CZ2 1 
ATOM   1746 C  CZ3 . TRP   A 1 217 ? 18.844 -11.180 21.997 1.00 17.23 ? 237 TRP   A CZ3 1 
ATOM   1747 C  CH2 . TRP   A 1 217 ? 18.826 -11.038 23.386 1.00 17.01 ? 237 TRP   A CH2 1 
ATOM   1748 N  N   . ILE   A 1 218 ? 16.624 -14.279 19.360 1.00 21.67 ? 238 ILE   A N   1 
ATOM   1749 C  CA  . ILE   A 1 218 ? 15.600 -13.243 19.435 1.00 21.59 ? 238 ILE   A CA  1 
ATOM   1750 C  C   . ILE   A 1 218 ? 14.214 -13.888 19.536 1.00 23.34 ? 238 ILE   A C   1 
ATOM   1751 O  O   . ILE   A 1 218 ? 13.438 -13.539 20.427 1.00 22.67 ? 238 ILE   A O   1 
ATOM   1752 C  CB  . ILE   A 1 218 ? 15.687 -12.270 18.241 1.00 20.92 ? 238 ILE   A CB  1 
ATOM   1753 C  CG1 . ILE   A 1 218 ? 16.976 -11.440 18.274 1.00 19.98 ? 238 ILE   A CG1 1 
ATOM   1754 C  CG2 . ILE   A 1 218 ? 14.449 -11.369 18.184 1.00 20.74 ? 238 ILE   A CG2 1 
ATOM   1755 C  CD1 . ILE   A 1 218 ? 17.223 -10.617 17.021 1.00 19.58 ? 238 ILE   A CD1 1 
ATOM   1756 N  N   . ARG   A 1 219 ? 13.909 -14.802 18.603 1.00 25.09 ? 239 ARG   A N   1 
ATOM   1757 C  CA  . ARG   A 1 219 ? 12.615 -15.466 18.542 1.00 27.36 ? 239 ARG   A CA  1 
ATOM   1758 C  C   . ARG   A 1 219 ? 12.319 -16.224 19.830 1.00 27.76 ? 239 ARG   A C   1 
ATOM   1759 O  O   . ARG   A 1 219 ? 11.225 -16.110 20.372 1.00 27.68 ? 239 ARG   A O   1 
ATOM   1760 C  CB  . ARG   A 1 219 ? 12.541 -16.467 17.384 1.00 29.81 ? 239 ARG   A CB  1 
ATOM   1761 C  CG  . ARG   A 1 219 ? 12.533 -15.813 16.013 1.00 31.29 ? 239 ARG   A CG  1 
ATOM   1762 C  CD  . ARG   A 1 219 ? 13.092 -16.773 14.971 1.00 34.09 ? 239 ARG   A CD  1 
ATOM   1763 N  NE  . ARG   A 1 219 ? 13.063 -16.223 13.611 1.00 35.94 ? 239 ARG   A NE  1 
ATOM   1764 C  CZ  . ARG   A 1 219 ? 13.709 -16.742 12.569 1.00 37.96 ? 239 ARG   A CZ  1 
ATOM   1765 N  NH1 . ARG   A 1 219 ? 14.526 -17.774 12.732 1.00 39.28 ? 239 ARG   A NH1 1 
ATOM   1766 N  NH2 . ARG   A 1 219 ? 13.553 -16.207 11.371 1.00 38.47 ? 239 ARG   A NH2 1 
ATOM   1767 N  N   . THR   A 1 220 ? 13.295 -17.008 20.297 1.00 28.51 ? 240 THR   A N   1 
ATOM   1768 C  CA  . THR   A 1 220 ? 13.130 -17.818 21.496 1.00 29.62 ? 240 THR   A CA  1 
ATOM   1769 C  C   . THR   A 1 220 ? 12.812 -16.934 22.703 1.00 28.63 ? 240 THR   A C   1 
ATOM   1770 O  O   . THR   A 1 220 ? 11.933 -17.268 23.501 1.00 28.88 ? 240 THR   A O   1 
ATOM   1771 C  CB  . THR   A 1 220 ? 14.392 -18.657 21.709 1.00 30.55 ? 240 THR   A CB  1 
ATOM   1772 O  OG1 . THR   A 1 220 ? 14.477 -19.488 20.554 1.00 31.86 ? 240 THR   A OG1 1 
ATOM   1773 C  CG2 . THR   A 1 220 ? 14.319 -19.529 22.949 1.00 31.65 ? 240 THR   A CG2 1 
ATOM   1774 N  N   . THR   A 1 221 ? 13.529 -15.807 22.822 1.00 27.35 ? 241 THR   A N   1 
ATOM   1775 C  CA  . THR   A 1 221 ? 13.387 -14.890 23.946 1.00 26.60 ? 241 THR   A CA  1 
ATOM   1776 C  C   . THR   A 1 221 ? 11.997 -14.253 23.964 1.00 27.08 ? 241 THR   A C   1 
ATOM   1777 O  O   . THR   A 1 221 ? 11.341 -14.217 25.001 1.00 26.65 ? 241 THR   A O   1 
ATOM   1778 C  CB  . THR   A 1 221 ? 14.476 -13.820 23.864 1.00 25.05 ? 241 THR   A CB  1 
ATOM   1779 O  OG1 . THR   A 1 221 ? 15.726 -14.498 23.954 1.00 24.57 ? 241 THR   A OG1 1 
ATOM   1780 C  CG2 . THR   A 1 221 ? 14.365 -12.799 24.978 1.00 24.19 ? 241 THR   A CG2 1 
ATOM   1781 N  N   . MET   A 1 222 ? 11.565 -13.725 22.814 1.00 28.06 ? 242 MET   A N   1 
ATOM   1782 C  CA  . MET   A 1 222 ? 10.298 -13.015 22.722 1.00 29.40 ? 242 MET   A CA  1 
ATOM   1783 C  C   . MET   A 1 222 ? 9.125  -13.985 22.896 1.00 31.83 ? 242 MET   A C   1 
ATOM   1784 O  O   . MET   A 1 222 ? 8.078  -13.603 23.411 1.00 31.33 ? 242 MET   A O   1 
ATOM   1785 C  CB  . MET   A 1 222 ? 10.185 -12.272 21.384 1.00 29.32 ? 242 MET   A CB  1 
ATOM   1786 C  CG  . MET   A 1 222 ? 11.158 -11.109 21.244 1.00 28.54 ? 242 MET   A CG  1 
ATOM   1787 S  SD  . MET   A 1 222 ? 10.696 -9.972  19.920 1.00 28.88 ? 242 MET   A SD  1 
ATOM   1788 C  CE  . MET   A 1 222 ? 10.585 -11.031 18.474 1.00 30.28 ? 242 MET   A CE  1 
ATOM   1789 N  N   . ARG   A 1 223 ? 9.308  -15.241 22.482 1.00 34.20 ? 243 ARG   A N   1 
ATOM   1790 C  CA  . ARG   A 1 223 ? 8.254  -16.236 22.595 1.00 38.55 ? 243 ARG   A CA  1 
ATOM   1791 C  C   . ARG   A 1 223 ? 8.012  -16.595 24.060 1.00 38.41 ? 243 ARG   A C   1 
ATOM   1792 O  O   . ARG   A 1 223 ? 6.865  -16.768 24.463 1.00 39.41 ? 243 ARG   A O   1 
ATOM   1793 C  CB  . ARG   A 1 223 ? 8.565  -17.481 21.754 1.00 41.96 ? 243 ARG   A CB  1 
ATOM   1794 C  CG  . ARG   A 1 223 ? 7.550  -18.610 21.887 1.00 46.23 ? 243 ARG   A CG  1 
ATOM   1795 C  CD  . ARG   A 1 223 ? 7.697  -19.701 20.828 1.00 50.68 ? 243 ARG   A CD  1 
ATOM   1796 N  NE  . ARG   A 1 223 ? 7.056  -19.356 19.551 1.00 54.59 ? 243 ARG   A NE  1 
ATOM   1797 C  CZ  . ARG   A 1 223 ? 7.626  -19.391 18.345 1.00 56.99 ? 243 ARG   A CZ  1 
ATOM   1798 N  NH1 . ARG   A 1 223 ? 8.887  -19.770 18.213 1.00 57.92 ? 243 ARG   A NH1 1 
ATOM   1799 N  NH2 . ARG   A 1 223 ? 6.924  -19.063 17.273 1.00 57.12 ? 243 ARG   A NH2 1 
ATOM   1800 N  N   . SER   A 1 224 ? 9.088  -16.715 24.846 1.00 37.66 ? 244 SER   A N   1 
ATOM   1801 C  CA  . SER   A 1 224 ? 8.987  -17.212 26.211 1.00 39.04 ? 244 SER   A CA  1 
ATOM   1802 C  C   . SER   A 1 224 ? 8.329  -16.162 27.123 1.00 38.66 ? 244 SER   A C   1 
ATOM   1803 O  O   . SER   A 1 224 ? 8.731  -14.975 27.023 1.00 38.97 ? 244 SER   A O   1 
ATOM   1804 C  CB  . SER   A 1 224 ? 10.340 -17.632 26.740 1.00 39.12 ? 244 SER   A CB  1 
ATOM   1805 O  OG  . SER   A 1 224 ? 11.112 -16.510 27.149 1.00 38.40 ? 244 SER   A OG  1 
HETATM 1806 ZN ZN  . ZN    B 2 .   ? 5.704  15.910  16.265 1.00 28.06 ? 301 ZN    A ZN  1 
HETATM 1807 N  N1  . A1AO6 C 3 .   ? 29.341 3.217   22.743 1.00 16.71 ? 302 A1AO6 A N1  1 
HETATM 1808 C  C4  . A1AO6 C 3 .   ? 29.822 2.139   23.475 1.00 15.90 ? 302 A1AO6 A C4  1 
HETATM 1809 C  C5  . A1AO6 C 3 .   ? 29.591 2.395   24.835 1.00 16.24 ? 302 A1AO6 A C5  1 
HETATM 1810 C  C6  . A1AO6 C 3 .   ? 29.419 3.338   21.280 1.00 16.79 ? 302 A1AO6 A C6  1 
HETATM 1811 C  C7  . A1AO6 C 3 .   ? 28.502 4.341   26.197 1.00 17.56 ? 302 A1AO6 A C7  1 
HETATM 1812 C  C8  . A1AO6 C 3 .   ? 27.111 3.210   27.848 1.00 19.92 ? 302 A1AO6 A C8  1 
HETATM 1813 C  C17 . A1AO6 C 3 .   ? 32.198 5.183   17.548 1.00 17.06 ? 302 A1AO6 A C17 1 
HETATM 1814 C  C21 . A1AO6 C 3 .   ? 31.182 4.948   16.667 1.00 17.01 ? 302 A1AO6 A C21 1 
HETATM 1815 C  C24 . A1AO6 C 3 .   ? 29.991 1.452   25.779 1.00 15.44 ? 302 A1AO6 A C24 1 
HETATM 1816 C  C26 . A1AO6 C 3 .   ? 26.076 4.040   25.768 1.00 17.98 ? 302 A1AO6 A C26 1 
HETATM 1817 C  C28 . A1AO6 C 3 .   ? 33.094 5.113   19.859 1.00 16.98 ? 302 A1AO6 A C28 1 
HETATM 1818 C  C2  . A1AO6 C 3 .   ? 28.959 3.677   24.919 1.00 16.93 ? 302 A1AO6 A C2  1 
HETATM 1819 C  C3  . A1AO6 C 3 .   ? 28.836 4.146   23.638 1.00 16.89 ? 302 A1AO6 A C3  1 
HETATM 1820 C  C9  . A1AO6 C 3 .   ? 28.234 5.434   23.214 1.00 17.49 ? 302 A1AO6 A C9  1 
HETATM 1821 N  N10 . A1AO6 C 3 .   ? 27.215 3.834   26.653 1.00 18.05 ? 302 A1AO6 A N10 1 
HETATM 1822 C  C11 . A1AO6 C 3 .   ? 30.699 3.965   20.771 1.00 16.57 ? 302 A1AO6 A C11 1 
HETATM 1823 C  C12 . A1AO6 C 3 .   ? 30.843 4.277   19.377 1.00 17.27 ? 302 A1AO6 A C12 1 
HETATM 1824 O  O13 . A1AO6 C 3 .   ? 28.038 3.058   28.610 1.00 20.42 ? 302 A1AO6 A O13 1 
HETATM 1825 C  C14 . A1AO6 C 3 .   ? 29.804 4.050   18.432 1.00 17.14 ? 302 A1AO6 A C14 1 
HETATM 1826 O  O15 . A1AO6 C 3 .   ? 28.499 6.499   23.788 1.00 16.95 ? 302 A1AO6 A O15 1 
HETATM 1827 C  C16 . A1AO6 C 3 .   ? 32.060 4.867   18.923 1.00 16.63 ? 302 A1AO6 A C16 1 
HETATM 1828 C  C18 . A1AO6 C 3 .   ? 30.011 4.392   17.133 1.00 17.91 ? 302 A1AO6 A C18 1 
HETATM 1829 O  O19 . A1AO6 C 3 .   ? 25.857 2.771   28.071 1.00 19.86 ? 302 A1AO6 A O19 1 
HETATM 1830 O  O20 . A1AO6 C 3 .   ? 27.410 5.311   22.215 1.00 16.38 ? 302 A1AO6 A O20 1 
HETATM 1831 F  F22 . A1AO6 C 3 .   ? 29.012 4.151   16.239 1.00 17.60 ? 302 A1AO6 A F22 1 
HETATM 1832 C  C23 . A1AO6 C 3 .   ? 30.430 0.966   23.045 1.00 16.23 ? 302 A1AO6 A C23 1 
HETATM 1833 C  C25 . A1AO6 C 3 .   ? 31.747 4.231   21.627 1.00 17.02 ? 302 A1AO6 A C25 1 
HETATM 1834 C  C27 . A1AO6 C 3 .   ? 32.938 4.781   21.175 1.00 16.55 ? 302 A1AO6 A C27 1 
HETATM 1835 C  C29 . A1AO6 C 3 .   ? 25.644 2.109   29.346 1.00 18.82 ? 302 A1AO6 A C29 1 
HETATM 1836 C  C30 . A1AO6 C 3 .   ? 30.602 0.281   25.361 1.00 15.68 ? 302 A1AO6 A C30 1 
HETATM 1837 C  C31 . A1AO6 C 3 .   ? 30.817 0.037   24.003 1.00 16.01 ? 302 A1AO6 A C31 1 
HETATM 1838 S  S   . SO4   D 4 .   ? 40.095 -5.555  -0.018 0.50 21.03 ? 303 SO4   A S   1 
HETATM 1839 O  O1  . SO4   D 4 .   ? 41.103 -6.404  0.562  0.50 21.18 ? 303 SO4   A O1  1 
HETATM 1840 O  O2  . SO4   D 4 .   ? 39.331 -6.320  -0.968 0.50 21.20 ? 303 SO4   A O2  1 
HETATM 1841 O  O3  . SO4   D 4 .   ? 39.219 -5.062  1.009  0.50 20.73 ? 303 SO4   A O3  1 
HETATM 1842 O  O4  . SO4   D 4 .   ? 40.723 -4.449  -0.687 0.50 20.17 ? 303 SO4   A O4  1 
HETATM 1843 S  S   . SO4   E 4 .   ? 2.052  15.517  27.389 0.80 36.86 ? 304 SO4   A S   1 
HETATM 1844 O  O1  . SO4   E 4 .   ? 1.708  14.229  26.836 0.80 34.42 ? 304 SO4   A O1  1 
HETATM 1845 O  O2  . SO4   E 4 .   ? 3.432  15.491  27.819 0.80 34.91 ? 304 SO4   A O2  1 
HETATM 1846 O  O3  . SO4   E 4 .   ? 1.858  16.541  26.394 0.80 38.79 ? 304 SO4   A O3  1 
HETATM 1847 O  O4  . SO4   E 4 .   ? 1.203  15.796  28.510 0.80 35.94 ? 304 SO4   A O4  1 
HETATM 1848 O  O   . HOH   F 5 .   ? 29.108 -10.249 17.772 1.00 22.65 ? 401 HOH   A O   1 
HETATM 1849 O  O   . HOH   F 5 .   ? 31.499 -8.245  7.363  1.00 32.49 ? 402 HOH   A O   1 
HETATM 1850 O  O   . HOH   F 5 .   ? 5.351  15.832  18.509 1.00 21.04 ? 403 HOH   A O   1 
HETATM 1851 O  O   . HOH   F 5 .   ? 9.377  17.476  18.530 1.00 32.13 ? 404 HOH   A O   1 
HETATM 1852 O  O   . HOH   F 5 .   ? -3.595 9.162   12.883 1.00 37.48 ? 405 HOH   A O   1 
HETATM 1853 O  O   . HOH   F 5 .   ? 18.061 5.035   38.549 1.00 35.70 ? 406 HOH   A O   1 
HETATM 1854 O  O   . HOH   F 5 .   ? 20.039 -12.350 6.244  1.00 26.42 ? 407 HOH   A O   1 
HETATM 1855 O  O   . HOH   F 5 .   ? 30.984 -5.028  33.144 1.00 34.42 ? 408 HOH   A O   1 
HETATM 1856 O  O   . HOH   F 5 .   ? 2.813  11.943  12.758 1.00 31.27 ? 409 HOH   A O   1 
HETATM 1857 O  O   . HOH   F 5 .   ? 40.436 6.865   17.403 1.00 28.08 ? 410 HOH   A O   1 
HETATM 1858 O  O   . HOH   F 5 .   ? 23.206 -14.306 9.825  1.00 25.13 ? 411 HOH   A O   1 
HETATM 1859 O  O   . HOH   F 5 .   ? 28.955 -12.423 7.033  1.00 34.44 ? 412 HOH   A O   1 
HETATM 1860 O  O   . HOH   F 5 .   ? 29.363 -3.734  28.686 1.00 18.02 ? 413 HOH   A O   1 
HETATM 1861 O  O   . HOH   F 5 .   ? 18.879 17.624  14.816 1.00 28.46 ? 414 HOH   A O   1 
HETATM 1862 O  O   . HOH   F 5 .   ? -0.246 0.521   27.250 1.00 41.61 ? 415 HOH   A O   1 
HETATM 1863 O  O   . HOH   F 5 .   ? 28.250 -0.647  28.842 1.00 22.09 ? 416 HOH   A O   1 
HETATM 1864 O  O   . HOH   F 5 .   ? 1.452  3.730   25.965 1.00 34.05 ? 417 HOH   A O   1 
HETATM 1865 O  O   . HOH   F 5 .   ? 4.501  8.432   11.190 1.00 31.06 ? 418 HOH   A O   1 
HETATM 1866 O  O   . HOH   F 5 .   ? 13.505 -9.273  4.577  1.00 36.56 ? 419 HOH   A O   1 
HETATM 1867 O  O   . HOH   F 5 .   ? 11.313 20.635  17.745 1.00 37.28 ? 420 HOH   A O   1 
HETATM 1868 O  O   . HOH   F 5 .   ? 28.625 6.408   1.467  1.00 36.81 ? 421 HOH   A O   1 
HETATM 1869 O  O   . HOH   F 5 .   ? 21.300 -8.790  9.544  1.00 19.88 ? 422 HOH   A O   1 
HETATM 1870 O  O   . HOH   F 5 .   ? 11.730 -9.332  6.706  1.00 29.70 ? 423 HOH   A O   1 
HETATM 1871 O  O   . HOH   F 5 .   ? 39.317 -11.197 20.231 1.00 27.14 ? 424 HOH   A O   1 
HETATM 1872 O  O   . HOH   F 5 .   ? 15.019 21.729  22.329 1.00 36.20 ? 425 HOH   A O   1 
HETATM 1873 O  O   . HOH   F 5 .   ? 39.228 4.487   8.455  1.00 20.07 ? 426 HOH   A O   1 
HETATM 1874 O  O   . HOH   F 5 .   ? 24.741 5.561   22.798 1.00 37.33 ? 427 HOH   A O   1 
HETATM 1875 O  O   . HOH   F 5 .   ? 12.847 -12.851 10.717 1.00 23.87 ? 428 HOH   A O   1 
HETATM 1876 O  O   . HOH   F 5 .   ? 29.804 -5.665  18.306 1.00 19.25 ? 429 HOH   A O   1 
HETATM 1877 O  O   . HOH   F 5 .   ? 33.707 -0.878  0.269  1.00 20.00 ? 430 HOH   A O   1 
HETATM 1878 O  O   . HOH   F 5 .   ? 16.611 -10.204 32.755 1.00 35.60 ? 431 HOH   A O   1 
HETATM 1879 O  O   . HOH   F 5 .   ? 39.515 -9.242  33.233 1.00 31.33 ? 432 HOH   A O   1 
HETATM 1880 O  O   . HOH   F 5 .   ? 26.313 7.528   1.914  1.00 34.21 ? 433 HOH   A O   1 
HETATM 1881 O  O   . HOH   F 5 .   ? 13.379 11.056  7.548  1.00 17.06 ? 434 HOH   A O   1 
HETATM 1882 O  O   . HOH   F 5 .   ? 36.600 -5.169  20.251 1.00 18.05 ? 435 HOH   A O   1 
HETATM 1883 O  O   . HOH   F 5 .   ? 7.267  0.955   10.945 1.00 32.02 ? 436 HOH   A O   1 
HETATM 1884 O  O   . HOH   F 5 .   ? 20.352 -13.256 29.222 1.00 29.01 ? 437 HOH   A O   1 
HETATM 1885 O  O   . HOH   F 5 .   ? 1.077  14.656  30.897 1.00 21.44 ? 438 HOH   A O   1 
HETATM 1886 O  O   . HOH   F 5 .   ? 37.608 13.131  14.307 1.00 40.67 ? 439 HOH   A O   1 
HETATM 1887 O  O   . HOH   F 5 .   ? 42.524 -8.537  -0.111 1.00 19.19 ? 440 HOH   A O   1 
HETATM 1888 O  O   . HOH   F 5 .   ? 13.508 7.995   27.656 1.00 14.39 ? 441 HOH   A O   1 
HETATM 1889 O  O   . HOH   F 5 .   ? 1.721  8.065   20.741 1.00 16.94 ? 442 HOH   A O   1 
HETATM 1890 O  O   . HOH   F 5 .   ? 23.350 14.057  21.228 1.00 18.09 ? 443 HOH   A O   1 
HETATM 1891 O  O   . HOH   F 5 .   ? 38.905 -4.411  25.547 1.00 26.38 ? 444 HOH   A O   1 
HETATM 1892 O  O   . HOH   F 5 .   ? 31.705 -3.653  25.521 1.00 30.16 ? 445 HOH   A O   1 
HETATM 1893 O  O   . HOH   F 5 .   ? 28.190 -7.838  4.812  1.00 14.17 ? 446 HOH   A O   1 
HETATM 1894 O  O   . HOH   F 5 .   ? 25.226 -11.378 3.917  1.00 38.21 ? 447 HOH   A O   1 
HETATM 1895 O  O   . HOH   F 5 .   ? 26.469 10.057  34.792 1.00 32.03 ? 448 HOH   A O   1 
HETATM 1896 O  O   . HOH   F 5 .   ? 9.712  -7.055  14.003 1.00 25.60 ? 449 HOH   A O   1 
HETATM 1897 O  O   . HOH   F 5 .   ? 43.448 -7.527  4.133  1.00 18.69 ? 450 HOH   A O   1 
HETATM 1898 O  O   . HOH   F 5 .   ? 24.538 4.420   32.648 1.00 20.84 ? 451 HOH   A O   1 
HETATM 1899 O  O   . HOH   F 5 .   ? 33.048 9.913   25.779 1.00 44.15 ? 452 HOH   A O   1 
HETATM 1900 O  O   . HOH   F 5 .   ? 4.191  0.838   32.389 1.00 29.70 ? 453 HOH   A O   1 
HETATM 1901 O  O   . HOH   F 5 .   ? 16.014 -6.608  3.147  1.00 21.23 ? 454 HOH   A O   1 
HETATM 1902 O  O   . HOH   F 5 .   ? 24.354 14.824  11.444 1.00 14.13 ? 455 HOH   A O   1 
HETATM 1903 O  O   . HOH   F 5 .   ? 19.140 19.974  18.450 1.00 45.50 ? 456 HOH   A O   1 
HETATM 1904 O  O   . HOH   F 5 .   ? 8.953  6.222   17.804 1.00 12.11 ? 457 HOH   A O   1 
HETATM 1905 O  O   . HOH   F 5 .   ? 35.257 2.112   20.484 1.00 34.60 ? 458 HOH   A O   1 
HETATM 1906 O  O   . HOH   F 5 .   ? 23.949 13.289  4.731  1.00 38.14 ? 459 HOH   A O   1 
HETATM 1907 O  O   . HOH   F 5 .   ? 18.383 9.115   4.893  1.00 30.27 ? 460 HOH   A O   1 
HETATM 1908 O  O   . HOH   F 5 .   ? 3.226  4.477   10.804 1.00 36.61 ? 461 HOH   A O   1 
HETATM 1909 O  O   . HOH   F 5 .   ? 13.764 -0.197  36.291 1.00 22.72 ? 462 HOH   A O   1 
HETATM 1910 O  O   . HOH   F 5 .   ? 35.129 3.769   13.111 1.00 21.32 ? 463 HOH   A O   1 
HETATM 1911 O  O   . HOH   F 5 .   ? 23.493 -10.878 6.980  1.00 20.14 ? 464 HOH   A O   1 
HETATM 1912 O  O   . HOH   F 5 .   ? 27.827 16.403  11.515 1.00 18.16 ? 465 HOH   A O   1 
HETATM 1913 O  O   . HOH   F 5 .   ? 2.008  17.826  21.925 1.00 30.59 ? 466 HOH   A O   1 
HETATM 1914 O  O   . HOH   F 5 .   ? 26.310 -4.455  29.460 1.00 18.30 ? 467 HOH   A O   1 
HETATM 1915 O  O   . HOH   F 5 .   ? 33.348 10.926  10.592 1.00 19.99 ? 468 HOH   A O   1 
HETATM 1916 O  O   . HOH   F 5 .   ? 8.063  -12.345 27.161 1.00 30.84 ? 469 HOH   A O   1 
HETATM 1917 O  O   . HOH   F 5 .   ? 24.920 1.373   32.637 1.00 23.91 ? 470 HOH   A O   1 
HETATM 1918 O  O   . HOH   F 5 .   ? 3.555  12.314  26.267 1.00 34.94 ? 471 HOH   A O   1 
HETATM 1919 O  O   . HOH   F 5 .   ? 14.362 -0.704  33.987 1.00 14.37 ? 472 HOH   A O   1 
HETATM 1920 O  O   . HOH   F 5 .   ? 35.370 -2.851  26.002 1.00 34.07 ? 473 HOH   A O   1 
HETATM 1921 O  O   . HOH   F 5 .   ? 31.624 -14.349 24.681 1.00 39.06 ? 474 HOH   A O   1 
HETATM 1922 O  O   . HOH   F 5 .   ? 29.488 6.618   39.322 1.00 25.90 ? 475 HOH   A O   1 
HETATM 1923 O  O   . HOH   F 5 .   ? 9.408  -2.945  8.650  1.00 28.01 ? 476 HOH   A O   1 
HETATM 1924 O  O   . HOH   F 5 .   ? 7.334  9.012   15.933 1.00 13.72 ? 477 HOH   A O   1 
HETATM 1925 O  O   . HOH   F 5 .   ? 16.584 5.018   33.515 1.00 38.87 ? 478 HOH   A O   1 
HETATM 1926 O  O   . HOH   F 5 .   ? 27.371 14.889  4.753  1.00 41.98 ? 479 HOH   A O   1 
HETATM 1927 O  O   . HOH   F 5 .   ? 40.493 -8.931  12.470 1.00 22.92 ? 480 HOH   A O   1 
HETATM 1928 O  O   . HOH   F 5 .   ? 10.096 -13.116 28.529 1.00 44.16 ? 481 HOH   A O   1 
HETATM 1929 O  O   . HOH   F 5 .   ? 27.629 -10.997 29.596 1.00 43.15 ? 482 HOH   A O   1 
HETATM 1930 O  O   . HOH   F 5 .   ? 30.818 6.960   5.644  1.00 14.42 ? 483 HOH   A O   1 
HETATM 1931 O  O   . HOH   F 5 .   ? 39.527 8.243   5.832  1.00 42.75 ? 484 HOH   A O   1 
HETATM 1932 O  O   . HOH   F 5 .   ? 14.389 -17.773 8.347  1.00 43.33 ? 485 HOH   A O   1 
HETATM 1933 O  O   . HOH   F 5 .   ? 20.120 7.615   19.474 1.00 10.85 ? 486 HOH   A O   1 
HETATM 1934 O  O   . HOH   F 5 .   ? 36.635 3.412   1.204  1.00 27.60 ? 487 HOH   A O   1 
HETATM 1935 O  O   . HOH   F 5 .   ? 33.246 15.103  13.541 1.00 35.58 ? 488 HOH   A O   1 
HETATM 1936 O  O   . HOH   F 5 .   ? 34.120 -7.135  18.181 1.00 12.68 ? 489 HOH   A O   1 
HETATM 1937 O  O   . HOH   F 5 .   ? 29.113 5.075   3.637  1.00 14.10 ? 490 HOH   A O   1 
HETATM 1938 O  O   . HOH   F 5 .   ? 29.901 -9.769  4.017  1.00 24.45 ? 491 HOH   A O   1 
HETATM 1939 O  O   . HOH   F 5 .   ? 10.450 8.040   29.690 1.00 35.52 ? 492 HOH   A O   1 
HETATM 1940 O  O   . HOH   F 5 .   ? 30.088 -6.014  5.906  1.00 16.76 ? 493 HOH   A O   1 
HETATM 1941 O  O   . HOH   F 5 .   ? 8.974  -15.302 18.919 1.00 23.43 ? 494 HOH   A O   1 
HETATM 1942 O  O   . HOH   F 5 .   ? 2.638  -10.357 20.809 1.00 44.69 ? 495 HOH   A O   1 
HETATM 1943 O  O   . HOH   F 5 .   ? 20.318 13.261  24.348 1.00 29.75 ? 496 HOH   A O   1 
HETATM 1944 O  O   . HOH   F 5 .   ? 22.197 12.485  15.815 1.00 17.87 ? 497 HOH   A O   1 
HETATM 1945 O  O   . HOH   F 5 .   ? 25.037 -11.373 29.294 1.00 17.74 ? 498 HOH   A O   1 
HETATM 1946 O  O   . HOH   F 5 .   ? 34.853 -12.536 21.768 1.00 31.62 ? 499 HOH   A O   1 
HETATM 1947 O  O   . HOH   F 5 .   ? 40.982 -0.664  3.221  1.00 33.76 ? 500 HOH   A O   1 
HETATM 1948 O  O   . HOH   F 5 .   ? -3.090 5.376   11.465 1.00 44.87 ? 501 HOH   A O   1 
HETATM 1949 O  O   . HOH   F 5 .   ? 5.923  -9.260  27.387 1.00 36.14 ? 502 HOH   A O   1 
HETATM 1950 O  O   . HOH   F 5 .   ? 10.772 11.644  14.768 1.00 22.42 ? 503 HOH   A O   1 
HETATM 1951 O  O   . HOH   F 5 .   ? 31.102 -13.083 28.045 1.00 36.65 ? 504 HOH   A O   1 
HETATM 1952 O  O   . HOH   F 5 .   ? 17.929 1.067   1.931  1.00 23.73 ? 505 HOH   A O   1 
HETATM 1953 O  O   . HOH   F 5 .   ? 20.566 9.444   30.685 1.00 40.65 ? 506 HOH   A O   1 
HETATM 1954 O  O   . HOH   F 5 .   ? 39.163 -11.326 13.949 1.00 36.40 ? 507 HOH   A O   1 
HETATM 1955 O  O   . HOH   F 5 .   ? 11.332 4.162   8.019  1.00 35.20 ? 508 HOH   A O   1 
HETATM 1956 O  O   . HOH   F 5 .   ? 39.630 -0.023  6.477  1.00 25.58 ? 509 HOH   A O   1 
HETATM 1957 O  O   . HOH   F 5 .   ? 31.482 -9.190  29.655 1.00 26.77 ? 510 HOH   A O   1 
HETATM 1958 O  O   . HOH   F 5 .   ? 20.342 5.427   17.489 1.00 11.25 ? 511 HOH   A O   1 
HETATM 1959 O  O   . HOH   F 5 .   ? 10.524 9.249   13.664 1.00 15.18 ? 512 HOH   A O   1 
HETATM 1960 O  O   . HOH   F 5 .   ? 30.607 -16.059 21.429 1.00 42.62 ? 513 HOH   A O   1 
HETATM 1961 O  O   . HOH   F 5 .   ? 19.114 2.555   38.414 1.00 34.75 ? 514 HOH   A O   1 
HETATM 1962 O  O   . HOH   F 5 .   ? 25.755 8.135   27.082 1.00 16.11 ? 515 HOH   A O   1 
HETATM 1963 O  O   . HOH   F 5 .   ? 3.047  19.021  25.498 1.00 33.21 ? 516 HOH   A O   1 
HETATM 1964 O  O   . HOH   F 5 .   ? 19.774 15.716  23.543 1.00 41.44 ? 517 HOH   A O   1 
HETATM 1965 O  O   . HOH   F 5 .   ? 0.439  -4.354  28.283 1.00 29.13 ? 518 HOH   A O   1 
HETATM 1966 O  O   . HOH   F 5 .   ? 25.483 17.464  8.609  1.00 35.82 ? 519 HOH   A O   1 
HETATM 1967 O  O   . HOH   F 5 .   ? 28.156 1.350   14.301 1.00 30.64 ? 520 HOH   A O   1 
HETATM 1968 O  O   . HOH   F 5 .   ? 20.637 8.698   22.740 1.00 32.76 ? 521 HOH   A O   1 
HETATM 1969 O  O   . HOH   F 5 .   ? 31.477 -2.118  -0.409 1.00 29.05 ? 522 HOH   A O   1 
HETATM 1970 O  O   . HOH   F 5 .   ? 10.070 -9.163  11.536 1.00 32.09 ? 523 HOH   A O   1 
HETATM 1971 O  O   . HOH   F 5 .   ? 10.967 7.894   20.059 1.00 17.99 ? 524 HOH   A O   1 
HETATM 1972 O  O   . HOH   F 5 .   ? 29.869 8.244   37.173 1.00 37.78 ? 525 HOH   A O   1 
HETATM 1973 O  O   . HOH   F 5 .   ? 14.464 -10.081 0.963  1.00 43.22 ? 526 HOH   A O   1 
HETATM 1974 O  O   . HOH   F 5 .   ? 26.609 8.488   24.790 1.00 20.96 ? 527 HOH   A O   1 
HETATM 1975 O  O   . HOH   F 5 .   ? 1.363  17.042  18.581 1.00 43.30 ? 528 HOH   A O   1 
HETATM 1976 O  O   . HOH   F 5 .   ? 36.139 2.501   3.781  1.00 22.35 ? 529 HOH   A O   1 
HETATM 1977 O  O   . HOH   F 5 .   ? 6.411  -13.329 26.321 1.00 24.33 ? 530 HOH   A O   1 
HETATM 1978 O  O   . HOH   F 5 .   ? 13.429 17.485  8.983  1.00 33.11 ? 531 HOH   A O   1 
HETATM 1979 O  O   . HOH   F 5 .   ? 16.253 -7.891  33.550 1.00 18.09 ? 532 HOH   A O   1 
HETATM 1980 O  O   . HOH   F 5 .   ? 18.952 -15.313 27.038 1.00 24.16 ? 533 HOH   A O   1 
HETATM 1981 O  O   . HOH   F 5 .   ? 27.518 7.228   29.033 1.00 33.18 ? 534 HOH   A O   1 
HETATM 1982 O  O   . HOH   F 5 .   ? 12.497 14.934  3.455  1.00 36.97 ? 535 HOH   A O   1 
HETATM 1983 O  O   . HOH   F 5 .   ? 36.308 -8.874  2.367  1.00 11.33 ? 536 HOH   A O   1 
HETATM 1984 O  O   . HOH   F 5 .   ? 21.005 -9.792  6.871  1.00 25.23 ? 537 HOH   A O   1 
HETATM 1985 O  O   . HOH   F 5 .   ? 22.465 -11.384 0.123  1.00 32.78 ? 538 HOH   A O   1 
HETATM 1986 O  O   . HOH   F 5 .   ? 6.500  -15.118 19.878 1.00 33.15 ? 539 HOH   A O   1 
HETATM 1987 O  O   . HOH   F 5 .   ? 26.285 -9.350  34.974 1.00 32.99 ? 540 HOH   A O   1 
HETATM 1988 O  O   . HOH   F 5 .   ? 23.137 10.823  3.887  1.00 17.47 ? 541 HOH   A O   1 
HETATM 1989 O  O   . HOH   F 5 .   ? 26.490 -1.896  30.626 1.00 16.93 ? 542 HOH   A O   1 
HETATM 1990 O  O   . HOH   F 5 .   ? 9.951  8.407   16.596 1.00 18.68 ? 543 HOH   A O   1 
HETATM 1991 O  O   . HOH   F 5 .   ? 42.029 -0.890  5.847  1.00 31.18 ? 544 HOH   A O   1 
HETATM 1992 O  O   . HOH   F 5 .   ? 27.019 11.023  23.855 1.00 32.10 ? 545 HOH   A O   1 
HETATM 1993 O  O   . HOH   F 5 .   ? 15.832 1.617   4.270  1.00 25.77 ? 546 HOH   A O   1 
HETATM 1994 O  O   . HOH   F 5 .   ? 3.635  8.094   28.583 1.00 17.54 ? 547 HOH   A O   1 
HETATM 1995 O  O   . HOH   F 5 .   ? 26.753 -16.097 19.175 1.00 30.60 ? 548 HOH   A O   1 
HETATM 1996 O  O   . HOH   F 5 .   ? 15.958 10.151  37.309 1.00 44.88 ? 549 HOH   A O   1 
HETATM 1997 O  O   . HOH   F 5 .   ? 14.017 -19.687 17.565 1.00 46.06 ? 550 HOH   A O   1 
HETATM 1998 O  O   . HOH   F 5 .   ? 22.568 -12.185 -2.513 1.00 35.90 ? 551 HOH   A O   1 
HETATM 1999 O  O   . HOH   F 5 .   ? 39.057 4.549   11.083 1.00 46.74 ? 552 HOH   A O   1 
HETATM 2000 O  O   . HOH   F 5 .   ? 24.716 7.761   -2.619 1.00 39.11 ? 553 HOH   A O   1 
HETATM 2001 O  O   . HOH   F 5 .   ? 18.712 19.030  8.397  1.00 22.98 ? 554 HOH   A O   1 
HETATM 2002 O  O   . HOH   F 5 .   ? 37.902 -4.958  17.607 1.00 13.48 ? 555 HOH   A O   1 
HETATM 2003 O  O   . HOH   F 5 .   ? 6.226  14.191  26.820 1.00 22.20 ? 556 HOH   A O   1 
HETATM 2004 O  O   . HOH   F 5 .   ? 19.013 10.454  28.813 1.00 41.69 ? 557 HOH   A O   1 
HETATM 2005 O  O   . HOH   F 5 .   ? 33.364 -8.841  1.824  1.00 20.66 ? 558 HOH   A O   1 
HETATM 2006 O  O   . HOH   F 5 .   ? 40.669 2.204   7.181  1.00 23.67 ? 559 HOH   A O   1 
HETATM 2007 O  O   . HOH   F 5 .   ? 19.813 21.999  20.458 1.00 43.92 ? 560 HOH   A O   1 
HETATM 2008 O  O   . HOH   F 5 .   ? 31.672 2.390   -0.192 1.00 26.04 ? 561 HOH   A O   1 
HETATM 2009 O  O   . HOH   F 5 .   ? 43.875 -7.264  12.464 1.00 41.89 ? 562 HOH   A O   1 
HETATM 2010 O  O   . HOH   F 5 .   ? -0.049 11.886  25.553 1.00 26.63 ? 563 HOH   A O   1 
HETATM 2011 O  O   . HOH   F 5 .   ? 28.118 -7.841  17.988 1.00 18.08 ? 564 HOH   A O   1 
HETATM 2012 O  O   . HOH   F 5 .   ? 14.830 3.616   5.498  1.00 39.57 ? 565 HOH   A O   1 
HETATM 2013 O  O   . HOH   F 5 .   ? 34.630 12.683  12.591 1.00 38.59 ? 566 HOH   A O   1 
HETATM 2014 O  O   . HOH   F 5 .   ? 29.408 -9.081  -3.373 1.00 23.18 ? 567 HOH   A O   1 
HETATM 2015 O  O   . HOH   F 5 .   ? 6.108  2.649   32.692 1.00 25.14 ? 568 HOH   A O   1 
HETATM 2016 O  O   . HOH   F 5 .   ? 38.530 0.897   4.541  1.00 16.17 ? 569 HOH   A O   1 
HETATM 2017 O  O   . HOH   F 5 .   ? 20.700 19.932  9.090  1.00 38.48 ? 570 HOH   A O   1 
HETATM 2018 O  O   . HOH   F 5 .   ? 33.249 -0.812  28.116 1.00 33.75 ? 571 HOH   A O   1 
HETATM 2019 O  O   . HOH   F 5 .   ? 9.202  -1.802  35.458 1.00 23.49 ? 572 HOH   A O   1 
HETATM 2020 O  O   . HOH   F 5 .   ? 42.082 -3.062  16.882 1.00 38.37 ? 573 HOH   A O   1 
HETATM 2021 O  O   . HOH   F 5 .   ? 4.142  16.381  14.571 1.00 22.39 ? 574 HOH   A O   1 
HETATM 2022 O  O   . HOH   F 5 .   ? 21.611 2.738   39.991 1.00 38.15 ? 575 HOH   A O   1 
HETATM 2023 O  O   . HOH   F 5 .   ? 21.150 -17.085 17.998 1.00 29.66 ? 576 HOH   A O   1 
HETATM 2024 O  O   . HOH   F 5 .   ? 22.621 16.092  23.221 1.00 38.03 ? 577 HOH   A O   1 
HETATM 2025 O  O   . HOH   F 5 .   ? 40.105 4.570   0.000  0.50 13.27 ? 578 HOH   A O   1 
HETATM 2026 O  O   . HOH   F 5 .   ? 22.141 17.663  5.363  1.00 39.45 ? 579 HOH   A O   1 
HETATM 2027 O  O   . HOH   F 5 .   ? 24.126 8.489   -0.100 1.00 33.48 ? 580 HOH   A O   1 
HETATM 2028 O  O   . HOH   F 5 .   ? 24.305 -3.746  -3.333 1.00 46.25 ? 581 HOH   A O   1 
HETATM 2029 O  O   . HOH   F 5 .   ? 36.232 -11.688 29.182 1.00 35.42 ? 582 HOH   A O   1 
HETATM 2030 O  O   . HOH   F 5 .   ? 7.377  17.189  15.918 1.00 12.73 ? 583 HOH   A O   1 
HETATM 2031 O  O   . HOH   F 5 .   ? 35.750 -17.983 16.044 1.00 43.33 ? 584 HOH   A O   1 
HETATM 2032 O  O   . HOH   F 5 .   ? 4.223  -6.760  28.456 1.00 41.27 ? 585 HOH   A O   1 
HETATM 2033 O  O   . HOH   F 5 .   ? 40.024 4.163   19.090 1.00 38.00 ? 586 HOH   A O   1 
HETATM 2034 O  O   . HOH   F 5 .   ? 44.395 0.725   3.151  1.00 28.53 ? 587 HOH   A O   1 
HETATM 2035 O  O   . HOH   F 5 .   ? 21.963 10.911  23.231 1.00 32.57 ? 588 HOH   A O   1 
HETATM 2036 O  O   . HOH   F 5 .   ? -3.074 7.018   14.394 1.00 41.84 ? 589 HOH   A O   1 
HETATM 2037 O  O   . HOH   F 5 .   ? 37.899 -11.891 26.176 1.00 31.63 ? 590 HOH   A O   1 
HETATM 2038 O  O   . HOH   F 5 .   ? 36.492 -12.334 3.892  1.00 35.69 ? 591 HOH   A O   1 
HETATM 2039 O  O   . HOH   F 5 .   ? 16.105 -19.775 10.310 1.00 46.57 ? 592 HOH   A O   1 
HETATM 2040 O  O   . HOH   F 5 .   ? 9.680  12.257  2.542  1.00 17.22 ? 593 HOH   A O   1 
HETATM 2041 O  O   . HOH   F 5 .   ? 25.417 17.535  11.318 1.00 24.72 ? 594 HOH   A O   1 
HETATM 2042 O  O   . HOH   F 5 .   ? 4.735  -13.495 24.792 1.00 42.54 ? 595 HOH   A O   1 
HETATM 2043 O  O   . HOH   F 5 .   ? 41.057 -11.762 5.814  1.00 29.40 ? 596 HOH   A O   1 
HETATM 2044 O  O   . HOH   F 5 .   ? 43.716 -12.545 3.206  1.00 30.56 ? 597 HOH   A O   1 
HETATM 2045 O  O   . HOH   F 5 .   ? 34.824 17.641  15.494 1.00 36.23 ? 598 HOH   A O   1 
HETATM 2046 O  O   . HOH   F 5 .   ? 44.032 -9.439  1.849  1.00 25.37 ? 599 HOH   A O   1 
HETATM 2047 O  O   . HOH   F 5 .   ? 29.487 -8.067  31.048 1.00 35.12 ? 600 HOH   A O   1 
HETATM 2048 O  O   . HOH   F 5 .   ? 41.772 -11.790 32.697 1.00 30.53 ? 601 HOH   A O   1 
HETATM 2049 O  O   . HOH   F 5 .   ? 25.032 10.495  28.118 1.00 49.72 ? 602 HOH   A O   1 
HETATM 2050 O  O   . HOH   F 5 .   ? 14.265 2.541   1.600  1.00 43.97 ? 603 HOH   A O   1 
HETATM 2051 O  O   . HOH   F 5 .   ? 38.758 -13.103 5.063  1.00 30.03 ? 604 HOH   A O   1 
HETATM 2052 O  O   . HOH   F 5 .   ? -1.249 8.967   16.276 1.00 35.68 ? 605 HOH   A O   1 
HETATM 2053 O  O   . HOH   F 5 .   ? 28.280 -14.058 -5.302 1.00 32.74 ? 606 HOH   A O   1 
HETATM 2054 O  O   . HOH   F 5 .   ? 40.188 7.893   2.560  1.00 31.72 ? 607 HOH   A O   1 
HETATM 2055 O  O   . HOH   F 5 .   ? 43.101 -15.442 1.795  1.00 37.71 ? 608 HOH   A O   1 
HETATM 2056 O  O   . HOH   F 5 .   ? 33.014 -14.296 22.095 1.00 45.61 ? 609 HOH   A O   1 
HETATM 2057 O  O   . HOH   F 5 .   ? 39.725 -3.092  18.043 1.00 37.90 ? 610 HOH   A O   1 
HETATM 2058 O  O   . HOH   F 5 .   ? 6.540  13.535  0.772  1.00 25.78 ? 611 HOH   A O   1 
HETATM 2059 O  O   . HOH   F 5 .   ? 32.101 -3.918  -2.281 1.00 41.34 ? 612 HOH   A O   1 
HETATM 2060 O  O   . HOH   F 5 .   ? 30.905 -14.751 7.047  1.00 34.91 ? 613 HOH   A O   1 
HETATM 2061 O  O   . HOH   F 5 .   ? 41.853 -8.861  6.089  1.00 29.49 ? 614 HOH   A O   1 
HETATM 2062 O  O   . HOH   F 5 .   ? 24.566 11.727  22.928 1.00 43.24 ? 615 HOH   A O   1 
HETATM 2063 O  O   . HOH   F 5 .   ? 20.511 18.831  6.697  1.00 47.18 ? 616 HOH   A O   1 
HETATM 2064 O  O   . HOH   F 5 .   ? 36.879 0.170   20.425 1.00 24.99 ? 617 HOH   A O   1 
HETATM 2065 O  O   . HOH   F 5 .   ? 3.736  19.681  20.887 1.00 46.96 ? 618 HOH   A O   1 
HETATM 2066 O  O   . HOH   F 5 .   ? 32.319 -11.425 30.062 1.00 46.97 ? 619 HOH   A O   1 
HETATM 2067 O  O   . HOH   F 5 .   ? 43.175 2.090   8.219  1.00 32.50 ? 620 HOH   A O   1 
HETATM 2068 O  O   . HOH   F 5 .   ? 41.827 5.944   15.129 1.00 40.45 ? 621 HOH   A O   1 
HETATM 2069 O  O   . HOH   F 5 .   ? 24.355 19.672  12.956 1.00 34.76 ? 622 HOH   A O   1 
HETATM 2070 O  O   . HOH   F 5 .   ? 36.678 4.354   21.849 1.00 36.19 ? 623 HOH   A O   1 
HETATM 2071 O  O   . HOH   F 5 .   ? 8.395  15.680  3.088  1.00 32.43 ? 624 HOH   A O   1 
HETATM 2072 O  O   . HOH   F 5 .   ? 24.517 -12.977 1.281  1.00 31.89 ? 625 HOH   A O   1 
HETATM 2073 O  O   . HOH   F 5 .   ? 36.446 10.065  -4.054 1.00 37.01 ? 626 HOH   A O   1 
HETATM 2074 O  O   . HOH   F 5 .   ? 2.840  10.918  10.242 1.00 42.46 ? 627 HOH   A O   1 
HETATM 2075 O  O   . HOH   F 5 .   ? 14.949 19.420  7.893  1.00 36.05 ? 628 HOH   A O   1 
HETATM 2076 O  O   . HOH   F 5 .   ? 1.270  9.695   8.456  1.00 27.98 ? 629 HOH   A O   1 
HETATM 2077 O  O   . HOH   F 5 .   ? 36.845 11.289  -2.030 1.00 40.14 ? 630 HOH   A O   1 
HETATM 2078 O  O   . HOH   F 5 .   ? 30.762 -10.518 1.212  1.00 35.75 ? 631 HOH   A O   1 
HETATM 2079 O  O   . HOH   F 5 .   ? 40.832 6.572   7.408  1.00 22.04 ? 632 HOH   A O   1 
HETATM 2080 O  O   . HOH   F 5 .   ? 9.436  -7.423  6.014  1.00 41.01 ? 633 HOH   A 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   . ILE A 1   ? 0.2204 0.2546 0.2022 0.0435  0.0116  0.0407  16  ILE A N   
2    C CA  . ILE A 1   ? 0.2216 0.2676 0.2037 0.0489  0.0131  0.0466  16  ILE A CA  
3    C C   . ILE A 1   ? 0.2325 0.2753 0.2209 0.0470  0.0200  0.0525  16  ILE A C   
4    O O   . ILE A 1   ? 0.2422 0.2731 0.2322 0.0466  0.0263  0.0563  16  ILE A O   
5    C CB  . ILE A 1   ? 0.2195 0.2712 0.1965 0.0569  0.0141  0.0513  16  ILE A CB  
6    C CG1 . ILE A 1   ? 0.2098 0.2658 0.1815 0.0575  0.0076  0.0453  16  ILE A CG1 
7    C CG2 . ILE A 1   ? 0.2226 0.2872 0.1988 0.0624  0.0164  0.0579  16  ILE A CG2 
8    C CD1 . ILE A 1   ? 0.2013 0.2669 0.1709 0.0567  0.0021  0.0401  16  ILE A CD1 
9    N N   . ILE A 2   ? 0.2366 0.2893 0.2284 0.0459  0.0194  0.0535  17  ILE A N   
10   C CA  . ILE A 2   ? 0.2468 0.2993 0.2451 0.0441  0.0262  0.0600  17  ILE A CA  
11   C C   . ILE A 2   ? 0.2485 0.3109 0.2440 0.0527  0.0301  0.0688  17  ILE A C   
12   O O   . ILE A 2   ? 0.2335 0.3091 0.2245 0.0573  0.0262  0.0675  17  ILE A O   
13   C CB  . ILE A 2   ? 0.2457 0.3058 0.2505 0.0378  0.0238  0.0565  17  ILE A CB  
14   C CG1 . ILE A 2   ? 0.2468 0.2998 0.2547 0.0287  0.0203  0.0487  17  ILE A CG1 
15   C CG2 . ILE A 2   ? 0.2547 0.3183 0.2665 0.0364  0.0310  0.0641  17  ILE A CG2 
16   C CD1 . ILE A 2   ? 0.2414 0.3067 0.2547 0.0245  0.0155  0.0448  17  ILE A CD1 
17   N N   . GLY A 3   ? 0.2625 0.3180 0.2603 0.0547  0.0385  0.0778  18  GLY A N   
18   C CA  . GLY A 3   ? 0.2705 0.3365 0.2666 0.0625  0.0435  0.0882  18  GLY A CA  
19   C C   . GLY A 3   ? 0.2716 0.3454 0.2594 0.0720  0.0420  0.0917  18  GLY A C   
20   O O   . GLY A 3   ? 0.2664 0.3552 0.2503 0.0788  0.0432  0.0978  18  GLY A O   
21   N N   . GLY A 4   ? 0.2674 0.3326 0.2526 0.0723  0.0397  0.0880  19  GLY A N   
22   C CA  . GLY A 4   ? 0.2645 0.3399 0.2430 0.0801  0.0370  0.0900  19  GLY A CA  
23   C C   . GLY A 4   ? 0.2791 0.3469 0.2578 0.0868  0.0443  0.0999  19  GLY A C   
24   O O   . GLY A 4   ? 0.2923 0.3480 0.2758 0.0869  0.0530  0.1075  19  GLY A O   
25   N N   . ARG A 5   ? 0.2785 0.3542 0.2526 0.0924  0.0411  0.1001  20  ARG A N   
26   C CA  . ARG A 5   ? 0.2937 0.3654 0.2680 0.1006  0.0474  0.1097  20  ARG A CA  
27   C C   . ARG A 5   ? 0.2850 0.3515 0.2578 0.0994  0.0434  0.1026  20  ARG A C   
28   O O   . ARG A 5   ? 0.2688 0.3408 0.2391 0.0939  0.0349  0.0920  20  ARG A O   
29   C CB  . ARG A 5   ? 0.3083 0.4033 0.2784 0.1113  0.0480  0.1201  20  ARG A CB  
30   C CG  . ARG A 5   ? 0.3104 0.4283 0.2744 0.1104  0.0378  0.1125  20  ARG A CG  
31   C CD  . ARG A 5   ? 0.3244 0.4669 0.2839 0.1205  0.0373  0.1213  20  ARG A CD  
32   N NE  . ARG A 5   ? 0.3368 0.4782 0.2977 0.1255  0.0385  0.1248  20  ARG A NE  
33   C CZ  . ARG A 5   ? 0.3539 0.5163 0.3128 0.1352  0.0389  0.1340  20  ARG A CZ  
34   N NH1 . ARG A 5   ? 0.3512 0.5386 0.3057 0.1407  0.0377  0.1405  20  ARG A NH1 
35   N NH2 . ARG A 5   ? 0.3607 0.5210 0.3221 0.1397  0.0406  0.1369  20  ARG A NH2 
36   N N   . GLU A 6   ? 0.2952 0.3511 0.2695 0.1053  0.0503  0.1092  21  GLU A N   
37   C CA  . GLU A 6   ? 0.2900 0.3451 0.2628 0.1069  0.0477  0.1051  21  GLU A CA  
38   C C   . GLU A 6   ? 0.2779 0.3606 0.2467 0.1118  0.0406  0.1061  21  GLU A C   
39   O O   . GLU A 6   ? 0.2791 0.3791 0.2467 0.1196  0.0424  0.1160  21  GLU A O   
40   C CB  . GLU A 6   ? 0.3130 0.3530 0.2880 0.1148  0.0584  0.1142  21  GLU A CB  
41   C CG  . GLU A 6   ? 0.3176 0.3467 0.2920 0.1135  0.0580  0.1073  21  GLU A CG  
42   C CD  . GLU A 6   ? 0.3396 0.3547 0.3157 0.1232  0.0692  0.1162  21  GLU A CD  
43   O OE1 . GLU A 6   ? 0.3594 0.3581 0.3381 0.1263  0.0795  0.1241  21  GLU A OE1 
44   O OE2 . GLU A 6   ? 0.3395 0.3592 0.3145 0.1277  0.0683  0.1154  21  GLU A OE2 
45   N N   . SER A 7   ? 0.2649 0.3527 0.2316 0.1065  0.0326  0.0957  22  SER A N   
46   C CA  . SER A 7   ? 0.2570 0.3699 0.2207 0.1092  0.0260  0.0951  22  SER A CA  
47   C C   . SER A 7   ? 0.2670 0.3895 0.2322 0.1202  0.0309  0.1061  22  SER A C   
48   O O   . SER A 7   ? 0.2684 0.3736 0.2365 0.1241  0.0382  0.1102  22  SER A O   
49   C CB  . SER A 7   ? 0.2466 0.3590 0.2087 0.1004  0.0180  0.0822  22  SER A CB  
50   O OG  . SER A 7   ? 0.2378 0.3442 0.1986 0.0918  0.0135  0.0731  22  SER A OG  
51   N N   . ARG A 8   ? 0.2710 0.4221 0.2342 0.1255  0.0272  0.1109  23  ARG A N   
52   C CA  . ARG A 8   ? 0.2777 0.4444 0.2428 0.1352  0.0295  0.1198  23  ARG A CA  
53   C C   . ARG A 8   ? 0.2700 0.4298 0.2365 0.1300  0.0264  0.1109  23  ARG A C   
54   O O   . ARG A 8   ? 0.2565 0.4196 0.2209 0.1200  0.0184  0.0990  23  ARG A O   
55   C CB  . ARG A 8   ? 0.2792 0.4820 0.2415 0.1397  0.0243  0.1247  23  ARG A CB  
56   C CG  . ARG A 8   ? 0.2874 0.5132 0.2523 0.1478  0.0241  0.1318  23  ARG A CG  
57   C CD  . ARG A 8   ? 0.2928 0.5584 0.2552 0.1531  0.0195  0.1384  23  ARG A CD  
58   N NE  . ARG A 8   ? 0.2828 0.5652 0.2403 0.1414  0.0090  0.1249  23  ARG A NE  
59   C CZ  . ARG A 8   ? 0.2808 0.5991 0.2356 0.1416  0.0028  0.1251  23  ARG A CZ  
60   N NH1 . ARG A 8   ? 0.2865 0.6318 0.2435 0.1536  0.0051  0.1391  23  ARG A NH1 
61   N NH2 . ARG A 8   ? 0.2748 0.6022 0.2246 0.1297  -0.0054 0.1110  23  ARG A NH2 
62   N N   . PRO A 9   ? 0.2805 0.4288 0.2504 0.1366  0.0334  0.1162  24  PRO A N   
63   C CA  . PRO A 9   ? 0.2777 0.4189 0.2485 0.1319  0.0313  0.1080  24  PRO A CA  
64   C C   . PRO A 9   ? 0.2668 0.4355 0.2373 0.1279  0.0222  0.1030  24  PRO A C   
65   O O   . PRO A 9   ? 0.2590 0.4552 0.2310 0.1350  0.0212  0.1110  24  PRO A O   
66   C CB  . PRO A 9   ? 0.2913 0.4224 0.2654 0.1434  0.0417  0.1177  24  PRO A CB  
67   C CG  . PRO A 9   ? 0.3057 0.4254 0.2805 0.1511  0.0506  0.1287  24  PRO A CG  
68   C CD  . PRO A 9   ? 0.2987 0.4392 0.2713 0.1494  0.0446  0.1307  24  PRO A CD  
69   N N   . HIS A 10  ? 0.2566 0.4179 0.2253 0.1161  0.0158  0.0899  25  HIS A N   
70   C CA  . HIS A 10  ? 0.2526 0.4334 0.2214 0.1098  0.0082  0.0834  25  HIS A CA  
71   C C   . HIS A 10  ? 0.2369 0.4413 0.2031 0.1059  0.0013  0.0810  25  HIS A C   
72   O O   . HIS A 10  ? 0.2246 0.4490 0.1913 0.1008  -0.0044 0.0763  25  HIS A O   
73   C CB  . HIS A 10  ? 0.2733 0.4695 0.2466 0.1169  0.0108  0.0898  25  HIS A CB  
74   C CG  . HIS A 10  ? 0.3038 0.4775 0.2787 0.1224  0.0190  0.0926  25  HIS A CG  
75   N ND1 . HIS A 10  ? 0.3107 0.4624 0.2839 0.1150  0.0190  0.0833  25  HIS A ND1 
76   C CD2 . HIS A 10  ? 0.3344 0.5039 0.3119 0.1350  0.0282  0.1037  25  HIS A CD2 
77   C CE1 . HIS A 10  ? 0.3363 0.4715 0.3104 0.1223  0.0276  0.0875  25  HIS A CE1 
78   N NE2 . HIS A 10  ? 0.3570 0.5014 0.3340 0.1347  0.0338  0.0999  25  HIS A NE2 
79   N N   . SER A 11  ? 0.2360 0.4369 0.1993 0.1070  0.0021  0.0828  26  SER A N   
80   C CA  . SER A 11  ? 0.2284 0.4498 0.1876 0.1037  -0.0035 0.0798  26  SER A CA  
81   C C   . SER A 11  ? 0.2221 0.4352 0.1779 0.0909  -0.0098 0.0651  26  SER A C   
82   O O   . SER A 11  ? 0.2140 0.4434 0.1659 0.0861  -0.0149 0.0596  26  SER A O   
83   C CB  . SER A 11  ? 0.2344 0.4546 0.1915 0.1102  0.0006  0.0876  26  SER A CB  
84   O OG  . SER A 11  ? 0.2307 0.4217 0.1877 0.1070  0.0040  0.0846  26  SER A OG  
85   N N   . ARG A 12  ? 0.2192 0.4068 0.1760 0.0856  -0.0090 0.0591  27  ARG A N   
86   C CA  . ARG A 12  ? 0.2168 0.3942 0.1709 0.0750  -0.0138 0.0469  27  ARG A CA  
87   C C   . ARG A 12  ? 0.2124 0.3810 0.1689 0.0703  -0.0147 0.0426  27  ARG A C   
88   O O   . ARG A 12  ? 0.2097 0.3565 0.1664 0.0679  -0.0132 0.0397  27  ARG A O   
89   C CB  . ARG A 12  ? 0.2219 0.3787 0.1745 0.0737  -0.0120 0.0449  27  ARG A CB  
90   C CG  . ARG A 12  ? 0.2305 0.3966 0.1808 0.0786  -0.0103 0.0500  27  ARG A CG  
91   C CD  . ARG A 12  ? 0.2362 0.3848 0.1859 0.0765  -0.0087 0.0476  27  ARG A CD  
92   N NE  . ARG A 12  ? 0.2431 0.4027 0.1907 0.0816  -0.0064 0.0535  27  ARG A NE  
93   C CZ  . ARG A 12  ? 0.2479 0.4256 0.1904 0.0809  -0.0096 0.0504  27  ARG A CZ  
94   N NH1 . ARG A 12  ? 0.2507 0.4332 0.1901 0.0737  -0.0150 0.0397  27  ARG A NH1 
95   N NH2 . ARG A 12  ? 0.2470 0.4371 0.1873 0.0870  -0.0070 0.0576  27  ARG A NH2 
96   N N   . PRO A 13  ? 0.2107 0.3983 0.1691 0.0688  -0.0172 0.0423  28  PRO A N   
97   C CA  . PRO A 13  ? 0.2057 0.3885 0.1672 0.0662  -0.0167 0.0408  28  PRO A CA  
98   C C   . PRO A 13  ? 0.2013 0.3689 0.1611 0.0560  -0.0197 0.0308  28  PRO A C   
99   O O   . PRO A 13  ? 0.1983 0.3607 0.1601 0.0539  -0.0189 0.0300  28  PRO A O   
100  C CB  . PRO A 13  ? 0.2085 0.4216 0.1733 0.0674  -0.0188 0.0441  28  PRO A CB  
101  C CG  . PRO A 13  ? 0.2128 0.4430 0.1740 0.0636  -0.0233 0.0402  28  PRO A CG  
102  C CD  . PRO A 13  ? 0.2134 0.4305 0.1713 0.0692  -0.0205 0.0436  28  PRO A CD  
103  N N   . TYR A 14  ? 0.1957 0.3563 0.1517 0.0506  -0.0225 0.0242  29  TYR A N   
104  C CA  . TYR A 14  ? 0.1947 0.3388 0.1488 0.0425  -0.0244 0.0160  29  TYR A CA  
105  C C   . TYR A 14  ? 0.1893 0.3106 0.1427 0.0446  -0.0219 0.0169  29  TYR A C   
106  O O   . TYR A 14  ? 0.1886 0.2965 0.1409 0.0396  -0.0229 0.0123  29  TYR A O   
107  C CB  . TYR A 14  ? 0.2005 0.3470 0.1508 0.0372  -0.0273 0.0088  29  TYR A CB  
108  C CG  . TYR A 14  ? 0.2086 0.3605 0.1566 0.0428  -0.0265 0.0118  29  TYR A CG  
109  C CD1 . TYR A 14  ? 0.2126 0.3484 0.1596 0.0460  -0.0243 0.0132  29  TYR A CD1 
110  C CD2 . TYR A 14  ? 0.2172 0.3926 0.1641 0.0451  -0.0277 0.0139  29  TYR A CD2 
111  C CE1 . TYR A 14  ? 0.2118 0.3532 0.1572 0.0510  -0.0229 0.0168  29  TYR A CE1 
112  C CE2 . TYR A 14  ? 0.2199 0.4014 0.1642 0.0508  -0.0265 0.0178  29  TYR A CE2 
113  C CZ  . TYR A 14  ? 0.2192 0.3828 0.1628 0.0537  -0.0238 0.0193  29  TYR A CZ  
114  O OH  . TYR A 14  ? 0.2178 0.3875 0.1593 0.0591  -0.0219 0.0237  29  TYR A OH  
115  N N   . MET A 15  ? 0.1814 0.2987 0.1356 0.0515  -0.0185 0.0230  30  MET A N   
116  C CA  . MET A 15  ? 0.1781 0.2760 0.1319 0.0520  -0.0165 0.0228  30  MET A CA  
117  C C   . MET A 15  ? 0.1780 0.2652 0.1320 0.0504  -0.0153 0.0219  30  MET A C   
118  O O   . MET A 15  ? 0.1794 0.2721 0.1349 0.0534  -0.0130 0.0252  30  MET A O   
119  C CB  . MET A 15  ? 0.1796 0.2754 0.1346 0.0586  -0.0122 0.0294  30  MET A CB  
120  C CG  . MET A 15  ? 0.1804 0.2836 0.1342 0.0600  -0.0129 0.0303  30  MET A CG  
121  S SD  . MET A 15  ? 0.1815 0.2746 0.1333 0.0542  -0.0159 0.0229  30  MET A SD  
122  C CE  . MET A 15  ? 0.1806 0.2544 0.1347 0.0533  -0.0135 0.0235  30  MET A CE  
123  N N   . ALA A 16  ? 0.1756 0.2491 0.1279 0.0463  -0.0166 0.0177  31  ALA A N   
124  C CA  . ALA A 16  ? 0.1792 0.2428 0.1303 0.0445  -0.0157 0.0164  31  ALA A CA  
125  C C   . ALA A 16  ? 0.1833 0.2337 0.1335 0.0447  -0.0142 0.0159  31  ALA A C   
126  O O   . ALA A 16  ? 0.1784 0.2259 0.1290 0.0433  -0.0158 0.0146  31  ALA A O   
127  C CB  . ALA A 16  ? 0.1791 0.2409 0.1286 0.0388  -0.0190 0.0122  31  ALA A CB  
128  N N   . TYR A 17  ? 0.1913 0.2349 0.1406 0.0463  -0.0107 0.0166  32  TYR A N   
129  C CA  . TYR A 17  ? 0.1981 0.2296 0.1460 0.0444  -0.0094 0.0144  32  TYR A CA  
130  C C   . TYR A 17  ? 0.1996 0.2272 0.1438 0.0402  -0.0119 0.0104  32  TYR A C   
131  O O   . TYR A 17  ? 0.1947 0.2240 0.1370 0.0408  -0.0108 0.0105  32  TYR A O   
132  C CB  . TYR A 17  ? 0.2121 0.2368 0.1603 0.0484  -0.0030 0.0167  32  TYR A CB  
133  C CG  . TYR A 17  ? 0.2280 0.2396 0.1746 0.0448  -0.0010 0.0130  32  TYR A CG  
134  C CD1 . TYR A 17  ? 0.2354 0.2430 0.1849 0.0435  0.0000  0.0137  32  TYR A CD1 
135  C CD2 . TYR A 17  ? 0.2431 0.2478 0.1851 0.0420  -0.0003 0.0083  32  TYR A CD2 
136  C CE1 . TYR A 17  ? 0.2481 0.2455 0.1968 0.0385  0.0016  0.0095  32  TYR A CE1 
137  C CE2 . TYR A 17  ? 0.2572 0.2518 0.1973 0.0373  0.0011  0.0036  32  TYR A CE2 
138  C CZ  . TYR A 17  ? 0.2602 0.2512 0.2041 0.0351  0.0020  0.0040  32  TYR A CZ  
139  O OH  . TYR A 17  ? 0.2843 0.2668 0.2270 0.0290  0.0033  -0.0012 32  TYR A OH  
140  N N   . LEU A 18  ? 0.2016 0.2254 0.1450 0.0365  -0.0148 0.0077  33  LEU A N   
141  C CA  . LEU A 18  ? 0.2056 0.2276 0.1452 0.0331  -0.0175 0.0052  33  LEU A CA  
142  C C   . LEU A 18  ? 0.2099 0.2257 0.1468 0.0304  -0.0165 0.0018  33  LEU A C   
143  O O   . LEU A 18  ? 0.2069 0.2211 0.1463 0.0286  -0.0167 0.0007  33  LEU A O   
144  C CB  . LEU A 18  ? 0.2049 0.2300 0.1455 0.0316  -0.0218 0.0054  33  LEU A CB  
145  C CG  . LEU A 18  ? 0.2092 0.2389 0.1522 0.0328  -0.0226 0.0068  33  LEU A CG  
146  C CD1 . LEU A 18  ? 0.2106 0.2394 0.1535 0.0317  -0.0254 0.0065  33  LEU A CD1 
147  C CD2 . LEU A 18  ? 0.2141 0.2476 0.1564 0.0330  -0.0214 0.0076  33  LEU A CD2 
148  N N   . GLN A 19  ? 0.2105 0.2240 0.1422 0.0296  -0.0152 -0.0003 34  GLN A N   
149  C CA  . GLN A 19  ? 0.2197 0.2290 0.1468 0.0258  -0.0149 -0.0051 34  GLN A CA  
150  C C   . GLN A 19  ? 0.2211 0.2365 0.1444 0.0236  -0.0197 -0.0053 34  GLN A C   
151  O O   . GLN A 19  ? 0.2177 0.2354 0.1378 0.0250  -0.0196 -0.0035 34  GLN A O   
152  C CB  . GLN A 19  ? 0.2312 0.2334 0.1540 0.0272  -0.0091 -0.0076 34  GLN A CB  
153  C CG  . GLN A 19  ? 0.2478 0.2456 0.1637 0.0225  -0.0084 -0.0143 34  GLN A CG  
154  C CD  . GLN A 19  ? 0.2559 0.2478 0.1657 0.0249  -0.0027 -0.0169 34  GLN A CD  
155  O OE1 . GLN A 19  ? 0.2684 0.2498 0.1754 0.0238  0.0026  -0.0219 34  GLN A OE1 
156  N NE2 . GLN A 19  ? 0.2511 0.2494 0.1591 0.0281  -0.0031 -0.0136 34  GLN A NE2 
157  N N   . ILE A 20  ? 0.2223 0.2415 0.1464 0.0204  -0.0235 -0.0065 35  ILE A N   
158  C CA  . ILE A 20  ? 0.2222 0.2491 0.1443 0.0199  -0.0282 -0.0045 35  ILE A CA  
159  C C   . ILE A 20  ? 0.2310 0.2620 0.1473 0.0155  -0.0299 -0.0090 35  ILE A C   
160  O O   . ILE A 20  ? 0.2340 0.2642 0.1514 0.0112  -0.0296 -0.0138 35  ILE A O   
161  C CB  . ILE A 20  ? 0.2161 0.2473 0.1448 0.0211  -0.0311 -0.0012 35  ILE A CB  
162  C CG1 . ILE A 20  ? 0.2119 0.2397 0.1451 0.0246  -0.0293 0.0016  35  ILE A CG1 
163  C CG2 . ILE A 20  ? 0.2169 0.2558 0.1441 0.0221  -0.0351 0.0022  35  ILE A CG2 
164  C CD1 . ILE A 20  ? 0.2084 0.2376 0.1479 0.0252  -0.0295 0.0023  35  ILE A CD1 
165  N N   . GLN A 21  ? 0.2385 0.2746 0.1485 0.0160  -0.0315 -0.0077 36  GLN A N   
166  C CA  . GLN A 21  ? 0.2534 0.2970 0.1565 0.0120  -0.0340 -0.0117 36  GLN A CA  
167  C C   . GLN A 21  ? 0.2511 0.3066 0.1531 0.0142  -0.0387 -0.0056 36  GLN A C   
168  O O   . GLN A 21  ? 0.2521 0.3060 0.1551 0.0188  -0.0381 0.0009  36  GLN A O   
169  C CB  . GLN A 21  ? 0.2694 0.3087 0.1634 0.0112  -0.0302 -0.0161 36  GLN A CB  
170  C CG  . GLN A 21  ? 0.2758 0.3021 0.1715 0.0127  -0.0239 -0.0187 36  GLN A CG  
171  C CD  . GLN A 21  ? 0.2915 0.3120 0.1785 0.0111  -0.0192 -0.0255 36  GLN A CD  
172  O OE1 . GLN A 21  ? 0.2966 0.3062 0.1847 0.0128  -0.0133 -0.0278 36  GLN A OE1 
173  N NE2 . GLN A 21  ? 0.3047 0.3329 0.1827 0.0084  -0.0213 -0.0287 36  GLN A NE2 
174  N N   . SER A 22  A 0.2528 0.3206 0.1534 0.0109  -0.0430 -0.0074 36  SER A N   
175  C CA  . SER A 22  A 0.2559 0.3378 0.1539 0.0137  -0.0473 -0.0011 36  SER A CA  
176  C C   . SER A 22  A 0.2629 0.3602 0.1559 0.0079  -0.0515 -0.0065 36  SER A C   
177  O O   . SER A 22  A 0.2613 0.3553 0.1528 0.0010  -0.0504 -0.0159 36  SER A O   
178  C CB  . SER A 22  A 0.2507 0.3353 0.1574 0.0188  -0.0490 0.0066  36  SER A CB  
179  O OG  . SER A 22  A 0.2497 0.3439 0.1625 0.0159  -0.0522 0.0044  36  SER A OG  
180  N N   . PRO A 23  B 0.2710 0.3858 0.1608 0.0103  -0.0560 -0.0008 36  PRO A N   
181  C CA  . PRO A 23  B 0.2835 0.4176 0.1688 0.0042  -0.0610 -0.0060 36  PRO A CA  
182  C C   . PRO A 23  B 0.2890 0.4276 0.1830 -0.0021 -0.0631 -0.0117 36  PRO A C   
183  O O   . PRO A 23  B 0.2983 0.4462 0.1890 -0.0110 -0.0654 -0.0208 36  PRO A O   
184  C CB  . PRO A 23  B 0.2838 0.4362 0.1677 0.0111  -0.0651 0.0052  36  PRO A CB  
185  C CG  . PRO A 23  B 0.2806 0.4190 0.1622 0.0187  -0.0605 0.0132  36  PRO A CG  
186  C CD  . PRO A 23  B 0.2685 0.3861 0.1586 0.0188  -0.0562 0.0109  36  PRO A CD  
187  N N   . ALA A 24  ? 0.2889 0.4207 0.1938 0.0018  -0.0618 -0.0066 37  ALA A N   
188  C CA  . ALA A 24  ? 0.2936 0.4296 0.2083 -0.0029 -0.0630 -0.0098 37  ALA A CA  
189  C C   . ALA A 24  ? 0.3004 0.4189 0.2154 -0.0101 -0.0582 -0.0197 37  ALA A C   
190  O O   . ALA A 24  ? 0.3131 0.4340 0.2357 -0.0157 -0.0583 -0.0233 37  ALA A O   
191  C CB  . ALA A 24  ? 0.2853 0.4195 0.2101 0.0049  -0.0624 -0.0008 37  ALA A CB  
192  N N   . GLY A 25  ? 0.2987 0.4003 0.2065 -0.0093 -0.0535 -0.0230 38  GLY A N   
193  C CA  . GLY A 25  ? 0.3047 0.3891 0.2115 -0.0148 -0.0479 -0.0316 38  GLY A CA  
194  C C   . GLY A 25  ? 0.3001 0.3663 0.2110 -0.0083 -0.0424 -0.0274 38  GLY A C   
195  O O   . GLY A 25  ? 0.2887 0.3538 0.1995 -0.0009 -0.0426 -0.0201 38  GLY A O   
196  N N   . GLN A 26  ? 0.3088 0.3612 0.2229 -0.0115 -0.0373 -0.0321 39  GLN A N   
197  C CA  . GLN A 26  ? 0.3125 0.3493 0.2296 -0.0059 -0.0317 -0.0288 39  GLN A CA  
198  C C   . GLN A 26  ? 0.2814 0.3191 0.2090 -0.0035 -0.0320 -0.0234 39  GLN A C   
199  O O   . GLN A 26  ? 0.2712 0.3141 0.2044 -0.0086 -0.0331 -0.0253 39  GLN A O   
200  C CB  . GLN A 26  ? 0.3519 0.3727 0.2663 -0.0094 -0.0247 -0.0359 39  GLN A CB  
201  C CG  . GLN A 26  ? 0.3987 0.4105 0.3041 -0.0062 -0.0204 -0.0381 39  GLN A CG  
202  C CD  . GLN A 26  ? 0.4496 0.4697 0.3447 -0.0098 -0.0232 -0.0434 39  GLN A CD  
203  O OE1 . GLN A 26  ? 0.4809 0.5056 0.3723 -0.0180 -0.0249 -0.0513 39  GLN A OE1 
204  N NE2 . GLN A 26  ? 0.4684 0.4913 0.3583 -0.0041 -0.0235 -0.0392 39  GLN A NE2 
205  N N   . SER A 27  ? 0.2585 0.2917 0.1888 0.0037  -0.0306 -0.0171 40  SER A N   
206  C CA  . SER A 27  ? 0.2459 0.2788 0.1845 0.0067  -0.0298 -0.0126 40  SER A CA  
207  C C   . SER A 27  ? 0.2389 0.2612 0.1779 0.0118  -0.0250 -0.0100 40  SER A C   
208  O O   . SER A 27  ? 0.2347 0.2522 0.1686 0.0141  -0.0230 -0.0104 40  SER A O   
209  C CB  . SER A 27  ? 0.2375 0.2810 0.1795 0.0105  -0.0344 -0.0071 40  SER A CB  
210  O OG  . SER A 27  ? 0.2443 0.3007 0.1857 0.0074  -0.0391 -0.0079 40  SER A OG  
211  N N   . ARG A 28  ? 0.2350 0.2565 0.1804 0.0140  -0.0233 -0.0067 41  ARG A N   
212  C CA  . ARG A 28  ? 0.2350 0.2509 0.1817 0.0192  -0.0194 -0.0033 41  ARG A CA  
213  C C   . ARG A 28  ? 0.2168 0.2393 0.1678 0.0231  -0.0214 0.0010  41  ARG A C   
214  O O   . ARG A 28  ? 0.2174 0.2452 0.1728 0.0217  -0.0230 0.0018  41  ARG A O   
215  C CB  . ARG A 28  ? 0.2494 0.2567 0.1987 0.0183  -0.0134 -0.0036 41  ARG A CB  
216  C CG  . ARG A 28  ? 0.2690 0.2667 0.2139 0.0137  -0.0099 -0.0093 41  ARG A CG  
217  C CD  . ARG A 28  ? 0.2785 0.2651 0.2266 0.0119  -0.0030 -0.0098 41  ARG A CD  
218  N NE  . ARG A 28  ? 0.2927 0.2681 0.2358 0.0067  0.0009  -0.0170 41  ARG A NE  
219  C CZ  . ARG A 28  ? 0.3058 0.2671 0.2502 0.0040  0.0083  -0.0191 41  ARG A CZ  
220  N NH1 . ARG A 28  ? 0.3057 0.2635 0.2567 0.0064  0.0125  -0.0132 41  ARG A NH1 
221  N NH2 . ARG A 28  ? 0.3212 0.2715 0.2599 -0.0011 0.0121  -0.0271 41  ARG A NH2 
222  N N   . CYS A 29  ? 0.2027 0.2254 0.1523 0.0274  -0.0211 0.0034  42  CYS A N   
223  C CA  . CYS A 29  ? 0.1897 0.2174 0.1421 0.0306  -0.0222 0.0062  42  CYS A CA  
224  C C   . CYS A 29  ? 0.1857 0.2137 0.1375 0.0342  -0.0196 0.0082  42  CYS A C   
225  O O   . CYS A 29  ? 0.1826 0.2078 0.1322 0.0349  -0.0174 0.0082  42  CYS A O   
226  C CB  . CYS A 29  ? 0.1858 0.2163 0.1366 0.0312  -0.0259 0.0062  42  CYS A CB  
227  S SG  . CYS A 29  ? 0.1808 0.2166 0.1341 0.0298  -0.0292 0.0063  42  CYS A SG  
228  N N   . GLY A 30  ? 0.1789 0.2121 0.1327 0.0366  -0.0199 0.0099  43  GLY A N   
229  C CA  . GLY A 30  ? 0.1728 0.2111 0.1257 0.0393  -0.0192 0.0112  43  GLY A CA  
230  C C   . GLY A 30  ? 0.1708 0.2110 0.1216 0.0380  -0.0221 0.0088  43  GLY A C   
231  O O   . GLY A 30  ? 0.1689 0.2054 0.1190 0.0362  -0.0241 0.0073  43  GLY A O   
232  N N   . GLY A 31  ? 0.1694 0.2161 0.1195 0.0388  -0.0219 0.0089  44  GLY A N   
233  C CA  . GLY A 31  ? 0.1719 0.2201 0.1203 0.0362  -0.0237 0.0060  44  GLY A CA  
234  C C   . GLY A 31  ? 0.1722 0.2317 0.1207 0.0365  -0.0234 0.0061  44  GLY A C   
235  O O   . GLY A 31  ? 0.1693 0.2353 0.1191 0.0401  -0.0217 0.0096  44  GLY A O   
236  N N   . PHE A 32  ? 0.1787 0.2412 0.1260 0.0327  -0.0248 0.0024  45  PHE A N   
237  C CA  . PHE A 32  ? 0.1812 0.2580 0.1287 0.0319  -0.0252 0.0019  45  PHE A CA  
238  C C   . PHE A 32  ? 0.1862 0.2647 0.1336 0.0257  -0.0262 -0.0017 45  PHE A C   
239  O O   . PHE A 32  ? 0.1863 0.2544 0.1323 0.0217  -0.0263 -0.0054 45  PHE A O   
240  C CB  . PHE A 32  ? 0.1853 0.2684 0.1311 0.0334  -0.0256 0.0000  45  PHE A CB  
241  C CG  . PHE A 32  ? 0.1910 0.2645 0.1345 0.0313  -0.0258 -0.0051 45  PHE A CG  
242  C CD1 . PHE A 32  ? 0.1907 0.2538 0.1349 0.0342  -0.0250 -0.0035 45  PHE A CD1 
243  C CD2 . PHE A 32  ? 0.2001 0.2759 0.1408 0.0265  -0.0264 -0.0118 45  PHE A CD2 
244  C CE1 . PHE A 32  ? 0.1958 0.2511 0.1385 0.0338  -0.0244 -0.0073 45  PHE A CE1 
245  C CE2 . PHE A 32  ? 0.2062 0.2713 0.1445 0.0257  -0.0253 -0.0165 45  PHE A CE2 
246  C CZ  . PHE A 32  ? 0.2052 0.2602 0.1446 0.0301  -0.0242 -0.0137 45  PHE A CZ  
247  N N   . LEU A 33  ? 0.1895 0.2823 0.1390 0.0253  -0.0263 0.0001  46  LEU A N   
248  C CA  . LEU A 33  ? 0.1975 0.2961 0.1483 0.0187  -0.0270 -0.0026 46  LEU A CA  
249  C C   . LEU A 33  ? 0.2051 0.3085 0.1542 0.0122  -0.0286 -0.0098 46  LEU A C   
250  O O   . LEU A 33  ? 0.2070 0.3237 0.1550 0.0135  -0.0298 -0.0109 46  LEU A O   
251  C CB  . LEU A 33  ? 0.1950 0.3112 0.1494 0.0216  -0.0265 0.0023  46  LEU A CB  
252  C CG  . LEU A 33  ? 0.1985 0.3235 0.1561 0.0158  -0.0265 0.0016  46  LEU A CG  
253  C CD1 . LEU A 33  ? 0.1977 0.3079 0.1549 0.0157  -0.0244 0.0035  46  LEU A CD1 
254  C CD2 . LEU A 33  ? 0.1982 0.3463 0.1599 0.0198  -0.0263 0.0067  46  LEU A CD2 
255  N N   . VAL A 34  ? 0.2127 0.3044 0.1609 0.0053  -0.0279 -0.0146 47  VAL A N   
256  C CA  . VAL A 34  ? 0.2247 0.3167 0.1705 -0.0018 -0.0283 -0.0230 47  VAL A CA  
257  C C   . VAL A 34  ? 0.2342 0.3342 0.1829 -0.0116 -0.0284 -0.0265 47  VAL A C   
258  O O   . VAL A 34  ? 0.2422 0.3466 0.1894 -0.0195 -0.0288 -0.0346 47  VAL A O   
259  C CB  . VAL A 34  ? 0.2306 0.3003 0.1730 -0.0018 -0.0262 -0.0265 47  VAL A CB  
260  C CG1 . VAL A 34  ? 0.2253 0.2924 0.1656 0.0064  -0.0263 -0.0242 47  VAL A CG1 
261  C CG2 . VAL A 34  ? 0.2309 0.2836 0.1745 -0.0023 -0.0240 -0.0232 47  VAL A CG2 
262  N N   . ARG A 35  ? 0.2342 0.3355 0.1867 -0.0115 -0.0275 -0.0211 48  ARG A N   
263  C CA  . ARG A 35  ? 0.2429 0.3563 0.1998 -0.0199 -0.0274 -0.0224 48  ARG A CA  
264  C C   . ARG A 35  ? 0.2313 0.3520 0.1920 -0.0144 -0.0266 -0.0139 48  ARG A C   
265  O O   . ARG A 35  ? 0.2266 0.3374 0.1855 -0.0060 -0.0257 -0.0087 48  ARG A O   
266  C CB  . ARG A 35  ? 0.2607 0.3557 0.2169 -0.0290 -0.0246 -0.0274 48  ARG A CB  
267  C CG  . ARG A 35  ? 0.2755 0.3820 0.2362 -0.0412 -0.0241 -0.0316 48  ARG A CG  
268  C CD  . ARG A 35  ? 0.2971 0.3825 0.2562 -0.0511 -0.0203 -0.0382 48  ARG A CD  
269  N NE  . ARG A 35  ? 0.3072 0.3732 0.2669 -0.0496 -0.0163 -0.0320 48  ARG A NE  
270  C CZ  . ARG A 35  ? 0.3298 0.3738 0.2883 -0.0558 -0.0116 -0.0347 48  ARG A CZ  
271  N NH1 . ARG A 35  ? 0.3511 0.3871 0.3075 -0.0639 -0.0100 -0.0446 48  ARG A NH1 
272  N NH2 . ARG A 35  ? 0.3318 0.3615 0.2906 -0.0535 -0.0080 -0.0274 48  ARG A NH2 
273  N N   . GLU A 36  ? 0.2327 0.3707 0.1987 -0.0195 -0.0266 -0.0128 49  GLU A N   
274  C CA  . GLU A 36  ? 0.2284 0.3755 0.1981 -0.0137 -0.0251 -0.0050 49  GLU A CA  
275  C C   . GLU A 36  ? 0.2262 0.3519 0.1931 -0.0103 -0.0221 -0.0013 49  GLU A C   
276  O O   . GLU A 36  ? 0.2183 0.3461 0.1856 -0.0029 -0.0205 0.0045  49  GLU A O   
277  C CB  . GLU A 36  ? 0.2331 0.4022 0.2098 -0.0211 -0.0250 -0.0049 49  GLU A CB  
278  C CG  . GLU A 36  ? 0.2310 0.4301 0.2115 -0.0204 -0.0281 -0.0047 49  GLU A CG  
279  C CD  . GLU A 36  ? 0.2370 0.4413 0.2142 -0.0254 -0.0316 -0.0125 49  GLU A CD  
280  O OE1 . GLU A 36  ? 0.2417 0.4276 0.2148 -0.0331 -0.0313 -0.0203 49  GLU A OE1 
281  O OE2 . GLU A 36  ? 0.2352 0.4625 0.2135 -0.0207 -0.0342 -0.0103 49  GLU A OE2 
282  N N   . ASP A 37  ? 0.2320 0.3375 0.1957 -0.0150 -0.0210 -0.0045 50  ASP A N   
283  C CA  . ASP A 37  ? 0.2331 0.3214 0.1940 -0.0123 -0.0185 -0.0005 50  ASP A CA  
284  C C   . ASP A 37  ? 0.2335 0.3024 0.1890 -0.0075 -0.0189 -0.0010 50  ASP A C   
285  O O   . ASP A 37  ? 0.2305 0.2867 0.1832 -0.0053 -0.0172 0.0023  50  ASP A O   
286  C CB  . ASP A 37  ? 0.2472 0.3300 0.2100 -0.0212 -0.0156 -0.0008 50  ASP A CB  
287  C CG  . ASP A 37  ? 0.2595 0.3326 0.2221 -0.0303 -0.0150 -0.0076 50  ASP A CG  
288  O OD1 . ASP A 37  ? 0.2561 0.3330 0.2177 -0.0308 -0.0175 -0.0132 50  ASP A OD1 
289  O OD2 . ASP A 37  ? 0.2716 0.3322 0.2345 -0.0363 -0.0115 -0.0071 50  ASP A OD2 
290  N N   . PHE A 38  ? 0.2296 0.2980 0.1835 -0.0056 -0.0210 -0.0047 51  PHE A N   
291  C CA  . PHE A 38  ? 0.2296 0.2816 0.1796 -0.0016 -0.0211 -0.0052 51  PHE A CA  
292  C C   . PHE A 38  ? 0.2169 0.2736 0.1658 0.0051  -0.0231 -0.0051 51  PHE A C   
293  O O   . PHE A 38  ? 0.2102 0.2795 0.1603 0.0047  -0.0245 -0.0074 51  PHE A O   
294  C CB  . PHE A 38  ? 0.2454 0.2855 0.1941 -0.0072 -0.0197 -0.0107 51  PHE A CB  
295  C CG  . PHE A 38  ? 0.2580 0.2830 0.2061 -0.0109 -0.0163 -0.0087 51  PHE A CG  
296  C CD1 . PHE A 38  ? 0.2618 0.2731 0.2071 -0.0050 -0.0152 -0.0039 51  PHE A CD1 
297  C CD2 . PHE A 38  ? 0.2701 0.2959 0.2210 -0.0202 -0.0139 -0.0110 51  PHE A CD2 
298  C CE1 . PHE A 38  ? 0.2723 0.2709 0.2169 -0.0071 -0.0115 -0.0004 51  PHE A CE1 
299  C CE2 . PHE A 38  ? 0.2815 0.2925 0.2320 -0.0232 -0.0098 -0.0079 51  PHE A CE2 
300  C CZ  . PHE A 38  ? 0.2827 0.2800 0.2299 -0.0160 -0.0085 -0.0020 51  PHE A CZ  
301  N N   . VAL A 39  ? 0.2065 0.2539 0.1533 0.0110  -0.0232 -0.0021 52  VAL A N   
302  C CA  . VAL A 39  ? 0.1969 0.2457 0.1431 0.0165  -0.0244 -0.0018 52  VAL A CA  
303  C C   . VAL A 39  ? 0.1959 0.2323 0.1401 0.0176  -0.0243 -0.0035 52  VAL A C   
304  O O   . VAL A 39  ? 0.2003 0.2264 0.1434 0.0176  -0.0235 -0.0017 52  VAL A O   
305  C CB  . VAL A 39  ? 0.1912 0.2410 0.1373 0.0216  -0.0240 0.0025  52  VAL A CB  
306  C CG1 . VAL A 39  ? 0.1879 0.2349 0.1337 0.0262  -0.0244 0.0032  52  VAL A CG1 
307  C CG2 . VAL A 39  ? 0.1909 0.2533 0.1392 0.0227  -0.0230 0.0046  52  VAL A CG2 
308  N N   . LEU A 40  ? 0.1894 0.2283 0.1333 0.0194  -0.0248 -0.0060 53  LEU A N   
309  C CA  . LEU A 40  ? 0.1896 0.2188 0.1324 0.0220  -0.0243 -0.0070 53  LEU A CA  
310  C C   . LEU A 40  ? 0.1776 0.2087 0.1214 0.0276  -0.0251 -0.0033 53  LEU A C   
311  O O   . LEU A 40  ? 0.1710 0.2108 0.1160 0.0293  -0.0255 -0.0018 53  LEU A O   
312  C CB  . LEU A 40  ? 0.1970 0.2275 0.1381 0.0198  -0.0235 -0.0130 53  LEU A CB  
313  C CG  . LEU A 40  ? 0.2052 0.2245 0.1447 0.0222  -0.0215 -0.0153 53  LEU A CG  
314  C CD1 . LEU A 40  ? 0.2158 0.2199 0.1550 0.0213  -0.0192 -0.0142 53  LEU A CD1 
315  C CD2 . LEU A 40  ? 0.2120 0.2342 0.1486 0.0197  -0.0205 -0.0226 53  LEU A CD2 
316  N N   . THR A 41  ? 0.1749 0.1986 0.1190 0.0302  -0.0250 -0.0014 54  THR A N   
317  C CA  . THR A 41  ? 0.1658 0.1919 0.1117 0.0338  -0.0258 0.0014  54  THR A CA  
318  C C   . THR A 41  ? 0.1649 0.1858 0.1116 0.0368  -0.0256 0.0026  54  THR A C   
319  O O   . THR A 41  ? 0.1694 0.1837 0.1149 0.0370  -0.0239 0.0008  54  THR A O   
320  C CB  . THR A 41  ? 0.1651 0.1924 0.1109 0.0330  -0.0267 0.0040  54  THR A CB  
321  O OG1 . THR A 41  ? 0.1630 0.1927 0.1107 0.0347  -0.0272 0.0055  54  THR A OG1 
322  C CG2 . THR A 41  ? 0.1694 0.1911 0.1132 0.0319  -0.0270 0.0056  54  THR A CG2 
323  N N   . ALA A 42  ? 0.1577 0.1820 0.1068 0.0390  -0.0268 0.0055  55  ALA A N   
324  C CA  . ALA A 42  ? 0.1612 0.1846 0.1122 0.0427  -0.0267 0.0078  55  ALA A CA  
325  C C   . ALA A 42  ? 0.1638 0.1856 0.1137 0.0429  -0.0281 0.0114  55  ALA A C   
326  O O   . ALA A 42  ? 0.1605 0.1846 0.1089 0.0401  -0.0297 0.0118  55  ALA A O   
327  C CB  . ALA A 42  ? 0.1566 0.1880 0.1117 0.0444  -0.0273 0.0090  55  ALA A CB  
328  N N   . ALA A 43  ? 0.1714 0.1899 0.1220 0.0471  -0.0270 0.0144  56  ALA A N   
329  C CA  . ALA A 43  ? 0.1778 0.1960 0.1270 0.0487  -0.0279 0.0193  56  ALA A CA  
330  C C   . ALA A 43  ? 0.1759 0.2066 0.1268 0.0484  -0.0317 0.0217  56  ALA A C   
331  O O   . ALA A 43  ? 0.1799 0.2136 0.1280 0.0475  -0.0334 0.0243  56  ALA A O   
332  C CB  . ALA A 43  ? 0.1859 0.1974 0.1358 0.0546  -0.0248 0.0231  56  ALA A CB  
333  N N   . HIS A 44  ? 0.1737 0.2125 0.1290 0.0484  -0.0327 0.0204  57  HIS A N   
334  C CA  . HIS A 44  ? 0.1712 0.2224 0.1288 0.0463  -0.0360 0.0212  57  HIS A CA  
335  C C   . HIS A 44  ? 0.1697 0.2201 0.1241 0.0399  -0.0372 0.0172  57  HIS A C   
336  O O   . HIS A 44  ? 0.1676 0.2263 0.1227 0.0364  -0.0395 0.0161  57  HIS A O   
337  C CB  . HIS A 44  ? 0.1669 0.2269 0.1313 0.0478  -0.0360 0.0215  57  HIS A CB  
338  C CG  . HIS A 44  ? 0.1615 0.2194 0.1273 0.0444  -0.0344 0.0175  57  HIS A CG  
339  N ND1 . HIS A 44  ? 0.1605 0.2151 0.1278 0.0473  -0.0314 0.0166  57  HIS A ND1 
340  C CD2 . HIS A 44  ? 0.1592 0.2179 0.1251 0.0389  -0.0348 0.0146  57  HIS A CD2 
341  C CE1 . HIS A 44  ? 0.1583 0.2132 0.1264 0.0441  -0.0304 0.0144  57  HIS A CE1 
342  N NE2 . HIS A 44  ? 0.1583 0.2145 0.1259 0.0391  -0.0320 0.0133  57  HIS A NE2 
343  N N   . CYS A 45  ? 0.1701 0.2112 0.1212 0.0383  -0.0351 0.0146  58  CYS A N   
344  C CA  . CYS A 45  ? 0.1714 0.2104 0.1190 0.0340  -0.0350 0.0116  58  CYS A CA  
345  C C   . CYS A 45  ? 0.1785 0.2159 0.1205 0.0334  -0.0356 0.0129  58  CYS A C   
346  O O   . CYS A 45  ? 0.1807 0.2160 0.1192 0.0306  -0.0348 0.0105  58  CYS A O   
347  C CB  . CYS A 45  ? 0.1688 0.2023 0.1165 0.0335  -0.0323 0.0094  58  CYS A CB  
348  S SG  . CYS A 45  ? 0.1657 0.2020 0.1186 0.0343  -0.0308 0.0086  58  CYS A SG  
349  N N   . TRP A 46  ? 0.1838 0.2223 0.1250 0.0366  -0.0364 0.0173  59  TRP A N   
350  C CA  . TRP A 46  ? 0.1908 0.2281 0.1265 0.0366  -0.0364 0.0199  59  TRP A CA  
351  C C   . TRP A 46  ? 0.1957 0.2411 0.1273 0.0334  -0.0388 0.0182  59  TRP A C   
352  O O   . TRP A 46  ? 0.1965 0.2508 0.1300 0.0320  -0.0415 0.0168  59  TRP A O   
353  C CB  . TRP A 46  ? 0.1964 0.2330 0.1323 0.0417  -0.0359 0.0265  59  TRP A CB  
354  C CG  . TRP A 46  ? 0.2028 0.2378 0.1331 0.0421  -0.0351 0.0308  59  TRP A CG  
355  C CD1 . TRP A 46  ? 0.2054 0.2300 0.1340 0.0418  -0.0315 0.0325  59  TRP A CD1 
356  C CD2 . TRP A 46  ? 0.2057 0.2513 0.1312 0.0424  -0.0377 0.0338  59  TRP A CD2 
357  N NE1 . TRP A 46  ? 0.2147 0.2417 0.1380 0.0424  -0.0312 0.0373  59  TRP A NE1 
358  C CE2 . TRP A 46  ? 0.2126 0.2529 0.1334 0.0431  -0.0351 0.0381  59  TRP A CE2 
359  C CE3 . TRP A 46  ? 0.2051 0.2651 0.1297 0.0414  -0.0419 0.0329  59  TRP A CE3 
360  C CZ2 . TRP A 46  ? 0.2200 0.2692 0.1344 0.0440  -0.0365 0.0423  59  TRP A CZ2 
361  C CZ3 . TRP A 46  ? 0.2119 0.2816 0.1300 0.0416  -0.0438 0.0360  59  TRP A CZ3 
362  C CH2 . TRP A 46  ? 0.2182 0.2827 0.1309 0.0434  -0.0411 0.0409  59  TRP A CH2 
363  N N   . GLY A 47  ? 0.2013 0.2439 0.1271 0.0318  -0.0376 0.0177  60  GLY A N   
364  C CA  . GLY A 47  ? 0.2094 0.2589 0.1290 0.0291  -0.0392 0.0157  60  GLY A CA  
365  C C   . GLY A 47  ? 0.2166 0.2639 0.1300 0.0301  -0.0374 0.0191  60  GLY A C   
366  O O   . GLY A 47  ? 0.2135 0.2530 0.1287 0.0314  -0.0345 0.0218  60  GLY A O   
367  N N   . SER A 48  ? 0.2267 0.2817 0.1329 0.0287  -0.0388 0.0185  61  SER A N   
368  C CA  . SER A 48  ? 0.2385 0.2933 0.1383 0.0298  -0.0367 0.0223  61  SER A CA  
369  C C   . SER A 48  ? 0.2447 0.2920 0.1428 0.0276  -0.0326 0.0182  61  SER A C   
370  O O   . SER A 48  ? 0.2470 0.2927 0.1422 0.0285  -0.0298 0.0219  61  SER A O   
371  C CB  . SER A 48  ? 0.2480 0.3156 0.1396 0.0296  -0.0394 0.0233  61  SER A CB  
372  O OG  . SER A 48  ? 0.2505 0.3231 0.1387 0.0248  -0.0412 0.0145  61  SER A OG  
373  N N   . ASN A 49  ? 0.2503 0.2940 0.1508 0.0253  -0.0318 0.0114  63  ASN A N   
374  C CA  . ASN A 49  ? 0.2634 0.3011 0.1637 0.0247  -0.0276 0.0083  63  ASN A CA  
375  C C   . ASN A 49  ? 0.2453 0.2777 0.1530 0.0246  -0.0268 0.0056  63  ASN A C   
376  O O   . ASN A 49  ? 0.2359 0.2684 0.1449 0.0230  -0.0283 0.0019  63  ASN A O   
377  C CB  . ASN A 49  ? 0.2972 0.3366 0.1894 0.0230  -0.0258 0.0030  63  ASN A CB  
378  C CG  . ASN A 49  ? 0.3320 0.3656 0.2243 0.0239  -0.0205 0.0001  63  ASN A CG  
379  O OD1 . ASN A 49  ? 0.3764 0.4057 0.2664 0.0228  -0.0182 -0.0060 63  ASN A OD1 
380  N ND2 . ASN A 49  ? 0.3383 0.3718 0.2333 0.0258  -0.0180 0.0047  63  ASN A ND2 
381  N N   . ILE A 50  ? 0.2363 0.2656 0.1488 0.0258  -0.0246 0.0077  64  ILE A N   
382  C CA  . ILE A 50  ? 0.2341 0.2605 0.1526 0.0265  -0.0236 0.0060  64  ILE A CA  
383  C C   . ILE A 50  ? 0.2335 0.2598 0.1528 0.0277  -0.0195 0.0059  64  ILE A C   
384  O O   . ILE A 50  ? 0.2333 0.2622 0.1530 0.0275  -0.0184 0.0087  64  ILE A O   
385  C CB  . ILE A 50  ? 0.2280 0.2539 0.1521 0.0270  -0.0255 0.0085  64  ILE A CB  
386  C CG1 . ILE A 50  ? 0.2317 0.2591 0.1558 0.0273  -0.0289 0.0098  64  ILE A CG1 
387  C CG2 . ILE A 50  ? 0.2228 0.2481 0.1522 0.0279  -0.0245 0.0070  64  ILE A CG2 
388  C CD1 . ILE A 50  ? 0.2297 0.2551 0.1578 0.0289  -0.0296 0.0128  64  ILE A CD1 
389  N N   . ASN A 51  ? 0.2377 0.2615 0.1579 0.0291  -0.0168 0.0033  65  ASN A N   
390  C CA  . ASN A 51  ? 0.2395 0.2649 0.1619 0.0320  -0.0127 0.0044  65  ASN A CA  
391  C C   . ASN A 51  ? 0.2272 0.2541 0.1561 0.0338  -0.0128 0.0059  65  ASN A C   
392  O O   . ASN A 51  ? 0.2284 0.2514 0.1588 0.0337  -0.0135 0.0046  65  ASN A O   
393  C CB  . ASN A 51  ? 0.2571 0.2777 0.1752 0.0340  -0.0079 0.0014  65  ASN A CB  
394  C CG  . ASN A 51  ? 0.2767 0.2974 0.1870 0.0325  -0.0072 -0.0005 65  ASN A CG  
395  O OD1 . ASN A 51  ? 0.3038 0.3189 0.2085 0.0322  -0.0044 -0.0053 65  ASN A OD1 
396  N ND2 . ASN A 51  ? 0.2748 0.3013 0.1840 0.0311  -0.0094 0.0026  65  ASN A ND2 
397  N N   . VAL A 52  ? 0.2174 0.2518 0.1504 0.0353  -0.0119 0.0088  66  VAL A N   
398  C CA  . VAL A 52  ? 0.2080 0.2473 0.1462 0.0371  -0.0123 0.0105  66  VAL A CA  
399  C C   . VAL A 52  ? 0.2091 0.2530 0.1496 0.0424  -0.0077 0.0132  66  VAL A C   
400  O O   . VAL A 52  ? 0.2128 0.2618 0.1531 0.0440  -0.0051 0.0147  66  VAL A O   
401  C CB  . VAL A 52  ? 0.2058 0.2524 0.1468 0.0339  -0.0153 0.0111  66  VAL A CB  
402  C CG1 . VAL A 52  ? 0.2029 0.2559 0.1479 0.0351  -0.0164 0.0117  66  VAL A CG1 
403  C CG2 . VAL A 52  ? 0.2075 0.2479 0.1462 0.0299  -0.0183 0.0096  66  VAL A CG2 
404  N N   . THR A 53  ? 0.2005 0.2433 0.1434 0.0459  -0.0062 0.0148  67  THR A N   
405  C CA  . THR A 53  ? 0.2032 0.2521 0.1492 0.0524  -0.0016 0.0194  67  THR A CA  
406  C C   . THR A 53  ? 0.1975 0.2593 0.1480 0.0538  -0.0038 0.0227  67  THR A C   
407  O O   . THR A 53  ? 0.1927 0.2519 0.1436 0.0529  -0.0057 0.0221  67  THR A O   
408  C CB  . THR A 53  ? 0.2109 0.2470 0.1555 0.0564  0.0039  0.0196  67  THR A CB  
409  O OG1 . THR A 53  ? 0.2172 0.2424 0.1564 0.0538  0.0055  0.0149  67  THR A OG1 
410  C CG2 . THR A 53  ? 0.2193 0.2602 0.1669 0.0649  0.0101  0.0257  67  THR A CG2 
411  N N   . LEU A 54  ? 0.1964 0.2740 0.1502 0.0558  -0.0037 0.0258  68  LEU A N   
412  C CA  . LEU A 54  ? 0.1952 0.2892 0.1528 0.0579  -0.0053 0.0293  68  LEU A CA  
413  C C   . LEU A 54  ? 0.1970 0.2989 0.1576 0.0675  0.0001  0.0368  68  LEU A C   
414  O O   . LEU A 54  ? 0.1999 0.2958 0.1600 0.0716  0.0051  0.0384  68  LEU A O   
415  C CB  . LEU A 54  ? 0.1969 0.3046 0.1562 0.0517  -0.0096 0.0268  68  LEU A CB  
416  C CG  . LEU A 54  ? 0.2061 0.3031 0.1623 0.0434  -0.0135 0.0205  68  LEU A CG  
417  C CD1 . LEU A 54  ? 0.2120 0.3145 0.1692 0.0375  -0.0145 0.0187  68  LEU A CD1 
418  C CD2 . LEU A 54  ? 0.2114 0.3102 0.1673 0.0406  -0.0170 0.0179  68  LEU A CD2 
419  N N   . GLY A 55  ? 0.1923 0.3077 0.1556 0.0717  -0.0002 0.0416  69  GLY A N   
420  C CA  . GLY A 55  ? 0.1961 0.3221 0.1627 0.0822  0.0050  0.0506  69  GLY A CA  
421  C C   . GLY A 55  ? 0.2036 0.3112 0.1690 0.0892  0.0120  0.0546  69  GLY A C   
422  O O   . GLY A 55  ? 0.2106 0.3216 0.1785 0.0992  0.0185  0.0627  69  GLY A O   
423  N N   . ALA A 56  ? 0.2017 0.2906 0.1639 0.0841  0.0112  0.0496  70  ALA A N   
424  C CA  . ALA A 56  ? 0.2153 0.2839 0.1764 0.0880  0.0182  0.0515  70  ALA A CA  
425  C C   . ALA A 56  ? 0.2229 0.2931 0.1856 0.0917  0.0198  0.0574  70  ALA A C   
426  O O   . ALA A 56  ? 0.2172 0.2996 0.1800 0.0886  0.0141  0.0567  70  ALA A O   
427  C CB  . ALA A 56  ? 0.2178 0.2671 0.1750 0.0796  0.0167  0.0426  70  ALA A CB  
428  N N   . HIS A 57  ? 0.2379 0.2948 0.2015 0.0986  0.0285  0.0632  71  HIS A N   
429  C CA  . HIS A 57  ? 0.2474 0.2989 0.2121 0.1006  0.0316  0.0682  71  HIS A CA  
430  C C   . HIS A 57  ? 0.2610 0.2851 0.2244 0.0967  0.0373  0.0640  71  HIS A C   
431  O O   . HIS A 57  ? 0.2606 0.2779 0.2236 0.0892  0.0344  0.0594  71  HIS A O   
432  C CB  . HIS A 57  ? 0.2499 0.3153 0.2177 0.1128  0.0368  0.0812  71  HIS A CB  
433  C CG  . HIS A 57  ? 0.2555 0.3172 0.2241 0.1150  0.0400  0.0874  71  HIS A CG  
434  N ND1 . HIS A 57  ? 0.2453 0.3171 0.2130 0.1093  0.0333  0.0846  71  HIS A ND1 
435  C CD2 . HIS A 57  ? 0.2690 0.3172 0.2395 0.1219  0.0498  0.0960  71  HIS A CD2 
436  C CE1 . HIS A 57  ? 0.2506 0.3170 0.2194 0.1128  0.0386  0.0917  71  HIS A CE1 
437  N NE2 . HIS A 57  ? 0.2668 0.3186 0.2376 0.1203  0.0487  0.0990  71  HIS A NE2 
438  N N   . ASN A 58  ? 0.2802 0.2894 0.2431 0.1012  0.0456  0.0651  72  ASN A N   
439  C CA  . ASN A 58  ? 0.2995 0.2825 0.2601 0.0955  0.0508  0.0583  72  ASN A CA  
440  C C   . ASN A 58  ? 0.3012 0.2801 0.2574 0.0885  0.0467  0.0475  72  ASN A C   
441  O O   . ASN A 58  ? 0.3024 0.2795 0.2569 0.0934  0.0508  0.0476  72  ASN A O   
442  C CB  . ASN A 58  ? 0.3220 0.2875 0.2838 0.1042  0.0638  0.0652  72  ASN A CB  
443  C CG  . ASN A 58  ? 0.3425 0.2801 0.3018 0.0965  0.0696  0.0568  72  ASN A CG  
444  O OD1 . ASN A 58  ? 0.3441 0.2775 0.2996 0.0861  0.0640  0.0453  72  ASN A OD1 
445  N ND2 . ASN A 58  ? 0.3634 0.2820 0.3245 0.1012  0.0811  0.0624  72  ASN A ND2 
446  N N   A ILE A 59  ? 0.2988 0.2769 0.2530 0.0777  0.0391  0.0389  73  ILE A N   
447  N N   B ILE A 59  ? 0.2949 0.2729 0.2492 0.0777  0.0392  0.0390  73  ILE A N   
448  C CA  A ILE A 59  ? 0.2993 0.2778 0.2490 0.0714  0.0340  0.0301  73  ILE A CA  
449  C CA  B ILE A 59  ? 0.2922 0.2705 0.2420 0.0712  0.0340  0.0300  73  ILE A CA  
450  C C   A ILE A 59  ? 0.3188 0.2768 0.2639 0.0682  0.0402  0.0230  73  ILE A C   
451  C C   B ILE A 59  ? 0.3153 0.2734 0.2605 0.0689  0.0406  0.0235  73  ILE A C   
452  O O   A ILE A 59  ? 0.3173 0.2751 0.2576 0.0638  0.0371  0.0160  73  ILE A O   
453  O O   B ILE A 59  ? 0.3150 0.2734 0.2554 0.0658  0.0383  0.0173  73  ILE A O   
454  C CB  A ILE A 59  ? 0.2891 0.2760 0.2386 0.0626  0.0241  0.0250  73  ILE A CB  
455  C CB  B ILE A 59  ? 0.2777 0.2617 0.2271 0.0618  0.0247  0.0243  73  ILE A CB  
456  C CG1 A ILE A 59  ? 0.2939 0.2725 0.2453 0.0570  0.0241  0.0231  73  ILE A CG1 
457  C CG1 B ILE A 59  ? 0.2688 0.2590 0.2142 0.0575  0.0186  0.0185  73  ILE A CG1 
458  C CG2 A ILE A 59  ? 0.2790 0.2860 0.2309 0.0651  0.0180  0.0293  73  ILE A CG2 
459  C CG2 B ILE A 59  ? 0.2860 0.2558 0.2354 0.0546  0.0263  0.0195  73  ILE A CG2 
460  C CD1 A ILE A 59  ? 0.3055 0.2687 0.2535 0.0491  0.0259  0.0145  73  ILE A CD1 
461  C CD1 B ILE A 59  ? 0.2594 0.2664 0.2062 0.0618  0.0155  0.0226  73  ILE A CD1 
462  N N   . GLN A 60  ? 0.3421 0.2825 0.2882 0.0700  0.0492  0.0246  74  GLN A N   
463  C CA  . GLN A 60  ? 0.3792 0.2980 0.3203 0.0663  0.0563  0.0166  74  GLN A CA  
464  C C   . GLN A 60  ? 0.3897 0.3006 0.3288 0.0767  0.0660  0.0199  74  GLN A C   
465  O O   . GLN A 60  ? 0.4124 0.3060 0.3458 0.0744  0.0722  0.0121  74  GLN A O   
466  C CB  . GLN A 60  ? 0.4077 0.3084 0.3507 0.0605  0.0618  0.0145  74  GLN A CB  
467  C CG  . GLN A 60  ? 0.4190 0.3253 0.3629 0.0483  0.0531  0.0081  74  GLN A CG  
468  C CD  . GLN A 60  ? 0.4376 0.3482 0.3753 0.0401  0.0460  -0.0026 74  GLN A CD  
469  O OE1 . GLN A 60  ? 0.4579 0.3857 0.3957 0.0380  0.0362  -0.0028 74  GLN A OE1 
470  N NE2 . GLN A 60  ? 0.4654 0.3601 0.3971 0.0356  0.0514  -0.0115 74  GLN A NE2 
471  N N   . ARG A 61  ? 0.3834 0.3082 0.3269 0.0881  0.0675  0.0310  75  ARG A N   
472  C CA  . ARG A 61  ? 0.3919 0.3132 0.3350 0.0999  0.0769  0.0361  75  ARG A CA  
473  C C   . ARG A 61  ? 0.3621 0.3085 0.3065 0.1044  0.0707  0.0396  75  ARG A C   
474  O O   . ARG A 61  ? 0.3349 0.3014 0.2821 0.1010  0.0608  0.0415  75  ARG A O   
475  C CB  . ARG A 61  ? 0.4117 0.3275 0.3602 0.1110  0.0864  0.0485  75  ARG A CB  
476  C CG  . ARG A 61  ? 0.4382 0.3294 0.3867 0.1054  0.0928  0.0460  75  ARG A CG  
477  C CD  . ARG A 61  ? 0.4636 0.3403 0.4159 0.1174  0.1066  0.0575  75  ARG A CD  
478  N NE  . ARG A 61  ? 0.4597 0.3551 0.4185 0.1254  0.1047  0.0717  75  ARG A NE  
479  C CZ  . ARG A 61  ? 0.4814 0.3669 0.4439 0.1350  0.1154  0.0837  75  ARG A CZ  
480  N NH1 . ARG A 61  ? 0.5107 0.3653 0.4717 0.1374  0.1292  0.0827  75  ARG A NH1 
481  N NH2 . ARG A 61  ? 0.4767 0.3827 0.4440 0.1423  0.1128  0.0965  75  ARG A NH2 
482  N N   . ARG A 62  ? 0.3602 0.3048 0.3024 0.1117  0.0773  0.0401  76  ARG A N   
483  C CA  . ARG A 62  ? 0.3441 0.3131 0.2889 0.1169  0.0735  0.0447  76  ARG A CA  
484  C C   . ARG A 62  ? 0.3432 0.3324 0.2961 0.1270  0.0736  0.0582  76  ARG A C   
485  O O   . ARG A 62  ? 0.3647 0.3454 0.3203 0.1366  0.0825  0.0664  76  ARG A O   
486  C CB  . ARG A 62  ? 0.3503 0.3137 0.2918 0.1245  0.0824  0.0437  76  ARG A CB  
487  C CG  . ARG A 62  ? 0.3474 0.3007 0.2801 0.1156  0.0808  0.0310  76  ARG A CG  
488  C CD  . ARG A 62  ? 0.3620 0.3045 0.2900 0.1236  0.0920  0.0290  76  ARG A CD  
489  N NE  . ARG A 62  ? 0.3491 0.3146 0.2815 0.1324  0.0926  0.0364  76  ARG A NE  
490  C CZ  . ARG A 62  ? 0.3560 0.3182 0.2865 0.1424  0.1028  0.0378  76  ARG A CZ  
491  N NH1 . ARG A 62  ? 0.3793 0.3136 0.3031 0.1458  0.1144  0.0321  76  ARG A NH1 
492  N NH2 . ARG A 62  ? 0.3448 0.3321 0.2807 0.1489  0.1019  0.0449  76  ARG A NH2 
493  N N   . GLU A 63  ? 0.3251 0.3415 0.2817 0.1247  0.0639  0.0607  77  GLU A N   
494  C CA  . GLU A 63  ? 0.3214 0.3630 0.2852 0.1344  0.0637  0.0727  77  GLU A CA  
495  C C   . GLU A 63  ? 0.2959 0.3632 0.2621 0.1321  0.0571  0.0721  77  GLU A C   
496  O O   . GLU A 63  ? 0.2794 0.3487 0.2429 0.1206  0.0489  0.0637  77  GLU A O   
497  C CB  . GLU A 63  ? 0.3229 0.3742 0.2895 0.1324  0.0581  0.0772  77  GLU A CB  
498  C CG  . GLU A 63  ? 0.3379 0.3657 0.3009 0.1248  0.0581  0.0714  77  GLU A CG  
499  C CD  . GLU A 63  ? 0.3361 0.3758 0.3011 0.1204  0.0506  0.0733  77  GLU A CD  
500  O OE1 . GLU A 63  ? 0.3090 0.3475 0.2715 0.1091  0.0425  0.0648  77  GLU A OE1 
501  O OE2 . GLU A 63  ? 0.3528 0.4036 0.3215 0.1294  0.0537  0.0842  77  GLU A OE2 
502  N N   . ASN A 64  ? 0.2882 0.3760 0.2603 0.1431  0.0610  0.0818  78  ASN A N   
503  C CA  . ASN A 64  ? 0.2719 0.3848 0.2476 0.1412  0.0563  0.0818  78  ASN A CA  
504  C C   . ASN A 64  ? 0.2509 0.3871 0.2296 0.1317  0.0444  0.0804  78  ASN A C   
505  O O   . ASN A 64  ? 0.2423 0.3997 0.2244 0.1273  0.0396  0.0794  78  ASN A O   
506  C CB  . ASN A 64  ? 0.2804 0.4092 0.2619 0.1559  0.0646  0.0925  78  ASN A CB  
507  C CG  . ASN A 64  ? 0.2803 0.4290 0.2686 0.1675  0.0666  0.1059  78  ASN A CG  
508  O OD1 . ASN A 64  ? 0.2890 0.4490 0.2824 0.1817  0.0747  0.1162  78  ASN A OD1 
509  N ND2 . ASN A 64  ? 0.2686 0.4234 0.2571 0.1628  0.0598  0.1067  78  ASN A ND2 
510  N N   . THR A 65  ? 0.2445 0.3761 0.2219 0.1281  0.0404  0.0799  79  THR A N   
511  C CA  . THR A 65  ? 0.2279 0.3771 0.2064 0.1186  0.0299  0.0767  79  THR A CA  
512  C C   . THR A 65  ? 0.2196 0.3539 0.1929 0.1048  0.0237  0.0648  79  THR A C   
513  O O   . THR A 65  ? 0.2093 0.3565 0.1834 0.0960  0.0159  0.0607  79  THR A O   
514  C CB  . THR A 65  ? 0.2276 0.3800 0.2066 0.1219  0.0289  0.0819  79  THR A CB  
515  O OG1 . THR A 65  ? 0.2314 0.3542 0.2057 0.1210  0.0329  0.0789  79  THR A OG1 
516  C CG2 . THR A 65  ? 0.2362 0.4075 0.2206 0.1363  0.0345  0.0955  79  THR A CG2 
517  N N   . GLN A 66  ? 0.2268 0.3345 0.1946 0.1030  0.0276  0.0592  80  GLN A N   
518  C CA  . GLN A 66  ? 0.2227 0.3167 0.1853 0.0914  0.0220  0.0493  80  GLN A CA  
519  C C   . GLN A 66  ? 0.2207 0.3234 0.1831 0.0852  0.0186  0.0454  80  GLN A C   
520  O O   . GLN A 66  ? 0.2258 0.3353 0.1899 0.0900  0.0231  0.0482  80  GLN A O   
521  C CB  . GLN A 66  ? 0.2322 0.2986 0.1890 0.0908  0.0267  0.0446  80  GLN A CB  
522  C CG  . GLN A 66  ? 0.2388 0.2942 0.1961 0.0938  0.0295  0.0473  80  GLN A CG  
523  C CD  . GLN A 66  ? 0.2561 0.2849 0.2083 0.0917  0.0347  0.0418  80  GLN A CD  
524  O OE1 . GLN A 66  ? 0.2614 0.2807 0.2086 0.0866  0.0344  0.0346  80  GLN A OE1 
525  N NE2 . GLN A 66  ? 0.2676 0.2849 0.2209 0.0949  0.0394  0.0451  80  GLN A NE2 
526  N N   . GLN A 67  ? 0.2092 0.3105 0.2062 0.0706  0.0128  0.0352  81  GLN A N   
527  C CA  . GLN A 67  ? 0.2142 0.3194 0.2072 0.0637  0.0113  0.0296  81  GLN A CA  
528  C C   . GLN A 67  ? 0.2149 0.3046 0.2011 0.0575  0.0101  0.0245  81  GLN A C   
529  O O   . GLN A 67  ? 0.2062 0.2902 0.1893 0.0543  0.0070  0.0249  81  GLN A O   
530  C CB  . GLN A 67  ? 0.2109 0.3323 0.2040 0.0590  0.0073  0.0302  81  GLN A CB  
531  C CG  . GLN A 67  ? 0.2135 0.3556 0.2135 0.0646  0.0080  0.0340  81  GLN A CG  
532  C CD  . GLN A 67  ? 0.2095 0.3696 0.2109 0.0586  0.0041  0.0324  81  GLN A CD  
533  O OE1 . GLN A 67  ? 0.2089 0.3688 0.2083 0.0500  0.0032  0.0277  81  GLN A OE1 
534  N NE2 . GLN A 67  ? 0.2149 0.3914 0.2201 0.0633  0.0021  0.0363  81  GLN A NE2 
535  N N   . HIS A 68  ? 0.2232 0.3085 0.2069 0.0565  0.0127  0.0198  82  HIS A N   
536  C CA  . HIS A 68  ? 0.2302 0.3044 0.2073 0.0519  0.0117  0.0148  82  HIS A CA  
537  C C   . HIS A 68  ? 0.2245 0.3043 0.1958 0.0463  0.0103  0.0136  82  HIS A C   
538  O O   . HIS A 68  ? 0.2242 0.3112 0.1954 0.0468  0.0130  0.0125  82  HIS A O   
539  C CB  . HIS A 68  ? 0.2505 0.3171 0.2287 0.0553  0.0161  0.0094  82  HIS A CB  
540  C CG  . HIS A 68  ? 0.2664 0.3245 0.2519 0.0608  0.0193  0.0107  82  HIS A CG  
541  N ND1 . HIS A 68  ? 0.2742 0.3212 0.2602 0.0592  0.0185  0.0105  82  HIS A ND1 
542  C CD2 . HIS A 68  ? 0.2775 0.3363 0.2706 0.0682  0.0241  0.0132  82  HIS A CD2 
543  C CE1 . HIS A 68  ? 0.2816 0.3217 0.2756 0.0649  0.0231  0.0131  82  HIS A CE1 
544  N NE2 . HIS A 68  ? 0.2812 0.3277 0.2795 0.0709  0.0266  0.0150  82  HIS A NE2 
545  N N   . ILE A 69  ? 0.2176 0.2935 0.1842 0.0412  0.0066  0.0143  83  ILE A N   
546  C CA  . ILE A 69  ? 0.2137 0.2926 0.1759 0.0360  0.0060  0.0151  83  ILE A CA  
547  C C   . ILE A 69  ? 0.2122 0.2820 0.1672 0.0338  0.0040  0.0138  83  ILE A C   
548  O O   . ILE A 69  ? 0.2028 0.2661 0.1574 0.0336  0.0012  0.0137  83  ILE A O   
549  C CB  . ILE A 69  ? 0.2109 0.2961 0.1768 0.0324  0.0041  0.0178  83  ILE A CB  
550  C CG1 . ILE A 69  ? 0.2111 0.3091 0.1847 0.0356  0.0052  0.0190  83  ILE A CG1 
551  C CG2 . ILE A 69  ? 0.2126 0.2990 0.1759 0.0266  0.0051  0.0188  83  ILE A CG2 
552  C CD1 . ILE A 69  ? 0.2080 0.3158 0.1859 0.0321  0.0027  0.0198  83  ILE A CD1 
553  N N   . THR A 70  ? 0.2187 0.2899 0.1679 0.0327  0.0055  0.0133  84  THR A N   
554  C CA  . THR A 70  ? 0.2265 0.2925 0.1685 0.0315  0.0036  0.0133  84  THR A CA  
555  C C   . THR A 70  ? 0.2249 0.2877 0.1662 0.0278  0.0022  0.0181  84  THR A C   
556  O O   . THR A 70  ? 0.2297 0.2962 0.1746 0.0250  0.0040  0.0206  84  THR A O   
557  C CB  . THR A 70  ? 0.2416 0.3129 0.1770 0.0328  0.0058  0.0116  84  THR A CB  
558  O OG1 . THR A 70  ? 0.2713 0.3488 0.2060 0.0310  0.0090  0.0161  84  THR A OG1 
559  C CG2 . THR A 70  ? 0.2422 0.3166 0.1794 0.0361  0.0081  0.0050  84  THR A CG2 
560  N N   . ALA A 71  ? 0.2211 0.2772 0.1590 0.0277  -0.0006 0.0186  85  ALA A N   
561  C CA  . ALA A 71  ? 0.2196 0.2707 0.1569 0.0250  -0.0012 0.0226  85  ALA A CA  
562  C C   . ALA A 71  ? 0.2246 0.2763 0.1561 0.0248  0.0015  0.0275  85  ALA A C   
563  O O   . ALA A 71  ? 0.2206 0.2744 0.1453 0.0279  0.0010  0.0278  85  ALA A O   
564  C CB  . ALA A 71  ? 0.2178 0.2626 0.1540 0.0261  -0.0049 0.0217  85  ALA A CB  
565  N N   . ARG A 72  ? 0.2252 0.2759 0.1598 0.0209  0.0048  0.0314  86  ARG A N   
566  C CA  . ARG A 72  ? 0.2351 0.2852 0.1654 0.0204  0.0088  0.0381  86  ARG A CA  
567  C C   . ARG A 72  ? 0.2464 0.2870 0.1728 0.0222  0.0080  0.0428  86  ARG A C   
568  O O   . ARG A 72  ? 0.2530 0.2948 0.1728 0.0252  0.0100  0.0489  86  ARG A O   
569  C CB  . ARG A 72  ? 0.2328 0.2843 0.1697 0.0147  0.0135  0.0405  86  ARG A CB  
570  C CG  . ARG A 72  ? 0.2432 0.2930 0.1769 0.0136  0.0192  0.0490  86  ARG A CG  
571  C CD  . ARG A 72  ? 0.2438 0.3039 0.1690 0.0181  0.0210  0.0517  86  ARG A CD  
572  N NE  . ARG A 72  ? 0.2543 0.3134 0.1748 0.0185  0.0265  0.0620  86  ARG A NE  
573  C CZ  . ARG A 72  ? 0.2623 0.3152 0.1765 0.0226  0.0267  0.0690  86  ARG A CZ  
574  N NH1 . ARG A 72  ? 0.2546 0.3025 0.1664 0.0262  0.0212  0.0659  86  ARG A NH1 
575  N NH2 . ARG A 72  ? 0.2758 0.3290 0.1860 0.0237  0.0327  0.0799  86  ARG A NH2 
576  N N   . ARG A 73  ? 0.2549 0.2878 0.1857 0.0209  0.0054  0.0402  87  ARG A N   
577  C CA  . ARG A 73  ? 0.2752 0.2987 0.2037 0.0233  0.0047  0.0438  87  ARG A CA  
578  C C   . ARG A 73  ? 0.2567 0.2787 0.1868 0.0248  -0.0005 0.0380  87  ARG A C   
579  O O   . ARG A 73  ? 0.2424 0.2660 0.1781 0.0219  -0.0021 0.0325  87  ARG A O   
580  C CB  . ARG A 73  ? 0.3083 0.3213 0.2427 0.0188  0.0093  0.0474  87  ARG A CB  
581  C CG  . ARG A 73  ? 0.3479 0.3594 0.2811 0.0175  0.0158  0.0558  87  ARG A CG  
582  C CD  . ARG A 73  ? 0.3865 0.3874 0.3163 0.0215  0.0190  0.0650  87  ARG A CD  
583  N NE  . ARG A 73  ? 0.4296 0.4158 0.3684 0.0165  0.0233  0.0653  87  ARG A NE  
584  C CZ  . ARG A 73  ? 0.4721 0.4448 0.4119 0.0196  0.0251  0.0694  87  ARG A CZ  
585  N NH1 . ARG A 73  ? 0.4983 0.4722 0.4305 0.0283  0.0219  0.0734  87  ARG A NH1 
586  N NH2 . ARG A 73  ? 0.4885 0.4472 0.4377 0.0140  0.0304  0.0685  87  ARG A NH2 
587  N N   . ALA A 74  ? 0.2527 0.2736 0.1779 0.0297  -0.0029 0.0396  88  ALA A N   
588  C CA  . ALA A 74  ? 0.2419 0.2614 0.1688 0.0312  -0.0072 0.0351  88  ALA A CA  
589  C C   . ALA A 74  ? 0.2455 0.2559 0.1725 0.0336  -0.0065 0.0391  88  ALA A C   
590  O O   . ALA A 74  ? 0.2519 0.2635 0.1735 0.0389  -0.0067 0.0441  88  ALA A O   
591  C CB  . ALA A 74  ? 0.2390 0.2671 0.1619 0.0344  -0.0107 0.0319  88  ALA A CB  
592  N N   . ILE A 75  ? 0.2397 0.2423 0.1730 0.0302  -0.0054 0.0364  89  ILE A N   
593  C CA  . ILE A 75  ? 0.2453 0.2366 0.1807 0.0317  -0.0031 0.0393  89  ILE A CA  
594  C C   . ILE A 75  ? 0.2406 0.2318 0.1774 0.0343  -0.0069 0.0345  89  ILE A C   
595  O O   . ILE A 75  ? 0.2257 0.2171 0.1674 0.0307  -0.0080 0.0279  89  ILE A O   
596  C CB  . ILE A 75  ? 0.2503 0.2328 0.1927 0.0253  0.0018  0.0382  89  ILE A CB  
597  C CG1 . ILE A 75  ? 0.2538 0.2391 0.1956 0.0219  0.0057  0.0426  89  ILE A CG1 
598  C CG2 . ILE A 75  ? 0.2629 0.2307 0.2085 0.0270  0.0057  0.0412  89  ILE A CG2 
599  C CD1 . ILE A 75  ? 0.2601 0.2398 0.2106 0.0140  0.0106  0.0402  89  ILE A CD1 
600  N N   . ARG A 76  ? 0.2461 0.2394 0.1784 0.0409  -0.0088 0.0380  90  ARG A N   
601  C CA  . ARG A 76  ? 0.2508 0.2446 0.1847 0.0441  -0.0117 0.0347  90  ARG A CA  
602  C C   . ARG A 76  ? 0.2588 0.2393 0.1971 0.0452  -0.0081 0.0355  90  ARG A C   
603  O O   . ARG A 76  ? 0.2679 0.2384 0.2067 0.0457  -0.0032 0.0414  90  ARG A O   
604  C CB  . ARG A 76  ? 0.2626 0.2653 0.1911 0.0509  -0.0147 0.0381  90  ARG A CB  
605  C CG  . ARG A 76  ? 0.2657 0.2812 0.1913 0.0492  -0.0180 0.0348  90  ARG A CG  
606  C CD  . ARG A 76  ? 0.2801 0.3069 0.2018 0.0548  -0.0213 0.0358  90  ARG A CD  
607  N NE  . ARG A 76  ? 0.3071 0.3365 0.2228 0.0602  -0.0197 0.0439  90  ARG A NE  
608  C CZ  . ARG A 76  ? 0.3337 0.3768 0.2448 0.0657  -0.0224 0.0457  90  ARG A CZ  
609  N NH1 . ARG A 76  ? 0.3407 0.3941 0.2538 0.0664  -0.0266 0.0398  90  ARG A NH1 
610  N NH2 . ARG A 76  ? 0.3501 0.3980 0.2547 0.0706  -0.0207 0.0536  90  ARG A NH2 
611  N N   . HIS A 77  ? 0.2528 0.2331 0.1947 0.0456  -0.0098 0.0293  91  HIS A N   
612  C CA  . HIS A 77  ? 0.2628 0.2311 0.2090 0.0480  -0.0065 0.0286  91  HIS A CA  
613  C C   . HIS A 77  ? 0.2748 0.2387 0.2177 0.0567  -0.0047 0.0382  91  HIS A C   
614  O O   . HIS A 77  ? 0.2642 0.2398 0.2020 0.0618  -0.0086 0.0412  91  HIS A O   
615  C CB  . HIS A 77  ? 0.2545 0.2278 0.2035 0.0488  -0.0095 0.0208  91  HIS A CB  
616  C CG  . HIS A 77  ? 0.2664 0.2275 0.2212 0.0495  -0.0055 0.0167  91  HIS A CG  
617  N ND1 . HIS A 77  ? 0.2800 0.2315 0.2356 0.0572  -0.0026 0.0214  91  HIS A ND1 
618  C CD2 . HIS A 77  ? 0.2700 0.2269 0.2305 0.0435  -0.0035 0.0079  91  HIS A CD2 
619  C CE1 . HIS A 77  ? 0.2888 0.2286 0.2510 0.0557  0.0014  0.0152  91  HIS A CE1 
620  N NE2 . HIS A 77  ? 0.2839 0.2276 0.2491 0.0470  0.0008  0.0062  91  HIS A NE2 
621  N N   . PRO A 78  ? 0.2969 0.2448 0.2429 0.0588  0.0014  0.0433  92  PRO A N   
622  C CA  . PRO A 78  ? 0.3145 0.2587 0.2573 0.0688  0.0039  0.0547  92  PRO A CA  
623  C C   . PRO A 78  ? 0.3213 0.2719 0.2632 0.0780  0.0007  0.0551  92  PRO A C   
624  O O   . PRO A 78  ? 0.3248 0.2801 0.2624 0.0872  0.0007  0.0647  92  PRO A O   
625  C CB  . PRO A 78  ? 0.3321 0.2545 0.2811 0.0678  0.0126  0.0590  92  PRO A CB  
626  C CG  . PRO A 78  ? 0.3277 0.2435 0.2847 0.0582  0.0137  0.0460  92  PRO A CG  
627  C CD  . PRO A 78  ? 0.3060 0.2394 0.2597 0.0517  0.0070  0.0388  92  PRO A CD  
628  N N   . GLN A 79  ? 0.3226 0.2760 0.2685 0.0760  -0.0019 0.0450  93  GLN A N   
629  C CA  . GLN A 79  ? 0.3309 0.2918 0.2770 0.0843  -0.0046 0.0445  93  GLN A CA  
630  C C   . GLN A 79  ? 0.3026 0.2834 0.2462 0.0818  -0.0116 0.0384  93  GLN A C   
631  O O   . GLN A 79  ? 0.2963 0.2849 0.2417 0.0861  -0.0140 0.0352  93  GLN A O   
632  C CB  . GLN A 79  ? 0.3588 0.3068 0.3121 0.0859  -0.0008 0.0386  93  GLN A CB  
633  C CG  . GLN A 79  ? 0.3989 0.3271 0.3559 0.0924  0.0067  0.0465  93  GLN A CG  
634  C CD  . GLN A 79  ? 0.4265 0.3365 0.3880 0.0841  0.0131  0.0453  93  GLN A CD  
635  O OE1 . GLN A 79  ? 0.4605 0.3611 0.4209 0.0855  0.0178  0.0557  93  GLN A OE1 
636  N NE2 . GLN A 79  ? 0.4314 0.3378 0.3985 0.0754  0.0136  0.0324  93  GLN A NE2 
637  N N   . TYR A 80  ? 0.2855 0.2741 0.2256 0.0752  -0.0143 0.0372  94  TYR A N   
638  C CA  . TYR A 80  ? 0.2660 0.2715 0.2046 0.0727  -0.0197 0.0325  94  TYR A CA  
639  C C   . TYR A 80  ? 0.2692 0.2883 0.2052 0.0806  -0.0228 0.0365  94  TYR A C   
640  O O   . TYR A 80  ? 0.2676 0.2887 0.1993 0.0861  -0.0221 0.0443  94  TYR A O   
641  C CB  . TYR A 80  ? 0.2568 0.2669 0.1928 0.0655  -0.0211 0.0310  94  TYR A CB  
642  C CG  . TYR A 80  ? 0.2440 0.2701 0.1788 0.0642  -0.0256 0.0276  94  TYR A CG  
643  C CD1 . TYR A 80  ? 0.2327 0.2645 0.1716 0.0612  -0.0275 0.0213  94  TYR A CD1 
644  C CD2 . TYR A 80  ? 0.2445 0.2810 0.1749 0.0658  -0.0275 0.0302  94  TYR A CD2 
645  C CE1 . TYR A 80  ? 0.2243 0.2690 0.1639 0.0592  -0.0304 0.0182  94  TYR A CE1 
646  C CE2 . TYR A 80  ? 0.2344 0.2848 0.1655 0.0634  -0.0310 0.0253  94  TYR A CE2 
647  C CZ  . TYR A 80  ? 0.2254 0.2788 0.1617 0.0599  -0.0321 0.0195  94  TYR A CZ  
648  O OH  . TYR A 80  ? 0.2232 0.2885 0.1620 0.0568  -0.0343 0.0147  94  TYR A OH  
649  N N   . ASN A 81  ? 0.2633 0.2938 0.2022 0.0811  -0.0259 0.0312  95  ASN A N   
650  C CA  . ASN A 81  ? 0.2692 0.3156 0.2075 0.0880  -0.0290 0.0332  95  ASN A CA  
651  C C   . ASN A 81  ? 0.2534 0.3162 0.1927 0.0822  -0.0332 0.0271  95  ASN A C   
652  O O   . ASN A 81  ? 0.2421 0.3068 0.1857 0.0776  -0.0337 0.0211  95  ASN A O   
653  C CB  . ASN A 81  ? 0.2807 0.3263 0.2236 0.0945  -0.0281 0.0322  95  ASN A CB  
654  C CG  . ASN A 81  ? 0.2911 0.3540 0.2340 0.1034  -0.0308 0.0356  95  ASN A CG  
655  O OD1 . ASN A 81  ? 0.2881 0.3697 0.2313 0.1010  -0.0350 0.0322  95  ASN A OD1 
656  N ND2 . ASN A 81  ? 0.3132 0.3707 0.2567 0.1138  -0.0282 0.0420  95  ASN A ND2 
657  N N   . GLN A 82  ? 0.2532 0.3285 0.1888 0.0825  -0.0357 0.0284  96  GLN A N   
658  C CA  . GLN A 82  ? 0.2429 0.3327 0.1806 0.0763  -0.0387 0.0216  96  GLN A CA  
659  C C   . GLN A 82  ? 0.2333 0.3363 0.1770 0.0774  -0.0408 0.0174  96  GLN A C   
660  O O   . GLN A 82  ? 0.2175 0.3243 0.1661 0.0705  -0.0411 0.0113  96  GLN A O   
661  C CB  . GLN A 82  ? 0.2525 0.3561 0.1854 0.0775  -0.0410 0.0225  96  GLN A CB  
662  C CG  . GLN A 82  ? 0.2522 0.3698 0.1885 0.0702  -0.0435 0.0136  96  GLN A CG  
663  C CD  . GLN A 82  ? 0.2646 0.3965 0.1959 0.0706  -0.0455 0.0123  96  GLN A CD  
664  O OE1 . GLN A 82  ? 0.2837 0.4184 0.2081 0.0777  -0.0456 0.0195  96  GLN A OE1 
665  N NE2 . GLN A 82  ? 0.2612 0.4031 0.1963 0.0632  -0.0468 0.0029  96  GLN A NE2 
666  N N   . ARG A 83  ? 0.2350 0.3458 0.1787 0.0867  -0.0417 0.0214  97  ARG A N   
667  C CA  . ARG A 83  ? 0.2341 0.3621 0.1835 0.0890  -0.0439 0.0179  97  ARG A CA  
668  C C   . ARG A 83  ? 0.2246 0.3459 0.1797 0.0858  -0.0419 0.0140  97  ARG A C   
669  O O   . ARG A 83  ? 0.2150 0.3489 0.1758 0.0815  -0.0430 0.0087  97  ARG A O   
670  C CB  . ARG A 83  ? 0.2501 0.3866 0.1977 0.1016  -0.0447 0.0248  97  ARG A CB  
671  C CG  . ARG A 83  ? 0.2553 0.4141 0.2087 0.1062  -0.0475 0.0222  97  ARG A CG  
672  C CD  . ARG A 83  ? 0.2726 0.4380 0.2237 0.1205  -0.0476 0.0309  97  ARG A CD  
673  N NE  . ARG A 83  ? 0.2874 0.4583 0.2310 0.1253  -0.0489 0.0377  97  ARG A NE  
674  C CZ  . ARG A 83  ? 0.2987 0.4780 0.2391 0.1386  -0.0490 0.0474  97  ARG A CZ  
675  N NH1 . ARG A 83  ? 0.3037 0.4894 0.2486 0.1487  -0.0486 0.0505  97  ARG A NH1 
676  N NH2 . ARG A 83  ? 0.3076 0.4903 0.2402 0.1424  -0.0493 0.0545  97  ARG A NH2 
677  N N   . THR A 84  ? 0.2268 0.3297 0.1807 0.0879  -0.0386 0.0163  98  THR A N   
678  C CA  . THR A 84  ? 0.2241 0.3226 0.1823 0.0857  -0.0367 0.0121  98  THR A CA  
679  C C   . THR A 84  ? 0.2192 0.3075 0.1768 0.0764  -0.0352 0.0091  98  THR A C   
680  O O   . THR A 84  ? 0.2119 0.3009 0.1726 0.0735  -0.0339 0.0056  98  THR A O   
681  C CB  . THR A 84  ? 0.2332 0.3202 0.1916 0.0938  -0.0338 0.0143  98  THR A CB  
682  O OG1 . THR A 84  ? 0.2402 0.3089 0.1945 0.0936  -0.0313 0.0179  98  THR A OG1 
683  C CG2 . THR A 84  ? 0.2412 0.3387 0.2011 0.1048  -0.0346 0.0181  98  THR A CG2 
684  N N   . ILE A 85  ? 0.2205 0.3014 0.1742 0.0726  -0.0352 0.0109  99  ILE A N   
685  C CA  . ILE A 85  ? 0.2249 0.2961 0.1778 0.0652  -0.0336 0.0092  99  ILE A CA  
686  C C   . ILE A 85  ? 0.2326 0.2918 0.1856 0.0660  -0.0310 0.0083  99  ILE A C   
687  O O   . ILE A 85  ? 0.2387 0.2970 0.1931 0.0614  -0.0300 0.0052  99  ILE A O   
688  C CB  . ILE A 85  ? 0.2143 0.2940 0.1712 0.0586  -0.0339 0.0056  99  ILE A CB  
689  C CG1 . ILE A 85  ? 0.2160 0.3104 0.1758 0.0575  -0.0361 0.0039  99  ILE A CG1 
690  C CG2 . ILE A 85  ? 0.2109 0.2822 0.1665 0.0525  -0.0325 0.0056  99  ILE A CG2 
691  C CD1 . ILE A 85  ? 0.2116 0.3118 0.1772 0.0503  -0.0350 0.0006  99  ILE A CD1 
692  N N   . GLN A 86  ? 0.2443 0.2947 0.1960 0.0721  -0.0294 0.0108  100 GLN A N   
693  C CA  . GLN A 86  ? 0.2528 0.2902 0.2056 0.0721  -0.0262 0.0084  100 GLN A CA  
694  C C   . GLN A 86  ? 0.2461 0.2704 0.1965 0.0686  -0.0242 0.0108  100 GLN A C   
695  O O   . GLN A 86  ? 0.2439 0.2673 0.1909 0.0694  -0.0247 0.0162  100 GLN A O   
696  C CB  . GLN A 86  ? 0.2749 0.3081 0.2300 0.0807  -0.0243 0.0091  100 GLN A CB  
697  C CG  . GLN A 86  ? 0.2826 0.3264 0.2413 0.0834  -0.0248 0.0042  100 GLN A CG  
698  C CD  . GLN A 86  ? 0.2901 0.3326 0.2505 0.0782  -0.0233 -0.0030 100 GLN A CD  
699  O OE1 . GLN A 86  ? 0.3054 0.3379 0.2649 0.0733  -0.0217 -0.0052 100 GLN A OE1 
700  N NE2 . GLN A 86  ? 0.2889 0.3438 0.2517 0.0794  -0.0238 -0.0069 100 GLN A NE2 
701  N N   . ASN A 87  ? 0.2423 0.2584 0.1946 0.0644  -0.0219 0.0062  101 ASN A N   
702  C CA  . ASN A 87  ? 0.2413 0.2463 0.1930 0.0597  -0.0195 0.0070  101 ASN A CA  
703  C C   . ASN A 87  ? 0.2259 0.2370 0.1745 0.0550  -0.0217 0.0095  101 ASN A C   
704  O O   . ASN A 87  ? 0.2260 0.2313 0.1723 0.0541  -0.0204 0.0140  101 ASN A O   
705  C CB  . ASN A 87  ? 0.2586 0.2494 0.2105 0.0642  -0.0158 0.0123  101 ASN A CB  
706  C CG  . ASN A 87  ? 0.2728 0.2554 0.2290 0.0692  -0.0127 0.0091  101 ASN A CG  
707  O OD1 . ASN A 87  ? 0.2746 0.2559 0.2345 0.0658  -0.0115 0.0005  101 ASN A OD1 
708  N ND2 . ASN A 87  ? 0.2847 0.2634 0.2406 0.0780  -0.0113 0.0155  101 ASN A ND2 
709  N N   . ASP A 88  ? 0.2116 0.2339 0.1607 0.0522  -0.0241 0.0068  102 ASP A N   
710  C CA  . ASP A 88  ? 0.1976 0.2255 0.1450 0.0485  -0.0256 0.0085  102 ASP A CA  
711  C C   . ASP A 88  ? 0.1945 0.2197 0.1426 0.0432  -0.0244 0.0069  102 ASP A C   
712  O O   . ASP A 88  ? 0.1864 0.2182 0.1363 0.0407  -0.0248 0.0043  102 ASP A O   
713  C CB  . ASP A 88  ? 0.1881 0.2275 0.1372 0.0483  -0.0276 0.0073  102 ASP A CB  
714  C CG  . ASP A 88  ? 0.1824 0.2262 0.1310 0.0453  -0.0285 0.0085  102 ASP A CG  
715  O OD1 . ASP A 88  ? 0.1831 0.2229 0.1289 0.0447  -0.0282 0.0106  102 ASP A OD1 
716  O OD2 . ASP A 88  ? 0.1779 0.2289 0.1295 0.0435  -0.0288 0.0073  102 ASP A OD2 
717  N N   . ILE A 89  ? 0.1956 0.2127 0.1424 0.0418  -0.0225 0.0092  103 ILE A N   
718  C CA  . ILE A 89  ? 0.1951 0.2109 0.1435 0.0367  -0.0210 0.0074  103 ILE A CA  
719  C C   . ILE A 89  ? 0.1972 0.2066 0.1434 0.0357  -0.0191 0.0119  103 ILE A C   
720  O O   . ILE A 89  ? 0.1991 0.2016 0.1435 0.0390  -0.0176 0.0159  103 ILE A O   
721  C CB  . ILE A 89  ? 0.1997 0.2127 0.1518 0.0347  -0.0195 0.0016  103 ILE A CB  
722  C CG1 . ILE A 89  ? 0.2000 0.2167 0.1545 0.0290  -0.0186 -0.0015 103 ILE A CG1 
723  C CG2 . ILE A 89  ? 0.2139 0.2139 0.1672 0.0370  -0.0164 0.0021  103 ILE A CG2 
724  C CD1 . ILE A 89  ? 0.2044 0.2237 0.1630 0.0263  -0.0178 -0.0095 103 ILE A CD1 
725  N N   . MET A 90  ? 0.1933 0.2064 0.1398 0.0319  -0.0188 0.0120  104 MET A N   
726  C CA  . MET A 90  ? 0.1994 0.2094 0.1438 0.0308  -0.0167 0.0160  104 MET A CA  
727  C C   . MET A 90  ? 0.1978 0.2113 0.1453 0.0258  -0.0154 0.0141  104 MET A C   
728  O O   . MET A 90  ? 0.1864 0.2081 0.1357 0.0248  -0.0171 0.0114  104 MET A O   
729  C CB  . MET A 90  ? 0.1987 0.2139 0.1387 0.0335  -0.0184 0.0187  104 MET A CB  
730  C CG  . MET A 90  ? 0.2051 0.2208 0.1424 0.0324  -0.0165 0.0219  104 MET A CG  
731  S SD  . MET A 90  ? 0.2089 0.2317 0.1404 0.0363  -0.0183 0.0235  104 MET A SD  
732  C CE  . MET A 90  ? 0.1956 0.2250 0.1306 0.0343  -0.0202 0.0178  104 MET A CE  
733  N N   . LEU A 91  ? 0.2042 0.2124 0.1526 0.0230  -0.0121 0.0161  105 LEU A N   
734  C CA  . LEU A 91  ? 0.2031 0.2165 0.1549 0.0182  -0.0105 0.0145  105 LEU A CA  
735  C C   . LEU A 91  ? 0.2061 0.2220 0.1544 0.0191  -0.0093 0.0191  105 LEU A C   
736  O O   . LEU A 91  ? 0.2141 0.2246 0.1584 0.0212  -0.0075 0.0241  105 LEU A O   
737  C CB  . LEU A 91  ? 0.2129 0.2203 0.1703 0.0130  -0.0069 0.0120  105 LEU A CB  
738  C CG  . LEU A 91  ? 0.2117 0.2224 0.1743 0.0102  -0.0080 0.0040  105 LEU A CG  
739  C CD1 . LEU A 91  ? 0.2254 0.2254 0.1937 0.0054  -0.0035 0.0009  105 LEU A CD1 
740  C CD2 . LEU A 91  ? 0.2041 0.2305 0.1695 0.0076  -0.0101 0.0000  105 LEU A CD2 
741  N N   . LEU A 92  ? 0.2039 0.2290 0.1538 0.0181  -0.0100 0.0175  106 LEU A N   
742  C CA  . LEU A 92  ? 0.2078 0.2366 0.1556 0.0185  -0.0083 0.0202  106 LEU A CA  
743  C C   . LEU A 92  ? 0.2123 0.2454 0.1651 0.0136  -0.0052 0.0198  106 LEU A C   
744  O O   . LEU A 92  ? 0.2062 0.2473 0.1641 0.0116  -0.0062 0.0161  106 LEU A O   
745  C CB  . LEU A 92  ? 0.2008 0.2362 0.1480 0.0215  -0.0104 0.0187  106 LEU A CB  
746  C CG  . LEU A 92  ? 0.1998 0.2327 0.1437 0.0251  -0.0130 0.0181  106 LEU A CG  
747  C CD1 . LEU A 92  ? 0.1983 0.2357 0.1439 0.0269  -0.0135 0.0163  106 LEU A CD1 
748  C CD2 . LEU A 92  ? 0.2053 0.2350 0.1434 0.0271  -0.0126 0.0207  106 LEU A CD2 
749  N N   . GLN A 93  ? 0.2249 0.2542 0.1764 0.0119  -0.0014 0.0238  107 GLN A N   
750  C CA  . GLN A 93  ? 0.2344 0.2697 0.1907 0.0072  0.0020  0.0239  107 GLN A CA  
751  C C   . GLN A 93  ? 0.2266 0.2718 0.1809 0.0101  0.0020  0.0245  107 GLN A C   
752  O O   . GLN A 93  ? 0.2287 0.2729 0.1766 0.0138  0.0025  0.0274  107 GLN A O   
753  C CB  . GLN A 93  ? 0.2565 0.2834 0.2132 0.0040  0.0073  0.0288  107 GLN A CB  
754  C CG  . GLN A 93  ? 0.2667 0.2998 0.2303 -0.0024 0.0117  0.0284  107 GLN A CG  
755  C CD  . GLN A 93  ? 0.2915 0.3188 0.2533 -0.0038 0.0178  0.0361  107 GLN A CD  
756  O OE1 . GLN A 93  ? 0.3059 0.3315 0.2592 0.0016  0.0182  0.0422  107 GLN A OE1 
757  N NE2 . GLN A 93  ? 0.3079 0.3330 0.2780 -0.0114 0.0231  0.0360  107 GLN A NE2 
758  N N   . LEU A 94  ? 0.2206 0.2767 0.1806 0.0089  0.0014  0.0212  108 LEU A N   
759  C CA  . LEU A 94  ? 0.2177 0.2829 0.1775 0.0122  0.0021  0.0213  108 LEU A CA  
760  C C   . LEU A 94  ? 0.2280 0.2969 0.1878 0.0097  0.0068  0.0243  108 LEU A C   
761  O O   . LEU A 94  ? 0.2248 0.2936 0.1890 0.0039  0.0097  0.0251  108 LEU A O   
762  C CB  . LEU A 94  ? 0.2121 0.2890 0.1784 0.0130  0.0005  0.0184  108 LEU A CB  
763  C CG  . LEU A 94  ? 0.2078 0.2837 0.1744 0.0156  -0.0034 0.0166  108 LEU A CG  
764  C CD1 . LEU A 94  ? 0.2062 0.2969 0.1791 0.0172  -0.0044 0.0154  108 LEU A CD1 
765  C CD2 . LEU A 94  ? 0.2090 0.2770 0.1704 0.0208  -0.0048 0.0176  108 LEU A CD2 
766  N N   . SER A 95  ? 0.2402 0.3127 0.1957 0.0139  0.0082  0.0252  109 SER A N   
767  C CA  . SER A 95  ? 0.2542 0.3321 0.2085 0.0125  0.0129  0.0283  109 SER A CA  
768  C C   . SER A 95  ? 0.2604 0.3510 0.2234 0.0092  0.0154  0.0270  109 SER A C   
769  O O   . SER A 95  ? 0.2678 0.3632 0.2325 0.0055  0.0200  0.0298  109 SER A O   
770  C CB  . SER A 95  ? 0.2581 0.3385 0.2054 0.0180  0.0135  0.0278  109 SER A CB  
771  O OG  . SER A 95  ? 0.2590 0.3454 0.2098 0.0219  0.0125  0.0234  109 SER A OG  
772  N N   . ARG A 96  ? 0.2635 0.3611 0.2322 0.0109  0.0125  0.0233  110 ARG A N   
773  C CA  . ARG A 96  ? 0.2669 0.3794 0.2450 0.0077  0.0137  0.0215  110 ARG A CA  
774  C C   . ARG A 96  ? 0.2490 0.3651 0.2318 0.0077  0.0093  0.0183  110 ARG A C   
775  O O   . ARG A 96  ? 0.2416 0.3496 0.2204 0.0117  0.0059  0.0180  110 ARG A O   
776  C CB  . ARG A 96  ? 0.2836 0.4082 0.2633 0.0130  0.0160  0.0215  110 ARG A CB  
777  C CG  . ARG A 96  ? 0.2994 0.4239 0.2785 0.0213  0.0134  0.0201  110 ARG A CG  
778  C CD  . ARG A 96  ? 0.3172 0.4527 0.2994 0.0272  0.0165  0.0198  110 ARG A CD  
779  N NE  . ARG A 96  ? 0.3290 0.4661 0.3145 0.0346  0.0147  0.0195  110 ARG A NE  
780  C CZ  . ARG A 96  ? 0.3434 0.4698 0.3257 0.0405  0.0148  0.0186  110 ARG A CZ  
781  N NH1 . ARG A 96  ? 0.3555 0.4714 0.3306 0.0399  0.0160  0.0166  110 ARG A NH1 
782  N NH2 . ARG A 96  ? 0.3543 0.4810 0.3408 0.0470  0.0141  0.0199  110 ARG A NH2 
783  N N   A ARG A 97  ? 0.2422 0.3725 0.2337 0.0029  0.0095  0.0155  111 ARG A N   
784  N N   B ARG A 97  ? 0.2464 0.3768 0.2379 0.0029  0.0095  0.0155  111 ARG A N   
785  C CA  A ARG A 97  ? 0.2316 0.3708 0.2275 0.0032  0.0054  0.0120  111 ARG A CA  
786  C CA  B ARG A 97  ? 0.2386 0.3781 0.2345 0.0032  0.0054  0.0120  111 ARG A CA  
787  C C   A ARG A 97  ? 0.2258 0.3746 0.2219 0.0127  0.0035  0.0139  111 ARG A C   
788  C C   B ARG A 97  ? 0.2294 0.3778 0.2254 0.0128  0.0035  0.0140  111 ARG A C   
789  O O   A ARG A 97  ? 0.2226 0.3779 0.2200 0.0170  0.0061  0.0159  111 ARG A O   
790  O O   B ARG A 97  ? 0.2261 0.3799 0.2228 0.0173  0.0061  0.0161  111 ARG A O   
791  C CB  A ARG A 97  ? 0.2307 0.3854 0.2364 -0.0051 0.0063  0.0072  111 ARG A CB  
792  C CB  B ARG A 97  ? 0.2427 0.3994 0.2487 -0.0044 0.0061  0.0072  111 ARG A CB  
793  C CG  A ARG A 97  ? 0.2348 0.3776 0.2417 -0.0139 0.0071  0.0036  111 ARG A CG  
794  C CG  B ARG A 97  ? 0.2455 0.4231 0.2583 -0.0030 0.0082  0.0076  111 ARG A CG  
795  C CD  A ARG A 97  ? 0.2360 0.3916 0.2539 -0.0242 0.0099  -0.0018 111 ARG A CD  
796  C CD  B ARG A 97  ? 0.2488 0.4473 0.2727 -0.0110 0.0080  0.0014  111 ARG A CD  
797  N NE  A ARG A 97  ? 0.2375 0.3890 0.2594 -0.0311 0.0087  -0.0090 111 ARG A NE  
798  N NE  B ARG A 97  ? 0.2507 0.4715 0.2819 -0.0096 0.0102  0.0019  111 ARG A NE  
799  C CZ  A ARG A 97  ? 0.2301 0.3997 0.2574 -0.0327 0.0047  -0.0166 111 ARG A CZ  
800  C CZ  B ARG A 97  ? 0.2610 0.4896 0.2994 -0.0179 0.0149  0.0002  111 ARG A CZ  
801  N NH1 A ARG A 97  ? 0.2201 0.4123 0.2489 -0.0266 0.0015  -0.0160 111 ARG A NH1 
802  N NH1 B ARG A 97  ? 0.2695 0.4832 0.3088 -0.0280 0.0184  -0.0011 111 ARG A NH1 
803  N NH2 A ARG A 97  ? 0.2338 0.3995 0.2649 -0.0396 0.0043  -0.0246 111 ARG A NH2 
804  N NH2 B ARG A 97  ? 0.2600 0.5113 0.3055 -0.0159 0.0166  0.0005  111 ARG A NH2 
805  N N   . VAL A 98  ? 0.2226 0.3722 0.2179 0.0163  -0.0002 0.0136  112 VAL A N   
806  C CA  . VAL A 98  ? 0.2252 0.3844 0.2222 0.0255  -0.0013 0.0168  112 VAL A CA  
807  C C   . VAL A 98  ? 0.2211 0.4061 0.2266 0.0260  -0.0014 0.0158  112 VAL A C   
808  O O   . VAL A 98  ? 0.2207 0.4169 0.2311 0.0180  -0.0020 0.0110  112 VAL A O   
809  C CB  . VAL A 98  ? 0.2257 0.3806 0.2197 0.0289  -0.0048 0.0178  112 VAL A CB  
810  C CG1 . VAL A 98  ? 0.2292 0.3613 0.2158 0.0282  -0.0050 0.0182  112 VAL A CG1 
811  C CG2 . VAL A 98  ? 0.2252 0.3935 0.2224 0.0238  -0.0081 0.0132  112 VAL A CG2 
812  N N   . ARG A 99  ? 0.2231 0.4178 0.2312 0.0355  -0.0003 0.0203  113 ARG A N   
813  C CA  . ARG A 99  ? 0.2251 0.4473 0.2409 0.0391  -0.0014 0.0209  113 ARG A CA  
814  C C   . ARG A 99  ? 0.2246 0.4548 0.2395 0.0438  -0.0053 0.0230  113 ARG A C   
815  O O   . ARG A 99  ? 0.2249 0.4458 0.2367 0.0525  -0.0048 0.0291  113 ARG A O   
816  C CB  . ARG A 99  ? 0.2266 0.4563 0.2463 0.0485  0.0021  0.0255  113 ARG A CB  
817  C CG  . ARG A 99  ? 0.2323 0.4572 0.2524 0.0445  0.0064  0.0234  113 ARG A CG  
818  C CD  . ARG A 99  ? 0.2339 0.4651 0.2576 0.0546  0.0104  0.0270  113 ARG A CD  
819  N NE  . ARG A 99  ? 0.2366 0.4500 0.2565 0.0640  0.0119  0.0311  113 ARG A NE  
820  C CZ  . ARG A 99  ? 0.2396 0.4332 0.2547 0.0651  0.0152  0.0299  113 ARG A CZ  
821  N NH1 . ARG A 99  ? 0.2403 0.4300 0.2524 0.0583  0.0171  0.0260  113 ARG A NH1 
822  N NH2 . ARG A 99  ? 0.2433 0.4218 0.2569 0.0727  0.0170  0.0325  113 ARG A NH2 
823  N N   . ARG A 100 ? 0.2307 0.4785 0.2488 0.0376  -0.0088 0.0175  114 ARG A N   
824  C CA  . ARG A 100 ? 0.2344 0.4925 0.2508 0.0409  -0.0127 0.0182  114 ARG A CA  
825  C C   . ARG A 100 ? 0.2384 0.5203 0.2586 0.0529  -0.0132 0.0256  114 ARG A C   
826  O O   . ARG A 100 ? 0.2332 0.5365 0.2604 0.0546  -0.0125 0.0253  114 ARG A O   
827  C CB  . ARG A 100 ? 0.2395 0.5111 0.2588 0.0302  -0.0160 0.0081  114 ARG A CB  
828  C CG  . ARG A 100 ? 0.2484 0.5283 0.2641 0.0325  -0.0200 0.0072  114 ARG A CG  
829  C CD  . ARG A 100 ? 0.2532 0.5542 0.2736 0.0230  -0.0231 -0.0044 114 ARG A CD  
830  N NE  . ARG A 100 ? 0.2560 0.5750 0.2735 0.0278  -0.0271 -0.0046 114 ARG A NE  
831  C CZ  . ARG A 100 ? 0.2598 0.5776 0.2750 0.0214  -0.0293 -0.0132 114 ARG A CZ  
832  N NH1 . ARG A 100 ? 0.2652 0.5628 0.2815 0.0102  -0.0277 -0.0219 114 ARG A NH1 
833  N NH2 . ARG A 100 ? 0.2571 0.5940 0.2690 0.0269  -0.0327 -0.0127 114 ARG A NH2 
834  N N   . ASN A 101 ? 0.2365 0.5148 0.2526 0.0619  -0.0137 0.0331  115 ASN A N   
835  C CA  . ASN A 101 ? 0.2441 0.5438 0.2633 0.0749  -0.0135 0.0424  115 ASN A CA  
836  C C   . ASN A 101 ? 0.2473 0.5445 0.2612 0.0809  -0.0148 0.0488  115 ASN A C   
837  O O   . ASN A 101 ? 0.2489 0.5309 0.2572 0.0740  -0.0164 0.0442  115 ASN A O   
838  C CB  . ASN A 101 ? 0.2442 0.5350 0.2667 0.0840  -0.0083 0.0498  115 ASN A CB  
839  C CG  . ASN A 101 ? 0.2403 0.4952 0.2579 0.0847  -0.0044 0.0523  115 ASN A CG  
840  O OD1 . ASN A 101 ? 0.2361 0.4776 0.2488 0.0858  -0.0049 0.0555  115 ASN A OD1 
841  N ND2 . ASN A 101 ? 0.2311 0.4720 0.2501 0.0836  -0.0007 0.0503  115 ASN A ND2 
842  N N   . ARG A 102 ? 0.2566 0.5685 0.2723 0.0943  -0.0134 0.0602  116 ARG A N   
843  C CA  . ARG A 102 ? 0.2650 0.5766 0.2763 0.1019  -0.0133 0.0693  116 ARG A CA  
844  C C   . ARG A 102 ? 0.2597 0.5349 0.2660 0.0989  -0.0104 0.0705  116 ARG A C   
845  O O   . ARG A 102 ? 0.2617 0.5350 0.2632 0.0990  -0.0117 0.0727  116 ARG A O   
846  C CB  . ARG A 102 ? 0.2828 0.6080 0.2979 0.1185  -0.0098 0.0843  116 ARG A CB  
847  C CG  . ARG A 102 ? 0.3004 0.6621 0.3146 0.1261  -0.0134 0.0901  116 ARG A CG  
848  C CD  . ARG A 102 ? 0.3150 0.6989 0.3349 0.1422  -0.0106 0.1035  116 ARG A CD  
849  N NE  . ARG A 102 ? 0.3127 0.7258 0.3389 0.1401  -0.0138 0.0960  116 ARG A NE  
850  C CZ  . ARG A 102 ? 0.3150 0.7715 0.3433 0.1443  -0.0184 0.0960  116 ARG A CZ  
851  N NH1 . ARG A 102 ? 0.3154 0.7927 0.3392 0.1522  -0.0204 0.1039  116 ARG A NH1 
852  N NH2 . ARG A 102 ? 0.3141 0.7953 0.3494 0.1406  -0.0209 0.0878  116 ARG A NH2 
853  N N   . ASN A 103 ? 0.2538 0.5026 0.2611 0.0966  -0.0066 0.0688  117 ASN A N   
854  C CA  . ASN A 103 ? 0.2471 0.4640 0.2512 0.0952  -0.0033 0.0704  117 ASN A CA  
855  C C   . ASN A 103 ? 0.2320 0.4315 0.2315 0.0822  -0.0057 0.0591  117 ASN A C   
856  O O   . ASN A 103 ? 0.2245 0.4016 0.2208 0.0799  -0.0042 0.0591  117 ASN A O   
857  C CB  . ASN A 103 ? 0.2542 0.4536 0.2627 0.1021  0.0030  0.0758  117 ASN A CB  
858  C CG  . ASN A 103 ? 0.2645 0.4778 0.2784 0.1165  0.0067  0.0886  117 ASN A CG  
859  O OD1 . ASN A 103 ? 0.2708 0.4972 0.2833 0.1221  0.0058  0.0966  117 ASN A OD1 
860  N ND2 . ASN A 103 ? 0.2630 0.4746 0.2828 0.1233  0.0111  0.0913  117 ASN A ND2 
861  N N   . VAL A 104 ? 0.2244 0.4344 0.2244 0.0740  -0.0089 0.0500  118 VAL A N   
862  C CA  . VAL A 104 ? 0.2200 0.4144 0.2165 0.0627  -0.0104 0.0407  118 VAL A CA  
863  C C   . VAL A 104 ? 0.2220 0.4347 0.2193 0.0548  -0.0146 0.0325  118 VAL A C   
864  O O   . VAL A 104 ? 0.2182 0.4476 0.2205 0.0523  -0.0150 0.0289  118 VAL A O   
865  C CB  . VAL A 104 ? 0.2137 0.3955 0.2116 0.0603  -0.0072 0.0382  118 VAL A CB  
866  C CG1 . VAL A 104 ? 0.2077 0.3755 0.2018 0.0496  -0.0082 0.0304  118 VAL A CG1 
867  C CG2 . VAL A 104 ? 0.2178 0.3819 0.2158 0.0674  -0.0026 0.0439  118 VAL A CG2 
868  N N   . ASN A 105 ? 0.2278 0.4378 0.2211 0.0505  -0.0174 0.0286  119 ASN A N   
869  C CA  . ASN A 105 ? 0.2324 0.4543 0.2269 0.0414  -0.0205 0.0183  119 ASN A CA  
870  C C   . ASN A 105 ? 0.2180 0.4258 0.2073 0.0368  -0.0220 0.0140  119 ASN A C   
871  O O   . ASN A 105 ? 0.2050 0.4021 0.1900 0.0418  -0.0215 0.0197  119 ASN A O   
872  C CB  . ASN A 105 ? 0.2532 0.5095 0.2521 0.0437  -0.0233 0.0167  119 ASN A CB  
873  C CG  . ASN A 105 ? 0.2786 0.5479 0.2743 0.0533  -0.0246 0.0244  119 ASN A CG  
874  O OD1 . ASN A 105 ? 0.3078 0.5728 0.2988 0.0518  -0.0261 0.0224  119 ASN A OD1 
875  N ND2 . ASN A 105 ? 0.3000 0.5853 0.2983 0.0638  -0.0235 0.0340  119 ASN A ND2 
876  N N   . PRO A 106 ? 0.2079 0.4148 0.1984 0.0271  -0.0233 0.0036  120 PRO A N   
877  C CA  . PRO A 106 ? 0.2053 0.3964 0.1916 0.0230  -0.0240 -0.0008 120 PRO A CA  
878  C C   . PRO A 106 ? 0.1996 0.4045 0.1832 0.0258  -0.0268 -0.0026 120 PRO A C   
879  O O   . PRO A 106 ? 0.1989 0.4300 0.1841 0.0294  -0.0288 -0.0023 120 PRO A O   
880  C CB  . PRO A 106 ? 0.2104 0.3961 0.2008 0.0123  -0.0232 -0.0110 120 PRO A CB  
881  C CG  . PRO A 106 ? 0.2135 0.4122 0.2102 0.0100  -0.0218 -0.0114 120 PRO A CG  
882  C CD  . PRO A 106 ? 0.2094 0.4294 0.2066 0.0194  -0.0233 -0.0042 120 PRO A CD  
883  N N   . VAL A 107 ? 0.1972 0.3861 0.1765 0.0244  -0.0269 -0.0045 121 VAL A N   
884  C CA  . VAL A 107 ? 0.1965 0.3967 0.1728 0.0264  -0.0290 -0.0072 121 VAL A CA  
885  C C   . VAL A 107 ? 0.1983 0.3937 0.1759 0.0180  -0.0296 -0.0201 121 VAL A C   
886  O O   . VAL A 107 ? 0.1974 0.3717 0.1763 0.0126  -0.0276 -0.0231 121 VAL A O   
887  C CB  . VAL A 107 ? 0.1928 0.3808 0.1638 0.0330  -0.0280 0.0019  121 VAL A CB  
888  C CG1 . VAL A 107 ? 0.1930 0.3528 0.1621 0.0299  -0.0264 0.0014  121 VAL A CG1 
889  C CG2 . VAL A 107 ? 0.1963 0.4001 0.1640 0.0362  -0.0297 0.0009  121 VAL A CG2 
890  N N   . ALA A 108 ? 0.1978 0.4135 0.1752 0.0174  -0.0319 -0.0277 122 ALA A N   
891  C CA  . ALA A 108 ? 0.2047 0.4178 0.1847 0.0096  -0.0319 -0.0418 122 ALA A CA  
892  C C   . ALA A 108 ? 0.2072 0.3981 0.1829 0.0108  -0.0307 -0.0414 122 ALA A C   
893  O O   . ALA A 108 ? 0.1938 0.3818 0.1641 0.0177  -0.0310 -0.0322 122 ALA A O   
894  C CB  . ALA A 108 ? 0.2070 0.4522 0.1880 0.0090  -0.0348 -0.0512 122 ALA A CB  
895  N N   . LEU A 109 ? 0.2245 0.4004 0.2035 0.0040  -0.0288 -0.0514 123 LEU A N   
896  C CA  . LEU A 109 ? 0.2392 0.3968 0.2154 0.0051  -0.0276 -0.0532 123 LEU A CA  
897  C C   . LEU A 109 ? 0.2600 0.4325 0.2370 0.0033  -0.0286 -0.0661 123 LEU A C   
898  O O   . LEU A 109 ? 0.2690 0.4618 0.2502 -0.0013 -0.0297 -0.0763 123 LEU A O   
899  C CB  . LEU A 109 ? 0.2459 0.3764 0.2257 0.0001  -0.0240 -0.0546 123 LEU A CB  
900  C CG  . LEU A 109 ? 0.2431 0.3588 0.2214 0.0017  -0.0227 -0.0428 123 LEU A CG  
901  C CD1 . LEU A 109 ? 0.2484 0.3384 0.2287 -0.0014 -0.0190 -0.0429 123 LEU A CD1 
902  C CD2 . LEU A 109 ? 0.2377 0.3524 0.2095 0.0098  -0.0243 -0.0316 123 LEU A CD2 
903  N N   . PRO A 110 ? 0.3556 0.4241 0.2881 -0.0519 0.0368  -0.0855 124 PRO A N   
904  C CA  . PRO A 110 ? 0.3728 0.4546 0.3119 -0.0537 0.0345  -0.0990 124 PRO A CA  
905  C C   . PRO A 110 ? 0.4223 0.4802 0.3625 -0.0677 0.0459  -0.1132 124 PRO A C   
906  O O   . PRO A 110 ? 0.4257 0.4513 0.3580 -0.0750 0.0560  -0.1099 124 PRO A O   
907  C CB  . PRO A 110 ? 0.3694 0.4383 0.2974 -0.0403 0.0266  -0.0892 124 PRO A CB  
908  C CG  . PRO A 110 ? 0.3731 0.4068 0.2857 -0.0352 0.0279  -0.0737 124 PRO A CG  
909  C CD  . PRO A 110 ? 0.3602 0.4033 0.2768 -0.0400 0.0317  -0.0695 124 PRO A CD  
910  N N   . ARG A 111 ? 0.4614 0.5355 0.4108 -0.0717 0.0450  -0.1295 125 ARG A N   
911  C CA  . ARG A 111 ? 0.5081 0.5560 0.4584 -0.0837 0.0557  -0.1442 125 ARG A CA  
912  C C   . ARG A 111 ? 0.5435 0.5528 0.4777 -0.0734 0.0540  -0.1365 125 ARG A C   
913  O O   . ARG A 111 ? 0.5354 0.5510 0.4631 -0.0587 0.0436  -0.1247 125 ARG A O   
914  C CB  . ARG A 111 ? 0.5178 0.6056 0.4868 -0.0922 0.0545  -0.1671 125 ARG A CB  
915  C CG  . ARG A 111 ? 0.5055 0.6417 0.4914 -0.0975 0.0519  -0.1740 125 ARG A CG  
916  C CD  . ARG A 111 ? 0.5321 0.6592 0.5274 -0.1150 0.0655  -0.1829 125 ARG A CD  
917  N NE  . ARG A 111 ? 0.5627 0.6904 0.5708 -0.1316 0.0746  -0.2078 125 ARG A NE  
918  C CZ  . ARG A 111 ? 0.5992 0.6794 0.6009 -0.1421 0.0881  -0.2130 125 ARG A CZ  
919  N NH1 . ARG A 111 ? 0.6209 0.6491 0.6020 -0.1373 0.0940  -0.1942 125 ARG A NH1 
920  N NH2 . ARG A 111 ? 0.6144 0.6989 0.6300 -0.1570 0.0958  -0.2376 125 ARG A NH2 
921  N N   . ALA A 112 ? 0.5929 0.5628 0.5218 -0.0809 0.0649  -0.1438 126 ALA A N   
922  C CA  . ALA A 112 ? 0.6179 0.5434 0.5290 -0.0698 0.0648  -0.1338 126 ALA A CA  
923  C C   . ALA A 112 ? 0.6093 0.5500 0.5235 -0.0580 0.0549  -0.1389 126 ALA A C   
924  O O   . ALA A 112 ? 0.6086 0.5382 0.5122 -0.0426 0.0470  -0.1259 126 ALA A O   
925  C CB  . ALA A 112 ? 0.6638 0.5413 0.5676 -0.0805 0.0803  -0.1397 126 ALA A CB  
926  N N   . GLN A 113 ? 0.5912 0.5591 0.5205 -0.0654 0.0556  -0.1591 127 GLN A N   
927  C CA  . GLN A 113 ? 0.5780 0.5585 0.5099 -0.0555 0.0486  -0.1663 127 GLN A CA  
928  C C   . GLN A 113 ? 0.5271 0.5642 0.4689 -0.0517 0.0380  -0.1689 127 GLN A C   
929  O O   . GLN A 113 ? 0.5251 0.5826 0.4712 -0.0469 0.0336  -0.1789 127 GLN A O   
930  C CB  . GLN A 113 ? 0.6070 0.5673 0.5442 -0.0646 0.0585  -0.1870 127 GLN A CB  
931  C CG  . GLN A 113 ? 0.6427 0.5404 0.5656 -0.0632 0.0685  -0.1805 127 GLN A CG  
932  C CD  . GLN A 113 ? 0.6709 0.5451 0.5968 -0.0643 0.0753  -0.1977 127 GLN A CD  
933  O OE1 . GLN A 113 ? 0.7019 0.5448 0.6294 -0.0778 0.0894  -0.2089 127 GLN A OE1 
934  N NE2 . GLN A 113 ? 0.6609 0.5490 0.5883 -0.0505 0.0664  -0.2007 127 GLN A NE2 
935  N N   . GLU A 114 ? 0.4958 0.5562 0.4393 -0.0522 0.0340  -0.1584 128 GLU A N   
936  C CA  . GLU A 114 ? 0.4537 0.5649 0.4043 -0.0478 0.0248  -0.1581 128 GLU A CA  
937  C C   . GLU A 114 ? 0.4177 0.5354 0.3613 -0.0322 0.0162  -0.1465 128 GLU A C   
938  O O   . GLU A 114 ? 0.4108 0.5583 0.3580 -0.0285 0.0119  -0.1546 128 GLU A O   
939  C CB  . GLU A 114 ? 0.4466 0.5708 0.4004 -0.0517 0.0249  -0.1492 128 GLU A CB  
940  C CG  . GLU A 114 ? 0.4234 0.5750 0.3750 -0.0400 0.0154  -0.1330 128 GLU A CG  
941  C CD  . GLU A 114 ? 0.4123 0.5887 0.3719 -0.0441 0.0153  -0.1310 128 GLU A CD  
942  O OE1 . GLU A 114 ? 0.4157 0.5752 0.3783 -0.0543 0.0231  -0.1338 128 GLU A OE1 
943  O OE2 . GLU A 114 ? 0.3967 0.6091 0.3590 -0.0364 0.0077  -0.1261 128 GLU A OE2 
944  N N   . GLY A 115 ? 0.3856 0.4771 0.3193 -0.0238 0.0144  -0.1284 129 GLY A N   
945  C CA  . GLY A 115 ? 0.3615 0.4542 0.2901 -0.0104 0.0077  -0.1180 129 GLY A CA  
946  C C   . GLY A 115 ? 0.3269 0.4450 0.2554 -0.0047 0.0017  -0.1033 129 GLY A C   
947  O O   . GLY A 115 ? 0.3084 0.4465 0.2409 -0.0094 0.0018  -0.1019 129 GLY A O   
948  N N   . LEU A 116 ? 0.3150 0.4307 0.2398 0.0056  -0.0027 -0.0929 130 LEU A N   
949  C CA  . LEU A 116 ? 0.2926 0.4308 0.2178 0.0114  -0.0070 -0.0800 130 LEU A CA  
950  C C   . LEU A 116 ? 0.2885 0.4334 0.2141 0.0198  -0.0097 -0.0788 130 LEU A C   
951  O O   . LEU A 116 ? 0.2812 0.4037 0.2047 0.0251  -0.0110 -0.0753 130 LEU A O   
952  C CB  . LEU A 116 ? 0.2885 0.4077 0.2094 0.0125  -0.0074 -0.0654 130 LEU A CB  
953  C CG  . LEU A 116 ? 0.2707 0.4078 0.1925 0.0175  -0.0102 -0.0518 130 LEU A CG  
954  C CD1 . LEU A 116 ? 0.2629 0.4313 0.1887 0.0151  -0.0101 -0.0527 130 LEU A CD1 
955  C CD2 . LEU A 116 ? 0.2716 0.3865 0.1892 0.0187  -0.0103 -0.0401 130 LEU A CD2 
956  N N   . ARG A 117 ? 0.2783 0.4559 0.2065 0.0213  -0.0104 -0.0819 131 ARG A N   
957  C CA  . ARG A 117 ? 0.2836 0.4710 0.2133 0.0274  -0.0108 -0.0851 131 ARG A CA  
958  C C   . ARG A 117 ? 0.2701 0.4710 0.1995 0.0323  -0.0116 -0.0704 131 ARG A C   
959  O O   . ARG A 117 ? 0.2556 0.4677 0.1825 0.0316  -0.0116 -0.0598 131 ARG A O   
960  C CB  . ARG A 117 ? 0.2939 0.5070 0.2250 0.0250  -0.0094 -0.1006 131 ARG A CB  
961  C CG  . ARG A 117 ? 0.3137 0.5089 0.2474 0.0202  -0.0071 -0.1178 131 ARG A CG  
962  C CD  . ARG A 117 ? 0.3215 0.5442 0.2573 0.0156  -0.0056 -0.1357 131 ARG A CD  
963  N NE  . ARG A 117 ? 0.3230 0.5689 0.2582 0.0217  -0.0056 -0.1395 131 ARG A NE  
964  C CZ  . ARG A 117 ? 0.3339 0.6101 0.2684 0.0200  -0.0048 -0.1536 131 ARG A CZ  
965  N NH1 . ARG A 117 ? 0.3405 0.6275 0.2769 0.0120  -0.0046 -0.1676 131 ARG A NH1 
966  N NH2 . ARG A 117 ? 0.3296 0.6270 0.2617 0.0257  -0.0037 -0.1548 131 ARG A NH2 
967  N N   . PRO A 118 ? 0.2709 0.4714 0.2038 0.0375  -0.0113 -0.0702 132 PRO A N   
968  C CA  . PRO A 118 ? 0.2605 0.4736 0.1949 0.0403  -0.0098 -0.0583 132 PRO A CA  
969  C C   . PRO A 118 ? 0.2587 0.4998 0.1875 0.0395  -0.0070 -0.0524 132 PRO A C   
970  O O   . PRO A 118 ? 0.2550 0.5154 0.1805 0.0386  -0.0066 -0.0621 132 PRO A O   
971  C CB  . PRO A 118 ? 0.2676 0.4847 0.2087 0.0447  -0.0088 -0.0664 132 PRO A CB  
972  C CG  . PRO A 118 ? 0.2768 0.4693 0.2195 0.0468  -0.0121 -0.0769 132 PRO A CG  
973  C CD  . PRO A 118 ? 0.2814 0.4697 0.2182 0.0411  -0.0118 -0.0825 132 PRO A CD  
974  N N   . GLY A 119 ? 0.2545 0.4969 0.1816 0.0404  -0.0051 -0.0368 133 GLY A N   
975  C CA  . GLY A 119 ? 0.2585 0.5238 0.1779 0.0420  -0.0022 -0.0276 133 GLY A CA  
976  C C   . GLY A 119 ? 0.2573 0.5238 0.1722 0.0419  -0.0051 -0.0216 133 GLY A C   
977  O O   . GLY A 119 ? 0.2658 0.5482 0.1735 0.0456  -0.0036 -0.0111 133 GLY A O   
978  N N   . THR A 120 ? 0.2519 0.5021 0.1706 0.0384  -0.0087 -0.0282 134 THR A N   
979  C CA  . THR A 120 ? 0.2447 0.4982 0.1619 0.0377  -0.0108 -0.0245 134 THR A CA  
980  C C   . THR A 120 ? 0.2403 0.4802 0.1574 0.0404  -0.0092 -0.0076 134 THR A C   
981  O O   . THR A 120 ? 0.2314 0.4491 0.1521 0.0393  -0.0081 -0.0041 134 THR A O   
982  C CB  . THR A 120 ? 0.2420 0.4806 0.1636 0.0315  -0.0128 -0.0365 134 THR A CB  
983  O OG1 . THR A 120 ? 0.2457 0.4923 0.1683 0.0288  -0.0129 -0.0529 134 THR A OG1 
984  C CG2 . THR A 120 ? 0.2383 0.4865 0.1612 0.0298  -0.0142 -0.0360 134 THR A CG2 
985  N N   . LEU A 121 ? 0.2409 0.4950 0.1543 0.0447  -0.0094 0.0017  135 LEU A N   
986  C CA  . LEU A 121 ? 0.2454 0.4858 0.1591 0.0478  -0.0071 0.0169  135 LEU A CA  
987  C C   . LEU A 121 ? 0.2348 0.4649 0.1533 0.0452  -0.0095 0.0140  135 LEU A C   
988  O O   . LEU A 121 ? 0.2376 0.4838 0.1575 0.0441  -0.0124 0.0057  135 LEU A O   
989  C CB  . LEU A 121 ? 0.2674 0.5249 0.1734 0.0560  -0.0048 0.0310  135 LEU A CB  
990  C CG  . LEU A 121 ? 0.2814 0.5209 0.1878 0.0598  -0.0005 0.0474  135 LEU A CG  
991  C CD1 . LEU A 121 ? 0.2839 0.5041 0.1931 0.0560  0.0054  0.0520  135 LEU A CD1 
992  C CD2 . LEU A 121 ? 0.3024 0.5573 0.1996 0.0701  0.0009  0.0617  135 LEU A CD2 
993  N N   . CYS A 122 ? 0.2218 0.4263 0.1432 0.0436  -0.0077 0.0197  136 CYS A N   
994  C CA  . CYS A 122 ? 0.2146 0.4056 0.1393 0.0406  -0.0083 0.0175  136 CYS A CA  
995  C C   . CYS A 122 ? 0.2168 0.3943 0.1425 0.0443  -0.0054 0.0303  136 CYS A C   
996  O O   . CYS A 122 ? 0.2207 0.3950 0.1451 0.0476  -0.0024 0.0397  136 CYS A O   
997  C CB  . CYS A 122 ? 0.2092 0.3774 0.1340 0.0340  -0.0089 0.0082  136 CYS A CB  
998  S SG  . CYS A 122 ? 0.2094 0.3856 0.1337 0.0297  -0.0109 -0.0076 136 CYS A SG  
999  N N   . THR A 123 ? 0.2111 0.3798 0.1395 0.0429  -0.0050 0.0296  137 THR A N   
1000 C CA  . THR A 123 ? 0.2101 0.3628 0.1401 0.0457  -0.0018 0.0389  137 THR A CA  
1001 C C   . THR A 123 ? 0.2025 0.3311 0.1320 0.0394  -0.0013 0.0332  137 THR A C   
1002 O O   . THR A 123 ? 0.2001 0.3273 0.1286 0.0343  -0.0022 0.0243  137 THR A O   
1003 C CB  . THR A 123 ? 0.2157 0.3835 0.1490 0.0524  -0.0013 0.0441  137 THR A CB  
1004 O OG1 . THR A 123 ? 0.2213 0.4110 0.1515 0.0599  -0.0024 0.0506  137 THR A OG1 
1005 C CG2 . THR A 123 ? 0.2223 0.3727 0.1580 0.0561  0.0028  0.0529  137 THR A CG2 
1006 N N   . VAL A 124 ? 0.1994 0.3091 0.1289 0.0396  0.0008  0.0382  138 VAL A N   
1007 C CA  . VAL A 124 ? 0.1982 0.2863 0.1250 0.0357  0.0013  0.0344  138 VAL A CA  
1008 C C   . VAL A 124 ? 0.1977 0.2784 0.1281 0.0389  0.0055  0.0410  138 VAL A C   
1009 O O   . VAL A 124 ? 0.1967 0.2795 0.1310 0.0433  0.0081  0.0492  138 VAL A O   
1010 C CB  . VAL A 124 ? 0.2025 0.2757 0.1259 0.0329  -0.0013 0.0305  138 VAL A CB  
1011 C CG1 . VAL A 124 ? 0.2048 0.2794 0.1336 0.0346  0.0000  0.0355  138 VAL A CG1 
1012 C CG2 . VAL A 124 ? 0.2070 0.2592 0.1242 0.0304  -0.0016 0.0270  138 VAL A CG2 
1013 N N   . ALA A 125 ? 0.1969 0.2671 0.1252 0.0365  0.0071  0.0373  139 ALA A N   
1014 C CA  . ALA A 125 ? 0.2004 0.2631 0.1324 0.0395  0.0116  0.0411  139 ALA A CA  
1015 C C   . ALA A 125 ? 0.2027 0.2443 0.1282 0.0350  0.0126  0.0357  139 ALA A C   
1016 O O   . ALA A 125 ? 0.1978 0.2325 0.1148 0.0302  0.0104  0.0297  139 ALA A O   
1017 C CB  . ALA A 125 ? 0.2015 0.2804 0.1388 0.0430  0.0134  0.0413  139 ALA A CB  
1018 N N   . GLY A 126 ? 0.2072 0.2377 0.1359 0.0369  0.0163  0.0379  140 GLY A N   
1019 C CA  . GLY A 126 ? 0.2158 0.2286 0.1377 0.0334  0.0173  0.0319  140 GLY A CA  
1020 C C   . GLY A 126 ? 0.2226 0.2248 0.1507 0.0355  0.0221  0.0332  140 GLY A C   
1021 O O   . GLY A 126 ? 0.2230 0.2284 0.1605 0.0400  0.0252  0.0402  140 GLY A O   
1022 N N   . TRP A 127 ? 0.2282 0.2167 0.1494 0.0325  0.0232  0.0263  141 TRP A N   
1023 C CA  . TRP A 127 ? 0.2387 0.2152 0.1648 0.0331  0.0280  0.0238  141 TRP A CA  
1024 C C   . TRP A 127 ? 0.2508 0.2186 0.1760 0.0289  0.0245  0.0179  141 TRP A C   
1025 O O   . TRP A 127 ? 0.2600 0.2170 0.1865 0.0271  0.0274  0.0114  141 TRP A O   
1026 C CB  . TRP A 127 ? 0.2422 0.2120 0.1612 0.0324  0.0320  0.0177  141 TRP A CB  
1027 C CG  . TRP A 127 ? 0.2348 0.2147 0.1602 0.0368  0.0372  0.0210  141 TRP A CG  
1028 C CD1 . TRP A 127 ? 0.2379 0.2180 0.1751 0.0432  0.0434  0.0237  141 TRP A CD1 
1029 C CD2 . TRP A 127 ? 0.2248 0.2172 0.1467 0.0354  0.0370  0.0208  141 TRP A CD2 
1030 N NE1 . TRP A 127 ? 0.2330 0.2283 0.1750 0.0470  0.0458  0.0251  141 TRP A NE1 
1031 C CE2 . TRP A 127 ? 0.2240 0.2278 0.1575 0.0412  0.0424  0.0225  141 TRP A CE2 
1032 C CE3 . TRP A 127 ? 0.2208 0.2153 0.1317 0.0300  0.0335  0.0188  141 TRP A CE3 
1033 C CZ2 . TRP A 127 ? 0.2183 0.2391 0.1547 0.0404  0.0440  0.0207  141 TRP A CZ2 
1034 C CZ3 . TRP A 127 ? 0.2174 0.2248 0.1304 0.0282  0.0364  0.0176  141 TRP A CZ3 
1035 C CH2 . TRP A 127 ? 0.2164 0.2385 0.1427 0.0326  0.0414  0.0177  141 TRP A CH2 
1036 N N   . GLY A 128 ? 0.2488 0.2233 0.1733 0.0273  0.0184  0.0186  142 GLY A N   
1037 C CA  . GLY A 128 ? 0.2572 0.2290 0.1822 0.0237  0.0137  0.0113  142 GLY A CA  
1038 C C   . GLY A 128 ? 0.2680 0.2371 0.2087 0.0212  0.0190  0.0113  142 GLY A C   
1039 O O   . GLY A 128 ? 0.2742 0.2399 0.2233 0.0235  0.0269  0.0188  142 GLY A O   
1040 N N   . ARG A 129 ? 0.2769 0.2477 0.2217 0.0168  0.0149  0.0025  143 ARG A N   
1041 C CA  . ARG A 129 ? 0.2906 0.2587 0.2515 0.0116  0.0208  -0.0004 143 ARG A CA  
1042 C C   . ARG A 129 ? 0.2880 0.2617 0.2582 0.0122  0.0265  0.0112  143 ARG A C   
1043 O O   . ARG A 129 ? 0.2713 0.2570 0.2370 0.0151  0.0220  0.0166  143 ARG A O   
1044 C CB  . ARG A 129 ? 0.2950 0.2701 0.2596 0.0066  0.0137  -0.0144 143 ARG A CB  
1045 C CG  . ARG A 129 ? 0.3061 0.2768 0.2599 0.0066  0.0078  -0.0266 143 ARG A CG  
1046 C CD  . ARG A 129 ? 0.3125 0.2938 0.2728 0.0024  0.0003  -0.0419 143 ARG A CD  
1047 N NE  . ARG A 129 ? 0.3190 0.3010 0.2616 0.0061  -0.0094 -0.0513 143 ARG A NE  
1048 C CZ  . ARG A 129 ? 0.3267 0.3199 0.2702 0.0052  -0.0185 -0.0658 143 ARG A CZ  
1049 N NH1 . ARG A 129 ? 0.3248 0.3314 0.2895 -0.0006 -0.0187 -0.0746 143 ARG A NH1 
1050 N NH2 . ARG A 129 ? 0.3365 0.3288 0.2594 0.0105  -0.0272 -0.0718 143 ARG A NH2 
1051 N N   . VAL A 130 ? 0.3059 0.2693 0.2881 0.0094  0.0371  0.0146  144 VAL A N   
1052 C CA  . VAL A 130 ? 0.3150 0.2798 0.3036 0.0103  0.0449  0.0273  144 VAL A CA  
1053 C C   . VAL A 130 ? 0.3267 0.2956 0.3285 0.0011  0.0484  0.0211  144 VAL A C   
1054 O O   . VAL A 130 ? 0.3257 0.2986 0.3314 0.0005  0.0546  0.0304  144 VAL A O   
1055 C CB  . VAL A 130 ? 0.3282 0.2759 0.3194 0.0149  0.0562  0.0381  144 VAL A CB  
1056 C CG1 . VAL A 130 ? 0.3273 0.2739 0.3089 0.0236  0.0532  0.0413  144 VAL A CG1 
1057 C CG2 . VAL A 130 ? 0.3475 0.2761 0.3509 0.0076  0.0658  0.0305  144 VAL A CG2 
1058 N N   . SER A 131 ? 0.3433 0.3123 0.3522 -0.0059 0.0451  0.0048  145 SER A N   
1059 C CA  . SER A 131 ? 0.3608 0.3402 0.3845 -0.0152 0.0458  -0.0056 145 SER A CA  
1060 C C   . SER A 131 ? 0.3719 0.3626 0.3945 -0.0167 0.0330  -0.0236 145 SER A C   
1061 O O   . SER A 131 ? 0.3631 0.3535 0.3699 -0.0098 0.0237  -0.0243 145 SER A O   
1062 C CB  . SER A 131 ? 0.3775 0.3421 0.4176 -0.0245 0.0609  -0.0068 145 SER A CB  
1063 O OG  . SER A 131 ? 0.3883 0.3411 0.4334 -0.0292 0.0621  -0.0202 145 SER A OG  
1064 N N   . MET A 132 ? 0.3941 0.3956 0.4331 -0.0255 0.0328  -0.0383 146 MET A N   
1065 C CA  . MET A 132 ? 0.4137 0.4300 0.4515 -0.0251 0.0190  -0.0557 146 MET A CA  
1066 C C   . MET A 132 ? 0.4265 0.4302 0.4541 -0.0237 0.0161  -0.0632 146 MET A C   
1067 O O   . MET A 132 ? 0.4221 0.4314 0.4336 -0.0167 0.0036  -0.0678 146 MET A O   
1068 C CB  . MET A 132 ? 0.4306 0.4644 0.4918 -0.0354 0.0199  -0.0723 146 MET A CB  
1069 C CG  . MET A 132 ? 0.4271 0.4799 0.4977 -0.0358 0.0200  -0.0690 146 MET A CG  
1070 S SD  . MET A 132 ? 0.4395 0.5067 0.4909 -0.0211 0.0034  -0.0636 146 MET A SD  
1071 C CE  . MET A 132 ? 0.4298 0.4821 0.4674 -0.0160 0.0123  -0.0393 146 MET A CE  
1072 N N   . ARG A 133 ? 0.4511 0.4364 0.4865 -0.0297 0.0283  -0.0639 147 ARG A N   
1073 C CA  . ARG A 133 ? 0.4716 0.4471 0.5008 -0.0302 0.0267  -0.0753 147 ARG A CA  
1074 C C   . ARG A 133 ? 0.4813 0.4336 0.5012 -0.0253 0.0358  -0.0631 147 ARG A C   
1075 O O   . ARG A 133 ? 0.5037 0.4481 0.5157 -0.0242 0.0347  -0.0713 147 ARG A O   
1076 C CB  . ARG A 133 ? 0.4853 0.4630 0.5361 -0.0429 0.0319  -0.0951 147 ARG A CB  
1077 C CG  . ARG A 133 ? 0.4998 0.4744 0.5458 -0.0447 0.0280  -0.1130 147 ARG A CG  
1078 C CD  . ARG A 133 ? 0.4961 0.4921 0.5268 -0.0382 0.0092  -0.1243 147 ARG A CD  
1079 N NE  . ARG A 133 ? 0.5091 0.4990 0.5263 -0.0367 0.0058  -0.1363 147 ARG A NE  
1080 C CZ  . ARG A 133 ? 0.5120 0.5162 0.5114 -0.0304 -0.0090 -0.1466 147 ARG A CZ  
1081 N NH1 . ARG A 133 ? 0.5026 0.5271 0.4965 -0.0241 -0.0226 -0.1464 147 ARG A NH1 
1082 N NH2 . ARG A 133 ? 0.5272 0.5249 0.5131 -0.0295 -0.0100 -0.1568 147 ARG A NH2 
1083 N N   . ARG A 134 ? 0.4697 0.4128 0.4900 -0.0214 0.0444  -0.0443 148 ARG A N   
1084 C CA  . ARG A 134 ? 0.4823 0.4055 0.4976 -0.0159 0.0534  -0.0342 148 ARG A CA  
1085 C C   . ARG A 134 ? 0.4647 0.3927 0.4632 -0.0048 0.0480  -0.0194 148 ARG A C   
1086 O O   . ARG A 134 ? 0.4448 0.3861 0.4393 -0.0021 0.0427  -0.0114 148 ARG A O   
1087 C CB  . ARG A 134 ? 0.5072 0.4116 0.5378 -0.0200 0.0698  -0.0266 148 ARG A CB  
1088 C CG  . ARG A 134 ? 0.5112 0.4154 0.5412 -0.0150 0.0755  -0.0060 148 ARG A CG  
1089 C CD  . ARG A 134 ? 0.5393 0.4229 0.5833 -0.0204 0.0927  0.0002  148 ARG A CD  
1090 N NE  . ARG A 134 ? 0.5421 0.4295 0.5837 -0.0169 0.0974  0.0185  148 ARG A NE  
1091 C CZ  . ARG A 134 ? 0.5559 0.4479 0.6079 -0.0261 0.1038  0.0184  148 ARG A CZ  
1092 N NH1 . ARG A 134 ? 0.5633 0.4567 0.6318 -0.0400 0.1067  0.0004  148 ARG A NH1 
1093 N NH2 . ARG A 134 ? 0.5588 0.4558 0.6050 -0.0217 0.1075  0.0353  148 ARG A NH2 
1094 N N   . GLY A 135 ? 0.4619 0.3797 0.4520 0.0009  0.0503  -0.0175 151 GLY A N   
1095 C CA  . GLY A 135 ? 0.4466 0.3704 0.4224 0.0097  0.0458  -0.0076 151 GLY A CA  
1096 C C   . GLY A 135 ? 0.4401 0.3547 0.4193 0.0174  0.0550  0.0057  151 GLY A C   
1097 O O   . GLY A 135 ? 0.4742 0.3765 0.4647 0.0172  0.0648  0.0112  151 GLY A O   
1098 N N   . THR A 136 ? 0.4155 0.3364 0.3846 0.0244  0.0521  0.0107  152 THR A N   
1099 C CA  . THR A 136 ? 0.4073 0.3260 0.3793 0.0339  0.0584  0.0222  152 THR A CA  
1100 C C   . THR A 136 ? 0.3942 0.3158 0.3582 0.0374  0.0573  0.0170  152 THR A C   
1101 O O   . THR A 136 ? 0.3884 0.3170 0.3408 0.0335  0.0506  0.0099  152 THR A O   
1102 C CB  . THR A 136 ? 0.3975 0.3310 0.3680 0.0388  0.0552  0.0358  152 THR A CB  
1103 O OG1 . THR A 136 ? 0.4058 0.3407 0.3791 0.0495  0.0597  0.0460  152 THR A OG1 
1104 C CG2 . THR A 136 ? 0.3770 0.3276 0.3366 0.0369  0.0451  0.0331  152 THR A CG2 
1105 N N   . ASP A 137 ? 0.3898 0.3059 0.3601 0.0454  0.0646  0.0212  153 ASP A N   
1106 C CA  . ASP A 137 ? 0.3906 0.3122 0.3567 0.0494  0.0657  0.0168  153 ASP A CA  
1107 C C   . ASP A 137 ? 0.3603 0.3021 0.3251 0.0558  0.0622  0.0260  153 ASP A C   
1108 O O   . ASP A 137 ? 0.3472 0.2989 0.3070 0.0557  0.0616  0.0213  153 ASP A O   
1109 C CB  . ASP A 137 ? 0.4165 0.3244 0.3926 0.0563  0.0757  0.0153  153 ASP A CB  
1110 C CG  . ASP A 137 ? 0.4468 0.3347 0.4254 0.0498  0.0809  0.0024  153 ASP A CG  
1111 O OD1 . ASP A 137 ? 0.4517 0.3400 0.4221 0.0400  0.0755  -0.0077 153 ASP A OD1 
1112 O OD2 . ASP A 137 ? 0.4764 0.3489 0.4652 0.0554  0.0903  0.0018  153 ASP A OD2 
1113 N N   . THR A 138 ? 0.3419 0.2906 0.3117 0.0610  0.0609  0.0383  154 THR A N   
1114 C CA  . THR A 138 ? 0.3217 0.2919 0.2928 0.0686  0.0577  0.0463  154 THR A CA  
1115 C C   . THR A 138 ? 0.2937 0.2773 0.2583 0.0637  0.0499  0.0496  154 THR A C   
1116 O O   . THR A 138 ? 0.2894 0.2656 0.2523 0.0588  0.0486  0.0512  154 THR A O   
1117 C CB  . THR A 138 ? 0.3395 0.3085 0.3202 0.0821  0.0627  0.0581  154 THR A CB  
1118 O OG1 . THR A 138 ? 0.3510 0.3081 0.3320 0.0818  0.0647  0.0673  154 THR A OG1 
1119 C CG2 . THR A 138 ? 0.3593 0.3127 0.3476 0.0880  0.0712  0.0542  154 THR A CG2 
1120 N N   . LEU A 139 ? 0.2690 0.2735 0.2317 0.0651  0.0457  0.0494  155 LEU A N   
1121 C CA  . LEU A 139 ? 0.2491 0.2678 0.2062 0.0610  0.0388  0.0506  155 LEU A CA  
1122 C C   . LEU A 139 ? 0.2463 0.2687 0.2058 0.0659  0.0379  0.0617  155 LEU A C   
1123 O O   . LEU A 139 ? 0.2528 0.2774 0.2177 0.0762  0.0412  0.0711  155 LEU A O   
1124 C CB  . LEU A 139 ? 0.2390 0.2801 0.1975 0.0623  0.0366  0.0475  155 LEU A CB  
1125 C CG  . LEU A 139 ? 0.2260 0.2825 0.1798 0.0575  0.0303  0.0463  155 LEU A CG  
1126 C CD1 . LEU A 139 ? 0.2239 0.2665 0.1665 0.0467  0.0280  0.0391  155 LEU A CD1 
1127 C CD2 . LEU A 139 ? 0.2186 0.3001 0.1781 0.0591  0.0293  0.0424  155 LEU A CD2 
1128 N N   . ARG A 140 ? 0.2603 0.2754 0.1902 0.0750  0.0479  0.0735  156 ARG A N   
1129 C CA  . ARG A 140 ? 0.2664 0.2823 0.1926 0.0772  0.0510  0.0774  156 ARG A CA  
1130 C C   . ARG A 140 ? 0.2496 0.2862 0.1772 0.0740  0.0376  0.0724  156 ARG A C   
1131 O O   . ARG A 140 ? 0.2342 0.2798 0.1671 0.0679  0.0276  0.0647  156 ARG A O   
1132 C CB  . ARG A 140 ? 0.2760 0.2709 0.2031 0.0688  0.0607  0.0721  156 ARG A CB  
1133 C CG  . ARG A 140 ? 0.2962 0.2677 0.2228 0.0711  0.0760  0.0753  156 ARG A CG  
1134 C CD  . ARG A 140 ? 0.3080 0.2601 0.2395 0.0616  0.0865  0.0685  156 ARG A CD  
1135 N NE  . ARG A 140 ? 0.3183 0.2679 0.2486 0.0662  0.0956  0.0776  156 ARG A NE  
1136 C CZ  . ARG A 140 ? 0.3397 0.2767 0.2654 0.0775  0.1111  0.0916  156 ARG A CZ  
1137 N NH1 . ARG A 140 ? 0.3514 0.2764 0.2751 0.0846  0.1194  0.0973  156 ARG A NH1 
1138 N NH2 . ARG A 140 ? 0.3514 0.2872 0.2741 0.0828  0.1195  0.1007  156 ARG A NH2 
1139 N N   . GLU A 141 ? 0.2529 0.2951 0.1748 0.0789  0.0389  0.0770  157 GLU A N   
1140 C CA  . GLU A 141 ? 0.2442 0.3051 0.1658 0.0770  0.0272  0.0715  157 GLU A CA  
1141 C C   . GLU A 141 ? 0.2550 0.3121 0.1698 0.0783  0.0331  0.0739  157 GLU A C   
1142 O O   . GLU A 141 ? 0.2704 0.3136 0.1803 0.0839  0.0466  0.0829  157 GLU A O   
1143 C CB  . GLU A 141 ? 0.2419 0.3262 0.1631 0.0862  0.0182  0.0746  157 GLU A CB  
1144 C CG  . GLU A 141 ? 0.2583 0.3468 0.1698 0.1021  0.0250  0.0882  157 GLU A CG  
1145 C CD  . GLU A 141 ? 0.2560 0.3723 0.1697 0.1113  0.0141  0.0895  157 GLU A CD  
1146 O OE1 . GLU A 141 ? 0.2496 0.3704 0.1736 0.1106  0.0117  0.0890  157 GLU A OE1 
1147 O OE2 . GLU A 141 ? 0.2596 0.3944 0.1654 0.1190  0.0079  0.0900  157 GLU A OE2 
1148 N N   . VAL A 142 ? 0.2500 0.3181 0.1653 0.0735  0.0244  0.0661  158 VAL A N   
1149 C CA  . VAL A 142 ? 0.2625 0.3296 0.1710 0.0757  0.0297  0.0683  158 VAL A CA  
1150 C C   . VAL A 142 ? 0.2586 0.3450 0.1640 0.0759  0.0175  0.0610  158 VAL A C   
1151 O O   . VAL A 142 ? 0.2421 0.3365 0.1556 0.0688  0.0066  0.0514  158 VAL A O   
1152 C CB  . VAL A 142 ? 0.2598 0.3097 0.1763 0.0647  0.0378  0.0635  158 VAL A CB  
1153 C CG1 . VAL A 142 ? 0.2423 0.2979 0.1678 0.0534  0.0269  0.0505  158 VAL A CG1 
1154 C CG2 . VAL A 142 ? 0.2770 0.3208 0.1886 0.0684  0.0497  0.0697  158 VAL A CG2 
1155 N N   . GLN A 143 ? 0.2762 0.3686 0.1695 0.0846  0.0207  0.0658  159 GLN A N   
1156 C CA  . GLN A 143 ? 0.2802 0.3892 0.1687 0.0852  0.0106  0.0576  159 GLN A CA  
1157 C C   . GLN A 143 ? 0.2683 0.3689 0.1606 0.0766  0.0142  0.0516  159 GLN A C   
1158 O O   . GLN A 143 ? 0.2698 0.3576 0.1607 0.0772  0.0271  0.0581  159 GLN A O   
1159 C CB  . GLN A 143 ? 0.3159 0.4387 0.1862 0.1011  0.0110  0.0649  159 GLN A CB  
1160 C CG  . GLN A 143 ? 0.3365 0.4749 0.2045 0.1109  0.0043  0.0691  159 GLN A CG  
1161 C CD  . GLN A 143 ? 0.3833 0.5389 0.2314 0.1289  0.0034  0.0762  159 GLN A CD  
1162 O OE1 . GLN A 143 ? 0.4241 0.5699 0.2587 0.1405  0.0172  0.0907  159 GLN A OE1 
1163 N NE2 . GLN A 143 ? 0.3897 0.5714 0.2362 0.1317  -0.0121 0.0657  159 GLN A NE2 
1164 N N   . LEU A 144 ? 0.2526 0.3609 0.1516 0.0689  0.0037  0.0394  160 LEU A N   
1165 C CA  . LEU A 144 ? 0.2449 0.3485 0.1490 0.0617  0.0054  0.0330  160 LEU A CA  
1166 C C   . LEU A 144 ? 0.2441 0.3610 0.1419 0.0639  -0.0026 0.0242  160 LEU A C   
1167 O O   . LEU A 144 ? 0.2387 0.3676 0.1368 0.0648  -0.0130 0.0179  160 LEU A O   
1168 C CB  . LEU A 144 ? 0.2286 0.3249 0.1483 0.0502  0.0022  0.0265  160 LEU A CB  
1169 C CG  . LEU A 144 ? 0.2291 0.3125 0.1554 0.0465  0.0086  0.0312  160 LEU A CG  
1170 C CD1 . LEU A 144 ? 0.2177 0.2981 0.1555 0.0375  0.0028  0.0237  160 LEU A CD1 
1171 C CD2 . LEU A 144 ? 0.2422 0.3150 0.1692 0.0464  0.0218  0.0366  160 LEU A CD2 
1172 N N   . ARG A 145 ? 0.2473 0.3619 0.1419 0.0640  0.0026  0.0226  161 ARG A N   
1173 C CA  . ARG A 145 ? 0.2535 0.3783 0.1414 0.0661  -0.0034 0.0131  161 ARG A CA  
1174 C C   . ARG A 145 ? 0.2340 0.3549 0.1364 0.0560  -0.0072 0.0032  161 ARG A C   
1175 O O   . ARG A 145 ? 0.2243 0.3362 0.1373 0.0502  -0.0019 0.0052  161 ARG A O   
1176 C CB  . ARG A 145 ? 0.2779 0.4034 0.1499 0.0757  0.0061  0.0188  161 ARG A CB  
1177 C CG  . ARG A 145 ? 0.2990 0.4402 0.1521 0.0863  -0.0005 0.0141  161 ARG A CG  
1178 C CD  . ARG A 145 ? 0.3232 0.4648 0.1561 0.0989  0.0104  0.0225  161 ARG A CD  
1179 N NE  . ARG A 145 ? 0.3394 0.4824 0.1583 0.1116  0.0169  0.0371  161 ARG A NE  
1180 C CZ  . ARG A 145 ? 0.3545 0.5142 0.1564 0.1240  0.0092  0.0378  161 ARG A CZ  
1181 N NH1 . ARG A 145 ? 0.3557 0.5333 0.1533 0.1242  -0.0058 0.0224  161 ARG A NH1 
1182 N NH2 . ARG A 145 ? 0.3701 0.5293 0.1599 0.1368  0.0169  0.0534  161 ARG A NH2 
1183 N N   . VAL A 146 ? 0.2314 0.3600 0.1344 0.0546  -0.0162 -0.0079 162 VAL A N   
1184 C CA  . VAL A 146 ? 0.2211 0.3454 0.1358 0.0474  -0.0185 -0.0168 162 VAL A CA  
1185 C C   . VAL A 146 ? 0.2267 0.3480 0.1374 0.0497  -0.0113 -0.0174 162 VAL A C   
1186 O O   . VAL A 146 ? 0.2376 0.3643 0.1336 0.0570  -0.0088 -0.0182 162 VAL A O   
1187 C CB  . VAL A 146 ? 0.2229 0.3542 0.1407 0.0452  -0.0276 -0.0293 162 VAL A CB  
1188 C CG1 . VAL A 146 ? 0.2179 0.3412 0.1481 0.0390  -0.0273 -0.0368 162 VAL A CG1 
1189 C CG2 . VAL A 146 ? 0.2157 0.3523 0.1403 0.0430  -0.0339 -0.0286 162 VAL A CG2 
1190 N N   . GLN A 147 ? 0.2162 0.3304 0.1398 0.0444  -0.0078 -0.0169 163 GLN A N   
1191 C CA  . GLN A 147 ? 0.2234 0.3361 0.1482 0.0460  -0.0004 -0.0170 163 GLN A CA  
1192 C C   . GLN A 147 ? 0.2238 0.3357 0.1528 0.0449  -0.0034 -0.0271 163 GLN A C   
1193 O O   . GLN A 147 ? 0.2194 0.3301 0.1530 0.0417  -0.0101 -0.0334 163 GLN A O   
1194 C CB  . GLN A 147 ? 0.2174 0.3262 0.1563 0.0415  0.0048  -0.0110 163 GLN A CB  
1195 C CG  . GLN A 147 ? 0.2184 0.3244 0.1568 0.0408  0.0092  -0.0023 163 GLN A CG  
1196 C CD  . GLN A 147 ? 0.2364 0.3423 0.1625 0.0476  0.0192  0.0046  163 GLN A CD  
1197 O OE1 . GLN A 147 ? 0.2432 0.3482 0.1737 0.0482  0.0292  0.0075  163 GLN A OE1 
1198 N NE2 . GLN A 147 ? 0.2469 0.3547 0.1580 0.0538  0.0173  0.0081  163 GLN A NE2 
1199 N N   . ARG A 148 ? 0.2297 0.3414 0.1581 0.0480  0.0033  -0.0284 164 ARG A N   
1200 C CA  . ARG A 148 ? 0.2323 0.3411 0.1655 0.0481  0.0032  -0.0369 164 ARG A CA  
1201 C C   . ARG A 148 ? 0.2192 0.3244 0.1704 0.0442  0.0025  -0.0346 164 ARG A C   
1202 O O   . ARG A 148 ? 0.2059 0.3134 0.1656 0.0422  0.0043  -0.0276 164 ARG A O   
1203 C CB  . ARG A 148 ? 0.2465 0.3568 0.1730 0.0542  0.0121  -0.0375 164 ARG A CB  
1204 C CG  . ARG A 148 ? 0.2652 0.3800 0.1700 0.0612  0.0140  -0.0391 164 ARG A CG  
1205 C CD  . ARG A 148 ? 0.2816 0.3967 0.1801 0.0679  0.0249  -0.0387 164 ARG A CD  
1206 N NE  . ARG A 148 ? 0.2778 0.3934 0.1880 0.0672  0.0348  -0.0275 164 ARG A NE  
1207 C CZ  . ARG A 148 ? 0.2840 0.4009 0.1890 0.0697  0.0422  -0.0172 164 ARG A CZ  
1208 N NH1 . ARG A 148 ? 0.2959 0.4144 0.1806 0.0755  0.0409  -0.0147 164 ARG A NH1 
1209 N NH2 . ARG A 148 ? 0.2819 0.3991 0.2032 0.0669  0.0516  -0.0095 164 ARG A NH2 
1210 N N   . ASP A 149 ? 0.2243 0.3238 0.1809 0.0438  0.0007  -0.0411 165 ASP A N   
1211 C CA  . ASP A 149 ? 0.2201 0.3163 0.1910 0.0430  0.0006  -0.0382 165 ASP A CA  
1212 C C   . ASP A 149 ? 0.2105 0.3136 0.1902 0.0454  0.0051  -0.0324 165 ASP A C   
1213 O O   . ASP A 149 ? 0.1958 0.3026 0.1850 0.0440  0.0024  -0.0275 165 ASP A O   
1214 C CB  . ASP A 149 ? 0.2381 0.3254 0.2129 0.0450  0.0027  -0.0450 165 ASP A CB  
1215 C CG  . ASP A 149 ? 0.2540 0.3341 0.2262 0.0413  -0.0005 -0.0537 165 ASP A CG  
1216 O OD1 . ASP A 149 ? 0.2480 0.3317 0.2172 0.0373  -0.0062 -0.0532 165 ASP A OD1 
1217 O OD2 . ASP A 149 ? 0.2769 0.3483 0.2519 0.0424  0.0033  -0.0616 165 ASP A OD2 
1218 N N   . ARG A 150 ? 0.2168 0.3228 0.1942 0.0494  0.0120  -0.0339 166 ARG A N   
1219 C CA  . ARG A 150 ? 0.2126 0.3272 0.2027 0.0516  0.0173  -0.0296 166 ARG A CA  
1220 C C   . ARG A 150 ? 0.1985 0.3211 0.1956 0.0469  0.0170  -0.0238 166 ARG A C   
1221 O O   . ARG A 150 ? 0.1909 0.3231 0.2039 0.0463  0.0179  -0.0216 166 ARG A O   
1222 C CB  . ARG A 150 ? 0.2308 0.3464 0.2168 0.0571  0.0265  -0.0320 166 ARG A CB  
1223 C CG  . ARG A 150 ? 0.2447 0.3532 0.2305 0.0624  0.0290  -0.0380 166 ARG A CG  
1224 C CD  . ARG A 150 ? 0.2625 0.3733 0.2461 0.0687  0.0394  -0.0396 166 ARG A CD  
1225 N NE  . ARG A 150 ? 0.2791 0.3812 0.2629 0.0743  0.0434  -0.0458 166 ARG A NE  
1226 C CZ  . ARG A 150 ? 0.2988 0.3888 0.2695 0.0748  0.0431  -0.0558 166 ARG A CZ  
1227 N NH1 . ARG A 150 ? 0.3080 0.3964 0.2633 0.0709  0.0379  -0.0610 166 ARG A NH1 
1228 N NH2 . ARG A 150 ? 0.3122 0.3925 0.2862 0.0797  0.0485  -0.0612 166 ARG A NH2 
1229 N N   . GLN A 151 ? 0.1962 0.3155 0.1826 0.0438  0.0162  -0.0219 167 GLN A N   
1230 C CA  . GLN A 151 ? 0.1902 0.3133 0.1832 0.0391  0.0180  -0.0168 167 GLN A CA  
1231 C C   . GLN A 151 ? 0.1781 0.3037 0.1818 0.0348  0.0101  -0.0168 167 GLN A C   
1232 O O   . GLN A 151 ? 0.1750 0.3070 0.1912 0.0306  0.0114  -0.0157 167 GLN A O   
1233 C CB  . GLN A 151 ? 0.1990 0.3166 0.1764 0.0393  0.0203  -0.0134 167 GLN A CB  
1234 C CG  . GLN A 151 ? 0.2161 0.3332 0.1801 0.0457  0.0287  -0.0127 167 GLN A CG  
1235 C CD  . GLN A 151 ? 0.2287 0.3425 0.1750 0.0488  0.0308  -0.0080 167 GLN A CD  
1236 O OE1 . GLN A 151 ? 0.2351 0.3484 0.1652 0.0528  0.0253  -0.0118 167 GLN A OE1 
1237 N NE2 . GLN A 151 ? 0.2338 0.3460 0.1843 0.0474  0.0391  0.0000  167 GLN A NE2 
1238 N N   . CYS A 152 ? 0.1697 0.2904 0.1691 0.0359  0.0027  -0.0187 168 CYS A N   
1239 C CA  . CYS A 152 ? 0.1634 0.2865 0.1699 0.0344  -0.0039 -0.0180 168 CYS A CA  
1240 C C   . CYS A 152 ? 0.1643 0.2947 0.1814 0.0395  -0.0052 -0.0187 168 CYS A C   
1241 O O   . CYS A 152 ? 0.1651 0.3043 0.1907 0.0397  -0.0099 -0.0183 168 CYS A O   
1242 C CB  . CYS A 152 ? 0.1594 0.2731 0.1564 0.0338  -0.0091 -0.0176 168 CYS A CB  
1243 S SG  . CYS A 152 ? 0.1560 0.2655 0.1450 0.0287  -0.0100 -0.0149 168 CYS A SG  
1244 N N   . LEU A 153 ? 0.1714 0.2985 0.1871 0.0446  -0.0012 -0.0202 169 LEU A N   
1245 C CA  . LEU A 153 ? 0.1773 0.3104 0.2027 0.0516  -0.0009 -0.0195 169 LEU A CA  
1246 C C   . LEU A 153 ? 0.1750 0.3264 0.2165 0.0517  0.0000  -0.0193 169 LEU A C   
1247 O O   . LEU A 153 ? 0.1715 0.3347 0.2232 0.0567  -0.0041 -0.0183 169 LEU A O   
1248 C CB  . LEU A 153 ? 0.1884 0.3122 0.2095 0.0569  0.0052  -0.0219 169 LEU A CB  
1249 C CG  . LEU A 153 ? 0.1947 0.3019 0.2064 0.0571  0.0045  -0.0239 169 LEU A CG  
1250 C CD1 . LEU A 153 ? 0.2075 0.3049 0.2139 0.0594  0.0111  -0.0301 169 LEU A CD1 
1251 C CD2 . LEU A 153 ? 0.1963 0.3007 0.2129 0.0628  0.0026  -0.0192 169 LEU A CD2 
1252 N N   . ARG A 154 ? 0.1762 0.3308 0.2206 0.0469  0.0058  -0.0203 170 ARG A N   
1253 C CA  . ARG A 154 ? 0.1765 0.3484 0.2403 0.0451  0.0089  -0.0211 170 ARG A CA  
1254 C C   . ARG A 154 ? 0.1707 0.3542 0.2455 0.0396  0.0013  -0.0233 170 ARG A C   
1255 O O   . ARG A 154 ? 0.1686 0.3714 0.2629 0.0398  -0.0004 -0.0261 170 ARG A O   
1256 C CB  . ARG A 154 ? 0.1814 0.3509 0.2451 0.0416  0.0199  -0.0203 170 ARG A CB  
1257 C CG  . ARG A 154 ? 0.1900 0.3575 0.2507 0.0486  0.0285  -0.0199 170 ARG A CG  
1258 C CD  . ARG A 154 ? 0.1966 0.3659 0.2607 0.0469  0.0411  -0.0178 170 ARG A CD  
1259 N NE  . ARG A 154 ? 0.2007 0.3562 0.2449 0.0444  0.0438  -0.0154 170 ARG A NE  
1260 C CZ  . ARG A 154 ? 0.2079 0.3516 0.2295 0.0493  0.0448  -0.0161 170 ARG A CZ  
1261 N NH1 . ARG A 154 ? 0.2156 0.3570 0.2318 0.0559  0.0459  -0.0197 170 ARG A NH1 
1262 N NH2 . ARG A 154 ? 0.2116 0.3467 0.2163 0.0481  0.0450  -0.0138 170 ARG A NH2 
1263 N N   . ILE A 155 ? 0.1715 0.3449 0.2351 0.0347  -0.0030 -0.0231 171 ILE A N   
1264 C CA  . ILE A 155 ? 0.1695 0.3517 0.2425 0.0284  -0.0083 -0.0269 171 ILE A CA  
1265 C C   . ILE A 155 ? 0.1659 0.3480 0.2304 0.0322  -0.0189 -0.0270 171 ILE A C   
1266 O O   . ILE A 155 ? 0.1621 0.3555 0.2342 0.0294  -0.0252 -0.0318 171 ILE A O   
1267 C CB  . ILE A 155 ? 0.1751 0.3464 0.2447 0.0197  -0.0020 -0.0264 171 ILE A CB  
1268 C CG1 . ILE A 155 ? 0.1780 0.3307 0.2254 0.0207  -0.0028 -0.0221 171 ILE A CG1 
1269 C CG2 . ILE A 155 ? 0.1813 0.3538 0.2601 0.0175  0.0104  -0.0249 171 ILE A CG2 
1270 C CD1 . ILE A 155 ? 0.1820 0.3247 0.2254 0.0145  0.0031  -0.0202 171 ILE A CD1 
1271 N N   . PHE A 156 ? 0.1678 0.3376 0.2175 0.0388  -0.0201 -0.0224 172 PHE A N   
1272 C CA  . PHE A 156 ? 0.1693 0.3369 0.2101 0.0438  -0.0274 -0.0204 172 PHE A CA  
1273 C C   . PHE A 156 ? 0.1724 0.3412 0.2124 0.0552  -0.0275 -0.0163 172 PHE A C   
1274 O O   . PHE A 156 ? 0.1737 0.3275 0.2060 0.0580  -0.0224 -0.0131 172 PHE A O   
1275 C CB  . PHE A 156 ? 0.1695 0.3183 0.1946 0.0404  -0.0267 -0.0178 172 PHE A CB  
1276 C CG  . PHE A 156 ? 0.1687 0.3140 0.1927 0.0313  -0.0258 -0.0201 172 PHE A CG  
1277 C CD1 . PHE A 156 ? 0.1732 0.3259 0.2010 0.0281  -0.0306 -0.0242 172 PHE A CD1 
1278 C CD2 . PHE A 156 ? 0.1709 0.3048 0.1884 0.0272  -0.0198 -0.0183 172 PHE A CD2 
1279 C CE1 . PHE A 156 ? 0.1747 0.3209 0.2019 0.0201  -0.0278 -0.0262 172 PHE A CE1 
1280 C CE2 . PHE A 156 ? 0.1700 0.2991 0.1858 0.0210  -0.0173 -0.0185 172 PHE A CE2 
1281 C CZ  . PHE A 156 ? 0.1727 0.3065 0.1941 0.0170  -0.0204 -0.0223 172 PHE A CZ  
1282 N N   . GLY A 157 ? 0.1740 0.3614 0.2223 0.0624  -0.0332 -0.0167 173 GLY A N   
1283 C CA  . GLY A 157 ? 0.1817 0.3735 0.2315 0.0755  -0.0324 -0.0116 173 GLY A CA  
1284 C C   . GLY A 157 ? 0.1920 0.3625 0.2268 0.0823  -0.0287 -0.0042 173 GLY A C   
1285 O O   . GLY A 157 ? 0.1958 0.3585 0.2313 0.0898  -0.0221 -0.0001 173 GLY A O   
1286 N N   . SER A 158 ? 0.1973 0.3577 0.2203 0.0794  -0.0314 -0.0028 174 SER A N   
1287 C CA  . SER A 158 ? 0.2132 0.3553 0.2249 0.0858  -0.0271 0.0045  174 SER A CA  
1288 C C   . SER A 158 ? 0.2161 0.3371 0.2234 0.0765  -0.0211 0.0030  174 SER A C   
1289 O O   . SER A 158 ? 0.2260 0.3313 0.2269 0.0786  -0.0170 0.0075  174 SER A O   
1290 C CB  . SER A 158 ? 0.2186 0.3643 0.2203 0.0907  -0.0328 0.0079  174 SER A CB  
1291 O OG  . SER A 158 ? 0.2330 0.3982 0.2365 0.1035  -0.0381 0.0104  174 SER A OG  
1292 N N   . TYR A 159 ? 0.2119 0.3337 0.2229 0.0670  -0.0202 -0.0032 175 TYR A N   
1293 C CA  . TYR A 159 ? 0.2088 0.3158 0.2150 0.0592  -0.0166 -0.0059 175 TYR A CA  
1294 C C   . TYR A 159 ? 0.2190 0.3118 0.2258 0.0629  -0.0093 -0.0057 175 TYR A C   
1295 O O   . TYR A 159 ? 0.2241 0.3189 0.2362 0.0690  -0.0054 -0.0056 175 TYR A O   
1296 C CB  . TYR A 159 ? 0.2058 0.3185 0.2138 0.0514  -0.0165 -0.0113 175 TYR A CB  
1297 C CG  . TYR A 159 ? 0.2044 0.3062 0.2053 0.0451  -0.0144 -0.0142 175 TYR A CG  
1298 C CD1 . TYR A 159 ? 0.1974 0.2959 0.1927 0.0401  -0.0174 -0.0134 175 TYR A CD1 
1299 C CD2 . TYR A 159 ? 0.2113 0.3076 0.2110 0.0453  -0.0098 -0.0186 175 TYR A CD2 
1300 C CE1 . TYR A 159 ? 0.2028 0.2953 0.1926 0.0358  -0.0167 -0.0161 175 TYR A CE1 
1301 C CE2 . TYR A 159 ? 0.2149 0.3053 0.2077 0.0405  -0.0098 -0.0228 175 TYR A CE2 
1302 C CZ  . TYR A 159 ? 0.2112 0.3010 0.1997 0.0361  -0.0136 -0.0213 175 TYR A CZ  
1303 O OH  . TYR A 159 ? 0.2166 0.3043 0.1994 0.0327  -0.0147 -0.0254 175 TYR A OH  
1304 N N   . ASP A 160 ? 0.2219 0.3007 0.2252 0.0587  -0.0070 -0.0065 176 ASP A N   
1305 C CA  . ASP A 160 ? 0.2356 0.2990 0.2419 0.0593  0.0003  -0.0091 176 ASP A CA  
1306 C C   . ASP A 160 ? 0.2397 0.2986 0.2442 0.0493  -0.0008 -0.0171 176 ASP A C   
1307 O O   . ASP A 160 ? 0.2324 0.2888 0.2358 0.0451  -0.0029 -0.0158 176 ASP A O   
1308 C CB  . ASP A 160 ? 0.2455 0.2969 0.2534 0.0660  0.0058  -0.0014 176 ASP A CB  
1309 C CG  . ASP A 160 ? 0.2601 0.2926 0.2747 0.0661  0.0161  -0.0043 176 ASP A CG  
1310 O OD1 . ASP A 160 ? 0.2582 0.2880 0.2753 0.0606  0.0176  -0.0144 176 ASP A OD1 
1311 O OD2 . ASP A 160 ? 0.2660 0.2860 0.2831 0.0719  0.0235  0.0032  176 ASP A OD2 
1312 N N   . PRO A 161 ? 0.2491 0.3083 0.2527 0.0463  0.0004  -0.0257 177 PRO A N   
1313 C CA  . PRO A 161 ? 0.2539 0.3130 0.2542 0.0387  -0.0022 -0.0342 177 PRO A CA  
1314 C C   . PRO A 161 ? 0.2692 0.3166 0.2768 0.0345  0.0008  -0.0397 177 PRO A C   
1315 O O   . PRO A 161 ? 0.2653 0.3161 0.2727 0.0281  -0.0030 -0.0467 177 PRO A O   
1316 C CB  . PRO A 161 ? 0.2608 0.3241 0.2562 0.0396  -0.0008 -0.0416 177 PRO A CB  
1317 C CG  . PRO A 161 ? 0.2687 0.3270 0.2695 0.0468  0.0058  -0.0391 177 PRO A CG  
1318 C CD  . PRO A 161 ? 0.2570 0.3184 0.2620 0.0515  0.0045  -0.0278 177 PRO A CD  
1319 N N   . ARG A 162 ? 0.2888 0.3229 0.3043 0.0385  0.0086  -0.0363 178 ARG A N   
1320 C CA  . ARG A 162 ? 0.3066 0.3275 0.3329 0.0341  0.0143  -0.0398 178 ARG A CA  
1321 C C   . ARG A 162 ? 0.2807 0.3047 0.3083 0.0309  0.0110  -0.0334 178 ARG A C   
1322 O O   . ARG A 162 ? 0.2763 0.2967 0.3134 0.0239  0.0124  -0.0392 178 ARG A O   
1323 C CB  . ARG A 162 ? 0.3436 0.3472 0.3775 0.0412  0.0262  -0.0343 178 ARG A CB  
1324 C CG  . ARG A 162 ? 0.3862 0.3844 0.4200 0.0459  0.0316  -0.0397 178 ARG A CG  
1325 C CD  . ARG A 162 ? 0.4344 0.4122 0.4772 0.0533  0.0456  -0.0342 178 ARG A CD  
1326 N NE  . ARG A 162 ? 0.4758 0.4510 0.5180 0.0613  0.0485  -0.0179 178 ARG A NE  
1327 C CZ  . ARG A 162 ? 0.5136 0.4902 0.5511 0.0750  0.0514  -0.0046 178 ARG A CZ  
1328 N NH1 . ARG A 162 ? 0.5379 0.5162 0.5747 0.0829  0.0541  -0.0047 178 ARG A NH1 
1329 N NH2 . ARG A 162 ? 0.5263 0.5039 0.5596 0.0819  0.0517  0.0085  178 ARG A NH2 
1330 N N   . ARG A 163 ? 0.2612 0.2928 0.2803 0.0359  0.0069  -0.0226 179 ARG A N   
1331 C CA  . ARG A 163 ? 0.2518 0.2839 0.2704 0.0353  0.0057  -0.0150 179 ARG A CA  
1332 C C   . ARG A 163 ? 0.2220 0.2683 0.2314 0.0327  -0.0036 -0.0143 179 ARG A C   
1333 O O   . ARG A 163 ? 0.2113 0.2585 0.2202 0.0311  -0.0048 -0.0101 179 ARG A O   
1334 C CB  . ARG A 163 ? 0.2664 0.2917 0.2823 0.0454  0.0111  -0.0025 179 ARG A CB  
1335 C CG  . ARG A 163 ? 0.2963 0.3032 0.3223 0.0486  0.0238  0.0007  179 ARG A CG  
1336 C CD  . ARG A 163 ? 0.3198 0.3213 0.3395 0.0622  0.0295  0.0150  179 ARG A CD  
1337 N NE  . ARG A 163 ? 0.3312 0.3412 0.3443 0.0708  0.0260  0.0169  179 ARG A NE  
1338 C CZ  . ARG A 163 ? 0.3541 0.3663 0.3604 0.0845  0.0278  0.0278  179 ARG A CZ  
1339 N NH1 . ARG A 163 ? 0.3722 0.3769 0.3738 0.0926  0.0337  0.0391  179 ARG A NH1 
1340 N NH2 . ARG A 163 ? 0.3571 0.3806 0.3613 0.0912  0.0238  0.0276  179 ARG A NH2 
1341 N N   . GLN A 164 ? 0.2036 0.2596 0.2065 0.0327  -0.0084 -0.0177 180 GLN A N   
1342 C CA  . GLN A 164 ? 0.1865 0.2532 0.1816 0.0311  -0.0145 -0.0158 180 GLN A CA  
1343 C C   . GLN A 164 ? 0.1811 0.2550 0.1723 0.0276  -0.0173 -0.0230 180 GLN A C   
1344 O O   . GLN A 164 ? 0.1877 0.2599 0.1803 0.0275  -0.0154 -0.0299 180 GLN A O   
1345 C CB  . GLN A 164 ? 0.1814 0.2533 0.1730 0.0362  -0.0157 -0.0105 180 GLN A CB  
1346 C CG  . GLN A 164 ? 0.1846 0.2530 0.1753 0.0416  -0.0148 -0.0030 180 GLN A CG  
1347 C CD  . GLN A 164 ? 0.1844 0.2608 0.1738 0.0484  -0.0167 -0.0001 180 GLN A CD  
1348 O OE1 . GLN A 164 ? 0.1865 0.2659 0.1799 0.0514  -0.0151 -0.0019 180 GLN A OE1 
1349 N NE2 . GLN A 164 ? 0.1821 0.2634 0.1663 0.0513  -0.0202 0.0036  180 GLN A NE2 
1350 N N   . ILE A 165 ? 0.1722 0.2531 0.1573 0.0258  -0.0209 -0.0209 181 ILE A N   
1351 C CA  . ILE A 165 ? 0.1718 0.2601 0.1498 0.0252  -0.0226 -0.0246 181 ILE A CA  
1352 C C   . ILE A 165 ? 0.1646 0.2567 0.1378 0.0268  -0.0213 -0.0195 181 ILE A C   
1353 O O   . ILE A 165 ? 0.1559 0.2472 0.1304 0.0263  -0.0217 -0.0144 181 ILE A O   
1354 C CB  . ILE A 165 ? 0.1730 0.2666 0.1490 0.0232  -0.0263 -0.0257 181 ILE A CB  
1355 C CG1 . ILE A 165 ? 0.1759 0.2671 0.1621 0.0198  -0.0271 -0.0311 181 ILE A CG1 
1356 C CG2 . ILE A 165 ? 0.1791 0.2815 0.1449 0.0255  -0.0279 -0.0290 181 ILE A CG2 
1357 C CD1 . ILE A 165 ? 0.1723 0.2701 0.1611 0.0182  -0.0304 -0.0297 181 ILE A CD1 
1358 N N   . CYS A 166 ? 0.1665 0.2627 0.1347 0.0285  -0.0190 -0.0216 182 CYS A N   
1359 C CA  . CYS A 166 ? 0.1669 0.2664 0.1334 0.0292  -0.0153 -0.0173 182 CYS A CA  
1360 C C   . CYS A 166 ? 0.1745 0.2762 0.1315 0.0303  -0.0141 -0.0139 182 CYS A C   
1361 O O   . CYS A 166 ? 0.1829 0.2882 0.1310 0.0334  -0.0145 -0.0167 182 CYS A O   
1362 C CB  . CYS A 166 ? 0.1703 0.2723 0.1378 0.0318  -0.0108 -0.0200 182 CYS A CB  
1363 S SG  . CYS A 166 ? 0.1662 0.2731 0.1410 0.0311  -0.0047 -0.0156 182 CYS A SG  
1364 N N   . VAL A 167 ? 0.1747 0.2744 0.1328 0.0287  -0.0120 -0.0081 183 VAL A N   
1365 C CA  . VAL A 167 ? 0.1824 0.2821 0.1320 0.0310  -0.0102 -0.0029 183 VAL A CA  
1366 C C   . VAL A 167 ? 0.1864 0.2821 0.1372 0.0305  -0.0018 0.0029  183 VAL A C   
1367 O O   . VAL A 167 ? 0.1759 0.2686 0.1364 0.0258  -0.0005 0.0025  183 VAL A O   
1368 C CB  . VAL A 167 ? 0.1781 0.2763 0.1289 0.0297  -0.0153 -0.0019 183 VAL A CB  
1369 C CG1 . VAL A 167 ? 0.1870 0.2865 0.1296 0.0339  -0.0136 0.0040  183 VAL A CG1 
1370 C CG2 . VAL A 167 ? 0.1757 0.2767 0.1297 0.0289  -0.0215 -0.0083 183 VAL A CG2 
1371 N N   . GLY A 168 ? 0.2004 0.2965 0.1412 0.0358  0.0044  0.0081  184 GLY A N   
1372 C CA  . GLY A 168 ? 0.2114 0.3008 0.1534 0.0360  0.0152  0.0155  184 GLY A CA  
1373 C C   . GLY A 168 ? 0.2227 0.3123 0.1670 0.0370  0.0251  0.0170  184 GLY A C   
1374 O O   . GLY A 168 ? 0.2156 0.3087 0.1710 0.0326  0.0241  0.0114  184 GLY A O   
1375 N N   . ASP A 169 A 0.2444 0.3306 0.1781 0.0440  0.0355  0.0257  184 ASP A N   
1376 C CA  . ASP A 169 A 0.2629 0.3475 0.1980 0.0463  0.0485  0.0297  184 ASP A CA  
1377 C C   . ASP A 169 A 0.2628 0.3393 0.2176 0.0378  0.0590  0.0312  184 ASP A C   
1378 O O   . ASP A 169 A 0.2661 0.3328 0.2216 0.0374  0.0656  0.0370  184 ASP A O   
1379 C CB  . ASP A 169 A 0.2874 0.3709 0.2015 0.0589  0.0567  0.0399  184 ASP A CB  
1380 C CG  . ASP A 169 A 0.3112 0.3922 0.2219 0.0644  0.0725  0.0466  184 ASP A CG  
1381 O OD1 . ASP A 169 A 0.3079 0.3873 0.2371 0.0568  0.0795  0.0438  184 ASP A OD1 
1382 O OD2 . ASP A 169 A 0.3403 0.4222 0.2295 0.0773  0.0784  0.0549  184 ASP A OD2 
1383 N N   . ARG A 170 ? 0.2634 0.3448 0.2353 0.0315  0.0611  0.0254  185 ARG A N   
1384 C CA  . ARG A 170 ? 0.2691 0.3472 0.2644 0.0217  0.0691  0.0230  185 ARG A CA  
1385 C C   . ARG A 170 ? 0.2940 0.3598 0.2908 0.0236  0.0890  0.0333  185 ARG A C   
1386 O O   . ARG A 170 ? 0.2951 0.3546 0.3116 0.0148  0.0976  0.0313  185 ARG A O   
1387 C CB  . ARG A 170 ? 0.2609 0.3511 0.2752 0.0163  0.0678  0.0151  185 ARG A CB  
1388 C CG  . ARG A 170 ? 0.2746 0.3675 0.2888 0.0215  0.0801  0.0198  185 ARG A CG  
1389 C CD  . ARG A 170 ? 0.2658 0.3730 0.2999 0.0171  0.0768  0.0116  185 ARG A CD  
1390 N NE  . ARG A 170 ? 0.2804 0.3903 0.3155 0.0223  0.0899  0.0161  185 ARG A NE  
1391 C CZ  . ARG A 170 ? 0.2778 0.4003 0.3269 0.0220  0.0894  0.0112  185 ARG A CZ  
1392 N NH1 . ARG A 170 ? 0.2640 0.3984 0.3270 0.0175  0.0761  0.0020  185 ARG A NH1 
1393 N NH2 . ARG A 170 ? 0.2938 0.4173 0.3420 0.0277  0.1031  0.0163  185 ARG A NH2 
1394 N N   . ARG A 171 ? 0.3193 0.3818 0.2953 0.0357  0.0969  0.0439  186 ARG A N   
1395 C CA  . ARG A 171 ? 0.3495 0.3990 0.3234 0.0408  0.1182  0.0567  186 ARG A CA  
1396 C C   . ARG A 171 ? 0.3662 0.4017 0.3348 0.0425  0.1226  0.0637  186 ARG A C   
1397 O O   . ARG A 171 ? 0.3877 0.4084 0.3621 0.0434  0.1421  0.0730  186 ARG A O   
1398 C CB  . ARG A 171 ? 0.3657 0.4174 0.3150 0.0560  0.1251  0.0666  186 ARG A CB  
1399 C CG  . ARG A 171 ? 0.3691 0.4290 0.3268 0.0551  0.1306  0.0633  186 ARG A CG  
1400 C CD  . ARG A 171 ? 0.3891 0.4515 0.3189 0.0712  0.1365  0.0716  186 ARG A CD  
1401 N NE  . ARG A 171 ? 0.3853 0.4578 0.2919 0.0781  0.1171  0.0656  186 ARG A NE  
1402 C CZ  . ARG A 171 ? 0.4028 0.4825 0.2838 0.0910  0.1151  0.0666  186 ARG A CZ  
1403 N NH1 . ARG A 171 ? 0.4246 0.5018 0.2955 0.1007  0.1319  0.0755  186 ARG A NH1 
1404 N NH2 . ARG A 171 ? 0.3967 0.4863 0.2631 0.0939  0.0965  0.0578  186 ARG A NH2 
1405 N N   . GLU A 172 ? 0.3681 0.4071 0.3268 0.0434  0.1063  0.0597  187 GLU A N   
1406 C CA  . GLU A 172 ? 0.3887 0.4156 0.3411 0.0467  0.1101  0.0667  187 GLU A CA  
1407 C C   . GLU A 172 ? 0.3700 0.3940 0.3394 0.0339  0.1017  0.0556  187 GLU A C   
1408 O O   . GLU A 172 ? 0.3379 0.3738 0.3125 0.0276  0.0856  0.0440  187 GLU A O   
1409 C CB  . GLU A 172 ? 0.4124 0.4469 0.3391 0.0600  0.0994  0.0723  187 GLU A CB  
1410 C CG  . GLU A 172 ? 0.4493 0.4905 0.3547 0.0745  0.1043  0.0811  187 GLU A CG  
1411 C CD  . GLU A 172 ? 0.4825 0.5327 0.3641 0.0886  0.0952  0.0868  187 GLU A CD  
1412 O OE1 . GLU A 172 ? 0.5049 0.5715 0.3751 0.0923  0.0808  0.0797  187 GLU A OE1 
1413 O OE2 . GLU A 172 ? 0.5093 0.5507 0.3851 0.0958  0.1026  0.0975  187 GLU A OE2 
1414 N N   . ARG A 173 ? 0.3726 0.3799 0.3488 0.0315  0.1137  0.0596  188 ARG A N   
1415 C CA  . ARG A 173 ? 0.3585 0.3610 0.3465 0.0214  0.1072  0.0494  188 ARG A CA  
1416 C C   . ARG A 173 ? 0.3421 0.3473 0.3122 0.0291  0.0949  0.0524  188 ARG A C   
1417 O O   . ARG A 173 ? 0.3563 0.3485 0.3212 0.0337  0.1023  0.0595  188 ARG A O   
1418 C CB  . ARG A 173 ? 0.3821 0.3643 0.3865 0.0148  0.1266  0.0505  188 ARG A CB  
1419 C CG  . ARG A 173 ? 0.3823 0.3617 0.4031 0.0015  0.1202  0.0351  188 ARG A CG  
1420 C CD  . ARG A 173 ? 0.4103 0.3667 0.4454 -0.0043 0.1398  0.0352  188 ARG A CD  
1421 N NE  . ARG A 173 ? 0.4111 0.3635 0.4509 -0.0120 0.1314  0.0223  188 ARG A NE  
1422 C CZ  . ARG A 173 ? 0.4256 0.3664 0.4515 -0.0054 0.1315  0.0274  188 ARG A CZ  
1423 N NH1 . ARG A 173 ? 0.4389 0.3707 0.4471 0.0090  0.1404  0.0456  188 ARG A NH1 
1424 N NH2 . ARG A 173 ? 0.4232 0.3628 0.4520 -0.0121 0.1226  0.0144  188 ARG A NH2 
1425 N N   . LYS A 174 A 0.3114 0.3333 0.2743 0.0303  0.0772  0.0468  188 LYS A N   
1426 C CA  . LYS A 174 A 0.2918 0.3198 0.2415 0.0365  0.0647  0.0481  188 LYS A CA  
1427 C C   . LYS A 174 A 0.2573 0.2977 0.2122 0.0297  0.0481  0.0360  188 LYS A C   
1428 O O   . LYS A 174 A 0.2464 0.2970 0.2030 0.0285  0.0431  0.0318  188 LYS A O   
1429 C CB  . LYS A 174 A 0.3019 0.3388 0.2329 0.0500  0.0633  0.0576  188 LYS A CB  
1430 C CG  . LYS A 174 A 0.3298 0.3565 0.2498 0.0618  0.0781  0.0727  188 LYS A CG  
1431 C CD  . LYS A 174 A 0.3446 0.3848 0.2443 0.0767  0.0745  0.0805  188 LYS A CD  
1432 C CE  . LYS A 174 A 0.3744 0.4064 0.2610 0.0913  0.0885  0.0970  188 LYS A CE  
1433 N NZ  . LYS A 174 A 0.3975 0.4432 0.2635 0.1063  0.0874  0.1041  188 LYS A NZ  
1434 N N   . ALA A 175 ? 0.2401 0.2784 0.1970 0.0264  0.0411  0.0315  189 ALA A N   
1435 C CA  . ALA A 175 ? 0.2186 0.2663 0.1795 0.0215  0.0276  0.0220  189 ALA A CA  
1436 C C   . ALA A 175 ? 0.2082 0.2528 0.1657 0.0220  0.0220  0.0212  189 ALA A C   
1437 O O   . ALA A 175 ? 0.2107 0.2442 0.1669 0.0231  0.0292  0.0247  189 ALA A O   
1438 C CB  . ALA A 175 ? 0.2145 0.2640 0.1899 0.0124  0.0277  0.0125  189 ALA A CB  
1439 N N   . ALA A 176 ? 0.1944 0.2479 0.1507 0.0220  0.0109  0.0172  190 ALA A N   
1440 C CA  . ALA A 176 ? 0.1894 0.2402 0.1455 0.0208  0.0063  0.0141  190 ALA A CA  
1441 C C   . ALA A 176 ? 0.1906 0.2398 0.1539 0.0141  0.0055  0.0051  190 ALA A C   
1442 O O   . ALA A 176 ? 0.1917 0.2469 0.1625 0.0105  0.0050  0.0007  190 ALA A O   
1443 C CB  . ALA A 176 ? 0.1787 0.2380 0.1326 0.0232  -0.0026 0.0138  190 ALA A CB  
1444 N N   . PHE A 177 ? 0.1946 0.2369 0.1563 0.0128  0.0059  0.0018  191 PHE A N   
1445 C CA  . PHE A 177 ? 0.1986 0.2418 0.1667 0.0068  0.0041  -0.0089 191 PHE A CA  
1446 C C   . PHE A 177 ? 0.2000 0.2418 0.1599 0.0094  -0.0010 -0.0121 191 PHE A C   
1447 O O   . PHE A 177 ? 0.1918 0.2335 0.1441 0.0151  -0.0033 -0.0054 191 PHE A O   
1448 C CB  . PHE A 177 ? 0.2096 0.2426 0.1861 0.0013  0.0152  -0.0116 191 PHE A CB  
1449 C CG  . PHE A 177 ? 0.2142 0.2521 0.2037 -0.0072 0.0138  -0.0253 191 PHE A CG  
1450 C CD1 . PHE A 177 ? 0.2070 0.2614 0.2049 -0.0093 0.0061  -0.0308 191 PHE A CD1 
1451 C CD2 . PHE A 177 ? 0.2288 0.2563 0.2231 -0.0128 0.0196  -0.0340 191 PHE A CD2 
1452 C CE1 . PHE A 177 ? 0.2110 0.2746 0.2230 -0.0166 0.0033  -0.0445 191 PHE A CE1 
1453 C CE2 . PHE A 177 ? 0.2351 0.2706 0.2436 -0.0214 0.0168  -0.0494 191 PHE A CE2 
1454 C CZ  . PHE A 177 ? 0.2249 0.2800 0.2429 -0.0233 0.0081  -0.0546 191 PHE A CZ  
1455 N N   . LYS A 178 ? 0.2077 0.2498 0.1701 0.0053  -0.0028 -0.0230 192 LYS A N   
1456 C CA  . LYS A 178 ? 0.2167 0.2585 0.1687 0.0089  -0.0077 -0.0272 192 LYS A CA  
1457 C C   . LYS A 178 ? 0.2235 0.2511 0.1665 0.0131  -0.0007 -0.0201 192 LYS A C   
1458 O O   . LYS A 178 ? 0.2289 0.2448 0.1750 0.0109  0.0085  -0.0179 192 LYS A O   
1459 C CB  . LYS A 178 ? 0.2271 0.2725 0.1837 0.0032  -0.0104 -0.0427 192 LYS A CB  
1460 C CG  . LYS A 178 ? 0.2228 0.2864 0.1909 -0.0002 -0.0182 -0.0509 192 LYS A CG  
1461 C CD  . LYS A 178 ? 0.2366 0.3064 0.2136 -0.0074 -0.0208 -0.0686 192 LYS A CD  
1462 C CE  . LYS A 178 ? 0.2330 0.3263 0.2198 -0.0080 -0.0315 -0.0775 192 LYS A CE  
1463 N NZ  . LYS A 178 ? 0.2482 0.3507 0.2442 -0.0150 -0.0357 -0.0970 192 LYS A NZ  
1464 N N   . GLY A 179 ? 0.2268 0.2552 0.1591 0.0199  -0.0041 -0.0158 193 GLY A N   
1465 C CA  . GLY A 179 ? 0.2322 0.2503 0.1576 0.0250  0.0021  -0.0079 193 GLY A CA  
1466 C C   . GLY A 179 ? 0.2187 0.2409 0.1475 0.0286  0.0027  0.0040  193 GLY A C   
1467 O O   . GLY A 179 ? 0.2182 0.2378 0.1435 0.0338  0.0055  0.0107  193 GLY A O   
1468 N N   . ASP A 180 ? 0.2064 0.2364 0.1428 0.0259  0.0000  0.0054  194 ASP A N   
1469 C CA  . ASP A 180 ? 0.1956 0.2320 0.1355 0.0287  -0.0009 0.0134  194 ASP A CA  
1470 C C   . ASP A 180 ? 0.1868 0.2318 0.1283 0.0299  -0.0073 0.0135  194 ASP A C   
1471 O O   . ASP A 180 ? 0.1764 0.2269 0.1226 0.0312  -0.0084 0.0178  194 ASP A O   
1472 C CB  . ASP A 180 ? 0.1917 0.2313 0.1365 0.0267  0.0005  0.0149  194 ASP A CB  
1473 C CG  . ASP A 180 ? 0.2038 0.2333 0.1480 0.0268  0.0097  0.0175  194 ASP A CG  
1474 O OD1 . ASP A 180 ? 0.2092 0.2316 0.1498 0.0310  0.0148  0.0224  194 ASP A OD1 
1475 O OD2 . ASP A 180 ? 0.2074 0.2356 0.1555 0.0233  0.0130  0.0155  194 ASP A OD2 
1476 N N   . SER A 181 ? 0.1901 0.2366 0.1283 0.0300  -0.0111 0.0085  195 SER A N   
1477 C CA  . SER A 181 ? 0.1855 0.2374 0.1248 0.0327  -0.0149 0.0101  195 SER A CA  
1478 C C   . SER A 181 ? 0.1841 0.2341 0.1255 0.0359  -0.0116 0.0173  195 SER A C   
1479 O O   . SER A 181 ? 0.1904 0.2349 0.1278 0.0384  -0.0073 0.0204  195 SER A O   
1480 C CB  . SER A 181 ? 0.1986 0.2517 0.1300 0.0365  -0.0179 0.0066  195 SER A CB  
1481 O OG  . SER A 181 ? 0.2045 0.2623 0.1361 0.0332  -0.0217 -0.0020 195 SER A OG  
1482 N N   . GLY A 182 ? 0.1756 0.2299 0.1246 0.0355  -0.0128 0.0190  196 GLY A N   
1483 C CA  . GLY A 182 ? 0.1798 0.2334 0.1354 0.0373  -0.0090 0.0242  196 GLY A CA  
1484 C C   . GLY A 182 ? 0.1772 0.2368 0.1422 0.0347  -0.0089 0.0251  196 GLY A C   
1485 O O   . GLY A 182 ? 0.1768 0.2403 0.1531 0.0340  -0.0073 0.0266  196 GLY A O   
1486 N N   . GLY A 183 ? 0.1747 0.2331 0.1205 0.0332  -0.0173 0.0151  197 GLY A N   
1487 C CA  . GLY A 183 ? 0.1755 0.2442 0.1232 0.0373  -0.0157 0.0188  197 GLY A CA  
1488 C C   . GLY A 183 ? 0.1728 0.2512 0.1207 0.0371  -0.0194 0.0170  197 GLY A C   
1489 O O   . GLY A 183 ? 0.1656 0.2404 0.1124 0.0349  -0.0218 0.0134  197 GLY A O   
1490 N N   . PRO A 184 ? 0.1745 0.2663 0.1235 0.0394  -0.0197 0.0195  198 PRO A N   
1491 C CA  . PRO A 184 ? 0.1775 0.2796 0.1250 0.0379  -0.0233 0.0165  198 PRO A CA  
1492 C C   . PRO A 184 ? 0.1800 0.2860 0.1258 0.0417  -0.0221 0.0185  198 PRO A C   
1493 O O   . PRO A 184 ? 0.1827 0.2891 0.1293 0.0468  -0.0182 0.0246  198 PRO A O   
1494 C CB  . PRO A 184 ? 0.1787 0.2968 0.1285 0.0383  -0.0243 0.0187  198 PRO A CB  
1495 C CG  . PRO A 184 ? 0.1809 0.2998 0.1334 0.0451  -0.0194 0.0264  198 PRO A CG  
1496 C CD  . PRO A 184 ? 0.1807 0.2798 0.1321 0.0440  -0.0165 0.0253  198 PRO A CD  
1497 N N   . LEU A 185 ? 0.1837 0.2912 0.1263 0.0394  -0.0246 0.0135  199 LEU A N   
1498 C CA  . LEU A 185 ? 0.1878 0.3046 0.1272 0.0424  -0.0241 0.0146  199 LEU A CA  
1499 C C   . LEU A 185 ? 0.1905 0.3243 0.1274 0.0407  -0.0274 0.0129  199 LEU A C   
1500 O O   . LEU A 185 ? 0.1895 0.3230 0.1241 0.0346  -0.0304 0.0056  199 LEU A O   
1501 C CB  . LEU A 185 ? 0.1925 0.3013 0.1296 0.0409  -0.0241 0.0094  199 LEU A CB  
1502 C CG  . LEU A 185 ? 0.2014 0.3171 0.1348 0.0443  -0.0223 0.0104  199 LEU A CG  
1503 C CD1 . LEU A 185 ? 0.2001 0.3127 0.1364 0.0486  -0.0177 0.0173  199 LEU A CD1 
1504 C CD2 . LEU A 185 ? 0.2071 0.3175 0.1372 0.0423  -0.0227 0.0032  199 LEU A CD2 
1505 N N   . LEU A 186 ? 0.1930 0.3416 0.1300 0.0460  -0.0266 0.0199  200 LEU A N   
1506 C CA  . LEU A 186 ? 0.2006 0.3707 0.1357 0.0449  -0.0303 0.0195  200 LEU A CA  
1507 C C   . LEU A 186 ? 0.2069 0.3863 0.1345 0.0462  -0.0310 0.0182  200 LEU A C   
1508 O O   . LEU A 186 ? 0.2035 0.3836 0.1297 0.0532  -0.0274 0.0253  200 LEU A O   
1509 C CB  . LEU A 186 ? 0.2027 0.3879 0.1422 0.0513  -0.0292 0.0291  200 LEU A CB  
1510 C CG  . LEU A 186 ? 0.2007 0.3810 0.1472 0.0511  -0.0278 0.0312  200 LEU A CG  
1511 C CD1 . LEU A 186 ? 0.1994 0.3753 0.1470 0.0413  -0.0313 0.0221  200 LEU A CD1 
1512 C CD2 . LEU A 186 ? 0.2017 0.3612 0.1498 0.0555  -0.0219 0.0354  200 LEU A CD2 
1513 N N   . CYS A 187 ? 0.2174 0.4035 0.1396 0.0392  -0.0349 0.0091  201 CYS A N   
1514 C CA  . CYS A 187 ? 0.2322 0.4297 0.1455 0.0395  -0.0358 0.0065  201 CYS A CA  
1515 C C   . CYS A 187 ? 0.2458 0.4678 0.1563 0.0343  -0.0413 0.0032  201 CYS A C   
1516 O O   . CYS A 187 ? 0.2409 0.4622 0.1523 0.0251  -0.0442 -0.0051 201 CYS A O   
1517 C CB  . CYS A 187 ? 0.2376 0.4185 0.1453 0.0358  -0.0341 -0.0026 201 CYS A CB  
1518 S SG  . CYS A 187 ? 0.2288 0.3835 0.1429 0.0388  -0.0294 -0.0008 201 CYS A SG  
1519 N N   . ASN A 188 ? 0.2667 0.5114 0.1741 0.0402  -0.0426 0.0105  202 ASN A N   
1520 C CA  . ASN A 188 ? 0.2820 0.5559 0.1873 0.0362  -0.0485 0.0090  202 ASN A CA  
1521 C C   . ASN A 188 ? 0.2761 0.5550 0.1918 0.0314  -0.0509 0.0086  202 ASN A C   
1522 O O   . ASN A 188 ? 0.2787 0.5696 0.1937 0.0208  -0.0555 -0.0001 202 ASN A O   
1523 C CB  . ASN A 188 ? 0.3046 0.5837 0.1983 0.0266  -0.0516 -0.0040 202 ASN A CB  
1524 C CG  . ASN A 188 ? 0.3282 0.6106 0.2110 0.0327  -0.0494 -0.0017 202 ASN A CG  
1525 O OD1 . ASN A 188 ? 0.3459 0.6507 0.2263 0.0402  -0.0506 0.0080  202 ASN A OD1 
1526 N ND2 . ASN A 188 ? 0.3400 0.6014 0.2164 0.0303  -0.0457 -0.0097 202 ASN A ND2 
1527 N N   . ASN A 189 ? 0.2683 0.5365 0.1930 0.0385  -0.0471 0.0176  203 ASN A N   
1528 C CA  . ASN A 189 ? 0.2650 0.5400 0.1999 0.0370  -0.0480 0.0202  203 ASN A CA  
1529 C C   . ASN A 189 ? 0.2544 0.5112 0.1914 0.0259  -0.0483 0.0096  203 ASN A C   
1530 O O   . ASN A 189 ? 0.2546 0.5181 0.1994 0.0226  -0.0491 0.0103  203 ASN A O   
1531 C CB  . ASN A 189 ? 0.2839 0.5958 0.2217 0.0369  -0.0531 0.0238  203 ASN A CB  
1532 C CG  . ASN A 189 ? 0.3021 0.6317 0.2381 0.0503  -0.0519 0.0370  203 ASN A CG  
1533 O OD1 . ASN A 189 ? 0.3174 0.6705 0.2465 0.0501  -0.0562 0.0369  203 ASN A OD1 
1534 N ND2 . ASN A 189 ? 0.3095 0.6273 0.2508 0.0620  -0.0456 0.0486  203 ASN A ND2 
1535 N N   . VAL A 190 ? 0.2438 0.4772 0.1745 0.0213  -0.0468 0.0012  204 VAL A N   
1536 C CA  . VAL A 190 ? 0.2360 0.4494 0.1676 0.0123  -0.0461 -0.0074 204 VAL A CA  
1537 C C   . VAL A 190 ? 0.2230 0.4088 0.1555 0.0174  -0.0415 -0.0050 204 VAL A C   
1538 O O   . VAL A 190 ? 0.2208 0.3998 0.1498 0.0236  -0.0394 -0.0024 204 VAL A O   
1539 C CB  . VAL A 190 ? 0.2460 0.4570 0.1686 0.0019  -0.0480 -0.0202 204 VAL A CB  
1540 C CG1 . VAL A 190 ? 0.2500 0.4346 0.1718 -0.0053 -0.0455 -0.0281 204 VAL A CG1 
1541 C CG2 . VAL A 190 ? 0.2544 0.4941 0.1760 -0.0061 -0.0532 -0.0245 204 VAL A CG2 
1542 N N   . ALA A 191 ? 0.2082 0.3796 0.1452 0.0143  -0.0402 -0.0060 209 ALA A N   
1543 C CA  . ALA A 191 ? 0.2016 0.3499 0.1395 0.0182  -0.0367 -0.0040 209 ALA A CA  
1544 C C   . ALA A 191 ? 0.2012 0.3313 0.1335 0.0140  -0.0360 -0.0120 209 ALA A C   
1545 O O   . ALA A 191 ? 0.2057 0.3244 0.1378 0.0080  -0.0357 -0.0166 209 ALA A O   
1546 C CB  . ALA A 191 ? 0.1961 0.3386 0.1400 0.0176  -0.0354 -0.0007 209 ALA A CB  
1547 N N   . HIS A 192 ? 0.1998 0.3264 0.1278 0.0181  -0.0348 -0.0126 210 HIS A N   
1548 C CA  . HIS A 192 ? 0.2058 0.3167 0.1287 0.0163  -0.0331 -0.0195 210 HIS A CA  
1549 C C   . HIS A 192 ? 0.1968 0.2902 0.1231 0.0204  -0.0308 -0.0164 210 HIS A C   
1550 O O   . HIS A 192 ? 0.2018 0.2807 0.1255 0.0193  -0.0292 -0.0208 210 HIS A O   
1551 C CB  . HIS A 192 ? 0.2154 0.3321 0.1321 0.0193  -0.0322 -0.0215 210 HIS A CB  
1552 C CG  . HIS A 192 ? 0.2276 0.3594 0.1376 0.0139  -0.0346 -0.0275 210 HIS A CG  
1553 N ND1 . HIS A 192 ? 0.2442 0.3686 0.1457 0.0082  -0.0335 -0.0380 210 HIS A ND1 
1554 C CD2 . HIS A 192 ? 0.2302 0.3848 0.1400 0.0134  -0.0379 -0.0247 210 HIS A CD2 
1555 C CE1 . HIS A 192 ? 0.2527 0.3954 0.1487 0.0028  -0.0365 -0.0424 210 HIS A CE1 
1556 N NE2 . HIS A 192 ? 0.2421 0.4051 0.1434 0.0062  -0.0396 -0.0339 210 HIS A NE2 
1557 N N   . GLY A 193 ? 0.1860 0.2808 0.1176 0.0252  -0.0303 -0.0090 211 GLY A N   
1558 C CA  . GLY A 193 ? 0.1818 0.2639 0.1161 0.0284  -0.0287 -0.0066 211 GLY A CA  
1559 C C   . GLY A 193 ? 0.1766 0.2564 0.1154 0.0290  -0.0286 -0.0014 211 GLY A C   
1560 O O   . GLY A 193 ? 0.1745 0.2625 0.1151 0.0287  -0.0287 0.0014  211 GLY A O   
1561 N N   . ILE A 194 ? 0.1725 0.2419 0.1129 0.0301  -0.0281 -0.0004 212 ILE A N   
1562 C CA  . ILE A 194 ? 0.1685 0.2340 0.1114 0.0301  -0.0277 0.0030  212 ILE A CA  
1563 C C   . ILE A 194 ? 0.1651 0.2284 0.1104 0.0326  -0.0265 0.0051  212 ILE A C   
1564 O O   . ILE A 194 ? 0.1646 0.2255 0.1104 0.0337  -0.0271 0.0036  212 ILE A O   
1565 C CB  . ILE A 194 ? 0.1724 0.2290 0.1137 0.0270  -0.0288 0.0015  212 ILE A CB  
1566 C CG1 . ILE A 194 ? 0.1759 0.2343 0.1154 0.0228  -0.0293 -0.0012 212 ILE A CG1 
1567 C CG2 . ILE A 194 ? 0.1717 0.2248 0.1138 0.0267  -0.0282 0.0046  212 ILE A CG2 
1568 C CD1 . ILE A 194 ? 0.1800 0.2275 0.1173 0.0195  -0.0293 -0.0023 212 ILE A CD1 
1569 N N   . VAL A 195 ? 0.1633 0.2273 0.1103 0.0332  -0.0243 0.0085  213 VAL A N   
1570 C CA  . VAL A 195 ? 0.1626 0.2248 0.1121 0.0333  -0.0228 0.0098  213 VAL A CA  
1571 C C   . VAL A 195 ? 0.1633 0.2209 0.1131 0.0311  -0.0254 0.0081  213 VAL A C   
1572 O O   . VAL A 195 ? 0.1636 0.2164 0.1110 0.0291  -0.0263 0.0078  213 VAL A O   
1573 C CB  . VAL A 195 ? 0.1648 0.2246 0.1148 0.0333  -0.0186 0.0130  213 VAL A CB  
1574 C CG1 . VAL A 195 ? 0.1689 0.2258 0.1213 0.0309  -0.0167 0.0130  213 VAL A CG1 
1575 C CG2 . VAL A 195 ? 0.1659 0.2313 0.1155 0.0372  -0.0156 0.0168  213 VAL A CG2 
1576 N N   . SER A 196 ? 0.1652 0.2256 0.1179 0.0322  -0.0265 0.0075  214 SER A N   
1577 C CA  . SER A 196 ? 0.1659 0.2254 0.1193 0.0316  -0.0294 0.0071  214 SER A CA  
1578 C C   . SER A 196 ? 0.1670 0.2319 0.1248 0.0292  -0.0294 0.0077  214 SER A C   
1579 O O   . SER A 196 ? 0.1641 0.2271 0.1203 0.0251  -0.0301 0.0072  214 SER A O   
1580 C CB  . SER A 196 ? 0.1702 0.2290 0.1235 0.0354  -0.0307 0.0063  214 SER A CB  
1581 O OG  . SER A 196 ? 0.1713 0.2303 0.1254 0.0365  -0.0333 0.0077  214 SER A OG  
1582 N N   . TYR A 197 ? 0.1675 0.2399 0.1307 0.0309  -0.0283 0.0082  215 TYR A N   
1583 C CA  . TYR A 197 ? 0.1701 0.2500 0.1387 0.0272  -0.0283 0.0084  215 TYR A CA  
1584 C C   . TYR A 197 ? 0.1735 0.2605 0.1479 0.0283  -0.0247 0.0095  215 TYR A C   
1585 O O   . TYR A 197 ? 0.1675 0.2541 0.1407 0.0328  -0.0226 0.0100  215 TYR A O   
1586 C CB  . TYR A 197 ? 0.1721 0.2594 0.1435 0.0279  -0.0330 0.0088  215 TYR A CB  
1587 C CG  . TYR A 197 ? 0.1716 0.2650 0.1470 0.0351  -0.0336 0.0105  215 TYR A CG  
1588 C CD1 . TYR A 197 ? 0.1738 0.2590 0.1445 0.0405  -0.0341 0.0108  215 TYR A CD1 
1589 C CD2 . TYR A 197 ? 0.1738 0.2807 0.1579 0.0363  -0.0330 0.0117  215 TYR A CD2 
1590 C CE1 . TYR A 197 ? 0.1772 0.2649 0.1507 0.0476  -0.0332 0.0120  215 TYR A CE1 
1591 C CE2 . TYR A 197 ? 0.1748 0.2869 0.1627 0.0441  -0.0324 0.0135  215 TYR A CE2 
1592 C CZ  . TYR A 197 ? 0.1796 0.2808 0.1617 0.0502  -0.0323 0.0136  215 TYR A CZ  
1593 O OH  . TYR A 197 ? 0.1893 0.2929 0.1743 0.0585  -0.0303 0.0151  215 TYR A OH  
1594 N N   . GLY A 198 ? 0.1829 0.2771 0.1631 0.0233  -0.0237 0.0094  216 GLY A N   
1595 C CA  . GLY A 198 ? 0.1926 0.2946 0.1791 0.0232  -0.0196 0.0109  216 GLY A CA  
1596 C C   . GLY A 198 ? 0.2066 0.3194 0.2008 0.0159  -0.0201 0.0100  216 GLY A C   
1597 O O   . GLY A 198 ? 0.2061 0.3223 0.2003 0.0121  -0.0247 0.0082  216 GLY A O   
1598 N N   . LYS A 199 ? 0.2203 0.3399 0.2210 0.0135  -0.0153 0.0113  217 LYS A N   
1599 C CA  . LYS A 199 ? 0.2362 0.3677 0.2452 0.0048  -0.0151 0.0100  217 LYS A CA  
1600 C C   . LYS A 199 ? 0.2461 0.3654 0.2502 -0.0052 -0.0126 0.0069  217 LYS A C   
1601 O O   . LYS A 199 ? 0.2495 0.3522 0.2465 -0.0043 -0.0076 0.0078  217 LYS A O   
1602 C CB  . LYS A 199 ? 0.2450 0.3869 0.2627 0.0045  -0.0096 0.0124  217 LYS A CB  
1603 C CG  . LYS A 199 ? 0.2500 0.4046 0.2729 0.0144  -0.0106 0.0149  217 LYS A CG  
1604 C CD  . LYS A 199 ? 0.2612 0.4325 0.2914 0.0167  -0.0171 0.0149  217 LYS A CD  
1605 C CE  . LYS A 199 ? 0.2681 0.4515 0.3048 0.0267  -0.0158 0.0177  217 LYS A CE  
1606 N NZ  . LYS A 199 ? 0.2750 0.4721 0.3173 0.0321  -0.0216 0.0192  217 LYS A NZ  
1607 N N   . SER A 200 ? 0.2534 0.3817 0.2612 -0.0146 -0.0157 0.0032  218 SER A N   
1608 C CA  . SER A 200 ? 0.2709 0.3872 0.2734 -0.0256 -0.0126 -0.0013 218 SER A CA  
1609 C C   . SER A 200 ? 0.2760 0.3797 0.2785 -0.0302 -0.0024 -0.0002 218 SER A C   
1610 O O   . SER A 200 ? 0.2814 0.3662 0.2762 -0.0351 0.0028  -0.0024 218 SER A O   
1611 C CB  . SER A 200 ? 0.2848 0.4170 0.2919 -0.0364 -0.0177 -0.0061 218 SER A CB  
1612 O OG  . SER A 200 ? 0.2927 0.4427 0.3123 -0.0417 -0.0159 -0.0055 218 SER A OG  
1613 N N   . SER A 201 ? 0.2711 0.3845 0.2819 -0.0280 0.0011  0.0036  219 SER A N   
1614 C CA  . SER A 201 ? 0.2785 0.3814 0.2898 -0.0315 0.0114  0.0062  219 SER A CA  
1615 C C   . SER A 201 ? 0.2793 0.3623 0.2806 -0.0226 0.0166  0.0107  219 SER A C   
1616 O O   . SER A 201 ? 0.2938 0.3630 0.2925 -0.0250 0.0260  0.0135  219 SER A O   
1617 C CB  . SER A 201 ? 0.2765 0.3969 0.2985 -0.0297 0.0135  0.0099  219 SER A CB  
1618 O OG  . SER A 201 ? 0.2651 0.3908 0.2859 -0.0162 0.0104  0.0138  219 SER A OG  
1619 N N   . GLY A 202 ? 0.2675 0.3502 0.2636 -0.0121 0.0111  0.0122  220 GLY A N   
1620 C CA  . GLY A 202 ? 0.2679 0.3378 0.2560 -0.0032 0.0148  0.0169  220 GLY A CA  
1621 C C   . GLY A 202 ? 0.2615 0.3385 0.2513 0.0041  0.0179  0.0224  220 GLY A C   
1622 O O   . GLY A 202 ? 0.2683 0.3387 0.2517 0.0117  0.0206  0.0269  220 GLY A O   
1623 N N   . VAL A 203 ? 0.2483 0.3407 0.2468 0.0024  0.0175  0.0223  221 VAL A N   
1624 C CA  . VAL A 203 ? 0.2435 0.3433 0.2430 0.0090  0.0213  0.0270  221 VAL A CA  
1625 C C   . VAL A 203 ? 0.2264 0.3340 0.2235 0.0184  0.0146  0.0259  221 VAL A C   
1626 O O   . VAL A 203 ? 0.2128 0.3297 0.2148 0.0185  0.0086  0.0224  221 VAL A O   
1627 C CB  . VAL A 203 ? 0.2479 0.3608 0.2582 0.0031  0.0254  0.0276  221 VAL A CB  
1628 C CG1 . VAL A 203 ? 0.2501 0.3696 0.2601 0.0100  0.0307  0.0328  221 VAL A CG1 
1629 C CG2 . VAL A 203 ? 0.2632 0.3675 0.2762 -0.0088 0.0320  0.0271  221 VAL A CG2 
1630 N N   . PRO A 204 ? 0.2235 0.3273 0.2126 0.0262  0.0161  0.0289  224 PRO A N   
1631 C CA  . PRO A 204 ? 0.2146 0.3237 0.1999 0.0336  0.0109  0.0266  224 PRO A CA  
1632 C C   . PRO A 204 ? 0.2090 0.3314 0.2001 0.0365  0.0121  0.0261  224 PRO A C   
1633 O O   . PRO A 204 ? 0.2149 0.3443 0.2133 0.0329  0.0169  0.0283  224 PRO A O   
1634 C CB  . PRO A 204 ? 0.2181 0.3216 0.1932 0.0391  0.0127  0.0299  224 PRO A CB  
1635 C CG  . PRO A 204 ? 0.2275 0.3270 0.2023 0.0374  0.0210  0.0361  224 PRO A CG  
1636 C CD  . PRO A 204 ? 0.2294 0.3247 0.2121 0.0284  0.0230  0.0348  224 PRO A CD  
1637 N N   . PRO A 205 ? 0.2011 0.3270 0.1891 0.0430  0.0089  0.0232  225 PRO A N   
1638 C CA  . PRO A 205 ? 0.1955 0.3136 0.1757 0.0459  0.0034  0.0199  225 PRO A CA  
1639 C C   . PRO A 205 ? 0.1835 0.2965 0.1660 0.0424  -0.0023 0.0175  225 PRO A C   
1640 O O   . PRO A 205 ? 0.1780 0.2964 0.1686 0.0387  -0.0035 0.0174  225 PRO A O   
1641 C CB  . PRO A 205 ? 0.1997 0.3220 0.1777 0.0523  0.0032  0.0167  225 PRO A CB  
1642 C CG  . PRO A 205 ? 0.2059 0.3400 0.1930 0.0534  0.0075  0.0184  225 PRO A CG  
1643 C CD  . PRO A 205 ? 0.2061 0.3427 0.1971 0.0479  0.0121  0.0231  225 PRO A CD  
1644 N N   . GLU A 206 ? 0.1811 0.2855 0.1562 0.0433  -0.0058 0.0157  226 GLU A N   
1645 C CA  . GLU A 206 ? 0.1767 0.2755 0.1520 0.0406  -0.0108 0.0137  226 GLU A CA  
1646 C C   . GLU A 206 ? 0.1761 0.2699 0.1454 0.0442  -0.0142 0.0106  226 GLU A C   
1647 O O   . GLU A 206 ? 0.1756 0.2701 0.1402 0.0478  -0.0127 0.0091  226 GLU A O   
1648 C CB  . GLU A 206 ? 0.1798 0.2712 0.1530 0.0359  -0.0099 0.0153  226 GLU A CB  
1649 C CG  . GLU A 206 ? 0.1812 0.2680 0.1472 0.0385  -0.0081 0.0173  226 GLU A CG  
1650 C CD  . GLU A 206 ? 0.1898 0.2689 0.1543 0.0358  -0.0050 0.0201  226 GLU A CD  
1651 O OE1 . GLU A 206 ? 0.1935 0.2681 0.1611 0.0304  -0.0045 0.0190  226 GLU A OE1 
1652 O OE2 . GLU A 206 ? 0.1902 0.2682 0.1502 0.0392  -0.0028 0.0234  226 GLU A OE2 
1653 N N   . VAL A 207 ? 0.1706 0.2592 0.1394 0.0425  -0.0183 0.0093  227 VAL A N   
1654 C CA  . VAL A 207 ? 0.1720 0.2546 0.1365 0.0451  -0.0209 0.0066  227 VAL A CA  
1655 C C   . VAL A 207 ? 0.1709 0.2460 0.1296 0.0421  -0.0228 0.0058  227 VAL A C   
1656 O O   . VAL A 207 ? 0.1605 0.2332 0.1198 0.0387  -0.0241 0.0071  227 VAL A O   
1657 C CB  . VAL A 207 ? 0.1728 0.2567 0.1416 0.0470  -0.0233 0.0071  227 VAL A CB  
1658 C CG1 . VAL A 207 ? 0.1806 0.2547 0.1441 0.0498  -0.0247 0.0053  227 VAL A CG1 
1659 C CG2 . VAL A 207 ? 0.1762 0.2705 0.1522 0.0509  -0.0211 0.0085  227 VAL A CG2 
1660 N N   . PHE A 208 ? 0.1742 0.2463 0.1272 0.0431  -0.0226 0.0031  228 PHE A N   
1661 C CA  . PHE A 208 ? 0.1740 0.2413 0.1226 0.0402  -0.0244 0.0018  228 PHE A CA  
1662 C C   . PHE A 208 ? 0.1756 0.2346 0.1209 0.0403  -0.0254 -0.0017 228 PHE A C   
1663 O O   . PHE A 208 ? 0.1809 0.2380 0.1251 0.0434  -0.0237 -0.0040 228 PHE A O   
1664 C CB  . PHE A 208 ? 0.1769 0.2502 0.1218 0.0399  -0.0234 0.0015  228 PHE A CB  
1665 C CG  . PHE A 208 ? 0.1776 0.2561 0.1245 0.0403  -0.0215 0.0063  228 PHE A CG  
1666 C CD1 . PHE A 208 ? 0.1791 0.2606 0.1292 0.0420  -0.0185 0.0093  228 PHE A CD1 
1667 C CD2 . PHE A 208 ? 0.1802 0.2605 0.1257 0.0394  -0.0219 0.0083  228 PHE A CD2 
1668 C CE1 . PHE A 208 ? 0.1796 0.2626 0.1306 0.0425  -0.0153 0.0142  228 PHE A CE1 
1669 C CE2 . PHE A 208 ? 0.1799 0.2627 0.1267 0.0412  -0.0188 0.0136  228 PHE A CE2 
1670 C CZ  . PHE A 208 ? 0.1798 0.2624 0.1288 0.0427  -0.0152 0.0165  228 PHE A CZ  
1671 N N   . THR A 209 ? 0.1721 0.2251 0.1152 0.0372  -0.0271 -0.0019 229 THR A N   
1672 C CA  . THR A 209 ? 0.1778 0.2209 0.1167 0.0360  -0.0269 -0.0051 229 THR A CA  
1673 C C   . THR A 209 ? 0.1841 0.2290 0.1184 0.0331  -0.0259 -0.0101 229 THR A C   
1674 O O   . THR A 209 ? 0.1780 0.2322 0.1124 0.0307  -0.0269 -0.0097 229 THR A O   
1675 C CB  . THR A 209 ? 0.1765 0.2138 0.1144 0.0327  -0.0284 -0.0034 229 THR A CB  
1676 O OG1 . THR A 209 ? 0.1715 0.2099 0.1124 0.0346  -0.0298 0.0006  229 THR A OG1 
1677 C CG2 . THR A 209 ? 0.1871 0.2118 0.1206 0.0315  -0.0269 -0.0058 229 THR A CG2 
1678 N N   . ARG A 210 ? 0.1987 0.2348 0.1286 0.0333  -0.0236 -0.0149 230 ARG A N   
1679 C CA  . ARG A 210 ? 0.2116 0.2484 0.1354 0.0290  -0.0226 -0.0215 230 ARG A CA  
1680 C C   . ARG A 210 ? 0.2222 0.2523 0.1433 0.0217  -0.0230 -0.0244 230 ARG A C   
1681 O O   . ARG A 210 ? 0.2334 0.2479 0.1520 0.0210  -0.0206 -0.0259 230 ARG A O   
1682 C CB  . ARG A 210 ? 0.2236 0.2525 0.1430 0.0326  -0.0185 -0.0262 230 ARG A CB  
1683 C CG  . ARG A 210 ? 0.2343 0.2645 0.1456 0.0279  -0.0170 -0.0345 230 ARG A CG  
1684 C CD  . ARG A 210 ? 0.2492 0.2681 0.1550 0.0321  -0.0115 -0.0396 230 ARG A CD  
1685 N NE  . ARG A 210 ? 0.2435 0.2713 0.1528 0.0399  -0.0101 -0.0359 230 ARG A NE  
1686 C CZ  . ARG A 210 ? 0.2427 0.2838 0.1494 0.0404  -0.0101 -0.0370 230 ARG A CZ  
1687 N NH1 . ARG A 210 ? 0.2468 0.2945 0.1458 0.0340  -0.0115 -0.0429 230 ARG A NH1 
1688 N NH2 . ARG A 210 ? 0.2371 0.2861 0.1488 0.0471  -0.0086 -0.0321 230 ARG A NH2 
1689 N N   . VAL A 211 ? 0.2230 0.2654 0.1452 0.0166  -0.0257 -0.0245 231 VAL A N   
1690 C CA  . VAL A 211 ? 0.2317 0.2720 0.1535 0.0092  -0.0262 -0.0262 231 VAL A CA  
1691 C C   . VAL A 211 ? 0.2534 0.2816 0.1685 0.0026  -0.0233 -0.0346 231 VAL A C   
1692 O O   . VAL A 211 ? 0.2625 0.2771 0.1763 -0.0013 -0.0211 -0.0354 231 VAL A O   
1693 C CB  . VAL A 211 ? 0.2217 0.2816 0.1470 0.0060  -0.0293 -0.0244 231 VAL A CB  
1694 C CG1 . VAL A 211 ? 0.2280 0.2888 0.1540 -0.0026 -0.0295 -0.0268 231 VAL A CG1 
1695 C CG2 . VAL A 211 ? 0.2084 0.2754 0.1395 0.0121  -0.0303 -0.0163 231 VAL A CG2 
1696 N N   . SER A 212 ? 0.2647 0.2969 0.1746 0.0013  -0.0226 -0.0410 232 SER A N   
1697 C CA  . SER A 212 ? 0.2897 0.3107 0.1915 -0.0064 -0.0193 -0.0510 232 SER A CA  
1698 C C   . SER A 212 ? 0.3091 0.3033 0.2078 -0.0046 -0.0137 -0.0518 232 SER A C   
1699 O O   . SER A 212 ? 0.3258 0.3056 0.2191 -0.0127 -0.0099 -0.0583 232 SER A O   
1700 C CB  . SER A 212 ? 0.2981 0.3252 0.1931 -0.0058 -0.0186 -0.0575 232 SER A CB  
1701 O OG  . SER A 212 ? 0.2975 0.3164 0.1922 0.0045  -0.0155 -0.0547 232 SER A OG  
1702 N N   . SER A 213 ? 0.3097 0.2974 0.2117 0.0059  -0.0127 -0.0448 233 SER A N   
1703 C CA  . SER A 213 ? 0.3247 0.2894 0.2243 0.0105  -0.0073 -0.0432 233 SER A CA  
1704 C C   . SER A 213 ? 0.3238 0.2795 0.2250 0.0068  -0.0071 -0.0389 233 SER A C   
1705 O O   . SER A 213 ? 0.3375 0.2717 0.2345 0.0076  -0.0016 -0.0388 233 SER A O   
1706 C CB  . SER A 213 ? 0.3239 0.2904 0.2279 0.0229  -0.0072 -0.0365 233 SER A CB  
1707 O OG  . SER A 213 ? 0.3272 0.3023 0.2296 0.0259  -0.0066 -0.0404 233 SER A OG  
1708 N N   . PHE A 214 ? 0.3106 0.2817 0.2173 0.0032  -0.0120 -0.0349 234 PHE A N   
1709 C CA  . PHE A 214 ? 0.3100 0.2742 0.2182 0.0009  -0.0116 -0.0297 234 PHE A CA  
1710 C C   . PHE A 214 ? 0.3142 0.2817 0.2219 -0.0115 -0.0113 -0.0345 234 PHE A C   
1711 O O   . PHE A 214 ? 0.3142 0.2794 0.2237 -0.0144 -0.0109 -0.0302 234 PHE A O   
1712 C CB  . PHE A 214 ? 0.2913 0.2682 0.2057 0.0073  -0.0161 -0.0211 234 PHE A CB  
1713 C CG  . PHE A 214 ? 0.2918 0.2653 0.2073 0.0181  -0.0160 -0.0164 234 PHE A CG  
1714 C CD1 . PHE A 214 ? 0.3003 0.2601 0.2141 0.0235  -0.0137 -0.0109 234 PHE A CD1 
1715 C CD2 . PHE A 214 ? 0.2820 0.2671 0.2003 0.0229  -0.0179 -0.0171 234 PHE A CD2 
1716 C CE1 . PHE A 214 ? 0.3004 0.2610 0.2163 0.0335  -0.0140 -0.0063 234 PHE A CE1 
1717 C CE2 . PHE A 214 ? 0.2828 0.2674 0.2036 0.0319  -0.0176 -0.0130 234 PHE A CE2 
1718 C CZ  . PHE A 214 ? 0.2942 0.2678 0.2143 0.0373  -0.0160 -0.0077 234 PHE A CZ  
1719 N N   . LEU A 215 ? 0.3199 0.2934 0.2248 -0.0193 -0.0113 -0.0435 235 LEU A N   
1720 C CA  . LEU A 215 ? 0.3215 0.3060 0.2280 -0.0318 -0.0124 -0.0480 235 LEU A CA  
1721 C C   . LEU A 215 ? 0.3364 0.3009 0.2402 -0.0394 -0.0068 -0.0487 235 LEU A C   
1722 O O   . LEU A 215 ? 0.3303 0.3031 0.2388 -0.0455 -0.0076 -0.0461 235 LEU A O   
1723 C CB  . LEU A 215 ? 0.3296 0.3255 0.2323 -0.0394 -0.0137 -0.0582 235 LEU A CB  
1724 C CG  . LEU A 215 ? 0.3159 0.3396 0.2227 -0.0350 -0.0201 -0.0561 235 LEU A CG  
1725 C CD1 . LEU A 215 ? 0.3247 0.3560 0.2246 -0.0404 -0.0207 -0.0660 235 LEU A CD1 
1726 C CD2 . LEU A 215 ? 0.3027 0.3495 0.2181 -0.0381 -0.0244 -0.0510 235 LEU A CD2 
1727 N N   . PRO A 216 ? 0.3567 0.2936 0.2529 -0.0386 0.0000  -0.0517 236 PRO A N   
1728 C CA  . PRO A 216 ? 0.3754 0.2898 0.2683 -0.0444 0.0066  -0.0506 236 PRO A CA  
1729 C C   . PRO A 216 ? 0.3637 0.2791 0.2610 -0.0392 0.0056  -0.0391 236 PRO A C   
1730 O O   . PRO A 216 ? 0.3673 0.2820 0.2661 -0.0480 0.0077  -0.0381 236 PRO A O   
1731 C CB  . PRO A 216 ? 0.3996 0.2846 0.2838 -0.0383 0.0141  -0.0527 236 PRO A CB  
1732 C CG  . PRO A 216 ? 0.3983 0.2920 0.2798 -0.0373 0.0121  -0.0611 236 PRO A CG  
1733 C CD  . PRO A 216 ? 0.3675 0.2927 0.2576 -0.0319 0.0027  -0.0558 236 PRO A CD  
1734 N N   . TRP A 217 ? 0.3478 0.2665 0.2471 -0.0256 0.0025  -0.0308 237 TRP A N   
1735 C CA  . TRP A 217 ? 0.3362 0.2573 0.2381 -0.0207 0.0011  -0.0207 237 TRP A CA  
1736 C C   . TRP A 217 ? 0.3222 0.2673 0.2310 -0.0262 -0.0036 -0.0200 237 TRP A C   
1737 O O   . TRP A 217 ? 0.3208 0.2658 0.2306 -0.0287 -0.0023 -0.0150 237 TRP A O   
1738 C CB  . TRP A 217 ? 0.3233 0.2450 0.2255 -0.0065 -0.0015 -0.0133 237 TRP A CB  
1739 C CG  . TRP A 217 ? 0.3086 0.2368 0.2126 -0.0025 -0.0041 -0.0044 237 TRP A CG  
1740 C CD1 . TRP A 217 ? 0.3198 0.2343 0.2193 -0.0003 -0.0006 0.0026  237 TRP A CD1 
1741 C CD2 . TRP A 217 ? 0.2844 0.2338 0.1938 -0.0007 -0.0100 -0.0019 237 TRP A CD2 
1742 N NE1 . TRP A 217 ? 0.3050 0.2320 0.2063 0.0022  -0.0044 0.0086  237 TRP A NE1 
1743 C CE2 . TRP A 217 ? 0.2829 0.2301 0.1902 0.0018  -0.0098 0.0055  237 TRP A CE2 
1744 C CE3 . TRP A 217 ? 0.2635 0.2321 0.1784 -0.0008 -0.0146 -0.0050 237 TRP A CE3 
1745 C CZ2 . TRP A 217 ? 0.2671 0.2295 0.1772 0.0035  -0.0138 0.0085  237 TRP A CZ2 
1746 C CZ3 . TRP A 217 ? 0.2512 0.2335 0.1696 0.0014  -0.0180 -0.0011 237 TRP A CZ3 
1747 C CH2 . TRP A 217 ? 0.2505 0.2292 0.1663 0.0033  -0.0174 0.0049  237 TRP A CH2 
1748 N N   . ILE A 218 ? 0.3147 0.2803 0.2280 -0.0272 -0.0085 -0.0243 238 ILE A N   
1749 C CA  . ILE A 218 ? 0.3036 0.2928 0.2240 -0.0305 -0.0124 -0.0228 238 ILE A CA  
1750 C C   . ILE A 218 ? 0.3240 0.3163 0.2463 -0.0436 -0.0096 -0.0266 238 ILE A C   
1751 O O   . ILE A 218 ? 0.3118 0.3113 0.2381 -0.0456 -0.0090 -0.0219 238 ILE A O   
1752 C CB  . ILE A 218 ? 0.2870 0.2968 0.2111 -0.0276 -0.0174 -0.0254 238 ILE A CB  
1753 C CG1 . ILE A 218 ? 0.2753 0.2846 0.1992 -0.0156 -0.0197 -0.0207 238 ILE A CG1 
1754 C CG2 . ILE A 218 ? 0.2740 0.3083 0.2055 -0.0313 -0.0202 -0.0240 238 ILE A CG2 
1755 C CD1 . ILE A 218 ? 0.2641 0.2895 0.1901 -0.0124 -0.0232 -0.0229 238 ILE A CD1 
1756 N N   . ARG A 219 ? 0.3487 0.3365 0.2681 -0.0531 -0.0077 -0.0356 239 ARG A N   
1757 C CA  . ARG A 219 ? 0.3752 0.3677 0.2967 -0.0679 -0.0052 -0.0409 239 ARG A CA  
1758 C C   . ARG A 219 ? 0.3872 0.3606 0.3068 -0.0716 0.0012  -0.0364 239 ARG A C   
1759 O O   . ARG A 219 ? 0.3803 0.3655 0.3056 -0.0789 0.0021  -0.0345 239 ARG A O   
1760 C CB  . ARG A 219 ? 0.4106 0.3954 0.3264 -0.0784 -0.0030 -0.0528 239 ARG A CB  
1761 C CG  . ARG A 219 ? 0.4212 0.4293 0.3384 -0.0779 -0.0093 -0.0584 239 ARG A CG  
1762 C CD  . ARG A 219 ? 0.4655 0.4570 0.3727 -0.0825 -0.0062 -0.0691 239 ARG A CD  
1763 N NE  . ARG A 219 ? 0.4816 0.4958 0.3882 -0.0829 -0.0119 -0.0749 239 ARG A NE  
1764 C CZ  . ARG A 219 ? 0.5135 0.5179 0.4109 -0.0836 -0.0103 -0.0835 239 ARG A CZ  
1765 N NH1 . ARG A 219 ? 0.5441 0.5154 0.4329 -0.0821 -0.0027 -0.0868 239 ARG A NH1 
1766 N NH2 . ARG A 219 ? 0.5124 0.5404 0.4088 -0.0846 -0.0157 -0.0882 239 ARG A NH2 
1767 N N   . THR A 220 ? 0.4091 0.3536 0.3205 -0.0660 0.0062  -0.0339 240 THR A N   
1768 C CA  . THR A 220 ? 0.4315 0.3549 0.3390 -0.0681 0.0132  -0.0283 240 THR A CA  
1769 C C   . THR A 220 ? 0.4133 0.3492 0.3252 -0.0627 0.0111  -0.0185 240 THR A C   
1770 O O   . THR A 220 ? 0.4166 0.3509 0.3297 -0.0700 0.0154  -0.0158 240 THR A O   
1771 C CB  . THR A 220 ? 0.4564 0.3496 0.3545 -0.0591 0.0182  -0.0256 240 THR A CB  
1772 O OG1 . THR A 220 ? 0.4783 0.3599 0.3721 -0.0661 0.0214  -0.0363 240 THR A OG1 
1773 C CG2 . THR A 220 ? 0.4800 0.3496 0.3727 -0.0594 0.0260  -0.0181 240 THR A CG2 
1774 N N   . THR A 221 ? 0.3925 0.3402 0.3062 -0.0505 0.0051  -0.0137 241 THR A N   
1775 C CA  . THR A 221 ? 0.3791 0.3367 0.2949 -0.0445 0.0034  -0.0055 241 THR A CA  
1776 C C   . THR A 221 ? 0.3745 0.3554 0.2989 -0.0519 0.0025  -0.0065 241 THR A C   
1777 O O   . THR A 221 ? 0.3685 0.3504 0.2935 -0.0541 0.0058  -0.0016 241 THR A O   
1778 C CB  . THR A 221 ? 0.3569 0.3219 0.2729 -0.0319 -0.0023 -0.0024 241 THR A CB  
1779 O OG1 . THR A 221 ? 0.3596 0.3050 0.2688 -0.0249 -0.0009 -0.0005 241 THR A OG1 
1780 C CG2 . THR A 221 ? 0.3427 0.3169 0.2595 -0.0265 -0.0038 0.0043  241 THR A CG2 
1781 N N   . MET A 222 ? 0.3780 0.3792 0.3090 -0.0549 -0.0017 -0.0122 242 MET A N   
1782 C CA  . MET A 222 ? 0.3829 0.4106 0.3235 -0.0597 -0.0032 -0.0121 242 MET A CA  
1783 C C   . MET A 222 ? 0.4123 0.4408 0.3560 -0.0743 0.0017  -0.0153 242 MET A C   
1784 O O   . MET A 222 ? 0.3980 0.4432 0.3489 -0.0778 0.0031  -0.0122 242 MET A O   
1785 C CB  . MET A 222 ? 0.3726 0.4226 0.3188 -0.0583 -0.0091 -0.0164 242 MET A CB  
1786 C CG  . MET A 222 ? 0.3623 0.4148 0.3072 -0.0447 -0.0131 -0.0125 242 MET A CG  
1787 S SD  . MET A 222 ? 0.3539 0.4368 0.3065 -0.0418 -0.0187 -0.0138 242 MET A SD  
1788 C CE  . MET A 222 ? 0.3715 0.4570 0.3218 -0.0524 -0.0205 -0.0242 242 MET A CE  
1789 N N   . ARG A 223 ? 0.4505 0.4602 0.3887 -0.0830 0.0051  -0.0215 243 ARG A N   
1790 C CA  . ARG A 223 ? 0.5055 0.5133 0.4459 -0.0989 0.0106  -0.0256 243 ARG A CA  
1791 C C   . ARG A 223 ? 0.5094 0.5026 0.4472 -0.0991 0.0175  -0.0175 243 ARG A C   
1792 O O   . ARG A 223 ? 0.5161 0.5208 0.4605 -0.1092 0.0210  -0.0171 243 ARG A O   
1793 C CB  . ARG A 223 ? 0.5578 0.5452 0.4913 -0.1085 0.0138  -0.0352 243 ARG A CB  
1794 C CG  . ARG A 223 ? 0.6137 0.5944 0.5483 -0.1270 0.0209  -0.0405 243 ARG A CG  
1795 C CD  . ARG A 223 ? 0.6775 0.6423 0.6056 -0.1387 0.0237  -0.0528 243 ARG A CD  
1796 N NE  . ARG A 223 ? 0.7148 0.7100 0.6492 -0.1477 0.0169  -0.0625 243 ARG A NE  
1797 C CZ  . ARG A 223 ? 0.7468 0.7425 0.6759 -0.1468 0.0131  -0.0709 243 ARG A CZ  
1798 N NH1 . ARG A 223 ? 0.7719 0.7384 0.6901 -0.1370 0.0157  -0.0711 243 ARG A NH1 
1799 N NH2 . ARG A 223 ? 0.7363 0.7630 0.6708 -0.1554 0.0067  -0.0787 243 ARG A NH2 
1800 N N   . SER A 224 ? 0.5108 0.4807 0.4392 -0.0879 0.0194  -0.0109 244 SER A N   
1801 C CA  . SER A 224 ? 0.5357 0.4886 0.4587 -0.0876 0.0263  -0.0029 244 SER A CA  
1802 C C   . SER A 224 ? 0.5223 0.4957 0.4507 -0.0835 0.0253  0.0037  244 SER A C   
1803 O O   . SER A 224 ? 0.5207 0.5086 0.4512 -0.0729 0.0191  0.0054  244 SER A O   
1804 C CB  . SER A 224 ? 0.5498 0.4755 0.4611 -0.0761 0.0279  0.0026  244 SER A CB  
1805 O OG  . SER A 224 ? 0.5378 0.4730 0.4482 -0.0620 0.0218  0.0081  244 SER A OG  
# 
