CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 19100413295094442

Job options:

ID        	=	 19100413295094442
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


data_4EBZ
# 
_entry.id   4EBZ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4EBZ         
RCSB  RCSB071426   
WWPDB D_1000071426 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          4EBY 
_pdbx_database_related.details        . 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4EBZ 
_pdbx_database_status.recvd_initial_deposition_date   2012-03-26 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Chai, J.' 1 
'Liu, T.'  2 
'Han, Z.'  3 
'She, J'   4 
'Wang, J.' 5 
# 
_citation.id                        primary 
_citation.title                     'Chitin-induced dimerization activates a plant immune receptor.' 
_citation.journal_abbrev            Science 
_citation.journal_volume            336 
_citation.page_first                1160 
_citation.page_last                 1164 
_citation.year                      2012 
_citation.journal_id_ASTM           SCIEAS 
_citation.country                   US 
_citation.journal_id_ISSN           0036-8075 
_citation.journal_id_CSD            0038 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   22654057 
_citation.pdbx_database_id_DOI      10.1126/science.1218867 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Liu, T.'    1  
primary 'Liu, Z.'    2  
primary 'Song, C.'   3  
primary 'Hu, Y.'     4  
primary 'Han, Z.'    5  
primary 'She, J.'    6  
primary 'Fan, F.'    7  
primary 'Wang, J.'   8  
primary 'Jin, C.'    9  
primary 'Chang, J.'  10 
primary 'Zhou, J.M.' 11 
primary 'Chai, J.'   12 
# 
_cell.entry_id           4EBZ 
_cell.length_a           57.465 
_cell.length_b           71.322 
_cell.length_c           72.171 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4EBZ 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
# 
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 'Chitin elicitor receptor kinase 1' 23456.076 1   ? ? 'UNP RESIDUES 25-230' ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE              221.208   12  ? ? ?                     ? 
3 non-polymer man BETA-D-MANNOSE                      180.156   2   ? ? ?                     ? 
4 non-polymer man ALPHA-D-MANNOSE                     180.156   1   ? ? ?                     ? 
5 water       nat water                               18.015    301 ? ? ?                     ? 
# 
_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       
;CRTSCPLALASYYLENGTTLSVINQNLNSSIAPYDQINFDPILRYNSNIKDKDRIQMGSRVLVPFPCECQPGDFLGHNFS
YSVRQEDTYERVAISNYANLTTMESLQARNPFPATNIPLSATLNVLVNCSCGDESVSKDFGLFVTYPLRPEDSLSSIARS
SGVSADILQRYNPGVNFNSGNGIVYVPGRDPNGAFPPFKSSKQDGVHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;CRTSCPLALASYYLENGTTLSVINQNLNSSIAPYDQINFDPILRYNSNIKDKDRIQMGSRVLVPFPCECQPGDFLGHNFS
YSVRQEDTYERVAISNYANLTTMESLQARNPFPATNIPLSATLNVLVNCSCGDESVSKDFGLFVTYPLRPEDSLSSIARS
SGVSADILQRYNPGVNFNSGNGIVYVPGRDPNGAFPPFKSSKQDGVHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   CYS n 
1 2   ARG n 
1 3   THR n 
1 4   SER n 
1 5   CYS n 
1 6   PRO n 
1 7   LEU n 
1 8   ALA n 
1 9   LEU n 
1 10  ALA n 
1 11  SER n 
1 12  TYR n 
1 13  TYR n 
1 14  LEU n 
1 15  GLU n 
1 16  ASN n 
1 17  GLY n 
1 18  THR n 
1 19  THR n 
1 20  LEU n 
1 21  SER n 
1 22  VAL n 
1 23  ILE n 
1 24  ASN n 
1 25  GLN n 
1 26  ASN n 
1 27  LEU n 
1 28  ASN n 
1 29  SER n 
1 30  SER n 
1 31  ILE n 
1 32  ALA n 
1 33  PRO n 
1 34  TYR n 
1 35  ASP n 
1 36  GLN n 
1 37  ILE n 
1 38  ASN n 
1 39  PHE n 
1 40  ASP n 
1 41  PRO n 
1 42  ILE n 
1 43  LEU n 
1 44  ARG n 
1 45  TYR n 
1 46  ASN n 
1 47  SER n 
1 48  ASN n 
1 49  ILE n 
1 50  LYS n 
1 51  ASP n 
1 52  LYS n 
1 53  ASP n 
1 54  ARG n 
1 55  ILE n 
1 56  GLN n 
1 57  MET n 
1 58  GLY n 
1 59  SER n 
1 60  ARG n 
1 61  VAL n 
1 62  LEU n 
1 63  VAL n 
1 64  PRO n 
1 65  PHE n 
1 66  PRO n 
1 67  CYS n 
1 68  GLU n 
1 69  CYS n 
1 70  GLN n 
1 71  PRO n 
1 72  GLY n 
1 73  ASP n 
1 74  PHE n 
1 75  LEU n 
1 76  GLY n 
1 77  HIS n 
1 78  ASN n 
1 79  PHE n 
1 80  SER n 
1 81  TYR n 
1 82  SER n 
1 83  VAL n 
1 84  ARG n 
1 85  GLN n 
1 86  GLU n 
1 87  ASP n 
1 88  THR n 
1 89  TYR n 
1 90  GLU n 
1 91  ARG n 
1 92  VAL n 
1 93  ALA n 
1 94  ILE n 
1 95  SER n 
1 96  ASN n 
1 97  TYR n 
1 98  ALA n 
1 99  ASN n 
1 100 LEU n 
1 101 THR n 
1 102 THR n 
1 103 MET n 
1 104 GLU n 
1 105 SER n 
1 106 LEU n 
1 107 GLN n 
1 108 ALA n 
1 109 ARG n 
1 110 ASN n 
1 111 PRO n 
1 112 PHE n 
1 113 PRO n 
1 114 ALA n 
1 115 THR n 
1 116 ASN n 
1 117 ILE n 
1 118 PRO n 
1 119 LEU n 
1 120 SER n 
1 121 ALA n 
1 122 THR n 
1 123 LEU n 
1 124 ASN n 
1 125 VAL n 
1 126 LEU n 
1 127 VAL n 
1 128 ASN n 
1 129 CYS n 
1 130 SER n 
1 131 CYS n 
1 132 GLY n 
1 133 ASP n 
1 134 GLU n 
1 135 SER n 
1 136 VAL n 
1 137 SER n 
1 138 LYS n 
1 139 ASP n 
1 140 PHE n 
1 141 GLY n 
1 142 LEU n 
1 143 PHE n 
1 144 VAL n 
1 145 THR n 
1 146 TYR n 
1 147 PRO n 
1 148 LEU n 
1 149 ARG n 
1 150 PRO n 
1 151 GLU n 
1 152 ASP n 
1 153 SER n 
1 154 LEU n 
1 155 SER n 
1 156 SER n 
1 157 ILE n 
1 158 ALA n 
1 159 ARG n 
1 160 SER n 
1 161 SER n 
1 162 GLY n 
1 163 VAL n 
1 164 SER n 
1 165 ALA n 
1 166 ASP n 
1 167 ILE n 
1 168 LEU n 
1 169 GLN n 
1 170 ARG n 
1 171 TYR n 
1 172 ASN n 
1 173 PRO n 
1 174 GLY n 
1 175 VAL n 
1 176 ASN n 
1 177 PHE n 
1 178 ASN n 
1 179 SER n 
1 180 GLY n 
1 181 ASN n 
1 182 GLY n 
1 183 ILE n 
1 184 VAL n 
1 185 TYR n 
1 186 VAL n 
1 187 PRO n 
1 188 GLY n 
1 189 ARG n 
1 190 ASP n 
1 191 PRO n 
1 192 ASN n 
1 193 GLY n 
1 194 ALA n 
1 195 PHE n 
1 196 PRO n 
1 197 PRO n 
1 198 PHE n 
1 199 LYS n 
1 200 SER n 
1 201 SER n 
1 202 LYS n 
1 203 GLN n 
1 204 ASP n 
1 205 GLY n 
1 206 VAL n 
1 207 HIS n 
1 208 HIS n 
1 209 HIS n 
1 210 HIS n 
1 211 HIS n 
1 212 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               'mouse-ear cress' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'CERK1, At3g21630, AT3G21630' 
_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      'Arabidopsis thaliana' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3702 
_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               'Fall armyworm' 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_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            sf-21 
_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          BACULOVIRUS 
_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                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A8R7E6_ARATH 
_struct_ref.pdbx_db_accession          A8R7E6 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;CRTSCPLALASYYLENGTTLSVINQNLNSSIAPYDQINFDPILRYNSNIKDKDRIQMGSRVLVPFPCECQPGDFLGHNFS
YSVRQEDTYERVAISNYANLTTMESLQARNPFPATNIPLSATLNVLVNCSCGDESVSKDFGLFVTYPLRPEDSLSSIARS
SGVSADILQRYNPGVNFNSGNGIVYVPGRDPNGAFPPFKSSKQDGV
;
_struct_ref.pdbx_align_begin           25 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              4EBZ 
_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                 206 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A8R7E6 
_struct_ref_seq.db_align_beg                  25 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  230 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       25 
_struct_ref_seq.pdbx_auth_seq_align_end       230 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 4EBZ HIS A 207 ? UNP A8R7E6 ? ? 'EXPRESSION TAG' 231 1 
1 4EBZ HIS A 208 ? UNP A8R7E6 ? ? 'EXPRESSION TAG' 232 2 
1 4EBZ HIS A 209 ? UNP A8R7E6 ? ? 'EXPRESSION TAG' 233 3 
1 4EBZ HIS A 210 ? UNP A8R7E6 ? ? 'EXPRESSION TAG' 234 4 
1 4EBZ HIS A 211 ? UNP A8R7E6 ? ? 'EXPRESSION TAG' 235 5 
1 4EBZ HIS A 212 ? UNP A8R7E6 ? ? 'EXPRESSION TAG' 236 6 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE               ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE             ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'        ? 'C4 H7 N O4'     133.103 
BMA D-saccharide        . BETA-D-MANNOSE         ? 'C6 H12 O6'      180.156 
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 
MAN D-saccharide        . ALPHA-D-MANNOSE        ? 'C6 H12 O6'      180.156 
MET 'L-peptide linking' y METHIONINE             ? 'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE          ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                 ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE              ? 'C4 H9 N O3'     119.119 
TYR 'L-peptide linking' y TYROSINE               ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                 ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          4EBZ 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.15 
_exptl_crystal.density_percent_sol   60.98 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            298.0 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pdbx_details    
'0.1M Sodium Cacodylate pH6.5, 0.2M sodium acetate and 30% (v/v) PEG 8000 , VAPOR DIFFUSION, HANGING DROP, temperature 298.0K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           298.00 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 210' 
_diffrn_detector.pdbx_collection_date   2011-05-16 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'SAGITALLY FOCUSED Si(111)' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SSRF BEAMLINE BL17U' 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_synchrotron_beamline   BL17U 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.0 
# 
_reflns.entry_id                     4EBZ 
_reflns.observed_criterion_sigma_I   1.0 
_reflns.observed_criterion_sigma_F   2.0 
_reflns.d_resolution_low             99.0 
_reflns.d_resolution_high            1.792 
_reflns.number_obs                   28130 
_reflns.number_all                   28271 
_reflns.percent_possible_obs         99.5 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              6.5 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_refine.entry_id                                 4EBZ 
_refine.ls_number_reflns_obs                     28060 
_refine.ls_number_reflns_all                     28453 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             14.941 
_refine.ls_d_res_high                            1.792 
_refine.ls_percent_reflns_obs                    98.62 
_refine.ls_R_factor_obs                          0.1762 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1746 
_refine.ls_R_factor_R_free                       0.2095 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.04 
_refine.ls_number_reflns_R_free                  1414 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            -3.6460 
_refine.aniso_B[2][2]                            -8.7490 
_refine.aniso_B[3][3]                            12.3949 
_refine.aniso_B[1][2]                            -0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            -0.0000 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 0.392 
_refine.solvent_model_param_bsol                 59.034 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.83 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.17 
_refine.pdbx_overall_phase_error                 19.27 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_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        1546 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         202 
_refine_hist.number_atoms_solvent             301 
_refine_hist.number_atoms_total               2049 
_refine_hist.d_res_high                       1.792 
_refine_hist.d_res_low                        14.941 
# 
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_restraint_function 
_refine_ls_restr.pdbx_refine_id 
f_bond_d           0.011  ? ? 1801 'X-RAY DIFFRACTION' 'X-RAY DIFFRACTION' 
f_angle_d          1.341  ? ? 2440 'X-RAY DIFFRACTION' 'X-RAY DIFFRACTION' 
f_dihedral_angle_d 15.734 ? ? 702  'X-RAY DIFFRACTION' 'X-RAY DIFFRACTION' 
f_chiral_restr     0.097  ? ? 299  'X-RAY DIFFRACTION' 'X-RAY DIFFRACTION' 
f_plane_restr      0.007  ? ? 303  'X-RAY DIFFRACTION' 'X-RAY DIFFRACTION' 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.number_reflns_obs 
'X-RAY DIFFRACTION' 10 1.7921 1.8560  2428 0.2158 92.00  0.2747 . . 133 . . . . 
'X-RAY DIFFRACTION' 10 1.8560 1.9302  2643 0.1851 100.00 0.2437 . . 157 . . . . 
'X-RAY DIFFRACTION' 10 1.9302 2.0178  2649 0.1715 100.00 0.2054 . . 159 . . . . 
'X-RAY DIFFRACTION' 10 2.0178 2.1239  2664 0.1796 100.00 0.2456 . . 153 . . . . 
'X-RAY DIFFRACTION' 10 2.1239 2.2566  2664 0.1689 100.00 0.1855 . . 146 . . . . 
'X-RAY DIFFRACTION' 10 2.2566 2.4301  2703 0.1674 100.00 0.2199 . . 124 . . . . 
'X-RAY DIFFRACTION' 10 2.4301 2.6734  2688 0.1739 100.00 0.2061 . . 143 . . . . 
'X-RAY DIFFRACTION' 10 2.6734 3.0574  2708 0.1792 100.00 0.2315 . . 145 . . . . 
'X-RAY DIFFRACTION' 10 3.0574 3.8411  2755 0.1605 100.00 0.1674 . . 127 . . . . 
'X-RAY DIFFRACTION' 10 3.8411 14.9414 2744 0.1808 95.00  0.2169 . . 127 . . . . 
# 
_struct.entry_id                  4EBZ 
_struct.title                     'Crystal structure of the ectodomain of a receptor like kinase' 
_struct.pdbx_descriptor           'Chitin elicitor receptor kinase 1' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4EBZ 
_struct_keywords.pdbx_keywords   TRANSFERASE 
_struct_keywords.text            
;pathogen-associated molecular patterns, Pattern recognition receptors, Chitin Elicitor Receptor Kinase 1, LysM, lysine motif, chitin oligomer, TRANSFERASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 3 ? 
K N N 3 ? 
L N N 4 ? 
M N N 2 ? 
N N N 2 ? 
O N N 2 ? 
P N N 2 ? 
Q N N 5 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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 1 THR A 19  ? LEU A 27  ? THR A 43  LEU A 51  1 ? 9  
HELX_P HELX_P2 2 PHE A 39  ? ARG A 44  ? PHE A 63  ARG A 68  1 ? 6  
HELX_P HELX_P3 3 THR A 88  ? SER A 95  ? THR A 112 SER A 119 1 ? 8  
HELX_P HELX_P4 4 THR A 102 ? ASN A 110 ? THR A 126 ASN A 134 1 ? 9  
HELX_P HELX_P5 5 PRO A 113 ? ILE A 117 ? PRO A 137 ILE A 141 5 ? 5  
HELX_P HELX_P6 6 SER A 153 ? GLY A 162 ? SER A 177 GLY A 186 1 ? 10 
HELX_P HELX_P7 7 SER A 164 ? ASN A 172 ? SER A 188 ASN A 196 1 ? 9  
# 
_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 
disulf1  disulf ? ? A CYS 1   SG  ? ? ? 1_555 A CYS 69  SG ? ? A CYS 25  A CYS 93  1_555 ? ? ? ? ? ? ? 2.070 ? 
disulf2  disulf ? ? A CYS 5   SG  ? ? ? 1_555 A CYS 131 SG ? ? A CYS 29  A CYS 155 1_555 ? ? ? ? ? ? ? 2.046 ? 
disulf3  disulf ? ? A CYS 67  SG  ? ? ? 1_555 A CYS 129 SG ? ? A CYS 91  A CYS 153 1_555 ? ? ? ? ? ? ? 2.055 ? 
covale1  covale ? ? A ASN 78  ND2 ? ? ? 1_555 H NAG .   C1 ? ? A ASN 102 A NAG 807 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale2  covale ? ? A ASN 99  ND2 ? ? ? 1_555 D NAG .   C1 ? ? A ASN 123 A NAG 803 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale3  covale ? ? M NAG .   O4  ? ? ? 1_555 N NAG .   C1 ? ? A NAG 812 A NAG 813 1_555 ? ? ? ? ? ? ? 1.450 ? 
covale4  covale ? ? A ASN 28  ND2 ? ? ? 1_555 B NAG .   C1 ? ? A ASN 52  A NAG 801 1_555 ? ? ? ? ? ? ? 1.457 ? 
covale5  covale ? ? D NAG .   O4  ? ? ? 1_555 E NAG .   C1 ? ? A NAG 803 A NAG 804 1_555 ? ? ? ? ? ? ? 1.457 ? 
covale6  covale ? ? N NAG .   O4  ? ? ? 1_555 O NAG .   C1 ? ? A NAG 813 A NAG 814 1_555 ? ? ? ? ? ? ? 1.459 ? 
covale7  covale ? ? A ASN 128 ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 152 A NAG 805 1_555 ? ? ? ? ? ? ? 1.459 ? 
covale8  covale ? ? H NAG .   O4  ? ? ? 1_555 I NAG .   C1 ? ? A NAG 807 A NAG 808 1_555 ? ? ? ? ? ? ? 1.463 ? 
covale9  covale ? ? F NAG .   O4  ? ? ? 1_555 G NAG .   C1 ? ? A NAG 805 A NAG 806 1_555 ? ? ? ? ? ? ? 1.464 ? 
covale10 covale ? ? O NAG .   O4  ? ? ? 1_555 P NAG .   C1 ? ? A NAG 814 A NAG 815 1_555 ? ? ? ? ? ? ? 1.464 ? 
covale11 covale ? ? B NAG .   O4  ? ? ? 1_555 C NAG .   C1 ? ? A NAG 801 A NAG 802 1_555 ? ? ? ? ? ? ? 1.469 ? 
covale12 covale ? ? J BMA .   O6  ? ? ? 1_555 K BMA .   C1 ? ? A BMA 809 A BMA 810 1_555 ? ? ? ? ? ? ? 1.460 ? 
covale13 covale ? ? I NAG .   O4  ? ? ? 1_555 J BMA .   C1 ? ? A NAG 808 A BMA 809 1_555 ? ? ? ? ? ? ? 1.461 ? 
covale14 covale ? ? J BMA .   O3  ? ? ? 1_555 L MAN .   C1 ? ? A BMA 809 A MAN 811 1_555 ? ? ? ? ? ? ? 1.461 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 4 ? 
B ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? anti-parallel 
A 2 3 ? parallel      
A 3 4 ? anti-parallel 
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ARG A 60  ? PHE A 65  ? ARG A 84  PHE A 89  
A 2 ALA A 8   ? TYR A 13  ? ALA A 32  TYR A 37  
A 3 PHE A 143 ? PRO A 147 ? PHE A 167 PRO A 171 
A 4 ILE A 183 ? PRO A 187 ? ILE A 207 PRO A 211 
B 1 GLU A 68  ? GLN A 70  ? GLU A 92  GLN A 94  
B 2 PHE A 74  ? SER A 82  ? PHE A 98  SER A 106 
B 3 THR A 122 ? ASN A 128 ? THR A 146 ASN A 152 
# 
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 
A 1 2 O VAL A 61  ? O VAL A 85  N TYR A 12  ? N TYR A 36  
A 2 3 N LEU A 9   ? N LEU A 33  O THR A 145 ? O THR A 169 
A 3 4 N VAL A 144 ? N VAL A 168 O VAL A 186 ? O VAL A 210 
B 1 2 N GLN A 70  ? N GLN A 94  O PHE A 74  ? O PHE A 98  
B 2 3 N PHE A 79  ? N PHE A 103 O VAL A 125 ? O VAL A 149 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE NAG A 812'            
AC2 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE NAG A 813'            
AC3 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE NAG A 814'            
AC4 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG A 815'            
AC5 Software ? ? ? ? 10 'BINDING SITE FOR LINKED RESIDUES A 801 TO 802' 
AC6 Software ? ? ? ? 10 'BINDING SITE FOR LINKED RESIDUES A 803 TO 804' 
AC7 Software ? ? ? ? 6  'BINDING SITE FOR LINKED RESIDUES A 805 TO 806' 
AC8 Software ? ? ? ? 14 'BINDING SITE FOR LINKED RESIDUES A 807 TO 811' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 9  THR A 88  ? THR A 112  . ? 1_555 ? 
2  AC1 9  TYR A 89  ? TYR A 113  . ? 1_555 ? 
3  AC1 9  GLU A 90  ? GLU A 114  . ? 1_555 ? 
4  AC1 9  MET A 103 ? MET A 127  . ? 1_555 ? 
5  AC1 9  GLN A 107 ? GLN A 131  . ? 1_555 ? 
6  AC1 9  ALA A 114 ? ALA A 138  . ? 1_555 ? 
7  AC1 9  NAG N .   ? NAG A 813  . ? 1_555 ? 
8  AC1 9  HOH Q .   ? HOH A 918  . ? 1_555 ? 
9  AC1 9  HOH Q .   ? HOH A 996  . ? 1_555 ? 
10 AC2 7  ASP A 87  ? ASP A 111  . ? 1_555 ? 
11 AC2 7  ALA A 114 ? ALA A 138  . ? 1_555 ? 
12 AC2 7  THR A 115 ? THR A 139  . ? 1_555 ? 
13 AC2 7  ASN A 116 ? ASN A 140  . ? 1_555 ? 
14 AC2 7  ILE A 117 ? ILE A 141  . ? 1_555 ? 
15 AC2 7  NAG M .   ? NAG A 812  . ? 1_555 ? 
16 AC2 7  NAG O .   ? NAG A 814  . ? 1_555 ? 
17 AC3 11 VAL A 83  ? VAL A 107  . ? 1_555 ? 
18 AC3 11 ARG A 84  ? ARG A 108  . ? 1_555 ? 
19 AC3 11 GLU A 86  ? GLU A 110  . ? 1_555 ? 
20 AC3 11 ASP A 87  ? ASP A 111  . ? 1_555 ? 
21 AC3 11 ILE A 117 ? ILE A 141  . ? 1_555 ? 
22 AC3 11 LEU A 119 ? LEU A 143  . ? 1_555 ? 
23 AC3 11 NAG N .   ? NAG A 813  . ? 1_555 ? 
24 AC3 11 NAG P .   ? NAG A 815  . ? 1_555 ? 
25 AC3 11 HOH Q .   ? HOH A 989  . ? 1_555 ? 
26 AC3 11 HOH Q .   ? HOH A 1052 . ? 1_555 ? 
27 AC3 11 HOH Q .   ? HOH A 1072 . ? 1_555 ? 
28 AC4 4  ASN A 116 ? ASN A 140  . ? 1_555 ? 
29 AC4 4  NAG O .   ? NAG A 814  . ? 1_555 ? 
30 AC4 4  HOH Q .   ? HOH A 1024 . ? 1_555 ? 
31 AC4 4  HOH Q .   ? HOH A 1052 . ? 1_555 ? 
32 AC5 10 ASN A 28  ? ASN A 52   . ? 1_555 ? 
33 AC5 10 SER A 30  ? SER A 54   . ? 1_555 ? 
34 AC5 10 ASN A 192 ? ASN A 216  . ? 4_545 ? 
35 AC5 10 HOH Q .   ? HOH A 1007 . ? 4_445 ? 
36 AC5 10 HOH Q .   ? HOH A 1029 . ? 1_555 ? 
37 AC5 10 HOH Q .   ? HOH A 1032 . ? 1_555 ? 
38 AC5 10 HOH Q .   ? HOH A 1050 . ? 1_555 ? 
39 AC5 10 HOH Q .   ? HOH A 1108 . ? 1_555 ? 
40 AC5 10 HOH Q .   ? HOH A 1135 . ? 1_555 ? 
41 AC5 10 HOH Q .   ? HOH A 1146 . ? 4_545 ? 
42 AC6 10 TYR A 13  ? TYR A 37   . ? 1_555 ? 
43 AC6 10 GLU A 15  ? GLU A 39   . ? 1_555 ? 
44 AC6 10 ILE A 94  ? ILE A 118  . ? 1_555 ? 
45 AC6 10 ALA A 98  ? ALA A 122  . ? 1_555 ? 
46 AC6 10 ASN A 99  ? ASN A 123  . ? 1_555 ? 
47 AC6 10 ARG A 149 ? ARG A 173  . ? 1_555 ? 
48 AC6 10 HOH Q .   ? HOH A 985  . ? 1_555 ? 
49 AC6 10 HOH Q .   ? HOH A 1054 . ? 1_555 ? 
50 AC6 10 HOH Q .   ? HOH A 1082 . ? 1_555 ? 
51 AC6 10 HOH Q .   ? HOH A 1114 . ? 1_555 ? 
52 AC7 6  THR A 101 ? THR A 125  . ? 1_555 ? 
53 AC7 6  SER A 105 ? SER A 129  . ? 1_555 ? 
54 AC7 6  LEU A 126 ? LEU A 150  . ? 1_555 ? 
55 AC7 6  ASN A 128 ? ASN A 152  . ? 1_555 ? 
56 AC7 6  HOH Q .   ? HOH A 972  . ? 1_555 ? 
57 AC7 6  HOH Q .   ? HOH A 1074 . ? 1_555 ? 
58 AC8 14 ASN A 38  ? ASN A 62   . ? 4_545 ? 
59 AC8 14 ASP A 40  ? ASP A 64   . ? 4_545 ? 
60 AC8 14 LYS A 52  ? LYS A 76   . ? 4_545 ? 
61 AC8 14 GLN A 70  ? GLN A 94   . ? 1_555 ? 
62 AC8 14 PRO A 71  ? PRO A 95   . ? 1_555 ? 
63 AC8 14 ASN A 78  ? ASN A 102  . ? 1_555 ? 
64 AC8 14 ARG A 109 ? ARG A 133  . ? 1_555 ? 
65 AC8 14 ASN A 124 ? ASN A 148  . ? 1_555 ? 
66 AC8 14 HOH Q .   ? HOH A 998  . ? 1_555 ? 
67 AC8 14 HOH Q .   ? HOH A 1028 . ? 1_555 ? 
68 AC8 14 HOH Q .   ? HOH A 1038 . ? 1_555 ? 
69 AC8 14 HOH Q .   ? HOH A 1069 . ? 1_555 ? 
70 AC8 14 HOH Q .   ? HOH A 1091 . ? 4_545 ? 
71 AC8 14 HOH Q .   ? HOH A 1177 . ? 4_545 ? 
# 
_database_PDB_matrix.entry_id          4EBZ 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    4EBZ 
_atom_sites.fract_transf_matrix[1][1]   0.017402 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014021 
_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]   0.013856 
_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 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . CYS A 1 1   ? 3.403   3.901   5.212   1.00 58.03 ? 25   CYS A N   1 
ATOM   2    C CA  . CYS A 1 1   ? 2.598   4.115   4.013   1.00 56.22 ? 25   CYS A CA  1 
ATOM   3    C C   . CYS A 1 1   ? 1.266   4.757   4.372   1.00 55.91 ? 25   CYS A C   1 
ATOM   4    O O   . CYS A 1 1   ? 0.743   4.544   5.468   1.00 56.22 ? 25   CYS A O   1 
ATOM   5    C CB  . CYS A 1 1   ? 2.354   2.792   3.279   1.00 53.90 ? 25   CYS A CB  1 
ATOM   6    S SG  . CYS A 1 1   ? 3.864   1.972   2.705   1.00 43.20 ? 25   CYS A SG  1 
ATOM   7    N N   . ARG A 1 2   ? 0.715   5.529   3.439   1.00 50.00 ? 26   ARG A N   1 
ATOM   8    C CA  . ARG A 1 2   ? -0.506  6.293   3.699   1.00 54.46 ? 26   ARG A CA  1 
ATOM   9    C C   . ARG A 1 2   ? -1.751  5.422   3.529   1.00 52.55 ? 26   ARG A C   1 
ATOM   10   O O   . ARG A 1 2   ? -2.859  5.813   3.908   1.00 47.76 ? 26   ARG A O   1 
ATOM   11   C CB  . ARG A 1 2   ? -0.578  7.504   2.767   1.00 62.50 ? 26   ARG A CB  1 
ATOM   12   C CG  . ARG A 1 2   ? 0.606   8.449   2.886   1.00 71.35 ? 26   ARG A CG  1 
ATOM   13   C CD  . ARG A 1 2   ? 0.584   9.493   1.781   1.00 80.56 ? 26   ARG A CD  1 
ATOM   14   N NE  . ARG A 1 2   ? 0.734   8.892   0.457   1.00 85.99 ? 26   ARG A NE  1 
ATOM   15   C CZ  . ARG A 1 2   ? 0.546   9.544   -0.687  1.00 91.12 ? 26   ARG A CZ  1 
ATOM   16   N NH1 . ARG A 1 2   ? 0.190   10.823  -0.671  1.00 94.48 ? 26   ARG A NH1 1 
ATOM   17   N NH2 . ARG A 1 2   ? 0.708   8.917   -1.846  1.00 90.67 ? 26   ARG A NH2 1 
ATOM   18   N N   . THR A 1 3   ? -1.565  4.238   2.949   1.00 45.53 ? 27   THR A N   1 
ATOM   19   C CA  . THR A 1 3   ? -2.673  3.323   2.737   1.00 44.31 ? 27   THR A CA  1 
ATOM   20   C C   . THR A 1 3   ? -2.256  1.922   3.160   1.00 41.95 ? 27   THR A C   1 
ATOM   21   O O   . THR A 1 3   ? -1.073  1.623   3.275   1.00 39.46 ? 27   THR A O   1 
ATOM   22   C CB  . THR A 1 3   ? -3.146  3.306   1.261   1.00 46.22 ? 27   THR A CB  1 
ATOM   23   O OG1 . THR A 1 3   ? -2.043  2.989   0.401   1.00 41.92 ? 27   THR A OG1 1 
ATOM   24   C CG2 . THR A 1 3   ? -3.738  4.663   0.856   1.00 47.37 ? 27   THR A CG2 1 
ATOM   25   N N   . SER A 1 4   ? -3.239  1.069   3.406   1.00 43.46 ? 28   SER A N   1 
ATOM   26   C CA  . SER A 1 4   ? -2.978  -0.303  3.806   1.00 42.70 ? 28   SER A CA  1 
ATOM   27   C C   . SER A 1 4   ? -4.144  -1.105  3.310   1.00 41.27 ? 28   SER A C   1 
ATOM   28   O O   . SER A 1 4   ? -5.214  -0.544  3.054   1.00 42.21 ? 28   SER A O   1 
ATOM   29   C CB  . SER A 1 4   ? -2.875  -0.421  5.328   1.00 48.33 ? 28   SER A CB  1 
ATOM   30   O OG  . SER A 1 4   ? -4.105  -0.082  5.951   1.00 48.00 ? 28   SER A OG  1 
ATOM   31   N N   . CYS A 1 5   ? -3.948  -2.412  3.168   1.00 33.52 ? 29   CYS A N   1 
ATOM   32   C CA  . CYS A 1 5   ? -5.028  -3.284  2.756   1.00 31.07 ? 29   CYS A CA  1 
ATOM   33   C C   . CYS A 1 5   ? -4.655  -4.758  2.984   1.00 29.27 ? 29   CYS A C   1 
ATOM   34   O O   . CYS A 1 5   ? -3.472  -5.102  3.079   1.00 31.05 ? 29   CYS A O   1 
ATOM   35   C CB  . CYS A 1 5   ? -5.417  -2.995  1.300   1.00 28.11 ? 29   CYS A CB  1 
ATOM   36   S SG  . CYS A 1 5   ? -4.113  -3.176  0.068   1.00 31.26 ? 29   CYS A SG  1 
ATOM   37   N N   . PRO A 1 6   ? -5.665  -5.637  3.090   1.00 31.41 ? 30   PRO A N   1 
ATOM   38   C CA  . PRO A 1 6   ? -5.349  -7.020  3.471   1.00 31.86 ? 30   PRO A CA  1 
ATOM   39   C C   . PRO A 1 6   ? -4.811  -7.879  2.326   1.00 32.47 ? 30   PRO A C   1 
ATOM   40   O O   . PRO A 1 6   ? -4.225  -8.928  2.589   1.00 31.27 ? 30   PRO A O   1 
ATOM   41   C CB  . PRO A 1 6   ? -6.701  -7.565  3.944   1.00 32.17 ? 30   PRO A CB  1 
ATOM   42   C CG  . PRO A 1 6   ? -7.715  -6.774  3.173   1.00 35.59 ? 30   PRO A CG  1 
ATOM   43   C CD  . PRO A 1 6   ? -7.119  -5.388  3.044   1.00 35.92 ? 30   PRO A CD  1 
ATOM   44   N N   . LEU A 1 7   ? -4.999  -7.457  1.080   1.00 26.63 ? 31   LEU A N   1 
ATOM   45   C CA  . LEU A 1 7   ? -4.441  -8.226  -0.015  1.00 24.70 ? 31   LEU A CA  1 
ATOM   46   C C   . LEU A 1 7   ? -4.381  -7.438  -1.309  1.00 25.40 ? 31   LEU A C   1 
ATOM   47   O O   . LEU A 1 7   ? -4.970  -6.378  -1.417  1.00 23.86 ? 31   LEU A O   1 
ATOM   48   C CB  . LEU A 1 7   ? -5.246  -9.515  -0.253  1.00 34.76 ? 31   LEU A CB  1 
ATOM   49   C CG  . LEU A 1 7   ? -6.546  -9.347  -1.050  1.00 31.83 ? 31   LEU A CG  1 
ATOM   50   C CD1 . LEU A 1 7   ? -6.807  -10.543 -1.941  1.00 38.31 ? 31   LEU A CD1 1 
ATOM   51   C CD2 . LEU A 1 7   ? -7.697  -9.147  -0.104  1.00 38.37 ? 31   LEU A CD2 1 
ATOM   52   N N   . ALA A 1 8   ? -3.660  -8.000  -2.279  1.00 22.94 ? 32   ALA A N   1 
ATOM   53   C CA  . ALA A 1 8   ? -3.647  -7.525  -3.662  1.00 22.42 ? 32   ALA A CA  1 
ATOM   54   C C   . ALA A 1 8   ? -3.746  -8.765  -4.555  1.00 22.37 ? 32   ALA A C   1 
ATOM   55   O O   . ALA A 1 8   ? -3.656  -9.890  -4.063  1.00 22.98 ? 32   ALA A O   1 
ATOM   56   C CB  . ALA A 1 8   ? -2.363  -6.731  -3.953  1.00 20.04 ? 32   ALA A CB  1 
ATOM   57   N N   . LEU A 1 9   ? -3.945  -8.562  -5.857  1.00 21.34 ? 33   LEU A N   1 
ATOM   58   C CA  . LEU A 1 9   ? -4.017  -9.659  -6.810  1.00 22.25 ? 33   LEU A CA  1 
ATOM   59   C C   . LEU A 1 9   ? -2.897  -9.467  -7.821  1.00 20.40 ? 33   LEU A C   1 
ATOM   60   O O   . LEU A 1 9   ? -2.599  -8.341  -8.219  1.00 19.18 ? 33   LEU A O   1 
ATOM   61   C CB  . LEU A 1 9   ? -5.368  -9.664  -7.549  1.00 21.16 ? 33   LEU A CB  1 
ATOM   62   C CG  . LEU A 1 9   ? -6.556  -10.033 -6.680  1.00 22.77 ? 33   LEU A CG  1 
ATOM   63   C CD1 . LEU A 1 9   ? -7.863  -9.751  -7.431  1.00 25.98 ? 33   LEU A CD1 1 
ATOM   64   C CD2 . LEU A 1 9   ? -6.456  -11.544 -6.360  1.00 21.95 ? 33   LEU A CD2 1 
ATOM   65   N N   . ALA A 1 10  ? -2.268  -10.565 -8.217  1.00 16.41 ? 34   ALA A N   1 
ATOM   66   C CA  . ALA A 1 10  ? -1.235  -10.507 -9.261  1.00 18.02 ? 34   ALA A CA  1 
ATOM   67   C C   . ALA A 1 10  ? -1.782  -11.102 -10.565 1.00 20.44 ? 34   ALA A C   1 
ATOM   68   O O   . ALA A 1 10  ? -2.304  -12.205 -10.549 1.00 22.09 ? 34   ALA A O   1 
ATOM   69   C CB  . ALA A 1 10  ? 0.020   -11.342 -8.810  1.00 20.30 ? 34   ALA A CB  1 
ATOM   70   N N   . SER A 1 11  ? -1.594  -10.429 -11.696 1.00 19.85 ? 35   SER A N   1 
ATOM   71   C CA  . SER A 1 11  ? -2.061  -10.955 -12.986 1.00 17.49 ? 35   SER A CA  1 
ATOM   72   C C   . SER A 1 11  ? -0.923  -11.702 -13.699 1.00 17.77 ? 35   SER A C   1 
ATOM   73   O O   . SER A 1 11  ? 0.058   -11.099 -14.153 1.00 17.74 ? 35   SER A O   1 
ATOM   74   C CB  . SER A 1 11  ? -2.578  -9.815  -13.878 1.00 20.03 ? 35   SER A CB  1 
ATOM   75   O OG  . SER A 1 11  ? -3.060  -10.328 -15.126 1.00 22.70 ? 35   SER A OG  1 
ATOM   76   N N   . TYR A 1 12  ? -1.044  -13.028 -13.782 1.00 17.67 ? 36   TYR A N   1 
ATOM   77   C CA  . TYR A 1 12  ? 0.022   -13.868 -14.317 1.00 19.31 ? 36   TYR A CA  1 
ATOM   78   C C   . TYR A 1 12  ? -0.383  -14.414 -15.686 1.00 18.48 ? 36   TYR A C   1 
ATOM   79   O O   . TYR A 1 12  ? -1.264  -15.289 -15.790 1.00 22.94 ? 36   TYR A O   1 
ATOM   80   C CB  . TYR A 1 12  ? 0.257   -15.022 -13.342 1.00 16.69 ? 36   TYR A CB  1 
ATOM   81   C CG  . TYR A 1 12  ? 1.534   -15.823 -13.544 1.00 19.61 ? 36   TYR A CG  1 
ATOM   82   C CD1 . TYR A 1 12  ? 2.548   -15.777 -12.596 1.00 19.03 ? 36   TYR A CD1 1 
ATOM   83   C CD2 . TYR A 1 12  ? 1.720   -16.600 -14.678 1.00 17.43 ? 36   TYR A CD2 1 
ATOM   84   C CE1 . TYR A 1 12  ? 3.724   -16.516 -12.750 1.00 20.20 ? 36   TYR A CE1 1 
ATOM   85   C CE2 . TYR A 1 12  ? 2.927   -17.326 -14.862 1.00 22.22 ? 36   TYR A CE2 1 
ATOM   86   C CZ  . TYR A 1 12  ? 3.904   -17.280 -13.887 1.00 22.17 ? 36   TYR A CZ  1 
ATOM   87   O OH  . TYR A 1 12  ? 5.058   -18.027 -14.060 1.00 20.15 ? 36   TYR A OH  1 
ATOM   88   N N   . TYR A 1 13  ? 0.230   -13.876 -16.732 1.00 19.31 ? 37   TYR A N   1 
ATOM   89   C CA  . TYR A 1 13  ? -0.047  -14.309 -18.115 1.00 20.09 ? 37   TYR A CA  1 
ATOM   90   C C   . TYR A 1 13  ? 0.596   -15.660 -18.416 1.00 20.79 ? 37   TYR A C   1 
ATOM   91   O O   . TYR A 1 13  ? 1.761   -15.901 -18.068 1.00 23.86 ? 37   TYR A O   1 
ATOM   92   C CB  . TYR A 1 13  ? 0.495   -13.267 -19.117 1.00 21.32 ? 37   TYR A CB  1 
ATOM   93   C CG  . TYR A 1 13  ? 0.236   -13.641 -20.573 1.00 23.93 ? 37   TYR A CG  1 
ATOM   94   C CD1 . TYR A 1 13  ? -1.023  -13.446 -21.149 1.00 28.51 ? 37   TYR A CD1 1 
ATOM   95   C CD2 . TYR A 1 13  ? 1.245   -14.191 -21.369 1.00 25.88 ? 37   TYR A CD2 1 
ATOM   96   C CE1 . TYR A 1 13  ? -1.277  -13.797 -22.492 1.00 29.16 ? 37   TYR A CE1 1 
ATOM   97   C CE2 . TYR A 1 13  ? 1.003   -14.537 -22.712 1.00 25.96 ? 37   TYR A CE2 1 
ATOM   98   C CZ  . TYR A 1 13  ? -0.253  -14.329 -23.259 1.00 28.84 ? 37   TYR A CZ  1 
ATOM   99   O OH  . TYR A 1 13  ? -0.486  -14.668 -24.575 1.00 32.80 ? 37   TYR A OH  1 
ATOM   100  N N   . LEU A 1 14  ? -0.158  -16.517 -19.105 1.00 22.60 ? 38   LEU A N   1 
ATOM   101  C CA  . LEU A 1 14  ? 0.251   -17.896 -19.346 1.00 20.49 ? 38   LEU A CA  1 
ATOM   102  C C   . LEU A 1 14  ? 0.888   -18.082 -20.721 1.00 23.21 ? 38   LEU A C   1 
ATOM   103  O O   . LEU A 1 14  ? 0.231   -17.901 -21.756 1.00 27.08 ? 38   LEU A O   1 
ATOM   104  C CB  . LEU A 1 14  ? -0.972  -18.816 -19.226 1.00 20.93 ? 38   LEU A CB  1 
ATOM   105  C CG  . LEU A 1 14  ? -1.632  -18.846 -17.849 1.00 21.30 ? 38   LEU A CG  1 
ATOM   106  C CD1 . LEU A 1 14  ? -2.794  -19.806 -17.876 1.00 22.47 ? 38   LEU A CD1 1 
ATOM   107  C CD2 . LEU A 1 14  ? -0.643  -19.299 -16.774 1.00 21.60 ? 38   LEU A CD2 1 
ATOM   108  N N   . GLU A 1 15  ? 2.161   -18.455 -20.741 1.00 24.85 ? 39   GLU A N   1 
ATOM   109  C CA  . GLU A 1 15  ? 2.760   -18.894 -21.993 1.00 26.03 ? 39   GLU A CA  1 
ATOM   110  C C   . GLU A 1 15  ? 3.863   -19.919 -21.757 1.00 21.69 ? 39   GLU A C   1 
ATOM   111  O O   . GLU A 1 15  ? 4.373   -20.066 -20.647 1.00 24.67 ? 39   GLU A O   1 
ATOM   112  C CB  . GLU A 1 15  ? 3.294   -17.719 -22.797 1.00 33.70 ? 39   GLU A CB  1 
ATOM   113  C CG  . GLU A 1 15  ? 4.506   -17.113 -22.169 1.00 34.95 ? 39   GLU A CG  1 
ATOM   114  C CD  . GLU A 1 15  ? 5.031   -15.911 -22.942 1.00 40.61 ? 39   GLU A CD  1 
ATOM   115  O OE1 . GLU A 1 15  ? 5.899   -15.215 -22.375 1.00 39.62 ? 39   GLU A OE1 1 
ATOM   116  O OE2 . GLU A 1 15  ? 4.593   -15.680 -24.098 1.00 38.72 ? 39   GLU A OE2 1 
ATOM   117  N N   . ASN A 1 16  ? 4.211   -20.623 -22.821 1.00 24.27 ? 40   ASN A N   1 
ATOM   118  C CA  . ASN A 1 16  ? 5.246   -21.659 -22.773 1.00 25.31 ? 40   ASN A CA  1 
ATOM   119  C C   . ASN A 1 16  ? 5.020   -22.759 -21.732 1.00 26.40 ? 40   ASN A C   1 
ATOM   120  O O   . ASN A 1 16  ? 5.982   -23.322 -21.204 1.00 29.37 ? 40   ASN A O   1 
ATOM   121  C CB  . ASN A 1 16  ? 6.640   -21.019 -22.586 1.00 30.29 ? 40   ASN A CB  1 
ATOM   122  C CG  . ASN A 1 16  ? 7.148   -20.340 -23.855 1.00 34.16 ? 40   ASN A CG  1 
ATOM   123  O OD1 . ASN A 1 16  ? 6.493   -20.381 -24.898 1.00 37.24 ? 40   ASN A OD1 1 
ATOM   124  N ND2 . ASN A 1 16  ? 8.312   -19.692 -23.763 1.00 33.04 ? 40   ASN A ND2 1 
ATOM   125  N N   . GLY A 1 17  ? 3.761   -23.066 -21.430 1.00 27.07 ? 41   GLY A N   1 
ATOM   126  C CA  . GLY A 1 17  ? 3.452   -24.293 -20.694 1.00 24.83 ? 41   GLY A CA  1 
ATOM   127  C C   . GLY A 1 17  ? 3.160   -24.225 -19.187 1.00 26.84 ? 41   GLY A C   1 
ATOM   128  O O   . GLY A 1 17  ? 2.876   -25.252 -18.555 1.00 26.08 ? 41   GLY A O   1 
ATOM   129  N N   . THR A 1 18  ? 3.236   -23.033 -18.614 1.00 21.97 ? 42   THR A N   1 
ATOM   130  C CA  . THR A 1 18  ? 3.078   -22.804 -17.167 1.00 19.64 ? 42   THR A CA  1 
ATOM   131  C C   . THR A 1 18  ? 1.857   -23.497 -16.595 1.00 21.62 ? 42   THR A C   1 
ATOM   132  O O   . THR A 1 18  ? 0.796   -23.449 -17.201 1.00 23.11 ? 42   THR A O   1 
ATOM   133  C CB  . THR A 1 18  ? 2.862   -21.284 -16.920 1.00 26.13 ? 42   THR A CB  1 
ATOM   134  O OG1 . THR A 1 18  ? 3.994   -20.577 -17.416 1.00 25.49 ? 42   THR A OG1 1 
ATOM   135  C CG2 . THR A 1 18  ? 2.664   -20.948 -15.420 1.00 22.28 ? 42   THR A CG2 1 
ATOM   136  N N   . THR A 1 19  ? 2.015   -24.122 -15.431 1.00 25.15 ? 43   THR A N   1 
ATOM   137  C CA  . THR A 1 19  ? 0.915   -24.840 -14.768 1.00 22.34 ? 43   THR A CA  1 
ATOM   138  C C   . THR A 1 19  ? 0.480   -24.105 -13.511 1.00 25.20 ? 43   THR A C   1 
ATOM   139  O O   . THR A 1 19  ? 1.197   -23.233 -13.014 1.00 20.36 ? 43   THR A O   1 
ATOM   140  C CB  . THR A 1 19  ? 1.338   -26.245 -14.328 1.00 22.80 ? 43   THR A CB  1 
ATOM   141  O OG1 . THR A 1 19  ? 2.432   -26.155 -13.385 1.00 22.86 ? 43   THR A OG1 1 
ATOM   142  C CG2 . THR A 1 19  ? 1.754   -27.073 -15.538 1.00 26.04 ? 43   THR A CG2 1 
ATOM   143  N N   . LEU A 1 20  ? -0.693  -24.448 -12.981 1.00 22.12 ? 44   LEU A N   1 
ATOM   144  C CA  . LEU A 1 20  ? -1.182  -23.708 -11.809 1.00 22.16 ? 44   LEU A CA  1 
ATOM   145  C C   . LEU A 1 20  ? -0.248  -23.982 -10.629 1.00 21.39 ? 44   LEU A C   1 
ATOM   146  O O   . LEU A 1 20  ? -0.003  -23.118 -9.786  1.00 21.69 ? 44   LEU A O   1 
ATOM   147  C CB  . LEU A 1 20  ? -2.605  -24.157 -11.458 1.00 25.45 ? 44   LEU A CB  1 
ATOM   148  C CG  . LEU A 1 20  ? -3.313  -23.334 -10.381 1.00 27.29 ? 44   LEU A CG  1 
ATOM   149  C CD1 . LEU A 1 20  ? -3.405  -21.919 -10.831 1.00 29.41 ? 44   LEU A CD1 1 
ATOM   150  C CD2 . LEU A 1 20  ? -4.723  -23.915 -10.119 1.00 27.79 ? 44   LEU A CD2 1 
ATOM   151  N N   . SER A 1 21  ? 0.277   -25.204 -10.571 1.00 21.57 ? 45   SER A N   1 
ATOM   152  C CA  . SER A 1 21  ? 1.164   -25.570 -9.474  1.00 24.29 ? 45   SER A CA  1 
ATOM   153  C C   . SER A 1 21  ? 2.428   -24.704 -9.448  1.00 26.02 ? 45   SER A C   1 
ATOM   154  O O   . SER A 1 21  ? 2.874   -24.247 -8.372  1.00 23.17 ? 45   SER A O   1 
ATOM   155  C CB  . SER A 1 21  ? 1.509   -27.071 -9.560  1.00 34.24 ? 45   SER A CB  1 
ATOM   156  O OG  . SER A 1 21  ? 2.375   -27.438 -8.518  1.00 43.50 ? 45   SER A OG  1 
ATOM   157  N N   . VAL A 1 22  ? 3.010   -24.459 -10.622 1.00 20.96 ? 46   VAL A N   1 
ATOM   158  C CA  . VAL A 1 22  ? 4.181   -23.576 -10.691 1.00 19.65 ? 46   VAL A CA  1 
ATOM   159  C C   . VAL A 1 22  ? 3.875   -22.132 -10.256 1.00 19.63 ? 46   VAL A C   1 
ATOM   160  O O   . VAL A 1 22  ? 4.669   -21.469 -9.552  1.00 20.09 ? 46   VAL A O   1 
ATOM   161  C CB  . VAL A 1 22  ? 4.797   -23.568 -12.114 1.00 25.86 ? 46   VAL A CB  1 
ATOM   162  C CG1 . VAL A 1 22  ? 5.801   -22.431 -12.245 1.00 32.68 ? 46   VAL A CG1 1 
ATOM   163  C CG2 . VAL A 1 22  ? 5.449   -24.917 -12.406 1.00 32.61 ? 46   VAL A CG2 1 
ATOM   164  N N   . ILE A 1 23  ? 2.712   -21.642 -10.665 1.00 18.57 ? 47   ILE A N   1 
ATOM   165  C CA  . ILE A 1 23  ? 2.285   -20.313 -10.249 1.00 16.94 ? 47   ILE A CA  1 
ATOM   166  C C   . ILE A 1 23  ? 2.158   -20.275 -8.729  1.00 19.81 ? 47   ILE A C   1 
ATOM   167  O O   . ILE A 1 23  ? 2.682   -19.380 -8.083  1.00 19.81 ? 47   ILE A O   1 
ATOM   168  C CB  . ILE A 1 23  ? 0.942   -19.936 -10.894 1.00 17.42 ? 47   ILE A CB  1 
ATOM   169  C CG1 . ILE A 1 23  ? 1.160   -19.753 -12.407 1.00 18.60 ? 47   ILE A CG1 1 
ATOM   170  C CG2 . ILE A 1 23  ? 0.408   -18.616 -10.302 1.00 18.20 ? 47   ILE A CG2 1 
ATOM   171  C CD1 . ILE A 1 23  ? -0.153  -19.516 -13.205 1.00 20.42 ? 47   ILE A CD1 1 
ATOM   172  N N   . ASN A 1 24  ? 1.488   -21.266 -8.152  1.00 18.72 ? 48   ASN A N   1 
ATOM   173  C CA  . ASN A 1 24  ? 1.271   -21.259 -6.711  1.00 17.14 ? 48   ASN A CA  1 
ATOM   174  C C   . ASN A 1 24  ? 2.582   -21.412 -5.946  1.00 19.94 ? 48   ASN A C   1 
ATOM   175  O O   . ASN A 1 24  ? 2.771   -20.797 -4.894  1.00 22.17 ? 48   ASN A O   1 
ATOM   176  C CB  . ASN A 1 24  ? 0.275   -22.347 -6.315  1.00 20.14 ? 48   ASN A CB  1 
ATOM   177  C CG  . ASN A 1 24  ? -0.299  -22.140 -4.930  1.00 22.51 ? 48   ASN A CG  1 
ATOM   178  O OD1 . ASN A 1 24  ? 0.175   -21.295 -4.128  1.00 28.19 ? 48   ASN A OD1 1 
ATOM   179  N ND2 . ASN A 1 24  ? -1.322  -22.892 -4.637  1.00 20.26 ? 48   ASN A ND2 1 
ATOM   180  N N   . GLN A 1 25  ? 3.498   -22.201 -6.490  1.00 18.41 ? 49   GLN A N   1 
ATOM   181  C CA  . GLN A 1 25  ? 4.813   -22.364 -5.872  1.00 17.35 ? 49   GLN A CA  1 
ATOM   182  C C   . GLN A 1 25  ? 5.567   -21.039 -5.875  1.00 20.45 ? 49   GLN A C   1 
ATOM   183  O O   . GLN A 1 25  ? 6.059   -20.573 -4.821  1.00 19.60 ? 49   GLN A O   1 
ATOM   184  C CB  . GLN A 1 25  ? 5.624   -23.401 -6.642  1.00 19.98 ? 49   GLN A CB  1 
ATOM   185  C CG  . GLN A 1 25  ? 7.009   -23.613 -6.099  1.00 25.88 ? 49   GLN A CG  1 
ATOM   186  C CD  . GLN A 1 25  ? 7.653   -24.855 -6.688  1.00 32.30 ? 49   GLN A CD  1 
ATOM   187  O OE1 . GLN A 1 25  ? 7.695   -25.043 -7.917  1.00 31.34 ? 49   GLN A OE1 1 
ATOM   188  N NE2 . GLN A 1 25  ? 8.127   -25.723 -5.812  1.00 31.65 ? 49   GLN A NE2 1 
ATOM   189  N N   . ASN A 1 26  ? 5.652   -20.417 -7.051  1.00 18.03 ? 50   ASN A N   1 
ATOM   190  C CA  . ASN A 1 26  ? 6.440   -19.172 -7.169  1.00 18.87 ? 50   ASN A CA  1 
ATOM   191  C C   . ASN A 1 26  ? 5.825   -18.046 -6.353  1.00 20.66 ? 50   ASN A C   1 
ATOM   192  O O   . ASN A 1 26  ? 6.542   -17.232 -5.748  1.00 18.73 ? 50   ASN A O   1 
ATOM   193  C CB  . ASN A 1 26  ? 6.556   -18.713 -8.633  1.00 19.18 ? 50   ASN A CB  1 
ATOM   194  C CG  . ASN A 1 26  ? 7.404   -19.658 -9.474  1.00 23.19 ? 50   ASN A CG  1 
ATOM   195  O OD1 . ASN A 1 26  ? 8.001   -20.601 -8.946  1.00 21.46 ? 50   ASN A OD1 1 
ATOM   196  N ND2 . ASN A 1 26  ? 7.478   -19.398 -10.782 1.00 22.47 ? 50   ASN A ND2 1 
ATOM   197  N N   . LEU A 1 27  ? 4.489   -17.988 -6.343  1.00 17.81 ? 51   LEU A N   1 
ATOM   198  C CA  . LEU A 1 27  ? 3.809   -16.907 -5.634  1.00 15.98 ? 51   LEU A CA  1 
ATOM   199  C C   . LEU A 1 27  ? 3.270   -17.411 -4.290  1.00 18.88 ? 51   LEU A C   1 
ATOM   200  O O   . LEU A 1 27  ? 2.313   -16.884 -3.763  1.00 18.36 ? 51   LEU A O   1 
ATOM   201  C CB  . LEU A 1 27  ? 2.674   -16.292 -6.480  1.00 15.19 ? 51   LEU A CB  1 
ATOM   202  C CG  . LEU A 1 27  ? 3.148   -15.275 -7.533  1.00 23.95 ? 51   LEU A CG  1 
ATOM   203  C CD1 . LEU A 1 27  ? 3.890   -15.976 -8.632  1.00 24.61 ? 51   LEU A CD1 1 
ATOM   204  C CD2 . LEU A 1 27  ? 1.945   -14.481 -8.088  1.00 25.76 ? 51   LEU A CD2 1 
ATOM   205  N N   . ASN A 1 28  ? 3.923   -18.420 -3.723  1.00 20.98 ? 52   ASN A N   1 
ATOM   206  C CA  . ASN A 1 28  ? 3.484   -18.916 -2.418  1.00 19.39 ? 52   ASN A CA  1 
ATOM   207  C C   . ASN A 1 28  ? 3.502   -17.826 -1.365  1.00 17.19 ? 52   ASN A C   1 
ATOM   208  O O   . ASN A 1 28  ? 4.418   -17.001 -1.346  1.00 19.07 ? 52   ASN A O   1 
ATOM   209  C CB  . ASN A 1 28  ? 4.392   -20.043 -1.951  1.00 17.84 ? 52   ASN A CB  1 
ATOM   210  C CG  . ASN A 1 28  ? 4.141   -20.411 -0.504  1.00 23.52 ? 52   ASN A CG  1 
ATOM   211  O OD1 . ASN A 1 28  ? 3.140   -21.031 -0.206  1.00 21.20 ? 52   ASN A OD1 1 
ATOM   212  N ND2 . ASN A 1 28  ? 5.062   -20.032 0.396   1.00 20.06 ? 52   ASN A ND2 1 
ATOM   213  N N   . SER A 1 29  ? 2.513   -17.828 -0.470  1.00 16.49 ? 53   SER A N   1 
ATOM   214  C CA  . SER A 1 29  ? 2.474   -16.866 0.640   1.00 16.96 ? 53   SER A CA  1 
ATOM   215  C C   . SER A 1 29  ? 1.491   -17.381 1.671   1.00 19.61 ? 53   SER A C   1 
ATOM   216  O O   . SER A 1 29  ? 0.880   -18.425 1.480   1.00 20.56 ? 53   SER A O   1 
ATOM   217  C CB  . SER A 1 29  ? 2.025   -15.477 0.177   1.00 19.53 ? 53   SER A CB  1 
ATOM   218  O OG  . SER A 1 29  ? 0.615   -15.484 -0.118  1.00 18.86 ? 53   SER A OG  1 
ATOM   219  N N   . SER A 1 30  ? 1.331   -16.635 2.758   1.00 19.40 ? 54   SER A N   1 
ATOM   220  C CA  . SER A 1 30  ? 0.343   -17.007 3.785   1.00 19.12 ? 54   SER A CA  1 
ATOM   221  C C   . SER A 1 30  ? -1.081  -16.989 3.226   1.00 21.46 ? 54   SER A C   1 
ATOM   222  O O   . SER A 1 30  ? -1.967  -17.726 3.684   1.00 22.41 ? 54   SER A O   1 
ATOM   223  C CB  . SER A 1 30  ? 0.429   -16.040 4.956   1.00 30.35 ? 54   SER A CB  1 
ATOM   224  O OG  . SER A 1 30  ? 1.594   -16.322 5.713   1.00 42.88 ? 54   SER A OG  1 
ATOM   225  N N   . ILE A 1 31  ? -1.289  -16.115 2.253   1.00 21.16 ? 55   ILE A N   1 
ATOM   226  C CA  . ILE A 1 31  ? -2.597  -15.946 1.628   1.00 19.97 ? 55   ILE A CA  1 
ATOM   227  C C   . ILE A 1 31  ? -2.886  -16.978 0.519   1.00 21.69 ? 55   ILE A C   1 
ATOM   228  O O   . ILE A 1 31  ? -4.052  -17.277 0.220   1.00 23.55 ? 55   ILE A O   1 
ATOM   229  C CB  . ILE A 1 31  ? -2.713  -14.502 1.090   1.00 24.99 ? 55   ILE A CB  1 
ATOM   230  C CG1 . ILE A 1 31  ? -3.270  -13.594 2.184   1.00 34.97 ? 55   ILE A CG1 1 
ATOM   231  C CG2 . ILE A 1 31  ? -3.537  -14.429 -0.183  1.00 26.39 ? 55   ILE A CG2 1 
ATOM   232  C CD1 . ILE A 1 31  ? -2.956  -12.121 1.956   1.00 38.46 ? 55   ILE A CD1 1 
ATOM   233  N N   . ALA A 1 32  ? -1.836  -17.483 -0.125  1.00 20.16 ? 56   ALA A N   1 
ATOM   234  C CA  . ALA A 1 32  ? -1.993  -18.617 -1.056  1.00 21.37 ? 56   ALA A CA  1 
ATOM   235  C C   . ALA A 1 32  ? -0.963  -19.719 -0.755  1.00 23.80 ? 56   ALA A C   1 
ATOM   236  O O   . ALA A 1 32  ? 0.038   -19.857 -1.478  1.00 21.16 ? 56   ALA A O   1 
ATOM   237  C CB  . ALA A 1 32  ? -1.817  -18.144 -2.488  1.00 22.81 ? 56   ALA A CB  1 
ATOM   238  N N   . PRO A 1 33  ? -1.186  -20.491 0.314   1.00 22.19 ? 57   PRO A N   1 
ATOM   239  C CA  . PRO A 1 33  ? -0.160  -21.452 0.725   1.00 18.42 ? 57   PRO A CA  1 
ATOM   240  C C   . PRO A 1 33  ? -0.088  -22.628 -0.236  1.00 25.04 ? 57   PRO A C   1 
ATOM   241  O O   . PRO A 1 33  ? -1.071  -23.299 -0.526  1.00 30.41 ? 57   PRO A O   1 
ATOM   242  C CB  . PRO A 1 33  ? -0.644  -21.963 2.094   1.00 24.83 ? 57   PRO A CB  1 
ATOM   243  C CG  . PRO A 1 33  ? -1.866  -21.187 2.430   1.00 25.41 ? 57   PRO A CG  1 
ATOM   244  C CD  . PRO A 1 33  ? -2.363  -20.502 1.192   1.00 25.04 ? 57   PRO A CD  1 
ATOM   245  N N   . TYR A 1 34  ? 1.113   -22.919 -0.692  1.00 20.49 ? 58   TYR A N   1 
ATOM   246  C CA  . TYR A 1 34  ? 1.308   -23.950 -1.676  1.00 21.91 ? 58   TYR A CA  1 
ATOM   247  C C   . TYR A 1 34  ? 1.414   -25.321 -1.012  1.00 25.19 ? 58   TYR A C   1 
ATOM   248  O O   . TYR A 1 34  ? 2.363   -25.589 -0.283  1.00 25.07 ? 58   TYR A O   1 
ATOM   249  C CB  . TYR A 1 34  ? 2.594   -23.648 -2.439  1.00 21.08 ? 58   TYR A CB  1 
ATOM   250  C CG  . TYR A 1 34  ? 2.948   -24.713 -3.463  1.00 23.35 ? 58   TYR A CG  1 
ATOM   251  C CD1 . TYR A 1 34  ? 2.067   -25.046 -4.490  1.00 24.97 ? 58   TYR A CD1 1 
ATOM   252  C CD2 . TYR A 1 34  ? 4.189   -25.332 -3.443  1.00 27.02 ? 58   TYR A CD2 1 
ATOM   253  C CE1 . TYR A 1 34  ? 2.403   -26.001 -5.451  1.00 27.60 ? 58   TYR A CE1 1 
ATOM   254  C CE2 . TYR A 1 34  ? 4.534   -26.285 -4.408  1.00 32.80 ? 58   TYR A CE2 1 
ATOM   255  C CZ  . TYR A 1 34  ? 3.652   -26.601 -5.412  1.00 32.10 ? 58   TYR A CZ  1 
ATOM   256  O OH  . TYR A 1 34  ? 4.000   -27.548 -6.359  1.00 34.19 ? 58   TYR A OH  1 
ATOM   257  N N   . ASP A 1 35  ? 0.433   -26.184 -1.234  1.00 25.35 ? 59   ASP A N   1 
ATOM   258  C CA  . ASP A 1 35  ? 0.553   -27.553 -0.713  1.00 30.42 ? 59   ASP A CA  1 
ATOM   259  C C   . ASP A 1 35  ? 0.381   -28.625 -1.777  1.00 30.52 ? 59   ASP A C   1 
ATOM   260  O O   . ASP A 1 35  ? 0.403   -29.816 -1.464  1.00 30.58 ? 59   ASP A O   1 
ATOM   261  C CB  . ASP A 1 35  ? -0.391  -27.792 0.472   1.00 35.38 ? 59   ASP A CB  1 
ATOM   262  C CG  . ASP A 1 35  ? -1.857  -27.720 0.084   1.00 37.64 ? 59   ASP A CG  1 
ATOM   263  O OD1 . ASP A 1 35  ? -2.183  -27.757 -1.124  1.00 31.07 ? 59   ASP A OD1 1 
ATOM   264  O OD2 . ASP A 1 35  ? -2.693  -27.651 1.007   1.00 44.90 ? 59   ASP A OD2 1 
ATOM   265  N N   . GLN A 1 36  ? 0.250   -28.205 -3.030  1.00 29.84 ? 60   GLN A N   1 
ATOM   266  C CA  . GLN A 1 36  ? 0.122   -29.114 -4.174  1.00 31.61 ? 60   GLN A CA  1 
ATOM   267  C C   . GLN A 1 36  ? -1.227  -29.829 -4.271  1.00 35.33 ? 60   GLN A C   1 
ATOM   268  O O   . GLN A 1 36  ? -1.496  -30.533 -5.253  1.00 41.69 ? 60   GLN A O   1 
ATOM   269  C CB  . GLN A 1 36  ? 1.240   -30.159 -4.183  1.00 35.66 ? 60   GLN A CB  1 
ATOM   270  C CG  . GLN A 1 36  ? 2.604   -29.637 -4.608  1.00 42.02 ? 60   GLN A CG  1 
ATOM   271  C CD  . GLN A 1 36  ? 3.606   -30.774 -4.827  1.00 47.96 ? 60   GLN A CD  1 
ATOM   272  O OE1 . GLN A 1 36  ? 4.144   -31.329 -3.867  1.00 49.41 ? 60   GLN A OE1 1 
ATOM   273  N NE2 . GLN A 1 36  ? 3.840   -31.136 -6.096  1.00 42.38 ? 60   GLN A NE2 1 
ATOM   274  N N   . ILE A 1 37  ? -2.058  -29.667 -3.252  1.00 30.82 ? 61   ILE A N   1 
ATOM   275  C CA  . ILE A 1 37  ? -3.329  -30.388 -3.162  1.00 35.17 ? 61   ILE A CA  1 
ATOM   276  C C   . ILE A 1 37  ? -4.538  -29.446 -3.304  1.00 38.09 ? 61   ILE A C   1 
ATOM   277  O O   . ILE A 1 37  ? -5.487  -29.720 -4.048  1.00 37.94 ? 61   ILE A O   1 
ATOM   278  C CB  . ILE A 1 37  ? -3.470  -31.050 -1.796  1.00 40.01 ? 61   ILE A CB  1 
ATOM   279  C CG1 . ILE A 1 37  ? -2.312  -32.022 -1.544  1.00 46.22 ? 61   ILE A CG1 1 
ATOM   280  C CG2 . ILE A 1 37  ? -4.810  -31.765 -1.697  1.00 44.87 ? 61   ILE A CG2 1 
ATOM   281  C CD1 . ILE A 1 37  ? -2.087  -32.310 -0.068  1.00 48.80 ? 61   ILE A CD1 1 
ATOM   282  N N   . ASN A 1 38  ? -4.485  -28.347 -2.564  1.00 28.12 ? 62   ASN A N   1 
ATOM   283  C CA  . ASN A 1 38  ? -5.595  -27.410 -2.440  1.00 28.37 ? 62   ASN A CA  1 
ATOM   284  C C   . ASN A 1 38  ? -5.214  -26.080 -3.059  1.00 28.68 ? 62   ASN A C   1 
ATOM   285  O O   . ASN A 1 38  ? -4.366  -25.388 -2.520  1.00 25.88 ? 62   ASN A O   1 
ATOM   286  C CB  . ASN A 1 38  ? -5.925  -27.217 -0.950  1.00 28.96 ? 62   ASN A CB  1 
ATOM   287  C CG  . ASN A 1 38  ? -7.179  -26.391 -0.718  1.00 32.35 ? 62   ASN A CG  1 
ATOM   288  O OD1 . ASN A 1 38  ? -7.502  -25.500 -1.495  1.00 34.25 ? 62   ASN A OD1 1 
ATOM   289  N ND2 . ASN A 1 38  ? -7.875  -26.675 0.376   1.00 28.47 ? 62   ASN A ND2 1 
ATOM   290  N N   . PHE A 1 39  ? -5.811  -25.755 -4.208  1.00 23.48 ? 63   PHE A N   1 
ATOM   291  C CA  . PHE A 1 39  ? -5.570  -24.507 -4.924  1.00 25.20 ? 63   PHE A CA  1 
ATOM   292  C C   . PHE A 1 39  ? -6.727  -23.502 -4.776  1.00 24.84 ? 63   PHE A C   1 
ATOM   293  O O   . PHE A 1 39  ? -6.785  -22.505 -5.482  1.00 23.42 ? 63   PHE A O   1 
ATOM   294  C CB  . PHE A 1 39  ? -5.326  -24.821 -6.405  1.00 24.51 ? 63   PHE A CB  1 
ATOM   295  C CG  . PHE A 1 39  ? -4.097  -25.668 -6.639  1.00 25.41 ? 63   PHE A CG  1 
ATOM   296  C CD1 . PHE A 1 39  ? -2.852  -25.062 -6.805  1.00 26.43 ? 63   PHE A CD1 1 
ATOM   297  C CD2 . PHE A 1 39  ? -4.178  -27.044 -6.669  1.00 30.16 ? 63   PHE A CD2 1 
ATOM   298  C CE1 . PHE A 1 39  ? -1.709  -25.827 -7.003  1.00 26.69 ? 63   PHE A CE1 1 
ATOM   299  C CE2 . PHE A 1 39  ? -3.022  -27.826 -6.870  1.00 32.85 ? 63   PHE A CE2 1 
ATOM   300  C CZ  . PHE A 1 39  ? -1.792  -27.198 -7.051  1.00 26.12 ? 63   PHE A CZ  1 
ATOM   301  N N   . ASP A 1 40  ? -7.624  -23.747 -3.824  1.00 25.46 ? 64   ASP A N   1 
ATOM   302  C CA  . ASP A 1 40  ? -8.794  -22.874 -3.640  1.00 24.11 ? 64   ASP A CA  1 
ATOM   303  C C   . ASP A 1 40  ? -8.537  -21.368 -3.472  1.00 25.50 ? 64   ASP A C   1 
ATOM   304  O O   . ASP A 1 40  ? -9.268  -20.556 -4.038  1.00 24.55 ? 64   ASP A O   1 
ATOM   305  C CB  . ASP A 1 40  ? -9.677  -23.389 -2.500  1.00 23.34 ? 64   ASP A CB  1 
ATOM   306  C CG  . ASP A 1 40  ? -10.408 -24.694 -2.873  1.00 34.57 ? 64   ASP A CG  1 
ATOM   307  O OD1 . ASP A 1 40  ? -10.332 -25.122 -4.042  1.00 35.88 ? 64   ASP A OD1 1 
ATOM   308  O OD2 . ASP A 1 40  ? -11.087 -25.275 -2.010  1.00 32.81 ? 64   ASP A OD2 1 
ATOM   309  N N   . PRO A 1 41  ? -7.517  -20.977 -2.677  1.00 24.63 ? 65   PRO A N   1 
ATOM   310  C CA  . PRO A 1 41  ? -7.280  -19.543 -2.531  1.00 24.03 ? 65   PRO A CA  1 
ATOM   311  C C   . PRO A 1 41  ? -7.070  -18.870 -3.874  1.00 24.48 ? 65   PRO A C   1 
ATOM   312  O O   . PRO A 1 41  ? -7.506  -17.742 -4.028  1.00 23.50 ? 65   PRO A O   1 
ATOM   313  C CB  . PRO A 1 41  ? -5.991  -19.491 -1.687  1.00 23.62 ? 65   PRO A CB  1 
ATOM   314  C CG  . PRO A 1 41  ? -6.081  -20.717 -0.857  1.00 23.60 ? 65   PRO A CG  1 
ATOM   315  C CD  . PRO A 1 41  ? -6.675  -21.769 -1.758  1.00 27.27 ? 65   PRO A CD  1 
ATOM   316  N N   . ILE A 1 42  ? -6.412  -19.549 -4.817  1.00 22.17 ? 66   ILE A N   1 
ATOM   317  C CA  . ILE A 1 42  ? -6.256  -19.003 -6.165  1.00 18.38 ? 66   ILE A CA  1 
ATOM   318  C C   . ILE A 1 42  ? -7.541  -19.149 -6.996  1.00 21.51 ? 66   ILE A C   1 
ATOM   319  O O   . ILE A 1 42  ? -8.022  -18.172 -7.599  1.00 23.70 ? 66   ILE A O   1 
ATOM   320  C CB  . ILE A 1 42  ? -5.050  -19.639 -6.898  1.00 18.86 ? 66   ILE A CB  1 
ATOM   321  C CG1 . ILE A 1 42  ? -3.760  -19.237 -6.189  1.00 22.04 ? 66   ILE A CG1 1 
ATOM   322  C CG2 . ILE A 1 42  ? -4.992  -19.142 -8.341  1.00 22.28 ? 66   ILE A CG2 1 
ATOM   323  C CD1 . ILE A 1 42  ? -2.522  -20.015 -6.658  1.00 22.11 ? 66   ILE A CD1 1 
ATOM   324  N N   . LEU A 1 43  ? -8.107  -20.354 -7.001  1.00 19.38 ? 67   LEU A N   1 
ATOM   325  C CA  . LEU A 1 43  ? -9.242  -20.639 -7.876  1.00 19.83 ? 67   LEU A CA  1 
ATOM   326  C C   . LEU A 1 43  ? -10.462 -19.769 -7.567  1.00 27.39 ? 67   LEU A C   1 
ATOM   327  O O   . LEU A 1 43  ? -11.269 -19.470 -8.460  1.00 24.98 ? 67   LEU A O   1 
ATOM   328  C CB  . LEU A 1 43  ? -9.630  -22.119 -7.794  1.00 21.96 ? 67   LEU A CB  1 
ATOM   329  C CG  . LEU A 1 43  ? -8.607  -23.124 -8.341  1.00 28.51 ? 67   LEU A CG  1 
ATOM   330  C CD1 . LEU A 1 43  ? -9.038  -24.583 -8.036  1.00 31.70 ? 67   LEU A CD1 1 
ATOM   331  C CD2 . LEU A 1 43  ? -8.399  -22.928 -9.832  1.00 24.20 ? 67   LEU A CD2 1 
ATOM   332  N N   . ARG A 1 44  ? -10.623 -19.414 -6.294  1.00 24.89 ? 68   ARG A N   1 
ATOM   333  C CA  . ARG A 1 44  ? -11.664 -18.450 -5.883  1.00 29.54 ? 68   ARG A CA  1 
ATOM   334  C C   . ARG A 1 44  ? -11.682 -17.170 -6.707  1.00 24.75 ? 68   ARG A C   1 
ATOM   335  O O   . ARG A 1 44  ? -12.739 -16.570 -6.906  1.00 25.55 ? 68   ARG A O   1 
ATOM   336  C CB  . ARG A 1 44  ? -11.426 -18.014 -4.441  1.00 36.45 ? 68   ARG A CB  1 
ATOM   337  C CG  . ARG A 1 44  ? -12.245 -18.774 -3.490  1.00 42.22 ? 68   ARG A CG  1 
ATOM   338  C CD  . ARG A 1 44  ? -11.860 -18.436 -2.083  1.00 43.49 ? 68   ARG A CD  1 
ATOM   339  N NE  . ARG A 1 44  ? -12.145 -19.618 -1.306  1.00 39.29 ? 68   ARG A NE  1 
ATOM   340  C CZ  . ARG A 1 44  ? -11.281 -20.254 -0.529  1.00 42.20 ? 68   ARG A CZ  1 
ATOM   341  N NH1 . ARG A 1 44  ? -10.024 -19.799 -0.345  1.00 31.72 ? 68   ARG A NH1 1 
ATOM   342  N NH2 . ARG A 1 44  ? -11.710 -21.347 0.086   1.00 41.88 ? 68   ARG A NH2 1 
ATOM   343  N N   . TYR A 1 45  ? -10.509 -16.720 -7.133  1.00 22.64 ? 69   TYR A N   1 
ATOM   344  C CA  . TYR A 1 45  ? -10.395 -15.478 -7.900  1.00 22.94 ? 69   TYR A CA  1 
ATOM   345  C C   . TYR A 1 45  ? -10.417 -15.696 -9.429  1.00 24.33 ? 69   TYR A C   1 
ATOM   346  O O   . TYR A 1 45  ? -10.244 -14.753 -10.190 1.00 26.25 ? 69   TYR A O   1 
ATOM   347  C CB  . TYR A 1 45  ? -9.148  -14.670 -7.461  1.00 21.74 ? 69   TYR A CB  1 
ATOM   348  C CG  . TYR A 1 45  ? -9.265  -14.127 -6.038  1.00 23.26 ? 69   TYR A CG  1 
ATOM   349  C CD1 . TYR A 1 45  ? -9.907  -12.902 -5.783  1.00 23.60 ? 69   TYR A CD1 1 
ATOM   350  C CD2 . TYR A 1 45  ? -8.765  -14.850 -4.956  1.00 26.39 ? 69   TYR A CD2 1 
ATOM   351  C CE1 . TYR A 1 45  ? -10.032 -12.422 -4.464  1.00 24.02 ? 69   TYR A CE1 1 
ATOM   352  C CE2 . TYR A 1 45  ? -8.885  -14.396 -3.649  1.00 23.27 ? 69   TYR A CE2 1 
ATOM   353  C CZ  . TYR A 1 45  ? -9.510  -13.167 -3.410  1.00 27.83 ? 69   TYR A CZ  1 
ATOM   354  O OH  . TYR A 1 45  ? -9.634  -12.733 -2.102  1.00 33.78 ? 69   TYR A OH  1 
ATOM   355  N N   . ASN A 1 46  ? -10.599 -16.943 -9.859  1.00 24.69 ? 70   ASN A N   1 
ATOM   356  C CA  . ASN A 1 46  ? -10.552 -17.316 -11.278 1.00 27.51 ? 70   ASN A CA  1 
ATOM   357  C C   . ASN A 1 46  ? -11.666 -18.300 -11.593 1.00 28.32 ? 70   ASN A C   1 
ATOM   358  O O   . ASN A 1 46  ? -11.416 -19.451 -11.976 1.00 26.85 ? 70   ASN A O   1 
ATOM   359  C CB  . ASN A 1 46  ? -9.215  -17.986 -11.615 1.00 23.33 ? 70   ASN A CB  1 
ATOM   360  C CG  . ASN A 1 46  ? -8.043  -17.046 -11.413 1.00 22.16 ? 70   ASN A CG  1 
ATOM   361  O OD1 . ASN A 1 46  ? -7.692  -16.272 -12.313 1.00 26.07 ? 70   ASN A OD1 1 
ATOM   362  N ND2 . ASN A 1 46  ? -7.455  -17.080 -10.220 1.00 19.34 ? 70   ASN A ND2 1 
ATOM   363  N N   . SER A 1 47  ? -12.903 -17.858 -11.438 1.00 31.85 ? 71   SER A N   1 
ATOM   364  C CA  . SER A 1 47  ? -14.018 -18.771 -11.636 1.00 35.41 ? 71   SER A CA  1 
ATOM   365  C C   . SER A 1 47  ? -14.105 -19.237 -13.098 1.00 37.30 ? 71   SER A C   1 
ATOM   366  O O   . SER A 1 47  ? -14.795 -20.206 -13.407 1.00 40.06 ? 71   SER A O   1 
ATOM   367  C CB  . SER A 1 47  ? -15.318 -18.088 -11.211 1.00 35.54 ? 71   SER A CB  1 
ATOM   368  O OG  . SER A 1 47  ? -15.512 -16.923 -11.991 1.00 38.83 ? 71   SER A OG  1 
ATOM   369  N N   . ASN A 1 48  ? -13.420 -18.529 -13.991 1.00 32.66 ? 72   ASN A N   1 
ATOM   370  C CA  . ASN A 1 48  ? -13.332 -18.922 -15.400 1.00 37.36 ? 72   ASN A CA  1 
ATOM   371  C C   . ASN A 1 48  ? -12.545 -20.225 -15.645 1.00 41.65 ? 72   ASN A C   1 
ATOM   372  O O   . ASN A 1 48  ? -12.773 -20.909 -16.635 1.00 47.85 ? 72   ASN A O   1 
ATOM   373  C CB  . ASN A 1 48  ? -12.673 -17.791 -16.202 1.00 40.38 ? 72   ASN A CB  1 
ATOM   374  C CG  . ASN A 1 48  ? -11.278 -17.475 -15.701 1.00 41.71 ? 72   ASN A CG  1 
ATOM   375  O OD1 . ASN A 1 48  ? -11.107 -17.050 -14.556 1.00 42.11 ? 72   ASN A OD1 1 
ATOM   376  N ND2 . ASN A 1 48  ? -10.270 -17.694 -16.547 1.00 41.66 ? 72   ASN A ND2 1 
ATOM   377  N N   . ILE A 1 49  ? -11.590 -20.551 -14.775 1.00 37.00 ? 73   ILE A N   1 
ATOM   378  C CA  . ILE A 1 49  ? -10.811 -21.789 -14.945 1.00 33.11 ? 73   ILE A CA  1 
ATOM   379  C C   . ILE A 1 49  ? -11.679 -23.034 -14.783 1.00 37.71 ? 73   ILE A C   1 
ATOM   380  O O   . ILE A 1 49  ? -12.144 -23.335 -13.685 1.00 37.64 ? 73   ILE A O   1 
ATOM   381  C CB  . ILE A 1 49  ? -9.615  -21.832 -13.961 1.00 28.14 ? 73   ILE A CB  1 
ATOM   382  C CG1 . ILE A 1 49  ? -8.661  -20.654 -14.253 1.00 27.25 ? 73   ILE A CG1 1 
ATOM   383  C CG2 . ILE A 1 49  ? -8.894  -23.178 -14.009 1.00 28.16 ? 73   ILE A CG2 1 
ATOM   384  C CD1 . ILE A 1 49  ? -7.418  -20.596 -13.338 1.00 27.04 ? 73   ILE A CD1 1 
ATOM   385  N N   . LYS A 1 50  ? -11.879 -23.762 -15.881 1.00 38.66 ? 74   LYS A N   1 
ATOM   386  C CA  . LYS A 1 50  ? -12.708 -24.972 -15.883 1.00 46.87 ? 74   LYS A CA  1 
ATOM   387  C C   . LYS A 1 50  ? -11.993 -26.174 -15.269 1.00 40.32 ? 74   LYS A C   1 
ATOM   388  O O   . LYS A 1 50  ? -12.586 -26.974 -14.529 1.00 37.34 ? 74   LYS A O   1 
ATOM   389  C CB  . LYS A 1 50  ? -13.127 -25.321 -17.317 1.00 58.18 ? 74   LYS A CB  1 
ATOM   390  C CG  . LYS A 1 50  ? -13.735 -24.162 -18.111 1.00 67.06 ? 74   LYS A CG  1 
ATOM   391  C CD  . LYS A 1 50  ? -15.010 -23.630 -17.461 1.00 74.68 ? 74   LYS A CD  1 
ATOM   392  C CE  . LYS A 1 50  ? -15.664 -22.533 -18.312 1.00 79.83 ? 74   LYS A CE  1 
ATOM   393  N NZ  . LYS A 1 50  ? -14.830 -21.293 -18.425 1.00 77.02 ? 74   LYS A NZ  1 
ATOM   394  N N   . ASP A 1 51  ? -10.708 -26.308 -15.581 1.00 35.76 ? 75   ASP A N   1 
ATOM   395  C CA  . ASP A 1 51  ? -9.952  -27.462 -15.123 1.00 33.83 ? 75   ASP A CA  1 
ATOM   396  C C   . ASP A 1 51  ? -8.602  -26.998 -14.576 1.00 30.12 ? 75   ASP A C   1 
ATOM   397  O O   . ASP A 1 51  ? -7.737  -26.557 -15.330 1.00 28.65 ? 75   ASP A O   1 
ATOM   398  C CB  . ASP A 1 51  ? -9.766  -28.448 -16.280 1.00 37.93 ? 75   ASP A CB  1 
ATOM   399  C CG  . ASP A 1 51  ? -9.068  -29.721 -15.855 1.00 36.69 ? 75   ASP A CG  1 
ATOM   400  O OD1 . ASP A 1 51  ? -8.578  -29.780 -14.703 1.00 34.00 ? 75   ASP A OD1 1 
ATOM   401  O OD2 . ASP A 1 51  ? -8.984  -30.661 -16.681 1.00 41.25 ? 75   ASP A OD2 1 
ATOM   402  N N   . LYS A 1 52  ? -8.434  -27.084 -13.259 1.00 28.43 ? 76   LYS A N   1 
ATOM   403  C CA  . LYS A 1 52  ? -7.228  -26.568 -12.617 1.00 30.62 ? 76   LYS A CA  1 
ATOM   404  C C   . LYS A 1 52  ? -5.981  -27.337 -13.070 1.00 28.06 ? 76   LYS A C   1 
ATOM   405  O O   . LYS A 1 52  ? -4.846  -26.836 -12.983 1.00 28.07 ? 76   LYS A O   1 
ATOM   406  C CB  . LYS A 1 52  ? -7.362  -26.688 -11.101 1.00 32.55 ? 76   LYS A CB  1 
ATOM   407  C CG  . LYS A 1 52  ? -7.408  -28.134 -10.601 1.00 32.66 ? 76   LYS A CG  1 
ATOM   408  C CD  . LYS A 1 52  ? -6.769  -28.214 -9.235  1.00 41.63 ? 76   LYS A CD  1 
ATOM   409  C CE  . LYS A 1 52  ? -7.683  -28.869 -8.232  1.00 45.12 ? 76   LYS A CE  1 
ATOM   410  N NZ  . LYS A 1 52  ? -8.077  -30.245 -8.655  1.00 39.47 ? 76   LYS A NZ  1 
ATOM   411  N N   . ASP A 1 53  ? -6.189  -28.560 -13.526 1.00 24.57 ? 77   ASP A N   1 
ATOM   412  C CA  . ASP A 1 53  ? -5.068  -29.433 -13.914 1.00 28.87 ? 77   ASP A CA  1 
ATOM   413  C C   . ASP A 1 53  ? -4.689  -29.346 -15.402 1.00 29.60 ? 77   ASP A C   1 
ATOM   414  O O   . ASP A 1 53  ? -3.712  -29.961 -15.840 1.00 31.00 ? 77   ASP A O   1 
ATOM   415  C CB  . ASP A 1 53  ? -5.359  -30.872 -13.502 1.00 30.76 ? 77   ASP A CB  1 
ATOM   416  C CG  . ASP A 1 53  ? -5.306  -31.066 -11.987 1.00 36.97 ? 77   ASP A CG  1 
ATOM   417  O OD1 . ASP A 1 53  ? -4.400  -30.509 -11.315 1.00 34.32 ? 77   ASP A OD1 1 
ATOM   418  O OD2 . ASP A 1 53  ? -6.183  -31.771 -11.465 1.00 42.85 ? 77   ASP A OD2 1 
ATOM   419  N N   . ARG A 1 54  ? -5.472  -28.583 -16.157 1.00 24.74 ? 78   ARG A N   1 
ATOM   420  C CA  . ARG A 1 54  ? -5.193  -28.251 -17.558 1.00 27.37 ? 78   ARG A CA  1 
ATOM   421  C C   . ARG A 1 54  ? -5.591  -26.816 -17.881 1.00 31.61 ? 78   ARG A C   1 
ATOM   422  O O   . ARG A 1 54  ? -6.673  -26.565 -18.434 1.00 33.71 ? 78   ARG A O   1 
ATOM   423  C CB  . ARG A 1 54  ? -5.929  -29.206 -18.493 1.00 28.25 ? 78   ARG A CB  1 
ATOM   424  C CG  . ARG A 1 54  ? -5.445  -30.615 -18.304 1.00 31.40 ? 78   ARG A CG  1 
ATOM   425  C CD  . ARG A 1 54  ? -6.019  -31.620 -19.299 1.00 36.69 ? 78   ARG A CD  1 
ATOM   426  N NE  . ARG A 1 54  ? -5.382  -32.903 -19.057 1.00 38.43 ? 78   ARG A NE  1 
ATOM   427  C CZ  . ARG A 1 54  ? -4.543  -33.501 -19.896 1.00 40.08 ? 78   ARG A CZ  1 
ATOM   428  N NH1 . ARG A 1 54  ? -4.288  -32.957 -21.084 1.00 42.05 ? 78   ARG A NH1 1 
ATOM   429  N NH2 . ARG A 1 54  ? -3.995  -34.664 -19.554 1.00 43.87 ? 78   ARG A NH2 1 
ATOM   430  N N   . ILE A 1 55  ? -4.713  -25.876 -17.549 1.00 25.00 ? 79   ILE A N   1 
ATOM   431  C CA  . ILE A 1 55  ? -5.015  -24.458 -17.737 1.00 24.51 ? 79   ILE A CA  1 
ATOM   432  C C   . ILE A 1 55  ? -4.636  -23.951 -19.140 1.00 30.33 ? 79   ILE A C   1 
ATOM   433  O O   . ILE A 1 55  ? -3.801  -24.541 -19.820 1.00 30.92 ? 79   ILE A O   1 
ATOM   434  C CB  . ILE A 1 55  ? -4.441  -23.577 -16.616 1.00 29.15 ? 79   ILE A CB  1 
ATOM   435  C CG1 . ILE A 1 55  ? -2.909  -23.626 -16.581 1.00 24.65 ? 79   ILE A CG1 1 
ATOM   436  C CG2 . ILE A 1 55  ? -5.044  -23.995 -15.252 1.00 26.12 ? 79   ILE A CG2 1 
ATOM   437  C CD1 . ILE A 1 55  ? -2.349  -22.673 -15.539 1.00 24.07 ? 79   ILE A CD1 1 
ATOM   438  N N   . GLN A 1 56  ? -5.279  -22.878 -19.591 1.00 29.60 ? 80   GLN A N   1 
ATOM   439  C CA  . GLN A 1 56  ? -5.210  -22.508 -21.011 1.00 33.00 ? 80   GLN A CA  1 
ATOM   440  C C   . GLN A 1 56  ? -4.198  -21.393 -21.328 1.00 30.76 ? 80   GLN A C   1 
ATOM   441  O O   . GLN A 1 56  ? -4.304  -20.283 -20.806 1.00 28.96 ? 80   GLN A O   1 
ATOM   442  C CB  . GLN A 1 56  ? -6.603  -22.105 -21.503 1.00 43.92 ? 80   GLN A CB  1 
ATOM   443  C CG  . GLN A 1 56  ? -6.829  -22.302 -22.997 1.00 58.22 ? 80   GLN A CG  1 
ATOM   444  C CD  . GLN A 1 56  ? -7.179  -23.750 -23.361 1.00 68.12 ? 80   GLN A CD  1 
ATOM   445  O OE1 . GLN A 1 56  ? -7.132  -24.651 -22.520 1.00 69.66 ? 80   GLN A OE1 1 
ATOM   446  N NE2 . GLN A 1 56  ? -7.534  -23.970 -24.622 1.00 71.65 ? 80   GLN A NE2 1 
ATOM   447  N N   . MET A 1 57  ? -3.236  -21.682 -22.207 1.00 29.00 ? 81   MET A N   1 
ATOM   448  C CA  . MET A 1 57  ? -2.246  -20.676 -22.605 1.00 27.69 ? 81   MET A CA  1 
ATOM   449  C C   . MET A 1 57  ? -2.936  -19.477 -23.228 1.00 28.35 ? 81   MET A C   1 
ATOM   450  O O   . MET A 1 57  ? -3.949  -19.619 -23.925 1.00 30.53 ? 81   MET A O   1 
ATOM   451  C CB  . MET A 1 57  ? -1.242  -21.250 -23.611 1.00 28.96 ? 81   MET A CB  1 
ATOM   452  C CG  . MET A 1 57  ? -0.387  -22.409 -23.071 1.00 28.37 ? 81   MET A CG  1 
ATOM   453  S SD  . MET A 1 57  ? 0.557   -22.025 -21.569 1.00 29.98 ? 81   MET A SD  1 
ATOM   454  C CE  . MET A 1 57  ? -0.512  -22.661 -20.256 1.00 25.60 ? 81   MET A CE  1 
ATOM   455  N N   . GLY A 1 58  ? -2.384  -18.296 -22.979 1.00 26.40 ? 82   GLY A N   1 
ATOM   456  C CA  . GLY A 1 58  ? -2.919  -17.080 -23.552 1.00 32.91 ? 82   GLY A CA  1 
ATOM   457  C C   . GLY A 1 58  ? -3.902  -16.371 -22.641 1.00 32.81 ? 82   GLY A C   1 
ATOM   458  O O   . GLY A 1 58  ? -4.405  -15.317 -22.996 1.00 32.74 ? 82   GLY A O   1 
ATOM   459  N N   . SER A 1 59  ? -4.199  -16.955 -21.483 1.00 28.58 ? 83   SER A N   1 
ATOM   460  C CA  . SER A 1 59  ? -5.074  -16.300 -20.510 1.00 29.56 ? 83   SER A CA  1 
ATOM   461  C C   . SER A 1 59  ? -4.253  -15.799 -19.320 1.00 26.83 ? 83   SER A C   1 
ATOM   462  O O   . SER A 1 59  ? -3.055  -16.084 -19.221 1.00 24.85 ? 83   SER A O   1 
ATOM   463  C CB  . SER A 1 59  ? -6.152  -17.278 -20.024 1.00 32.72 ? 83   SER A CB  1 
ATOM   464  O OG  . SER A 1 59  ? -5.548  -18.375 -19.344 1.00 30.88 ? 83   SER A OG  1 
ATOM   465  N N   . ARG A 1 60  ? -4.887  -15.040 -18.428 1.00 23.00 ? 84   ARG A N   1 
ATOM   466  C CA  . ARG A 1 60  ? -4.201  -14.547 -17.233 1.00 22.02 ? 84   ARG A CA  1 
ATOM   467  C C   . ARG A 1 60  ? -4.832  -15.153 -16.000 1.00 22.12 ? 84   ARG A C   1 
ATOM   468  O O   . ARG A 1 60  ? -6.060  -15.251 -15.905 1.00 23.91 ? 84   ARG A O   1 
ATOM   469  C CB  . ARG A 1 60  ? -4.298  -13.015 -17.149 1.00 24.44 ? 84   ARG A CB  1 
ATOM   470  C CG  . ARG A 1 60  ? -3.435  -12.291 -18.199 1.00 24.90 ? 84   ARG A CG  1 
ATOM   471  C CD  . ARG A 1 60  ? -3.851  -10.837 -18.311 1.00 25.66 ? 84   ARG A CD  1 
ATOM   472  N NE  . ARG A 1 60  ? -3.027  -10.072 -19.244 1.00 25.29 ? 84   ARG A NE  1 
ATOM   473  C CZ  . ARG A 1 60  ? -2.009  -9.313  -18.869 1.00 26.14 ? 84   ARG A CZ  1 
ATOM   474  N NH1 . ARG A 1 60  ? -1.665  -9.272  -17.579 1.00 21.81 ? 84   ARG A NH1 1 
ATOM   475  N NH2 . ARG A 1 60  ? -1.337  -8.602  -19.777 1.00 22.49 ? 84   ARG A NH2 1 
ATOM   476  N N   . VAL A 1 61  ? -3.990  -15.547 -15.053 1.00 21.11 ? 85   VAL A N   1 
ATOM   477  C CA  . VAL A 1 61  ? -4.443  -16.148 -13.797 1.00 23.17 ? 85   VAL A CA  1 
ATOM   478  C C   . VAL A 1 61  ? -4.242  -15.115 -12.689 1.00 23.09 ? 85   VAL A C   1 
ATOM   479  O O   . VAL A 1 61  ? -3.145  -14.561 -12.559 1.00 21.30 ? 85   VAL A O   1 
ATOM   480  C CB  . VAL A 1 61  ? -3.636  -17.421 -13.466 1.00 23.03 ? 85   VAL A CB  1 
ATOM   481  C CG1 . VAL A 1 61  ? -4.034  -17.980 -12.049 1.00 21.87 ? 85   VAL A CG1 1 
ATOM   482  C CG2 . VAL A 1 61  ? -3.838  -18.506 -14.560 1.00 21.30 ? 85   VAL A CG2 1 
ATOM   483  N N   . LEU A 1 62  ? -5.292  -14.842 -11.913 1.00 18.12 ? 86   LEU A N   1 
ATOM   484  C CA  . LEU A 1 62  ? -5.206  -13.865 -10.815 1.00 20.20 ? 86   LEU A CA  1 
ATOM   485  C C   . LEU A 1 62  ? -4.783  -14.558 -9.518  1.00 19.77 ? 86   LEU A C   1 
ATOM   486  O O   . LEU A 1 62  ? -5.372  -15.563 -9.145  1.00 21.42 ? 86   LEU A O   1 
ATOM   487  C CB  . LEU A 1 62  ? -6.557  -13.164 -10.604 1.00 20.76 ? 86   LEU A CB  1 
ATOM   488  C CG  . LEU A 1 62  ? -6.989  -12.230 -11.723 1.00 21.61 ? 86   LEU A CG  1 
ATOM   489  C CD1 . LEU A 1 62  ? -8.472  -11.789 -11.566 1.00 26.87 ? 86   LEU A CD1 1 
ATOM   490  C CD2 . LEU A 1 62  ? -6.064  -10.997 -11.775 1.00 24.13 ? 86   LEU A CD2 1 
ATOM   491  N N   . VAL A 1 63  ? -3.749  -14.038 -8.847  1.00 19.40 ? 87   VAL A N   1 
ATOM   492  C CA  . VAL A 1 63  ? -3.231  -14.703 -7.639  1.00 20.19 ? 87   VAL A CA  1 
ATOM   493  C C   . VAL A 1 63  ? -3.257  -13.733 -6.452  1.00 18.96 ? 87   VAL A C   1 
ATOM   494  O O   . VAL A 1 63  ? -2.607  -12.703 -6.509  1.00 17.99 ? 87   VAL A O   1 
ATOM   495  C CB  . VAL A 1 63  ? -1.765  -15.184 -7.854  1.00 22.74 ? 87   VAL A CB  1 
ATOM   496  C CG1 . VAL A 1 63  ? -1.265  -16.003 -6.636  1.00 21.05 ? 87   VAL A CG1 1 
ATOM   497  C CG2 . VAL A 1 63  ? -1.649  -15.986 -9.154  1.00 23.20 ? 87   VAL A CG2 1 
ATOM   498  N N   . PRO A 1 64  ? -3.973  -14.081 -5.364  1.00 20.20 ? 88   PRO A N   1 
ATOM   499  C CA  . PRO A 1 64  ? -3.982  -13.186 -4.199  1.00 18.82 ? 88   PRO A CA  1 
ATOM   500  C C   . PRO A 1 64  ? -2.626  -13.221 -3.482  1.00 20.12 ? 88   PRO A C   1 
ATOM   501  O O   . PRO A 1 64  ? -2.010  -14.276 -3.385  1.00 21.58 ? 88   PRO A O   1 
ATOM   502  C CB  . PRO A 1 64  ? -5.054  -13.789 -3.281  1.00 17.56 ? 88   PRO A CB  1 
ATOM   503  C CG  . PRO A 1 64  ? -5.034  -15.282 -3.612  1.00 19.78 ? 88   PRO A CG  1 
ATOM   504  C CD  . PRO A 1 64  ? -4.710  -15.338 -5.123  1.00 19.14 ? 88   PRO A CD  1 
ATOM   505  N N   . PHE A 1 65  ? -2.225  -12.090 -2.932  1.00 20.11 ? 89   PHE A N   1 
ATOM   506  C CA  . PHE A 1 65  ? -0.975  -12.027 -2.178  1.00 20.62 ? 89   PHE A CA  1 
ATOM   507  C C   . PHE A 1 65  ? -1.029  -10.873 -1.189  1.00 19.61 ? 89   PHE A C   1 
ATOM   508  O O   . PHE A 1 65  ? -1.855  -9.942  -1.329  1.00 19.74 ? 89   PHE A O   1 
ATOM   509  C CB  . PHE A 1 65  ? 0.252   -11.966 -3.117  1.00 17.55 ? 89   PHE A CB  1 
ATOM   510  C CG  . PHE A 1 65  ? 0.439   -10.634 -3.855  1.00 18.63 ? 89   PHE A CG  1 
ATOM   511  C CD1 . PHE A 1 65  ? 1.363   -9.694  -3.399  1.00 19.68 ? 89   PHE A CD1 1 
ATOM   512  C CD2 . PHE A 1 65  ? -0.255  -10.359 -5.029  1.00 18.68 ? 89   PHE A CD2 1 
ATOM   513  C CE1 . PHE A 1 65  ? 1.586   -8.512  -4.087  1.00 23.15 ? 89   PHE A CE1 1 
ATOM   514  C CE2 . PHE A 1 65  ? -0.025  -9.149  -5.735  1.00 18.21 ? 89   PHE A CE2 1 
ATOM   515  C CZ  . PHE A 1 65  ? 0.881   -8.235  -5.260  1.00 19.55 ? 89   PHE A CZ  1 
ATOM   516  N N   . PRO A 1 66  ? -0.181  -10.929 -0.149  1.00 21.49 ? 90   PRO A N   1 
ATOM   517  C CA  . PRO A 1 66  ? -0.204  -9.871  0.874   1.00 23.45 ? 90   PRO A CA  1 
ATOM   518  C C   . PRO A 1 66  ? 0.360   -8.570  0.325   1.00 23.74 ? 90   PRO A C   1 
ATOM   519  O O   . PRO A 1 66  ? 1.263   -8.601  -0.493  1.00 23.88 ? 90   PRO A O   1 
ATOM   520  C CB  . PRO A 1 66  ? 0.723   -10.427 1.980   1.00 26.48 ? 90   PRO A CB  1 
ATOM   521  C CG  . PRO A 1 66  ? 0.851   -11.949 1.681   1.00 20.28 ? 90   PRO A CG  1 
ATOM   522  C CD  . PRO A 1 66  ? 0.799   -11.984 0.166   1.00 20.95 ? 90   PRO A CD  1 
ATOM   523  N N   . CYS A 1 67  ? -0.178  -7.436  0.757   1.00 22.21 ? 91   CYS A N   1 
ATOM   524  C CA  . CYS A 1 67  ? 0.289   -6.158  0.247   1.00 21.61 ? 91   CYS A CA  1 
ATOM   525  C C   . CYS A 1 67  ? 0.748   -5.329  1.454   1.00 24.98 ? 91   CYS A C   1 
ATOM   526  O O   . CYS A 1 67  ? -0.074  -4.882  2.236   1.00 27.96 ? 91   CYS A O   1 
ATOM   527  C CB  . CYS A 1 67  ? -0.861  -5.481  -0.525  1.00 25.83 ? 91   CYS A CB  1 
ATOM   528  S SG  . CYS A 1 67  ? -0.441  -3.876  -1.342  1.00 29.84 ? 91   CYS A SG  1 
ATOM   529  N N   . GLU A 1 68  ? 2.065   -5.141  1.591   1.00 24.36 ? 92   GLU A N   1 
ATOM   530  C CA  . GLU A 1 68  ? 2.674   -4.676  2.841   1.00 25.62 ? 92   GLU A CA  1 
ATOM   531  C C   . GLU A 1 68  ? 3.512   -3.431  2.605   1.00 26.44 ? 92   GLU A C   1 
ATOM   532  O O   . GLU A 1 68  ? 4.071   -3.244  1.518   1.00 25.02 ? 92   GLU A O   1 
ATOM   533  C CB  . GLU A 1 68  ? 3.591   -5.791  3.402   1.00 26.70 ? 92   GLU A CB  1 
ATOM   534  C CG  . GLU A 1 68  ? 2.793   -7.060  3.786   1.00 36.03 ? 92   GLU A CG  1 
ATOM   535  C CD  . GLU A 1 68  ? 3.562   -8.349  3.613   1.00 41.50 ? 92   GLU A CD  1 
ATOM   536  O OE1 . GLU A 1 68  ? 4.404   -8.441  2.691   1.00 37.54 ? 92   GLU A OE1 1 
ATOM   537  O OE2 . GLU A 1 68  ? 3.307   -9.292  4.390   1.00 50.43 ? 92   GLU A OE2 1 
ATOM   538  N N   . CYS A 1 69  ? 3.615   -2.584  3.625   1.00 25.04 ? 93   CYS A N   1 
ATOM   539  C CA  . CYS A 1 69  ? 4.490   -1.415  3.519   1.00 28.02 ? 93   CYS A CA  1 
ATOM   540  C C   . CYS A 1 69  ? 5.954   -1.894  3.519   1.00 32.57 ? 93   CYS A C   1 
ATOM   541  O O   . CYS A 1 69  ? 6.345   -2.695  4.361   1.00 34.69 ? 93   CYS A O   1 
ATOM   542  C CB  . CYS A 1 69  ? 4.213   -0.433  4.654   1.00 34.78 ? 93   CYS A CB  1 
ATOM   543  S SG  . CYS A 1 69  ? 4.908   1.215   4.324   1.00 46.96 ? 93   CYS A SG  1 
ATOM   544  N N   . GLN A 1 70  ? 6.743   -1.403  2.561   1.00 32.53 ? 94   GLN A N   1 
ATOM   545  C CA  . GLN A 1 70  ? 8.131   -1.814  2.388   1.00 27.70 ? 94   GLN A CA  1 
ATOM   546  C C   . GLN A 1 70  ? 9.013   -0.664  2.830   1.00 29.73 ? 94   GLN A C   1 
ATOM   547  O O   . GLN A 1 70  ? 8.583   0.487   2.766   1.00 29.03 ? 94   GLN A O   1 
ATOM   548  C CB  . GLN A 1 70  ? 8.402   -2.104  0.909   1.00 26.30 ? 94   GLN A CB  1 
ATOM   549  C CG  . GLN A 1 70  ? 7.547   -3.275  0.362   1.00 24.63 ? 94   GLN A CG  1 
ATOM   550  C CD  . GLN A 1 70  ? 7.949   -4.604  0.971   1.00 26.64 ? 94   GLN A CD  1 
ATOM   551  O OE1 . GLN A 1 70  ? 9.107   -4.809  1.352   1.00 25.50 ? 94   GLN A OE1 1 
ATOM   552  N NE2 . GLN A 1 70  ? 6.991   -5.519  1.076   1.00 25.00 ? 94   GLN A NE2 1 
ATOM   553  N N   . PRO A 1 71  ? 10.253  -0.967  3.251   1.00 30.83 ? 95   PRO A N   1 
ATOM   554  C CA  . PRO A 1 71  ? 11.190  0.132   3.544   1.00 29.98 ? 95   PRO A CA  1 
ATOM   555  C C   . PRO A 1 71  ? 11.280  1.025   2.315   1.00 32.62 ? 95   PRO A C   1 
ATOM   556  O O   . PRO A 1 71  ? 11.433  0.522   1.207   1.00 31.40 ? 95   PRO A O   1 
ATOM   557  C CB  . PRO A 1 71  ? 12.519  -0.586  3.775   1.00 34.42 ? 95   PRO A CB  1 
ATOM   558  C CG  . PRO A 1 71  ? 12.125  -1.983  4.216   1.00 35.40 ? 95   PRO A CG  1 
ATOM   559  C CD  . PRO A 1 71  ? 10.854  -2.301  3.452   1.00 33.02 ? 95   PRO A CD  1 
ATOM   560  N N   . GLY A 1 72  ? 11.172  2.342   2.486   1.00 37.46 ? 96   GLY A N   1 
ATOM   561  C CA  . GLY A 1 72  ? 11.109  3.199   1.324   1.00 35.05 ? 96   GLY A CA  1 
ATOM   562  C C   . GLY A 1 72  ? 9.705   3.739   1.158   1.00 39.21 ? 96   GLY A C   1 
ATOM   563  O O   . GLY A 1 72  ? 9.425   4.532   0.257   1.00 40.46 ? 96   GLY A O   1 
ATOM   564  N N   . ASP A 1 73  ? 8.818   3.290   2.038   1.00 35.08 ? 97   ASP A N   1 
ATOM   565  C CA  . ASP A 1 73  ? 7.425   3.736   2.050   1.00 36.36 ? 97   ASP A CA  1 
ATOM   566  C C   . ASP A 1 73  ? 6.663   3.530   0.734   1.00 36.41 ? 97   ASP A C   1 
ATOM   567  O O   . ASP A 1 73  ? 6.072   4.457   0.187   1.00 35.78 ? 97   ASP A O   1 
ATOM   568  C CB  . ASP A 1 73  ? 7.340   5.196   2.522   1.00 50.59 ? 97   ASP A CB  1 
ATOM   569  C CG  . ASP A 1 73  ? 7.814   5.363   3.954   1.00 59.66 ? 97   ASP A CG  1 
ATOM   570  O OD1 . ASP A 1 73  ? 8.198   6.488   4.331   1.00 66.46 ? 97   ASP A OD1 1 
ATOM   571  O OD2 . ASP A 1 73  ? 7.808   4.359   4.702   1.00 61.17 ? 97   ASP A OD2 1 
ATOM   572  N N   . PHE A 1 74  ? 6.666   2.304   0.227   1.00 27.51 ? 98   PHE A N   1 
ATOM   573  C CA  . PHE A 1 74  ? 5.837   1.987   -0.922  1.00 31.15 ? 98   PHE A CA  1 
ATOM   574  C C   . PHE A 1 74  ? 5.250   0.616   -0.638  1.00 29.77 ? 98   PHE A C   1 
ATOM   575  O O   . PHE A 1 74  ? 5.730   -0.083  0.258   1.00 27.24 ? 98   PHE A O   1 
ATOM   576  C CB  . PHE A 1 74  ? 6.633   1.987   -2.239  1.00 30.48 ? 98   PHE A CB  1 
ATOM   577  C CG  . PHE A 1 74  ? 7.736   0.943   -2.304  1.00 32.83 ? 98   PHE A CG  1 
ATOM   578  C CD1 . PHE A 1 74  ? 7.466   -0.371  -2.718  1.00 27.59 ? 98   PHE A CD1 1 
ATOM   579  C CD2 . PHE A 1 74  ? 9.037   1.281   -1.961  1.00 33.11 ? 98   PHE A CD2 1 
ATOM   580  C CE1 . PHE A 1 74  ? 8.475   -1.311  -2.771  1.00 27.20 ? 98   PHE A CE1 1 
ATOM   581  C CE2 . PHE A 1 74  ? 10.048  0.358   -2.016  1.00 30.30 ? 98   PHE A CE2 1 
ATOM   582  C CZ  . PHE A 1 74  ? 9.779   -0.946  -2.421  1.00 27.72 ? 98   PHE A CZ  1 
ATOM   583  N N   . LEU A 1 75  ? 4.214   0.242   -1.382  1.00 24.68 ? 99   LEU A N   1 
ATOM   584  C CA  . LEU A 1 75  ? 3.551   -1.047  -1.135  1.00 22.52 ? 99   LEU A CA  1 
ATOM   585  C C   . LEU A 1 75  ? 4.023   -2.159  -2.020  1.00 18.90 ? 99   LEU A C   1 
ATOM   586  O O   . LEU A 1 75  ? 4.162   -1.982  -3.246  1.00 21.01 ? 99   LEU A O   1 
ATOM   587  C CB  . LEU A 1 75  ? 2.045   -0.888  -1.347  1.00 24.05 ? 99   LEU A CB  1 
ATOM   588  C CG  . LEU A 1 75  ? 1.370   0.076   -0.373  1.00 25.05 ? 99   LEU A CG  1 
ATOM   589  C CD1 . LEU A 1 75  ? -0.046  0.327   -0.876  1.00 25.17 ? 99   LEU A CD1 1 
ATOM   590  C CD2 . LEU A 1 75  ? 1.356   -0.478  1.057   1.00 26.72 ? 99   LEU A CD2 1 
ATOM   591  N N   . GLY A 1 76  ? 4.224   -3.335  -1.421  1.00 21.10 ? 100  GLY A N   1 
ATOM   592  C CA  . GLY A 1 76  ? 4.618   -4.497  -2.208  1.00 19.89 ? 100  GLY A CA  1 
ATOM   593  C C   . GLY A 1 76  ? 4.724   -5.738  -1.364  1.00 22.27 ? 100  GLY A C   1 
ATOM   594  O O   . GLY A 1 76  ? 4.320   -5.743  -0.198  1.00 21.06 ? 100  GLY A O   1 
ATOM   595  N N   . HIS A 1 77  ? 5.265   -6.803  -1.953  1.00 17.95 ? 101  HIS A N   1 
ATOM   596  C CA  . HIS A 1 77  ? 5.458   -8.031  -1.215  1.00 18.60 ? 101  HIS A CA  1 
ATOM   597  C C   . HIS A 1 77  ? 6.732   -8.745  -1.652  1.00 19.27 ? 101  HIS A C   1 
ATOM   598  O O   . HIS A 1 77  ? 7.041   -8.791  -2.839  1.00 18.04 ? 101  HIS A O   1 
ATOM   599  C CB  . HIS A 1 77  ? 4.278   -8.967  -1.446  1.00 16.69 ? 101  HIS A CB  1 
ATOM   600  C CG  . HIS A 1 77  ? 4.402   -10.275 -0.730  1.00 19.43 ? 101  HIS A CG  1 
ATOM   601  N ND1 . HIS A 1 77  ? 4.324   -10.375 0.645   1.00 21.03 ? 101  HIS A ND1 1 
ATOM   602  C CD2 . HIS A 1 77  ? 4.580   -11.536 -1.194  1.00 20.27 ? 101  HIS A CD2 1 
ATOM   603  C CE1 . HIS A 1 77  ? 4.473   -11.641 0.998   1.00 22.13 ? 101  HIS A CE1 1 
ATOM   604  N NE2 . HIS A 1 77  ? 4.613   -12.369 -0.101  1.00 21.19 ? 101  HIS A NE2 1 
ATOM   605  N N   . ASN A 1 78  ? 7.451   -9.307  -0.684  1.00 18.39 ? 102  ASN A N   1 
ATOM   606  C CA  . ASN A 1 78  ? 8.620   -10.148 -0.982  1.00 16.44 ? 102  ASN A CA  1 
ATOM   607  C C   . ASN A 1 78  ? 8.188   -11.638 -1.103  1.00 22.59 ? 102  ASN A C   1 
ATOM   608  O O   . ASN A 1 78  ? 7.890   -12.272 -0.087  1.00 20.26 ? 102  ASN A O   1 
ATOM   609  C CB  . ASN A 1 78  ? 9.625   -10.076 0.172   1.00 18.77 ? 102  ASN A CB  1 
ATOM   610  C CG  . ASN A 1 78  ? 10.213  -8.696  0.379   1.00 20.96 ? 102  ASN A CG  1 
ATOM   611  O OD1 . ASN A 1 78  ? 10.293  -7.881  -0.547  1.00 20.82 ? 102  ASN A OD1 1 
ATOM   612  N ND2 . ASN A 1 78  ? 10.649  -8.433  1.637   1.00 23.61 ? 102  ASN A ND2 1 
ATOM   613  N N   . PHE A 1 79  ? 8.148   -12.177 -2.325  1.00 17.70 ? 103  PHE A N   1 
ATOM   614  C CA  . PHE A 1 79  ? 8.056   -13.612 -2.539  1.00 16.46 ? 103  PHE A CA  1 
ATOM   615  C C   . PHE A 1 79  ? 9.436   -14.224 -2.375  1.00 17.66 ? 103  PHE A C   1 
ATOM   616  O O   . PHE A 1 79  ? 10.439  -13.511 -2.318  1.00 21.58 ? 103  PHE A O   1 
ATOM   617  C CB  . PHE A 1 79  ? 7.516   -13.911 -3.944  1.00 14.93 ? 103  PHE A CB  1 
ATOM   618  C CG  . PHE A 1 79  ? 6.079   -13.469 -4.135  1.00 16.45 ? 103  PHE A CG  1 
ATOM   619  C CD1 . PHE A 1 79  ? 5.026   -14.221 -3.593  1.00 18.31 ? 103  PHE A CD1 1 
ATOM   620  C CD2 . PHE A 1 79  ? 5.789   -12.312 -4.865  1.00 18.04 ? 103  PHE A CD2 1 
ATOM   621  C CE1 . PHE A 1 79  ? 3.678   -13.820 -3.764  1.00 17.31 ? 103  PHE A CE1 1 
ATOM   622  C CE2 . PHE A 1 79  ? 4.454   -11.882 -5.033  1.00 20.27 ? 103  PHE A CE2 1 
ATOM   623  C CZ  . PHE A 1 79  ? 3.394   -12.648 -4.488  1.00 20.17 ? 103  PHE A CZ  1 
ATOM   624  N N   . SER A 1 80  ? 9.464   -15.554 -2.259  1.00 17.07 ? 104  SER A N   1 
ATOM   625  C CA  . SER A 1 80  ? 10.732  -16.281 -2.206  1.00 19.65 ? 104  SER A CA  1 
ATOM   626  C C   . SER A 1 80  ? 10.739  -17.284 -3.337  1.00 24.73 ? 104  SER A C   1 
ATOM   627  O O   . SER A 1 80  ? 9.735   -17.947 -3.578  1.00 28.25 ? 104  SER A O   1 
ATOM   628  C CB  . SER A 1 80  ? 10.846  -17.025 -0.885  1.00 24.05 ? 104  SER A CB  1 
ATOM   629  O OG  . SER A 1 80  ? 10.885  -16.092 0.169   1.00 28.78 ? 104  SER A OG  1 
ATOM   630  N N   . TYR A 1 81  ? 11.863  -17.395 -4.035  1.00 19.36 ? 105  TYR A N   1 
ATOM   631  C CA  . TYR A 1 81  ? 11.968  -18.283 -5.188  1.00 20.19 ? 105  TYR A CA  1 
ATOM   632  C C   . TYR A 1 81  ? 13.185  -19.193 -5.047  1.00 21.33 ? 105  TYR A C   1 
ATOM   633  O O   . TYR A 1 81  ? 14.275  -18.711 -4.852  1.00 20.56 ? 105  TYR A O   1 
ATOM   634  C CB  . TYR A 1 81  ? 12.042  -17.464 -6.493  1.00 19.64 ? 105  TYR A CB  1 
ATOM   635  C CG  . TYR A 1 81  ? 12.270  -18.338 -7.698  1.00 21.69 ? 105  TYR A CG  1 
ATOM   636  C CD1 . TYR A 1 81  ? 11.245  -19.128 -8.199  1.00 21.77 ? 105  TYR A CD1 1 
ATOM   637  C CD2 . TYR A 1 81  ? 13.524  -18.420 -8.305  1.00 24.86 ? 105  TYR A CD2 1 
ATOM   638  C CE1 . TYR A 1 81  ? 11.452  -19.967 -9.282  1.00 23.58 ? 105  TYR A CE1 1 
ATOM   639  C CE2 . TYR A 1 81  ? 13.752  -19.257 -9.385  1.00 22.77 ? 105  TYR A CE2 1 
ATOM   640  C CZ  . TYR A 1 81  ? 12.702  -20.033 -9.872  1.00 25.69 ? 105  TYR A CZ  1 
ATOM   641  O OH  . TYR A 1 81  ? 12.916  -20.876 -10.944 1.00 28.06 ? 105  TYR A OH  1 
ATOM   642  N N   . SER A 1 82  ? 12.985  -20.518 -5.135  1.00 23.47 ? 106  SER A N   1 
ATOM   643  C CA  . SER A 1 82  ? 14.085  -21.475 -5.134  1.00 21.61 ? 106  SER A CA  1 
ATOM   644  C C   . SER A 1 82  ? 14.641  -21.661 -6.544  1.00 22.57 ? 106  SER A C   1 
ATOM   645  O O   . SER A 1 82  ? 13.925  -22.046 -7.472  1.00 22.20 ? 106  SER A O   1 
ATOM   646  C CB  . SER A 1 82  ? 13.588  -22.824 -4.595  1.00 31.78 ? 106  SER A CB  1 
ATOM   647  O OG  . SER A 1 82  ? 13.116  -22.673 -3.268  1.00 35.11 ? 106  SER A OG  1 
ATOM   648  N N   . VAL A 1 83  ? 15.920  -21.359 -6.704  1.00 24.18 ? 107  VAL A N   1 
ATOM   649  C CA  . VAL A 1 83  ? 16.574  -21.357 -8.003  1.00 27.04 ? 107  VAL A CA  1 
ATOM   650  C C   . VAL A 1 83  ? 16.719  -22.772 -8.584  1.00 32.95 ? 107  VAL A C   1 
ATOM   651  O O   . VAL A 1 83  ? 17.009  -23.719 -7.863  1.00 31.23 ? 107  VAL A O   1 
ATOM   652  C CB  . VAL A 1 83  ? 17.959  -20.656 -7.877  1.00 21.32 ? 107  VAL A CB  1 
ATOM   653  C CG1 . VAL A 1 83  ? 18.818  -20.862 -9.115  1.00 28.08 ? 107  VAL A CG1 1 
ATOM   654  C CG2 . VAL A 1 83  ? 17.732  -19.140 -7.562  1.00 19.75 ? 107  VAL A CG2 1 
ATOM   655  N N   . ARG A 1 84  ? 16.485  -22.899 -9.887  1.00 27.75 ? 108  ARG A N   1 
ATOM   656  C CA  . ARG A 1 84  ? 16.645  -24.161 -10.599 1.00 30.97 ? 108  ARG A CA  1 
ATOM   657  C C   . ARG A 1 84  ? 17.682  -23.999 -11.701 1.00 29.80 ? 108  ARG A C   1 
ATOM   658  O O   . ARG A 1 84  ? 17.976  -22.882 -12.144 1.00 27.63 ? 108  ARG A O   1 
ATOM   659  C CB  . ARG A 1 84  ? 15.309  -24.599 -11.223 1.00 33.56 ? 108  ARG A CB  1 
ATOM   660  C CG  . ARG A 1 84  ? 14.158  -24.812 -10.237 1.00 39.37 ? 108  ARG A CG  1 
ATOM   661  C CD  . ARG A 1 84  ? 12.810  -24.850 -10.976 1.00 51.03 ? 108  ARG A CD  1 
ATOM   662  N NE  . ARG A 1 84  ? 12.642  -23.657 -11.815 1.00 60.64 ? 108  ARG A NE  1 
ATOM   663  C CZ  . ARG A 1 84  ? 12.847  -23.619 -13.134 1.00 63.15 ? 108  ARG A CZ  1 
ATOM   664  N NH1 . ARG A 1 84  ? 12.697  -22.475 -13.798 1.00 51.76 ? 108  ARG A NH1 1 
ATOM   665  N NH2 . ARG A 1 84  ? 13.212  -24.722 -13.790 1.00 68.72 ? 108  ARG A NH2 1 
ATOM   666  N N   . GLN A 1 85  ? 18.247  -25.120 -12.148 1.00 31.82 ? 109  GLN A N   1 
ATOM   667  C CA  . GLN A 1 85  ? 19.218  -25.100 -13.231 1.00 34.18 ? 109  GLN A CA  1 
ATOM   668  C C   . GLN A 1 85  ? 18.813  -24.182 -14.386 1.00 32.32 ? 109  GLN A C   1 
ATOM   669  O O   . GLN A 1 85  ? 17.680  -24.240 -14.860 1.00 35.44 ? 109  GLN A O   1 
ATOM   670  C CB  . GLN A 1 85  ? 19.433  -26.520 -13.761 1.00 41.90 ? 109  GLN A CB  1 
ATOM   671  C CG  . GLN A 1 85  ? 20.444  -26.598 -14.879 1.00 53.50 ? 109  GLN A CG  1 
ATOM   672  C CD  . GLN A 1 85  ? 21.857  -26.453 -14.377 1.00 59.79 ? 109  GLN A CD  1 
ATOM   673  O OE1 . GLN A 1 85  ? 22.736  -25.973 -15.092 1.00 63.00 ? 109  GLN A OE1 1 
ATOM   674  N NE2 . GLN A 1 85  ? 22.087  -26.878 -13.139 1.00 62.13 ? 109  GLN A NE2 1 
ATOM   675  N N   . GLU A 1 86  ? 19.753  -23.338 -14.817 1.00 32.86 ? 110  GLU A N   1 
ATOM   676  C CA  . GLU A 1 86  ? 19.583  -22.447 -15.970 1.00 36.99 ? 110  GLU A CA  1 
ATOM   677  C C   . GLU A 1 86  ? 18.770  -21.180 -15.687 1.00 34.27 ? 110  GLU A C   1 
ATOM   678  O O   . GLU A 1 86  ? 18.562  -20.354 -16.574 1.00 32.32 ? 110  GLU A O   1 
ATOM   679  C CB  . GLU A 1 86  ? 19.021  -23.208 -17.168 1.00 45.47 ? 110  GLU A CB  1 
ATOM   680  C CG  . GLU A 1 86  ? 19.748  -24.543 -17.385 1.00 53.90 ? 110  GLU A CG  1 
ATOM   681  C CD  . GLU A 1 86  ? 20.103  -24.794 -18.828 1.00 64.37 ? 110  GLU A CD  1 
ATOM   682  O OE1 . GLU A 1 86  ? 19.198  -24.709 -19.686 1.00 67.14 ? 110  GLU A OE1 1 
ATOM   683  O OE2 . GLU A 1 86  ? 21.289  -25.068 -19.106 1.00 69.69 ? 110  GLU A OE2 1 
ATOM   684  N N   . ASP A 1 87  ? 18.316  -21.016 -14.455 1.00 29.70 ? 111  ASP A N   1 
ATOM   685  C CA  . ASP A 1 87  ? 17.647  -19.776 -14.099 1.00 26.49 ? 111  ASP A CA  1 
ATOM   686  C C   . ASP A 1 87  ? 18.634  -18.605 -14.212 1.00 25.67 ? 111  ASP A C   1 
ATOM   687  O O   . ASP A 1 87  ? 19.833  -18.744 -13.897 1.00 25.47 ? 111  ASP A O   1 
ATOM   688  C CB  . ASP A 1 87  ? 17.106  -19.843 -12.673 1.00 23.97 ? 111  ASP A CB  1 
ATOM   689  C CG  . ASP A 1 87  ? 15.785  -20.596 -12.565 1.00 29.36 ? 111  ASP A CG  1 
ATOM   690  O OD1 . ASP A 1 87  ? 15.145  -20.877 -13.613 1.00 28.05 ? 111  ASP A OD1 1 
ATOM   691  O OD2 . ASP A 1 87  ? 15.385  -20.901 -11.412 1.00 29.01 ? 111  ASP A OD2 1 
ATOM   692  N N   . THR A 1 88  ? 18.138  -17.451 -14.650 1.00 24.13 ? 112  THR A N   1 
ATOM   693  C CA  . THR A 1 88  ? 18.916  -16.204 -14.628 1.00 22.01 ? 112  THR A CA  1 
ATOM   694  C C   . THR A 1 88  ? 18.021  -15.101 -14.087 1.00 21.36 ? 112  THR A C   1 
ATOM   695  O O   . THR A 1 88  ? 16.801  -15.247 -14.065 1.00 22.00 ? 112  THR A O   1 
ATOM   696  C CB  . THR A 1 88  ? 19.394  -15.776 -16.026 1.00 28.88 ? 112  THR A CB  1 
ATOM   697  O OG1 . THR A 1 88  ? 18.258  -15.513 -16.855 1.00 27.33 ? 112  THR A OG1 1 
ATOM   698  C CG2 . THR A 1 88  ? 20.292  -16.857 -16.667 1.00 30.10 ? 112  THR A CG2 1 
ATOM   699  N N   . TYR A 1 89  ? 18.591  -13.983 -13.658 1.00 22.56 ? 113  TYR A N   1 
ATOM   700  C CA  . TYR A 1 89  ? 17.725  -12.911 -13.167 1.00 21.79 ? 113  TYR A CA  1 
ATOM   701  C C   . TYR A 1 89  ? 16.747  -12.429 -14.255 1.00 24.23 ? 113  TYR A C   1 
ATOM   702  O O   . TYR A 1 89  ? 15.594  -12.121 -13.974 1.00 23.03 ? 113  TYR A O   1 
ATOM   703  C CB  . TYR A 1 89  ? 18.541  -11.722 -12.656 1.00 24.04 ? 113  TYR A CB  1 
ATOM   704  C CG  . TYR A 1 89  ? 19.300  -11.969 -11.361 1.00 25.34 ? 113  TYR A CG  1 
ATOM   705  C CD1 . TYR A 1 89  ? 18.628  -12.338 -10.208 1.00 20.11 ? 113  TYR A CD1 1 
ATOM   706  C CD2 . TYR A 1 89  ? 20.679  -11.757 -11.281 1.00 23.56 ? 113  TYR A CD2 1 
ATOM   707  C CE1 . TYR A 1 89  ? 19.290  -12.509 -9.012  1.00 21.59 ? 113  TYR A CE1 1 
ATOM   708  C CE2 . TYR A 1 89  ? 21.363  -11.939 -10.084 1.00 27.21 ? 113  TYR A CE2 1 
ATOM   709  C CZ  . TYR A 1 89  ? 20.646  -12.313 -8.940  1.00 23.72 ? 113  TYR A CZ  1 
ATOM   710  O OH  . TYR A 1 89  ? 21.305  -12.503 -7.734  1.00 22.94 ? 113  TYR A OH  1 
ATOM   711  N N   . GLU A 1 90  ? 17.211  -12.369 -15.497 1.00 25.22 ? 114  GLU A N   1 
ATOM   712  C CA  . GLU A 1 90  ? 16.329  -11.985 -16.601 1.00 25.90 ? 114  GLU A CA  1 
ATOM   713  C C   . GLU A 1 90  ? 15.175  -12.978 -16.738 1.00 25.72 ? 114  GLU A C   1 
ATOM   714  O O   . GLU A 1 90  ? 14.000  -12.596 -16.782 1.00 24.67 ? 114  GLU A O   1 
ATOM   715  C CB  . GLU A 1 90  ? 17.099  -11.906 -17.931 1.00 27.28 ? 114  GLU A CB  1 
ATOM   716  C CG  . GLU A 1 90  ? 16.154  -11.508 -19.073 1.00 37.52 ? 114  GLU A CG  1 
ATOM   717  C CD  . GLU A 1 90  ? 16.720  -11.760 -20.460 1.00 50.06 ? 114  GLU A CD  1 
ATOM   718  O OE1 . GLU A 1 90  ? 17.588  -12.645 -20.602 1.00 54.71 ? 114  GLU A OE1 1 
ATOM   719  O OE2 . GLU A 1 90  ? 16.286  -11.071 -21.410 1.00 54.84 ? 114  GLU A OE2 1 
ATOM   720  N N   . ARG A 1 91  ? 15.502  -14.268 -16.793 1.00 22.00 ? 115  ARG A N   1 
ATOM   721  C CA  . ARG A 1 91  ? 14.460  -15.286 -16.956 1.00 21.86 ? 115  ARG A CA  1 
ATOM   722  C C   . ARG A 1 91  ? 13.525  -15.336 -15.774 1.00 24.18 ? 115  ARG A C   1 
ATOM   723  O O   . ARG A 1 91  ? 12.320  -15.485 -15.947 1.00 24.00 ? 115  ARG A O   1 
ATOM   724  C CB  . ARG A 1 91  ? 15.058  -16.686 -17.198 1.00 28.47 ? 115  ARG A CB  1 
ATOM   725  C CG  . ARG A 1 91  ? 15.557  -16.871 -18.633 1.00 43.32 ? 115  ARG A CG  1 
ATOM   726  C CD  . ARG A 1 91  ? 15.996  -18.307 -18.932 1.00 59.39 ? 115  ARG A CD  1 
ATOM   727  N NE  . ARG A 1 91  ? 15.514  -19.282 -17.952 1.00 67.93 ? 115  ARG A NE  1 
ATOM   728  C CZ  . ARG A 1 91  ? 15.805  -20.581 -17.990 1.00 75.66 ? 115  ARG A CZ  1 
ATOM   729  N NH1 . ARG A 1 91  ? 16.563  -21.065 -18.966 1.00 76.82 ? 115  ARG A NH1 1 
ATOM   730  N NH2 . ARG A 1 91  ? 15.339  -21.400 -17.053 1.00 78.09 ? 115  ARG A NH2 1 
ATOM   731  N N   . VAL A 1 92  ? 14.064  -15.244 -14.563 1.00 18.54 ? 116  VAL A N   1 
ATOM   732  C CA  . VAL A 1 92  ? 13.171  -15.213 -13.406 1.00 18.91 ? 116  VAL A CA  1 
ATOM   733  C C   . VAL A 1 92  ? 12.157  -14.063 -13.481 1.00 19.86 ? 116  VAL A C   1 
ATOM   734  O O   . VAL A 1 92  ? 10.984  -14.233 -13.140 1.00 20.88 ? 116  VAL A O   1 
ATOM   735  C CB  . VAL A 1 92  ? 13.966  -15.207 -12.087 1.00 21.14 ? 116  VAL A CB  1 
ATOM   736  C CG1 . VAL A 1 92  ? 13.033  -15.011 -10.895 1.00 19.74 ? 116  VAL A CG1 1 
ATOM   737  C CG2 . VAL A 1 92  ? 14.766  -16.553 -11.950 1.00 18.47 ? 116  VAL A CG2 1 
ATOM   738  N N   . ALA A 1 93  ? 12.590  -12.884 -13.935 1.00 18.20 ? 117  ALA A N   1 
ATOM   739  C CA  . ALA A 1 93  ? 11.641  -11.771 -13.997 1.00 16.45 ? 117  ALA A CA  1 
ATOM   740  C C   . ALA A 1 93  ? 10.653  -11.890 -15.150 1.00 21.40 ? 117  ALA A C   1 
ATOM   741  O O   . ALA A 1 93  ? 9.461   -11.607 -14.984 1.00 21.82 ? 117  ALA A O   1 
ATOM   742  C CB  . ALA A 1 93  ? 12.383  -10.443 -14.115 1.00 14.92 ? 117  ALA A CB  1 
ATOM   743  N N   . ILE A 1 94  ? 11.145  -12.238 -16.337 1.00 21.42 ? 118  ILE A N   1 
ATOM   744  C CA  . ILE A 1 94  ? 10.268  -12.204 -17.511 1.00 22.19 ? 118  ILE A CA  1 
ATOM   745  C C   . ILE A 1 94  ? 9.423   -13.459 -17.708 1.00 23.44 ? 118  ILE A C   1 
ATOM   746  O O   . ILE A 1 94  ? 8.371   -13.402 -18.343 1.00 24.33 ? 118  ILE A O   1 
ATOM   747  C CB  . ILE A 1 94  ? 11.026  -11.885 -18.831 1.00 26.47 ? 118  ILE A CB  1 
ATOM   748  C CG1 . ILE A 1 94  ? 11.803  -13.077 -19.343 1.00 31.00 ? 118  ILE A CG1 1 
ATOM   749  C CG2 . ILE A 1 94  ? 11.902  -10.601 -18.696 1.00 26.45 ? 118  ILE A CG2 1 
ATOM   750  C CD1 . ILE A 1 94  ? 12.463  -12.806 -20.707 1.00 39.73 ? 118  ILE A CD1 1 
ATOM   751  N N   . SER A 1 95  ? 9.888   -14.581 -17.158 1.00 20.06 ? 119  SER A N   1 
ATOM   752  C CA  . SER A 1 95  ? 9.214   -15.861 -17.339 1.00 21.42 ? 119  SER A CA  1 
ATOM   753  C C   . SER A 1 95  ? 8.657   -16.397 -16.017 1.00 19.49 ? 119  SER A C   1 
ATOM   754  O O   . SER A 1 95  ? 7.450   -16.513 -15.842 1.00 20.99 ? 119  SER A O   1 
ATOM   755  C CB  . SER A 1 95  ? 10.186  -16.852 -17.995 1.00 27.13 ? 119  SER A CB  1 
ATOM   756  O OG  . SER A 1 95  ? 9.570   -18.103 -18.215 1.00 32.98 ? 119  SER A OG  1 
ATOM   757  N N   . ASN A 1 96  ? 9.527   -16.701 -15.062 1.00 20.40 ? 120  ASN A N   1 
ATOM   758  C CA  . ASN A 1 96  ? 9.031   -17.294 -13.805 1.00 18.97 ? 120  ASN A CA  1 
ATOM   759  C C   . ASN A 1 96  ? 8.010   -16.423 -13.082 1.00 15.77 ? 120  ASN A C   1 
ATOM   760  O O   . ASN A 1 96  ? 7.056   -16.934 -12.480 1.00 19.44 ? 120  ASN A O   1 
ATOM   761  C CB  . ASN A 1 96  ? 10.175  -17.658 -12.859 1.00 18.63 ? 120  ASN A CB  1 
ATOM   762  C CG  . ASN A 1 96  ? 11.205  -18.552 -13.521 1.00 30.29 ? 120  ASN A CG  1 
ATOM   763  O OD1 . ASN A 1 96  ? 11.670  -18.276 -14.620 1.00 34.48 ? 120  ASN A OD1 1 
ATOM   764  N ND2 . ASN A 1 96  ? 11.550  -19.638 -12.852 1.00 35.45 ? 120  ASN A ND2 1 
ATOM   765  N N   . TYR A 1 97  ? 8.205   -15.105 -13.115 1.00 17.83 ? 121  TYR A N   1 
ATOM   766  C CA  . TYR A 1 97  ? 7.269   -14.207 -12.482 1.00 17.25 ? 121  TYR A CA  1 
ATOM   767  C C   . TYR A 1 97  ? 6.458   -13.374 -13.487 1.00 16.64 ? 121  TYR A C   1 
ATOM   768  O O   . TYR A 1 97  ? 5.746   -12.444 -13.095 1.00 17.09 ? 121  TYR A O   1 
ATOM   769  C CB  . TYR A 1 97  ? 7.977   -13.325 -11.417 1.00 16.83 ? 121  TYR A CB  1 
ATOM   770  C CG  . TYR A 1 97  ? 8.242   -14.137 -10.165 1.00 18.18 ? 121  TYR A CG  1 
ATOM   771  C CD1 . TYR A 1 97  ? 7.355   -14.122 -9.099  1.00 20.12 ? 121  TYR A CD1 1 
ATOM   772  C CD2 . TYR A 1 97  ? 9.345   -14.981 -10.087 1.00 16.44 ? 121  TYR A CD2 1 
ATOM   773  C CE1 . TYR A 1 97  ? 7.571   -14.921 -7.959  1.00 20.23 ? 121  TYR A CE1 1 
ATOM   774  C CE2 . TYR A 1 97  ? 9.569   -15.783 -8.956  1.00 17.97 ? 121  TYR A CE2 1 
ATOM   775  C CZ  . TYR A 1 97  ? 8.691   -15.732 -7.898  1.00 19.07 ? 121  TYR A CZ  1 
ATOM   776  O OH  . TYR A 1 97  ? 8.920   -16.538 -6.796  1.00 19.13 ? 121  TYR A OH  1 
ATOM   777  N N   . ALA A 1 98  ? 6.565   -13.712 -14.772 1.00 19.09 ? 122  ALA A N   1 
ATOM   778  C CA  . ALA A 1 98  ? 5.646   -13.168 -15.784 1.00 20.37 ? 122  ALA A CA  1 
ATOM   779  C C   . ALA A 1 98  ? 5.566   -11.641 -15.773 1.00 18.65 ? 122  ALA A C   1 
ATOM   780  O O   . ALA A 1 98  ? 4.475   -11.051 -15.898 1.00 17.34 ? 122  ALA A O   1 
ATOM   781  C CB  . ALA A 1 98  ? 4.218   -13.824 -15.629 1.00 19.27 ? 122  ALA A CB  1 
ATOM   782  N N   . ASN A 1 99  ? 6.735   -11.013 -15.636 1.00 19.05 ? 123  ASN A N   1 
ATOM   783  C CA  . ASN A 1 99  ? 6.873   -9.549  -15.621 1.00 16.94 ? 123  ASN A CA  1 
ATOM   784  C C   . ASN A 1 99  ? 6.209   -8.842  -14.443 1.00 18.92 ? 123  ASN A C   1 
ATOM   785  O O   . ASN A 1 99  ? 6.015   -7.595  -14.479 1.00 18.38 ? 123  ASN A O   1 
ATOM   786  C CB  . ASN A 1 99  ? 6.425   -8.935  -16.959 1.00 20.94 ? 123  ASN A CB  1 
ATOM   787  C CG  . ASN A 1 99  ? 7.285   -9.416  -18.120 1.00 24.22 ? 123  ASN A CG  1 
ATOM   788  O OD1 . ASN A 1 99  ? 8.520   -9.431  -18.016 1.00 21.49 ? 123  ASN A OD1 1 
ATOM   789  N ND2 . ASN A 1 99  ? 6.631   -9.844  -19.214 1.00 19.96 ? 123  ASN A ND2 1 
ATOM   790  N N   . LEU A 1 100 ? 5.887   -9.606  -13.398 1.00 19.44 ? 124  LEU A N   1 
ATOM   791  C CA  . LEU A 1 100 ? 5.420   -9.028  -12.133 1.00 19.72 ? 124  LEU A CA  1 
ATOM   792  C C   . LEU A 1 100 ? 6.561   -8.363  -11.356 1.00 20.02 ? 124  LEU A C   1 
ATOM   793  O O   . LEU A 1 100 ? 6.332   -7.595  -10.427 1.00 21.50 ? 124  LEU A O   1 
ATOM   794  C CB  . LEU A 1 100 ? 4.800   -10.132 -11.260 1.00 17.39 ? 124  LEU A CB  1 
ATOM   795  C CG  . LEU A 1 100 ? 3.439   -10.612 -11.786 1.00 17.14 ? 124  LEU A CG  1 
ATOM   796  C CD1 . LEU A 1 100 ? 3.043   -11.975 -11.171 1.00 18.64 ? 124  LEU A CD1 1 
ATOM   797  C CD2 . LEU A 1 100 ? 2.337   -9.557  -11.562 1.00 19.49 ? 124  LEU A CD2 1 
ATOM   798  N N   . THR A 1 101 ? 7.784   -8.711  -11.728 1.00 18.66 ? 125  THR A N   1 
ATOM   799  C CA  . THR A 1 101 ? 8.996   -8.118  -11.172 1.00 18.26 ? 125  THR A CA  1 
ATOM   800  C C   . THR A 1 101 ? 9.920   -7.791  -12.346 1.00 21.23 ? 125  THR A C   1 
ATOM   801  O O   . THR A 1 101 ? 9.602   -8.095  -13.510 1.00 20.25 ? 125  THR A O   1 
ATOM   802  C CB  . THR A 1 101 ? 9.706   -9.040  -10.119 1.00 20.80 ? 125  THR A CB  1 
ATOM   803  O OG1 . THR A 1 101 ? 10.616  -8.261  -9.317  1.00 21.29 ? 125  THR A OG1 1 
ATOM   804  C CG2 . THR A 1 101 ? 10.477  -10.195 -10.796 1.00 19.38 ? 125  THR A CG2 1 
ATOM   805  N N   . THR A 1 102 ? 11.035  -7.130  -12.053 1.00 19.62 ? 126  THR A N   1 
ATOM   806  C CA  . THR A 1 102 ? 11.981  -6.755  -13.096 1.00 19.55 ? 126  THR A CA  1 
ATOM   807  C C   . THR A 1 102 ? 13.348  -7.352  -12.789 1.00 21.77 ? 126  THR A C   1 
ATOM   808  O O   . THR A 1 102 ? 13.681  -7.601  -11.627 1.00 20.18 ? 126  THR A O   1 
ATOM   809  C CB  . THR A 1 102 ? 12.163  -5.220  -13.193 1.00 23.70 ? 126  THR A CB  1 
ATOM   810  O OG1 . THR A 1 102 ? 12.754  -4.725  -11.983 1.00 22.12 ? 126  THR A OG1 1 
ATOM   811  C CG2 . THR A 1 102 ? 10.816  -4.520  -13.443 1.00 25.47 ? 126  THR A CG2 1 
ATOM   812  N N   . MET A 1 103 ? 14.151  -7.554  -13.824 1.00 19.53 ? 127  MET A N   1 
ATOM   813  C CA  . MET A 1 103 ? 15.487  -8.081  -13.596 1.00 20.30 ? 127  MET A CA  1 
ATOM   814  C C   . MET A 1 103 ? 16.324  -7.110  -12.782 1.00 22.73 ? 127  MET A C   1 
ATOM   815  O O   . MET A 1 103 ? 17.139  -7.533  -11.950 1.00 24.78 ? 127  MET A O   1 
ATOM   816  C CB  . MET A 1 103 ? 16.180  -8.515  -14.900 1.00 23.78 ? 127  MET A CB  1 
ATOM   817  C CG  . MET A 1 103 ? 16.334  -7.472  -15.979 1.00 29.61 ? 127  MET A CG  1 
ATOM   818  S SD  . MET A 1 103 ? 17.477  -8.153  -17.233 1.00 51.91 ? 127  MET A SD  1 
ATOM   819  C CE  . MET A 1 103 ? 19.039  -7.637  -16.525 1.00 64.47 ? 127  MET A CE  1 
ATOM   820  N N   . GLU A 1 104 ? 16.116  -5.804  -12.984 1.00 21.83 ? 128  GLU A N   1 
ATOM   821  C CA  . GLU A 1 104 ? 16.911  -4.839  -12.240 1.00 24.65 ? 128  GLU A CA  1 
ATOM   822  C C   . GLU A 1 104 ? 16.619  -4.917  -10.746 1.00 22.03 ? 128  GLU A C   1 
ATOM   823  O O   . GLU A 1 104 ? 17.526  -4.782  -9.911  1.00 22.55 ? 128  GLU A O   1 
ATOM   824  C CB  . GLU A 1 104 ? 16.658  -3.420  -12.753 1.00 27.61 ? 128  GLU A CB  1 
ATOM   825  C CG  . GLU A 1 104 ? 17.192  -3.176  -14.160 1.00 35.49 ? 128  GLU A CG  1 
ATOM   826  C CD  . GLU A 1 104 ? 16.275  -3.684  -15.284 1.00 42.99 ? 128  GLU A CD  1 
ATOM   827  O OE1 . GLU A 1 104 ? 15.168  -4.254  -15.019 1.00 33.80 ? 128  GLU A OE1 1 
ATOM   828  O OE2 . GLU A 1 104 ? 16.683  -3.498  -16.457 1.00 44.30 ? 128  GLU A OE2 1 
ATOM   829  N N   . SER A 1 105 ? 15.348  -5.128  -10.420 1.00 21.73 ? 129  SER A N   1 
ATOM   830  C CA  . SER A 1 105 ? 14.926  -5.174  -9.027  1.00 21.47 ? 129  SER A CA  1 
ATOM   831  C C   . SER A 1 105 ? 15.516  -6.420  -8.357  1.00 20.57 ? 129  SER A C   1 
ATOM   832  O O   . SER A 1 105 ? 16.007  -6.374  -7.223  1.00 21.17 ? 129  SER A O   1 
ATOM   833  C CB  . SER A 1 105 ? 13.389  -5.207  -8.938  1.00 21.84 ? 129  SER A CB  1 
ATOM   834  O OG  . SER A 1 105 ? 12.997  -5.458  -7.594  1.00 20.38 ? 129  SER A OG  1 
ATOM   835  N N   . LEU A 1 106 ? 15.464  -7.544  -9.070  1.00 19.17 ? 130  LEU A N   1 
ATOM   836  C CA  . LEU A 1 106 ? 16.035  -8.796  -8.553  1.00 18.76 ? 130  LEU A CA  1 
ATOM   837  C C   . LEU A 1 106 ? 17.523  -8.673  -8.320  1.00 23.98 ? 130  LEU A C   1 
ATOM   838  O O   . LEU A 1 106 ? 18.044  -9.075  -7.284  1.00 21.45 ? 130  LEU A O   1 
ATOM   839  C CB  . LEU A 1 106 ? 15.804  -9.909  -9.560  1.00 19.36 ? 130  LEU A CB  1 
ATOM   840  C CG  . LEU A 1 106 ? 14.392  -10.441 -9.684  1.00 21.80 ? 130  LEU A CG  1 
ATOM   841  C CD1 . LEU A 1 106 ? 14.391  -11.451 -10.824 1.00 21.67 ? 130  LEU A CD1 1 
ATOM   842  C CD2 . LEU A 1 106 ? 13.983  -11.123 -8.344  1.00 20.30 ? 130  LEU A CD2 1 
ATOM   843  N N   . GLN A 1 107 ? 18.224  -8.096  -9.288  1.00 23.47 ? 131  GLN A N   1 
ATOM   844  C CA  . GLN A 1 107 ? 19.661  -7.940  -9.125  1.00 23.95 ? 131  GLN A CA  1 
ATOM   845  C C   . GLN A 1 107 ? 20.000  -7.063  -7.925  1.00 23.91 ? 131  GLN A C   1 
ATOM   846  O O   . GLN A 1 107 ? 20.975  -7.309  -7.215  1.00 26.23 ? 131  GLN A O   1 
ATOM   847  C CB  . GLN A 1 107 ? 20.282  -7.313  -10.371 1.00 30.23 ? 131  GLN A CB  1 
ATOM   848  C CG  . GLN A 1 107 ? 20.369  -8.219  -11.559 1.00 36.34 ? 131  GLN A CG  1 
ATOM   849  C CD  . GLN A 1 107 ? 21.783  -8.258  -12.121 1.00 42.00 ? 131  GLN A CD  1 
ATOM   850  O OE1 . GLN A 1 107 ? 21.990  -8.034  -13.301 1.00 45.09 ? 131  GLN A OE1 1 
ATOM   851  N NE2 . GLN A 1 107 ? 22.761  -8.537  -11.262 1.00 50.00 ? 131  GLN A NE2 1 
ATOM   852  N N   . ALA A 1 108 ? 19.228  -6.008  -7.710  1.00 22.39 ? 132  ALA A N   1 
ATOM   853  C CA  . ALA A 1 108 ? 19.570  -5.065  -6.657  1.00 23.56 ? 132  ALA A CA  1 
ATOM   854  C C   . ALA A 1 108 ? 19.402  -5.645  -5.254  1.00 24.74 ? 132  ALA A C   1 
ATOM   855  O O   . ALA A 1 108 ? 20.163  -5.317  -4.345  1.00 27.31 ? 132  ALA A O   1 
ATOM   856  C CB  . ALA A 1 108 ? 18.751  -3.790  -6.798  1.00 25.54 ? 132  ALA A CB  1 
ATOM   857  N N   . ARG A 1 109 ? 18.435  -6.544  -5.087  1.00 19.82 ? 133  ARG A N   1 
ATOM   858  C CA  . ARG A 1 109 ? 18.051  -6.983  -3.750  1.00 17.34 ? 133  ARG A CA  1 
ATOM   859  C C   . ARG A 1 109 ? 18.532  -8.414  -3.440  1.00 26.48 ? 133  ARG A C   1 
ATOM   860  O O   . ARG A 1 109 ? 18.242  -8.936  -2.368  1.00 25.88 ? 133  ARG A O   1 
ATOM   861  C CB  . ARG A 1 109 ? 16.527  -6.906  -3.589  1.00 18.38 ? 133  ARG A CB  1 
ATOM   862  C CG  . ARG A 1 109 ? 15.782  -7.979  -4.373  1.00 21.95 ? 133  ARG A CG  1 
ATOM   863  C CD  . ARG A 1 109 ? 14.341  -7.558  -4.603  1.00 23.24 ? 133  ARG A CD  1 
ATOM   864  N NE  . ARG A 1 109 ? 13.582  -7.525  -3.350  1.00 22.68 ? 133  ARG A NE  1 
ATOM   865  C CZ  . ARG A 1 109 ? 13.274  -6.411  -2.702  1.00 25.61 ? 133  ARG A CZ  1 
ATOM   866  N NH1 . ARG A 1 109 ? 12.580  -6.477  -1.566  1.00 28.58 ? 133  ARG A NH1 1 
ATOM   867  N NH2 . ARG A 1 109 ? 13.646  -5.237  -3.204  1.00 21.00 ? 133  ARG A NH2 1 
ATOM   868  N N   . ASN A 1 110 ? 19.271  -9.025  -4.368  1.00 18.85 ? 134  ASN A N   1 
ATOM   869  C CA  . ASN A 1 110 ? 19.896  -10.343 -4.132  1.00 18.39 ? 134  ASN A CA  1 
ATOM   870  C C   . ASN A 1 110 ? 21.403  -10.242 -4.304  1.00 22.72 ? 134  ASN A C   1 
ATOM   871  O O   . ASN A 1 110 ? 21.876  -9.511  -5.172  1.00 24.52 ? 134  ASN A O   1 
ATOM   872  C CB  . ASN A 1 110 ? 19.308  -11.380 -5.086  1.00 18.01 ? 134  ASN A CB  1 
ATOM   873  C CG  . ASN A 1 110 ? 17.819  -11.651 -4.809  1.00 21.59 ? 134  ASN A CG  1 
ATOM   874  O OD1 . ASN A 1 110 ? 16.913  -11.136 -5.500  1.00 21.63 ? 134  ASN A OD1 1 
ATOM   875  N ND2 . ASN A 1 110 ? 17.566  -12.428 -3.775  1.00 15.64 ? 134  ASN A ND2 1 
ATOM   876  N N   . PRO A 1 111 ? 22.166  -10.975 -3.474  1.00 19.67 ? 135  PRO A N   1 
ATOM   877  C CA  . PRO A 1 111 ? 23.619  -10.761 -3.446  1.00 19.86 ? 135  PRO A CA  1 
ATOM   878  C C   . PRO A 1 111 ? 24.414  -11.593 -4.468  1.00 27.98 ? 135  PRO A C   1 
ATOM   879  O O   . PRO A 1 111 ? 25.621  -11.366 -4.603  1.00 25.17 ? 135  PRO A O   1 
ATOM   880  C CB  . PRO A 1 111 ? 23.979  -11.181 -2.026  1.00 24.69 ? 135  PRO A CB  1 
ATOM   881  C CG  . PRO A 1 111 ? 23.054  -12.342 -1.775  1.00 26.33 ? 135  PRO A CG  1 
ATOM   882  C CD  . PRO A 1 111 ? 21.723  -11.878 -2.394  1.00 26.90 ? 135  PRO A CD  1 
ATOM   883  N N   . PHE A 1 112 ? 23.767  -12.513 -5.184  1.00 23.59 ? 136  PHE A N   1 
ATOM   884  C CA  . PHE A 1 112 ? 24.499  -13.390 -6.092  1.00 26.95 ? 136  PHE A CA  1 
ATOM   885  C C   . PHE A 1 112 ? 24.831  -12.659 -7.403  1.00 25.77 ? 136  PHE A C   1 
ATOM   886  O O   . PHE A 1 112 ? 23.982  -12.004 -7.988  1.00 25.91 ? 136  PHE A O   1 
ATOM   887  C CB  . PHE A 1 112 ? 23.665  -14.666 -6.378  1.00 27.34 ? 136  PHE A CB  1 
ATOM   888  C CG  . PHE A 1 112 ? 23.030  -15.255 -5.150  1.00 23.60 ? 136  PHE A CG  1 
ATOM   889  C CD1 . PHE A 1 112 ? 23.791  -15.992 -4.257  1.00 23.65 ? 136  PHE A CD1 1 
ATOM   890  C CD2 . PHE A 1 112 ? 21.667  -15.078 -4.894  1.00 24.04 ? 136  PHE A CD2 1 
ATOM   891  C CE1 . PHE A 1 112 ? 23.223  -16.519 -3.096  1.00 25.77 ? 136  PHE A CE1 1 
ATOM   892  C CE2 . PHE A 1 112 ? 21.092  -15.598 -3.741  1.00 24.19 ? 136  PHE A CE2 1 
ATOM   893  C CZ  . PHE A 1 112 ? 21.871  -16.329 -2.845  1.00 22.54 ? 136  PHE A CZ  1 
ATOM   894  N N   . PRO A 1 113 ? 26.070  -12.785 -7.884  1.00 30.13 ? 137  PRO A N   1 
ATOM   895  C CA  . PRO A 1 113 ? 26.395  -12.170 -9.182  1.00 28.40 ? 137  PRO A CA  1 
ATOM   896  C C   . PRO A 1 113 ? 25.538  -12.814 -10.261 1.00 28.16 ? 137  PRO A C   1 
ATOM   897  O O   . PRO A 1 113 ? 25.237  -14.006 -10.148 1.00 28.10 ? 137  PRO A O   1 
ATOM   898  C CB  . PRO A 1 113 ? 27.863  -12.567 -9.410  1.00 28.63 ? 137  PRO A CB  1 
ATOM   899  C CG  . PRO A 1 113 ? 28.357  -13.081 -8.097  1.00 37.68 ? 137  PRO A CG  1 
ATOM   900  C CD  . PRO A 1 113 ? 27.167  -13.605 -7.351  1.00 32.42 ? 137  PRO A CD  1 
ATOM   901  N N   . ALA A 1 114 ? 25.147  -12.070 -11.289 1.00 25.28 ? 138  ALA A N   1 
ATOM   902  C CA  . ALA A 1 114 ? 24.267  -12.646 -12.306 1.00 26.83 ? 138  ALA A CA  1 
ATOM   903  C C   . ALA A 1 114 ? 24.768  -13.975 -12.887 1.00 28.60 ? 138  ALA A C   1 
ATOM   904  O O   . ALA A 1 114 ? 23.976  -14.878 -13.162 1.00 26.32 ? 138  ALA A O   1 
ATOM   905  C CB  . ALA A 1 114 ? 24.024  -11.645 -13.430 1.00 27.98 ? 138  ALA A CB  1 
ATOM   906  N N   . THR A 1 115 ? 26.077  -14.095 -13.095 1.00 30.91 ? 139  THR A N   1 
ATOM   907  C CA  . THR A 1 115 ? 26.600  -15.287 -13.759 1.00 29.96 ? 139  THR A CA  1 
ATOM   908  C C   . THR A 1 115 ? 26.970  -16.414 -12.803 1.00 29.93 ? 139  THR A C   1 
ATOM   909  O O   . THR A 1 115 ? 27.522  -17.430 -13.223 1.00 33.01 ? 139  THR A O   1 
ATOM   910  C CB  . THR A 1 115 ? 27.799  -14.956 -14.641 1.00 31.52 ? 139  THR A CB  1 
ATOM   911  O OG1 . THR A 1 115 ? 28.857  -14.448 -13.815 1.00 33.09 ? 139  THR A OG1 1 
ATOM   912  C CG2 . THR A 1 115 ? 27.381  -13.928 -15.705 1.00 32.04 ? 139  THR A CG2 1 
ATOM   913  N N   . ASN A 1 116 ? 26.657  -16.250 -11.519 1.00 29.59 ? 140  ASN A N   1 
ATOM   914  C CA  . ASN A 1 116 ? 26.727  -17.385 -10.598 1.00 28.94 ? 140  ASN A CA  1 
ATOM   915  C C   . ASN A 1 116 ? 25.679  -17.333 -9.505  1.00 26.37 ? 140  ASN A C   1 
ATOM   916  O O   . ASN A 1 116 ? 25.986  -17.147 -8.331  1.00 27.86 ? 140  ASN A O   1 
ATOM   917  C CB  . ASN A 1 116 ? 28.111  -17.607 -9.994  1.00 33.95 ? 140  ASN A CB  1 
ATOM   918  C CG  . ASN A 1 116 ? 28.225  -18.982 -9.313  1.00 35.09 ? 140  ASN A CG  1 
ATOM   919  O OD1 . ASN A 1 116 ? 27.362  -19.855 -9.493  1.00 36.85 ? 140  ASN A OD1 1 
ATOM   920  N ND2 . ASN A 1 116 ? 29.265  -19.167 -8.525  1.00 36.84 ? 140  ASN A ND2 1 
ATOM   921  N N   . ILE A 1 117 ? 24.438  -17.505 -9.913  1.00 23.70 ? 141  ILE A N   1 
ATOM   922  C CA  . ILE A 1 117 ? 23.374  -17.774 -8.958  1.00 25.00 ? 141  ILE A CA  1 
ATOM   923  C C   . ILE A 1 117 ? 23.439  -19.270 -8.665  1.00 30.42 ? 141  ILE A C   1 
ATOM   924  O O   . ILE A 1 117 ? 23.209  -20.077 -9.563  1.00 30.56 ? 141  ILE A O   1 
ATOM   925  C CB  . ILE A 1 117 ? 22.018  -17.440 -9.551  1.00 23.18 ? 141  ILE A CB  1 
ATOM   926  C CG1 . ILE A 1 117 ? 22.003  -15.972 -10.009 1.00 23.40 ? 141  ILE A CG1 1 
ATOM   927  C CG2 . ILE A 1 117 ? 20.896  -17.663 -8.507  1.00 21.21 ? 141  ILE A CG2 1 
ATOM   928  C CD1 . ILE A 1 117 ? 20.750  -15.604 -10.792 1.00 26.22 ? 141  ILE A CD1 1 
ATOM   929  N N   . PRO A 1 118 ? 23.754  -19.648 -7.413  1.00 25.14 ? 142  PRO A N   1 
ATOM   930  C CA  . PRO A 1 118 ? 23.915  -21.080 -7.070  1.00 26.62 ? 142  PRO A CA  1 
ATOM   931  C C   . PRO A 1 118 ? 22.619  -21.898 -7.081  1.00 28.77 ? 142  PRO A C   1 
ATOM   932  O O   . PRO A 1 118 ? 21.527  -21.378 -6.825  1.00 28.07 ? 142  PRO A O   1 
ATOM   933  C CB  . PRO A 1 118 ? 24.488  -21.054 -5.644  1.00 32.95 ? 142  PRO A CB  1 
ATOM   934  C CG  . PRO A 1 118 ? 24.523  -19.619 -5.216  1.00 29.80 ? 142  PRO A CG  1 
ATOM   935  C CD  . PRO A 1 118 ? 23.849  -18.770 -6.238  1.00 25.99 ? 142  PRO A CD  1 
ATOM   936  N N   . LEU A 1 119 ? 22.742  -23.200 -7.362  1.00 28.66 ? 143  LEU A N   1 
ATOM   937  C CA  . LEU A 1 119 ? 21.577  -24.072 -7.337  1.00 29.70 ? 143  LEU A CA  1 
ATOM   938  C C   . LEU A 1 119 ? 21.023  -24.113 -5.916  1.00 30.42 ? 143  LEU A C   1 
ATOM   939  O O   . LEU A 1 119 ? 21.780  -24.151 -4.961  1.00 34.36 ? 143  LEU A O   1 
ATOM   940  C CB  . LEU A 1 119 ? 21.970  -25.486 -7.790  1.00 36.70 ? 143  LEU A CB  1 
ATOM   941  C CG  . LEU A 1 119 ? 21.606  -25.951 -9.209  1.00 40.29 ? 143  LEU A CG  1 
ATOM   942  C CD1 . LEU A 1 119 ? 21.400  -24.815 -10.200 1.00 39.58 ? 143  LEU A CD1 1 
ATOM   943  C CD2 . LEU A 1 119 ? 22.629  -26.956 -9.713  1.00 39.39 ? 143  LEU A CD2 1 
ATOM   944  N N   . SER A 1 120 ? 19.704  -24.073 -5.783  1.00 37.44 ? 144  SER A N   1 
ATOM   945  C CA  . SER A 1 120 ? 19.082  -24.050 -4.457  1.00 45.49 ? 144  SER A CA  1 
ATOM   946  C C   . SER A 1 120 ? 19.291  -22.759 -3.630  1.00 37.35 ? 144  SER A C   1 
ATOM   947  O O   . SER A 1 120 ? 18.843  -22.682 -2.489  1.00 34.06 ? 144  SER A O   1 
ATOM   948  C CB  . SER A 1 120 ? 19.468  -25.293 -3.646  1.00 50.20 ? 144  SER A CB  1 
ATOM   949  O OG  . SER A 1 120 ? 18.772  -26.438 -4.120  1.00 52.37 ? 144  SER A OG  1 
ATOM   950  N N   . ALA A 1 121 ? 19.946  -21.748 -4.196  1.00 28.82 ? 145  ALA A N   1 
ATOM   951  C CA  . ALA A 1 121 ? 19.796  -20.414 -3.628  1.00 24.57 ? 145  ALA A CA  1 
ATOM   952  C C   . ALA A 1 121 ? 18.306  -20.050 -3.579  1.00 24.33 ? 145  ALA A C   1 
ATOM   953  O O   . ALA A 1 121 ? 17.508  -20.553 -4.376  1.00 23.56 ? 145  ALA A O   1 
ATOM   954  C CB  . ALA A 1 121 ? 20.544  -19.381 -4.460  1.00 24.67 ? 145  ALA A CB  1 
ATOM   955  N N   . THR A 1 122 ? 17.951  -19.177 -2.640  1.00 21.22 ? 146  THR A N   1 
ATOM   956  C CA  . THR A 1 122 ? 16.614  -18.546 -2.617  1.00 19.79 ? 146  THR A CA  1 
ATOM   957  C C   . THR A 1 122 ? 16.773  -17.104 -3.041  1.00 21.61 ? 146  THR A C   1 
ATOM   958  O O   . THR A 1 122 ? 17.662  -16.402 -2.545  1.00 23.32 ? 146  THR A O   1 
ATOM   959  C CB  . THR A 1 122 ? 16.042  -18.556 -1.200  1.00 25.12 ? 146  THR A CB  1 
ATOM   960  O OG1 . THR A 1 122 ? 15.961  -19.914 -0.745  1.00 25.52 ? 146  THR A OG1 1 
ATOM   961  C CG2 . THR A 1 122 ? 14.645  -17.971 -1.183  1.00 24.69 ? 146  THR A CG2 1 
ATOM   962  N N   . LEU A 1 123 ? 15.903  -16.665 -3.946  1.00 19.04 ? 147  LEU A N   1 
ATOM   963  C CA  . LEU A 1 123 ? 15.827  -15.246 -4.284  1.00 19.84 ? 147  LEU A CA  1 
ATOM   964  C C   . LEU A 1 123 ? 14.684  -14.563 -3.558  1.00 21.27 ? 147  LEU A C   1 
ATOM   965  O O   . LEU A 1 123 ? 13.589  -15.109 -3.417  1.00 20.70 ? 147  LEU A O   1 
ATOM   966  C CB  . LEU A 1 123 ? 15.621  -15.056 -5.796  1.00 18.74 ? 147  LEU A CB  1 
ATOM   967  C CG  . LEU A 1 123 ? 16.701  -15.676 -6.686  1.00 21.86 ? 147  LEU A CG  1 
ATOM   968  C CD1 . LEU A 1 123 ? 16.433  -15.279 -8.156  1.00 19.91 ? 147  LEU A CD1 1 
ATOM   969  C CD2 . LEU A 1 123 ? 18.150  -15.312 -6.239  1.00 18.91 ? 147  LEU A CD2 1 
ATOM   970  N N   . ASN A 1 124 ? 14.953  -13.330 -3.139  1.00 18.12 ? 148  ASN A N   1 
ATOM   971  C CA  . ASN A 1 124 ? 13.936  -12.410 -2.654  1.00 21.08 ? 148  ASN A CA  1 
ATOM   972  C C   . ASN A 1 124 ? 13.368  -11.680 -3.881  1.00 20.06 ? 148  ASN A C   1 
ATOM   973  O O   . ASN A 1 124 ? 14.103  -11.005 -4.611  1.00 19.43 ? 148  ASN A O   1 
ATOM   974  C CB  . ASN A 1 124 ? 14.620  -11.430 -1.686  1.00 20.65 ? 148  ASN A CB  1 
ATOM   975  C CG  . ASN A 1 124 ? 13.658  -10.474 -1.032  1.00 27.22 ? 148  ASN A CG  1 
ATOM   976  O OD1 . ASN A 1 124 ? 12.901  -9.801  -1.704  1.00 25.20 ? 148  ASN A OD1 1 
ATOM   977  N ND2 . ASN A 1 124 ? 13.676  -10.429 0.296   1.00 31.14 ? 148  ASN A ND2 1 
ATOM   978  N N   . VAL A 1 125 ? 12.058  -11.833 -4.120  1.00 18.63 ? 149  VAL A N   1 
ATOM   979  C CA  . VAL A 1 125 ? 11.444  -11.343 -5.357  1.00 18.01 ? 149  VAL A CA  1 
ATOM   980  C C   . VAL A 1 125 ? 10.357  -10.322 -4.990  1.00 18.54 ? 149  VAL A C   1 
ATOM   981  O O   . VAL A 1 125 ? 9.347   -10.695 -4.387  1.00 17.80 ? 149  VAL A O   1 
ATOM   982  C CB  . VAL A 1 125 ? 10.788  -12.524 -6.149  1.00 19.83 ? 149  VAL A CB  1 
ATOM   983  C CG1 . VAL A 1 125 ? 10.092  -12.006 -7.443  1.00 22.41 ? 149  VAL A CG1 1 
ATOM   984  C CG2 . VAL A 1 125 ? 11.826  -13.621 -6.475  1.00 18.49 ? 149  VAL A CG2 1 
ATOM   985  N N   . LEU A 1 126 ? 10.574  -9.046  -5.323  1.00 18.39 ? 150  LEU A N   1 
ATOM   986  C CA  . LEU A 1 126 ? 9.606   -7.986  -4.964  1.00 15.88 ? 150  LEU A CA  1 
ATOM   987  C C   . LEU A 1 126 ? 8.566   -7.789  -6.059  1.00 18.56 ? 150  LEU A C   1 
ATOM   988  O O   . LEU A 1 126 ? 8.901   -7.633  -7.231  1.00 18.55 ? 150  LEU A O   1 
ATOM   989  C CB  . LEU A 1 126 ? 10.340  -6.652  -4.737  1.00 17.82 ? 150  LEU A CB  1 
ATOM   990  C CG  . LEU A 1 126 ? 9.484   -5.387  -4.476  1.00 21.49 ? 150  LEU A CG  1 
ATOM   991  C CD1 . LEU A 1 126 ? 8.664   -5.536  -3.216  1.00 19.21 ? 150  LEU A CD1 1 
ATOM   992  C CD2 . LEU A 1 126 ? 10.400  -4.143  -4.368  1.00 20.24 ? 150  LEU A CD2 1 
ATOM   993  N N   . VAL A 1 127 ? 7.299   -7.798  -5.666  1.00 17.62 ? 151  VAL A N   1 
ATOM   994  C CA  . VAL A 1 127 ? 6.202   -7.479  -6.589  1.00 16.11 ? 151  VAL A CA  1 
ATOM   995  C C   . VAL A 1 127 ? 5.426   -6.384  -5.887  1.00 19.38 ? 151  VAL A C   1 
ATOM   996  O O   . VAL A 1 127 ? 5.088   -6.503  -4.695  1.00 19.17 ? 151  VAL A O   1 
ATOM   997  C CB  . VAL A 1 127 ? 5.298   -8.691  -6.865  1.00 17.87 ? 151  VAL A CB  1 
ATOM   998  C CG1 . VAL A 1 127 ? 4.072   -8.285  -7.716  1.00 19.75 ? 151  VAL A CG1 1 
ATOM   999  C CG2 . VAL A 1 127 ? 6.132   -9.820  -7.565  1.00 17.40 ? 151  VAL A CG2 1 
ATOM   1000 N N   . ASN A 1 128 ? 5.202   -5.296  -6.614  1.00 16.79 ? 152  ASN A N   1 
ATOM   1001 C CA  . ASN A 1 128 ? 4.549   -4.130  -6.024  1.00 16.91 ? 152  ASN A CA  1 
ATOM   1002 C C   . ASN A 1 128 ? 3.055   -4.264  -6.092  1.00 19.68 ? 152  ASN A C   1 
ATOM   1003 O O   . ASN A 1 128 ? 2.533   -5.076  -6.862  1.00 20.11 ? 152  ASN A O   1 
ATOM   1004 C CB  . ASN A 1 128 ? 5.019   -2.824  -6.705  1.00 18.60 ? 152  ASN A CB  1 
ATOM   1005 C CG  . ASN A 1 128 ? 6.434   -2.469  -6.344  1.00 22.03 ? 152  ASN A CG  1 
ATOM   1006 O OD1 . ASN A 1 128 ? 6.956   -2.916  -5.307  1.00 21.13 ? 152  ASN A OD1 1 
ATOM   1007 N ND2 . ASN A 1 128 ? 7.070   -1.639  -7.194  1.00 23.88 ? 152  ASN A ND2 1 
ATOM   1008 N N   . CYS A 1 129 ? 2.362   -3.470  -5.274  1.00 23.79 ? 153  CYS A N   1 
ATOM   1009 C CA  . CYS A 1 129 ? 0.913   -3.492  -5.287  1.00 21.99 ? 153  CYS A CA  1 
ATOM   1010 C C   . CYS A 1 129 ? 0.341   -2.132  -4.935  1.00 19.94 ? 153  CYS A C   1 
ATOM   1011 O O   . CYS A 1 129 ? 1.071   -1.153  -4.677  1.00 22.09 ? 153  CYS A O   1 
ATOM   1012 C CB  . CYS A 1 129 ? 0.375   -4.561  -4.307  1.00 23.25 ? 153  CYS A CB  1 
ATOM   1013 S SG  . CYS A 1 129 ? 1.094   -4.374  -2.614  1.00 25.39 ? 153  CYS A SG  1 
ATOM   1014 N N   . SER A 1 130 ? -0.988  -2.057  -4.940  1.00 19.19 ? 154  SER A N   1 
ATOM   1015 C CA  . SER A 1 130 ? -1.647  -0.809  -4.563  1.00 22.76 ? 154  SER A CA  1 
ATOM   1016 C C   . SER A 1 130 ? -2.849  -1.138  -3.685  1.00 24.34 ? 154  SER A C   1 
ATOM   1017 O O   . SER A 1 130 ? -3.463  -2.165  -3.873  1.00 21.12 ? 154  SER A O   1 
ATOM   1018 C CB  . SER A 1 130 ? -2.141  -0.062  -5.803  1.00 27.99 ? 154  SER A CB  1 
ATOM   1019 O OG  . SER A 1 130 ? -2.955  1.048   -5.431  1.00 26.91 ? 154  SER A OG  1 
ATOM   1020 N N   . CYS A 1 131 ? -3.164  -0.252  -2.739  1.00 27.56 ? 155  CYS A N   1 
ATOM   1021 C CA  . CYS A 1 131 ? -4.362  -0.379  -1.921  1.00 28.51 ? 155  CYS A CA  1 
ATOM   1022 C C   . CYS A 1 131 ? -5.411  0.645   -2.355  1.00 30.09 ? 155  CYS A C   1 
ATOM   1023 O O   . CYS A 1 131 ? -6.450  0.770   -1.723  1.00 32.40 ? 155  CYS A O   1 
ATOM   1024 C CB  . CYS A 1 131 ? -4.017  -0.170  -0.435  1.00 25.49 ? 155  CYS A CB  1 
ATOM   1025 S SG  . CYS A 1 131 ? -2.979  -1.483  0.255   1.00 33.14 ? 155  CYS A SG  1 
ATOM   1026 N N   . GLY A 1 132 ? -5.125  1.375   -3.431  1.00 31.72 ? 156  GLY A N   1 
ATOM   1027 C CA  . GLY A 1 132 ? -6.032  2.401   -3.932  1.00 30.21 ? 156  GLY A CA  1 
ATOM   1028 C C   . GLY A 1 132 ? -5.658  3.815   -3.545  1.00 32.25 ? 156  GLY A C   1 
ATOM   1029 O O   . GLY A 1 132 ? -4.595  4.071   -2.985  1.00 31.85 ? 156  GLY A O   1 
ATOM   1030 N N   . ASP A 1 133 ? -6.568  4.745   -3.826  1.00 29.56 ? 157  ASP A N   1 
ATOM   1031 C CA  . ASP A 1 133 ? -6.309  6.163   -3.640  1.00 32.81 ? 157  ASP A CA  1 
ATOM   1032 C C   . ASP A 1 133 ? -7.663  6.826   -3.508  1.00 32.42 ? 157  ASP A C   1 
ATOM   1033 O O   . ASP A 1 133 ? -8.439  6.869   -4.464  1.00 33.59 ? 157  ASP A O   1 
ATOM   1034 C CB  . ASP A 1 133 ? -5.555  6.723   -4.847  1.00 37.24 ? 157  ASP A CB  1 
ATOM   1035 C CG  . ASP A 1 133 ? -5.192  8.194   -4.684  1.00 44.72 ? 157  ASP A CG  1 
ATOM   1036 O OD1 . ASP A 1 133 ? -5.744  8.847   -3.772  1.00 45.98 ? 157  ASP A OD1 1 
ATOM   1037 O OD2 . ASP A 1 133 ? -4.350  8.684   -5.471  1.00 44.32 ? 157  ASP A OD2 1 
ATOM   1038 N N   . GLU A 1 134 ? -7.958  7.270   -2.296  1.00 35.16 ? 158  GLU A N   1 
ATOM   1039 C CA  . GLU A 1 134 ? -9.262  7.854   -1.968  1.00 41.58 ? 158  GLU A CA  1 
ATOM   1040 C C   . GLU A 1 134 ? -9.591  9.076   -2.826  1.00 45.34 ? 158  GLU A C   1 
ATOM   1041 O O   . GLU A 1 134 ? -10.759 9.366   -3.078  1.00 42.80 ? 158  GLU A O   1 
ATOM   1042 C CB  . GLU A 1 134 ? -9.287  8.242   -0.489  1.00 51.22 ? 158  GLU A CB  1 
ATOM   1043 C CG  . GLU A 1 134 ? -10.670 8.469   0.080   1.00 64.65 ? 158  GLU A CG  1 
ATOM   1044 C CD  . GLU A 1 134 ? -10.642 8.646   1.588   1.00 73.01 ? 158  GLU A CD  1 
ATOM   1045 O OE1 . GLU A 1 134 ? -9.551  8.924   2.136   1.00 74.47 ? 158  GLU A OE1 1 
ATOM   1046 O OE2 . GLU A 1 134 ? -11.708 8.501   2.223   1.00 76.65 ? 158  GLU A OE2 1 
ATOM   1047 N N   . SER A 1 135 ? -8.561  9.792   -3.265  1.00 41.16 ? 159  SER A N   1 
ATOM   1048 C CA  . SER A 1 135 ? -8.762  10.990  -4.078  1.00 47.12 ? 159  SER A CA  1 
ATOM   1049 C C   . SER A 1 135 ? -9.100  10.628  -5.525  1.00 45.31 ? 159  SER A C   1 
ATOM   1050 O O   . SER A 1 135 ? -9.441  11.488  -6.330  1.00 44.77 ? 159  SER A O   1 
ATOM   1051 C CB  . SER A 1 135 ? -7.532  11.912  -4.018  1.00 47.88 ? 159  SER A CB  1 
ATOM   1052 O OG  . SER A 1 135 ? -6.440  11.394  -4.765  1.00 47.54 ? 159  SER A OG  1 
ATOM   1053 N N   . VAL A 1 136 ? -8.987  9.350   -5.863  1.00 37.58 ? 160  VAL A N   1 
ATOM   1054 C CA  . VAL A 1 136 ? -9.387  8.913   -7.188  1.00 38.62 ? 160  VAL A CA  1 
ATOM   1055 C C   . VAL A 1 136 ? -10.771 8.315   -7.077  1.00 41.35 ? 160  VAL A C   1 
ATOM   1056 O O   . VAL A 1 136 ? -11.646 8.600   -7.892  1.00 42.01 ? 160  VAL A O   1 
ATOM   1057 C CB  . VAL A 1 136 ? -8.429  7.869   -7.780  1.00 38.61 ? 160  VAL A CB  1 
ATOM   1058 C CG1 . VAL A 1 136 ? -9.036  7.259   -9.050  1.00 34.53 ? 160  VAL A CG1 1 
ATOM   1059 C CG2 . VAL A 1 136 ? -7.058  8.497   -8.052  1.00 36.95 ? 160  VAL A CG2 1 
ATOM   1060 N N   . SER A 1 137 ? -10.970 7.492   -6.052  1.00 36.86 ? 161  SER A N   1 
ATOM   1061 C CA  . SER A 1 137 ? -12.268 6.877   -5.835  1.00 36.94 ? 161  SER A CA  1 
ATOM   1062 C C   . SER A 1 137 ? -12.383 6.177   -4.491  1.00 38.31 ? 161  SER A C   1 
ATOM   1063 O O   . SER A 1 137 ? -11.448 5.522   -4.027  1.00 39.05 ? 161  SER A O   1 
ATOM   1064 C CB  . SER A 1 137 ? -12.570 5.879   -6.949  1.00 34.85 ? 161  SER A CB  1 
ATOM   1065 O OG  . SER A 1 137 ? -13.857 5.323   -6.785  1.00 40.30 ? 161  SER A OG  1 
ATOM   1066 N N   . LYS A 1 138 ? -13.551 6.292   -3.871  1.00 35.32 ? 162  LYS A N   1 
ATOM   1067 C CA  . LYS A 1 138 ? -13.818 5.516   -2.662  1.00 39.71 ? 162  LYS A CA  1 
ATOM   1068 C C   . LYS A 1 138 ? -14.279 4.094   -2.976  1.00 37.55 ? 162  LYS A C   1 
ATOM   1069 O O   . LYS A 1 138 ? -14.434 3.279   -2.071  1.00 37.92 ? 162  LYS A O   1 
ATOM   1070 C CB  . LYS A 1 138 ? -14.897 6.203   -1.823  1.00 45.98 ? 162  LYS A CB  1 
ATOM   1071 C CG  . LYS A 1 138 ? -14.433 7.444   -1.099  1.00 56.05 ? 162  LYS A CG  1 
ATOM   1072 C CD  . LYS A 1 138 ? -15.618 8.136   -0.430  1.00 65.62 ? 162  LYS A CD  1 
ATOM   1073 C CE  . LYS A 1 138 ? -16.447 7.144   0.391   1.00 70.86 ? 162  LYS A CE  1 
ATOM   1074 N NZ  . LYS A 1 138 ? -17.723 7.743   0.910   1.00 75.19 ? 162  LYS A NZ  1 
ATOM   1075 N N   . ASP A 1 139 ? -14.529 3.804   -4.249  1.00 33.09 ? 163  ASP A N   1 
ATOM   1076 C CA  . ASP A 1 139 ? -15.194 2.553   -4.607  1.00 35.86 ? 163  ASP A CA  1 
ATOM   1077 C C   . ASP A 1 139 ? -14.262 1.346   -4.727  1.00 32.80 ? 163  ASP A C   1 
ATOM   1078 O O   . ASP A 1 139 ? -14.733 0.199   -4.854  1.00 34.50 ? 163  ASP A O   1 
ATOM   1079 C CB  . ASP A 1 139 ? -15.987 2.708   -5.905  1.00 33.04 ? 163  ASP A CB  1 
ATOM   1080 C CG  . ASP A 1 139 ? -17.196 3.625   -5.750  1.00 46.08 ? 163  ASP A CG  1 
ATOM   1081 O OD1 . ASP A 1 139 ? -17.660 3.842   -4.604  1.00 46.58 ? 163  ASP A OD1 1 
ATOM   1082 O OD2 . ASP A 1 139 ? -17.669 4.128   -6.786  1.00 48.48 ? 163  ASP A OD2 1 
ATOM   1083 N N   . PHE A 1 140 ? -12.951 1.584   -4.695  1.00 30.39 ? 164  PHE A N   1 
ATOM   1084 C CA  . PHE A 1 140 ? -12.006 0.489   -4.956  1.00 29.68 ? 164  PHE A CA  1 
ATOM   1085 C C   . PHE A 1 140 ? -10.894 0.387   -3.923  1.00 25.65 ? 164  PHE A C   1 
ATOM   1086 O O   . PHE A 1 140 ? -10.172 1.359   -3.659  1.00 29.53 ? 164  PHE A O   1 
ATOM   1087 C CB  . PHE A 1 140 ? -11.383 0.633   -6.350  1.00 28.71 ? 164  PHE A CB  1 
ATOM   1088 C CG  . PHE A 1 140 ? -12.395 0.827   -7.451  1.00 27.45 ? 164  PHE A CG  1 
ATOM   1089 C CD1 . PHE A 1 140 ? -13.127 -0.247  -7.936  1.00 25.72 ? 164  PHE A CD1 1 
ATOM   1090 C CD2 . PHE A 1 140 ? -12.625 2.094   -7.986  1.00 33.24 ? 164  PHE A CD2 1 
ATOM   1091 C CE1 . PHE A 1 140 ? -14.055 -0.089  -8.947  1.00 29.19 ? 164  PHE A CE1 1 
ATOM   1092 C CE2 . PHE A 1 140 ? -13.549 2.272   -8.995  1.00 32.33 ? 164  PHE A CE2 1 
ATOM   1093 C CZ  . PHE A 1 140 ? -14.278 1.191   -9.476  1.00 29.53 ? 164  PHE A CZ  1 
ATOM   1094 N N   . GLY A 1 141 ? -10.733 -0.812  -3.367  1.00 27.63 ? 165  GLY A N   1 
ATOM   1095 C CA  . GLY A 1 141 ? -9.723  -1.045  -2.356  1.00 28.27 ? 165  GLY A CA  1 
ATOM   1096 C C   . GLY A 1 141 ? -8.966  -2.333  -2.590  1.00 26.08 ? 165  GLY A C   1 
ATOM   1097 O O   . GLY A 1 141 ? -8.158  -2.736  -1.753  1.00 30.39 ? 165  GLY A O   1 
ATOM   1098 N N   . LEU A 1 142 ? -9.243  -2.999  -3.707  1.00 24.24 ? 166  LEU A N   1 
ATOM   1099 C CA  . LEU A 1 142 ? -8.513  -4.222  -4.069  1.00 22.94 ? 166  LEU A CA  1 
ATOM   1100 C C   . LEU A 1 142 ? -7.979  -4.037  -5.485  1.00 24.12 ? 166  LEU A C   1 
ATOM   1101 O O   . LEU A 1 142 ? -8.759  -3.736  -6.395  1.00 24.49 ? 166  LEU A O   1 
ATOM   1102 C CB  . LEU A 1 142 ? -9.445  -5.455  -4.003  1.00 21.23 ? 166  LEU A CB  1 
ATOM   1103 C CG  . LEU A 1 142 ? -8.880  -6.810  -4.506  1.00 21.84 ? 166  LEU A CG  1 
ATOM   1104 C CD1 . LEU A 1 142 ? -7.588  -7.173  -3.792  1.00 21.96 ? 166  LEU A CD1 1 
ATOM   1105 C CD2 . LEU A 1 142 ? -9.898  -7.978  -4.426  1.00 24.94 ? 166  LEU A CD2 1 
ATOM   1106 N N   . PHE A 1 143 ? -6.670  -4.241  -5.675  1.00 20.40 ? 167  PHE A N   1 
ATOM   1107 C CA  . PHE A 1 143 ? -6.031  -3.928  -6.947  1.00 21.07 ? 167  PHE A CA  1 
ATOM   1108 C C   . PHE A 1 143 ? -5.230  -5.063  -7.505  1.00 22.49 ? 167  PHE A C   1 
ATOM   1109 O O   . PHE A 1 143 ? -4.545  -5.771  -6.768  1.00 22.34 ? 167  PHE A O   1 
ATOM   1110 C CB  . PHE A 1 143 ? -5.130  -2.694  -6.824  1.00 21.96 ? 167  PHE A CB  1 
ATOM   1111 C CG  . PHE A 1 143 ? -5.922  -1.450  -6.717  1.00 21.51 ? 167  PHE A CG  1 
ATOM   1112 C CD1 . PHE A 1 143 ? -6.135  -0.665  -7.843  1.00 19.59 ? 167  PHE A CD1 1 
ATOM   1113 C CD2 . PHE A 1 143 ? -6.555  -1.132  -5.522  1.00 20.07 ? 167  PHE A CD2 1 
ATOM   1114 C CE1 . PHE A 1 143 ? -6.966  0.471   -7.770  1.00 24.44 ? 167  PHE A CE1 1 
ATOM   1115 C CE2 . PHE A 1 143 ? -7.384  0.023   -5.434  1.00 23.12 ? 167  PHE A CE2 1 
ATOM   1116 C CZ  . PHE A 1 143 ? -7.580  0.810   -6.557  1.00 27.55 ? 167  PHE A CZ  1 
ATOM   1117 N N   . VAL A 1 144 ? -5.310  -5.186  -8.828  1.00 19.11 ? 168  VAL A N   1 
ATOM   1118 C CA  . VAL A 1 144 ? -4.518  -6.144  -9.579  1.00 20.64 ? 168  VAL A CA  1 
ATOM   1119 C C   . VAL A 1 144 ? -3.255  -5.452  -10.060 1.00 19.55 ? 168  VAL A C   1 
ATOM   1120 O O   . VAL A 1 144 ? -3.300  -4.381  -10.689 1.00 19.81 ? 168  VAL A O   1 
ATOM   1121 C CB  . VAL A 1 144 ? -5.288  -6.640  -10.840 1.00 22.71 ? 168  VAL A CB  1 
ATOM   1122 C CG1 . VAL A 1 144 ? -4.441  -7.586  -11.654 1.00 20.90 ? 168  VAL A CG1 1 
ATOM   1123 C CG2 . VAL A 1 144 ? -6.654  -7.270  -10.468 1.00 21.04 ? 168  VAL A CG2 1 
ATOM   1124 N N   . THR A 1 145 ? -2.118  -6.079  -9.764  1.00 16.31 ? 169  THR A N   1 
ATOM   1125 C CA  . THR A 1 145 ? -0.848  -5.695  -10.331 1.00 17.34 ? 169  THR A CA  1 
ATOM   1126 C C   . THR A 1 145 ? -0.778  -6.340  -11.711 1.00 16.01 ? 169  THR A C   1 
ATOM   1127 O O   . THR A 1 145 ? -0.658  -7.563  -11.833 1.00 18.67 ? 169  THR A O   1 
ATOM   1128 C CB  . THR A 1 145 ? 0.286   -6.200  -9.432  1.00 20.46 ? 169  THR A CB  1 
ATOM   1129 O OG1 . THR A 1 145 ? 0.192   -5.516  -8.178  1.00 20.25 ? 169  THR A OG1 1 
ATOM   1130 C CG2 . THR A 1 145 ? 1.658   -5.857  -10.071 1.00 19.38 ? 169  THR A CG2 1 
ATOM   1131 N N   . TYR A 1 146 ? -0.898  -5.512  -12.746 1.00 17.77 ? 170  TYR A N   1 
ATOM   1132 C CA  . TYR A 1 146 ? -1.161  -5.992  -14.105 1.00 19.77 ? 170  TYR A CA  1 
ATOM   1133 C C   . TYR A 1 146 ? -0.030  -5.640  -15.084 1.00 18.65 ? 170  TYR A C   1 
ATOM   1134 O O   . TYR A 1 146 ? 0.096   -4.502  -15.516 1.00 20.08 ? 170  TYR A O   1 
ATOM   1135 C CB  . TYR A 1 146 ? -2.499  -5.384  -14.574 1.00 20.17 ? 170  TYR A CB  1 
ATOM   1136 C CG  . TYR A 1 146 ? -3.034  -5.883  -15.914 1.00 22.89 ? 170  TYR A CG  1 
ATOM   1137 C CD1 . TYR A 1 146 ? -4.114  -6.764  -15.975 1.00 22.41 ? 170  TYR A CD1 1 
ATOM   1138 C CD2 . TYR A 1 146 ? -2.465  -5.458  -17.107 1.00 22.14 ? 170  TYR A CD2 1 
ATOM   1139 C CE1 . TYR A 1 146 ? -4.621  -7.202  -17.188 1.00 22.45 ? 170  TYR A CE1 1 
ATOM   1140 C CE2 . TYR A 1 146 ? -2.952  -5.896  -18.336 1.00 22.70 ? 170  TYR A CE2 1 
ATOM   1141 C CZ  . TYR A 1 146 ? -4.034  -6.752  -18.368 1.00 24.06 ? 170  TYR A CZ  1 
ATOM   1142 O OH  . TYR A 1 146 ? -4.527  -7.179  -19.580 1.00 28.00 ? 170  TYR A OH  1 
ATOM   1143 N N   . PRO A 1 147 ? 0.804   -6.630  -15.445 1.00 19.55 ? 171  PRO A N   1 
ATOM   1144 C CA  . PRO A 1 147 ? 1.871   -6.338  -16.407 1.00 19.07 ? 171  PRO A CA  1 
ATOM   1145 C C   . PRO A 1 147 ? 1.294   -6.215  -17.808 1.00 17.65 ? 171  PRO A C   1 
ATOM   1146 O O   . PRO A 1 147 ? 0.610   -7.121  -18.268 1.00 18.01 ? 171  PRO A O   1 
ATOM   1147 C CB  . PRO A 1 147 ? 2.811   -7.568  -16.296 1.00 18.22 ? 171  PRO A CB  1 
ATOM   1148 C CG  . PRO A 1 147 ? 2.459   -8.200  -14.938 1.00 19.31 ? 171  PRO A CG  1 
ATOM   1149 C CD  . PRO A 1 147 ? 0.968   -7.951  -14.802 1.00 18.53 ? 171  PRO A CD  1 
ATOM   1150 N N   . LEU A 1 148 ? 1.554   -5.083  -18.455 1.00 22.33 ? 172  LEU A N   1 
ATOM   1151 C CA  . LEU A 1 148 ? 1.003   -4.784  -19.777 1.00 22.00 ? 172  LEU A CA  1 
ATOM   1152 C C   . LEU A 1 148 ? 1.662   -5.642  -20.851 1.00 23.65 ? 172  LEU A C   1 
ATOM   1153 O O   . LEU A 1 148 ? 2.860   -5.925  -20.781 1.00 25.31 ? 172  LEU A O   1 
ATOM   1154 C CB  . LEU A 1 148 ? 1.248   -3.309  -20.124 1.00 21.85 ? 172  LEU A CB  1 
ATOM   1155 C CG  . LEU A 1 148 ? 0.440   -2.285  -19.340 1.00 17.89 ? 172  LEU A CG  1 
ATOM   1156 C CD1 . LEU A 1 148 ? 0.927   -0.844  -19.701 1.00 26.24 ? 172  LEU A CD1 1 
ATOM   1157 C CD2 . LEU A 1 148 ? -1.071  -2.452  -19.639 1.00 22.14 ? 172  LEU A CD2 1 
ATOM   1158 N N   . ARG A 1 149 ? 0.876   -6.030  -21.855 1.00 24.23 ? 173  ARG A N   1 
ATOM   1159 C CA  . ARG A 1 149 ? 1.383   -6.756  -23.018 1.00 25.95 ? 173  ARG A CA  1 
ATOM   1160 C C   . ARG A 1 149 ? 0.993   -5.990  -24.299 1.00 27.29 ? 173  ARG A C   1 
ATOM   1161 O O   . ARG A 1 149 ? 0.070   -5.175  -24.273 1.00 27.15 ? 173  ARG A O   1 
ATOM   1162 C CB  . ARG A 1 149 ? 0.841   -8.206  -23.040 1.00 20.05 ? 173  ARG A CB  1 
ATOM   1163 C CG  . ARG A 1 149 ? 1.420   -9.067  -21.916 1.00 24.90 ? 173  ARG A CG  1 
ATOM   1164 C CD  . ARG A 1 149 ? 0.868   -10.513 -22.002 1.00 32.53 ? 173  ARG A CD  1 
ATOM   1165 N NE  . ARG A 1 149 ? 0.923   -10.984 -23.383 1.00 30.45 ? 173  ARG A NE  1 
ATOM   1166 C CZ  . ARG A 1 149 ? 1.975   -11.571 -23.937 1.00 32.68 ? 173  ARG A CZ  1 
ATOM   1167 N NH1 . ARG A 1 149 ? 3.070   -11.812 -23.223 1.00 33.15 ? 173  ARG A NH1 1 
ATOM   1168 N NH2 . ARG A 1 149 ? 1.924   -11.929 -25.219 1.00 33.93 ? 173  ARG A NH2 1 
ATOM   1169 N N   . PRO A 1 150 ? 1.703   -6.255  -25.414 1.00 33.13 ? 174  PRO A N   1 
ATOM   1170 C CA  . PRO A 1 150 ? 1.488   -5.514  -26.666 1.00 33.89 ? 174  PRO A CA  1 
ATOM   1171 C C   . PRO A 1 150 ? 0.034   -5.504  -27.101 1.00 35.06 ? 174  PRO A C   1 
ATOM   1172 O O   . PRO A 1 150 ? -0.419  -4.518  -27.691 1.00 35.82 ? 174  PRO A O   1 
ATOM   1173 C CB  . PRO A 1 150 ? 2.339   -6.280  -27.685 1.00 37.66 ? 174  PRO A CB  1 
ATOM   1174 C CG  . PRO A 1 150 ? 3.410   -6.926  -26.878 1.00 36.07 ? 174  PRO A CG  1 
ATOM   1175 C CD  . PRO A 1 150 ? 2.762   -7.271  -25.551 1.00 32.51 ? 174  PRO A CD  1 
ATOM   1176 N N   . GLU A 1 151 ? -0.708  -6.559  -26.788 1.00 28.52 ? 175  GLU A N   1 
ATOM   1177 C CA  . GLU A 1 151 ? -2.106  -6.610  -27.195 1.00 36.78 ? 175  GLU A CA  1 
ATOM   1178 C C   . GLU A 1 151 ? -3.083  -5.800  -26.315 1.00 38.98 ? 175  GLU A C   1 
ATOM   1179 O O   . GLU A 1 151 ? -4.241  -5.644  -26.686 1.00 37.37 ? 175  GLU A O   1 
ATOM   1180 C CB  . GLU A 1 151 ? -2.591  -8.063  -27.353 1.00 39.67 ? 175  GLU A CB  1 
ATOM   1181 C CG  . GLU A 1 151 ? -2.704  -8.866  -26.059 1.00 37.68 ? 175  GLU A CG  1 
ATOM   1182 C CD  . GLU A 1 151 ? -1.390  -9.504  -25.626 1.00 37.38 ? 175  GLU A CD  1 
ATOM   1183 O OE1 . GLU A 1 151 ? -0.306  -9.133  -26.149 1.00 36.96 ? 175  GLU A OE1 1 
ATOM   1184 O OE2 . GLU A 1 151 ? -1.451  -10.401 -24.755 1.00 40.22 ? 175  GLU A OE2 1 
ATOM   1185 N N   . ASP A 1 152 ? -2.630  -5.291  -25.166 1.00 33.87 ? 176  ASP A N   1 
ATOM   1186 C CA  . ASP A 1 152 ? -3.505  -4.507  -24.269 1.00 29.15 ? 176  ASP A CA  1 
ATOM   1187 C C   . ASP A 1 152 ? -3.588  -3.052  -24.723 1.00 28.92 ? 176  ASP A C   1 
ATOM   1188 O O   . ASP A 1 152 ? -2.635  -2.530  -25.295 1.00 27.36 ? 176  ASP A O   1 
ATOM   1189 C CB  . ASP A 1 152 ? -2.924  -4.480  -22.841 1.00 29.05 ? 176  ASP A CB  1 
ATOM   1190 C CG  . ASP A 1 152 ? -2.936  -5.839  -22.163 1.00 31.03 ? 176  ASP A CG  1 
ATOM   1191 O OD1 . ASP A 1 152 ? -3.984  -6.506  -22.211 1.00 31.58 ? 176  ASP A OD1 1 
ATOM   1192 O OD2 . ASP A 1 152 ? -1.906  -6.216  -21.549 1.00 29.53 ? 176  ASP A OD2 1 
ATOM   1193 N N   . SER A 1 153 ? -4.714  -2.392  -24.444 1.00 29.22 ? 177  SER A N   1 
ATOM   1194 C CA  . SER A 1 153 ? -4.826  -0.945  -24.599 1.00 29.65 ? 177  SER A CA  1 
ATOM   1195 C C   . SER A 1 153 ? -5.668  -0.450  -23.442 1.00 24.07 ? 177  SER A C   1 
ATOM   1196 O O   . SER A 1 153 ? -6.223  -1.246  -22.695 1.00 28.01 ? 177  SER A O   1 
ATOM   1197 C CB  . SER A 1 153 ? -5.534  -0.572  -25.907 1.00 30.18 ? 177  SER A CB  1 
ATOM   1198 O OG  . SER A 1 153 ? -6.810  -1.200  -25.950 1.00 31.77 ? 177  SER A OG  1 
ATOM   1199 N N   . LEU A 1 154 ? -5.772  0.863   -23.285 1.00 29.20 ? 178  LEU A N   1 
ATOM   1200 C CA  . LEU A 1 154 ? -6.634  1.377   -22.240 1.00 30.04 ? 178  LEU A CA  1 
ATOM   1201 C C   . LEU A 1 154 ? -8.087  0.918   -22.422 1.00 31.81 ? 178  LEU A C   1 
ATOM   1202 O O   . LEU A 1 154 ? -8.752  0.531   -21.457 1.00 29.14 ? 178  LEU A O   1 
ATOM   1203 C CB  . LEU A 1 154 ? -6.542  2.898   -22.163 1.00 26.86 ? 178  LEU A CB  1 
ATOM   1204 C CG  . LEU A 1 154 ? -7.479  3.568   -21.154 1.00 31.92 ? 178  LEU A CG  1 
ATOM   1205 C CD1 . LEU A 1 154 ? -7.058  3.221   -19.738 1.00 29.99 ? 178  LEU A CD1 1 
ATOM   1206 C CD2 . LEU A 1 154 ? -7.448  5.071   -21.341 1.00 34.94 ? 178  LEU A CD2 1 
ATOM   1207 N N   . SER A 1 155 ? -8.593  0.969   -23.652 1.00 32.84 ? 179  SER A N   1 
ATOM   1208 C CA  . SER A 1 155 ? -9.993  0.596   -23.860 1.00 32.21 ? 179  SER A CA  1 
ATOM   1209 C C   . SER A 1 155 ? -10.206 -0.905  -23.639 1.00 33.63 ? 179  SER A C   1 
ATOM   1210 O O   . SER A 1 155 ? -11.231 -1.323  -23.106 1.00 32.51 ? 179  SER A O   1 
ATOM   1211 C CB  . SER A 1 155 ? -10.499 1.016   -25.247 1.00 40.01 ? 179  SER A CB  1 
ATOM   1212 O OG  . SER A 1 155 ? -9.644  0.547   -26.268 1.00 45.86 ? 179  SER A OG  1 
ATOM   1213 N N   . SER A 1 156 ? -9.233  -1.714  -24.025 1.00 34.80 ? 180  SER A N   1 
ATOM   1214 C CA  . SER A 1 156 ? -9.385  -3.164  -23.883 1.00 35.16 ? 180  SER A CA  1 
ATOM   1215 C C   . SER A 1 156 ? -9.368  -3.585  -22.417 1.00 35.97 ? 180  SER A C   1 
ATOM   1216 O O   . SER A 1 156 ? -10.152 -4.446  -21.999 1.00 30.96 ? 180  SER A O   1 
ATOM   1217 C CB  . SER A 1 156 ? -8.342  -3.919  -24.712 1.00 30.11 ? 180  SER A CB  1 
ATOM   1218 O OG  . SER A 1 156 ? -7.052  -3.941  -24.090 1.00 32.37 ? 180  SER A OG  1 
ATOM   1219 N N   . ILE A 1 157 ? -8.500  -2.955  -21.625 1.00 29.53 ? 181  ILE A N   1 
ATOM   1220 C CA  . ILE A 1 157 ? -8.487  -3.215  -20.188 1.00 27.57 ? 181  ILE A CA  1 
ATOM   1221 C C   . ILE A 1 157 ? -9.719  -2.633  -19.457 1.00 30.43 ? 181  ILE A C   1 
ATOM   1222 O O   . ILE A 1 157 ? -10.248 -3.241  -18.515 1.00 31.77 ? 181  ILE A O   1 
ATOM   1223 C CB  . ILE A 1 157 ? -7.156  -2.718  -19.574 1.00 29.90 ? 181  ILE A CB  1 
ATOM   1224 C CG1 . ILE A 1 157 ? -6.001  -3.558  -20.141 1.00 23.70 ? 181  ILE A CG1 1 
ATOM   1225 C CG2 . ILE A 1 157 ? -7.222  -2.776  -18.038 1.00 29.22 ? 181  ILE A CG2 1 
ATOM   1226 C CD1 . ILE A 1 157 ? -4.599  -3.010  -19.802 1.00 25.69 ? 181  ILE A CD1 1 
ATOM   1227 N N   . ALA A 1 158 ? -10.192 -1.465  -19.887 1.00 30.07 ? 182  ALA A N   1 
ATOM   1228 C CA  . ALA A 1 158 ? -11.392 -0.911  -19.270 1.00 31.29 ? 182  ALA A CA  1 
ATOM   1229 C C   . ALA A 1 158 ? -12.526 -1.884  -19.521 1.00 35.52 ? 182  ALA A C   1 
ATOM   1230 O O   . ALA A 1 158 ? -13.346 -2.146  -18.638 1.00 35.99 ? 182  ALA A O   1 
ATOM   1231 C CB  . ALA A 1 158 ? -11.734 0.466   -19.827 1.00 31.95 ? 182  ALA A CB  1 
ATOM   1232 N N   . ARG A 1 159 ? -12.561 -2.424  -20.732 1.00 38.13 ? 183  ARG A N   1 
ATOM   1233 C CA  . ARG A 1 159 ? -13.649 -3.329  -21.109 1.00 46.73 ? 183  ARG A CA  1 
ATOM   1234 C C   . ARG A 1 159 ? -13.626 -4.603  -20.269 1.00 42.36 ? 183  ARG A C   1 
ATOM   1235 O O   . ARG A 1 159 ? -14.642 -4.982  -19.694 1.00 47.48 ? 183  ARG A O   1 
ATOM   1236 C CB  . ARG A 1 159 ? -13.608 -3.645  -22.608 1.00 51.28 ? 183  ARG A CB  1 
ATOM   1237 C CG  . ARG A 1 159 ? -14.778 -4.472  -23.118 1.00 59.52 ? 183  ARG A CG  1 
ATOM   1238 C CD  . ARG A 1 159 ? -14.847 -4.443  -24.643 1.00 69.05 ? 183  ARG A CD  1 
ATOM   1239 N NE  . ARG A 1 159 ? -13.530 -4.616  -25.252 1.00 80.53 ? 183  ARG A NE  1 
ATOM   1240 C CZ  . ARG A 1 159 ? -13.008 -5.788  -25.608 1.00 86.01 ? 183  ARG A CZ  1 
ATOM   1241 N NH1 . ARG A 1 159 ? -13.698 -6.908  -25.424 1.00 87.81 ? 183  ARG A NH1 1 
ATOM   1242 N NH2 . ARG A 1 159 ? -11.794 -5.839  -26.149 1.00 84.18 ? 183  ARG A NH2 1 
ATOM   1243 N N   . SER A 1 160 ? -12.469 -5.249  -20.180 1.00 40.32 ? 184  SER A N   1 
ATOM   1244 C CA  . SER A 1 160 ? -12.362 -6.531  -19.482 1.00 41.43 ? 184  SER A CA  1 
ATOM   1245 C C   . SER A 1 160 ? -12.461 -6.406  -17.959 1.00 45.68 ? 184  SER A C   1 
ATOM   1246 O O   . SER A 1 160 ? -12.959 -7.310  -17.281 1.00 43.40 ? 184  SER A O   1 
ATOM   1247 C CB  . SER A 1 160 ? -11.063 -7.236  -19.857 1.00 40.06 ? 184  SER A CB  1 
ATOM   1248 O OG  . SER A 1 160 ? -9.929  -6.543  -19.363 1.00 36.04 ? 184  SER A OG  1 
ATOM   1249 N N   . SER A 1 161 ? -11.985 -5.286  -17.421 1.00 37.85 ? 185  SER A N   1 
ATOM   1250 C CA  . SER A 1 161 ? -11.949 -5.099  -15.979 1.00 31.05 ? 185  SER A CA  1 
ATOM   1251 C C   . SER A 1 161 ? -13.305 -4.627  -15.446 1.00 32.90 ? 185  SER A C   1 
ATOM   1252 O O   . SER A 1 161 ? -13.603 -4.789  -14.269 1.00 37.24 ? 185  SER A O   1 
ATOM   1253 C CB  . SER A 1 161 ? -10.868 -4.075  -15.606 1.00 31.53 ? 185  SER A CB  1 
ATOM   1254 O OG  . SER A 1 161 ? -11.216 -2.792  -16.127 1.00 29.22 ? 185  SER A OG  1 
ATOM   1255 N N   . GLY A 1 162 ? -14.118 -4.042  -16.314 1.00 34.61 ? 186  GLY A N   1 
ATOM   1256 C CA  . GLY A 1 162 ? -15.364 -3.414  -15.898 1.00 39.25 ? 186  GLY A CA  1 
ATOM   1257 C C   . GLY A 1 162 ? -15.169 -2.100  -15.151 1.00 37.99 ? 186  GLY A C   1 
ATOM   1258 O O   . GLY A 1 162 ? -16.046 -1.659  -14.411 1.00 37.10 ? 186  GLY A O   1 
ATOM   1259 N N   . VAL A 1 163 ? -14.008 -1.480  -15.334 1.00 30.99 ? 187  VAL A N   1 
ATOM   1260 C CA  . VAL A 1 163 ? -13.689 -0.189  -14.704 1.00 30.77 ? 187  VAL A CA  1 
ATOM   1261 C C   . VAL A 1 163 ? -13.569 0.877   -15.802 1.00 29.80 ? 187  VAL A C   1 
ATOM   1262 O O   . VAL A 1 163 ? -13.049 0.585   -16.874 1.00 32.98 ? 187  VAL A O   1 
ATOM   1263 C CB  . VAL A 1 163 ? -12.361 -0.271  -13.883 1.00 32.67 ? 187  VAL A CB  1 
ATOM   1264 C CG1 . VAL A 1 163 ? -12.008 1.072   -13.277 1.00 26.93 ? 187  VAL A CG1 1 
ATOM   1265 C CG2 . VAL A 1 163 ? -12.470 -1.323  -12.782 1.00 37.50 ? 187  VAL A CG2 1 
ATOM   1266 N N   . SER A 1 164 ? -14.084 2.091   -15.572 1.00 33.47 ? 188  SER A N   1 
ATOM   1267 C CA  . SER A 1 164 ? -14.011 3.116   -16.615 1.00 35.31 ? 188  SER A CA  1 
ATOM   1268 C C   . SER A 1 164 ? -12.568 3.474   -16.955 1.00 34.79 ? 188  SER A C   1 
ATOM   1269 O O   . SER A 1 164 ? -11.681 3.426   -16.093 1.00 31.51 ? 188  SER A O   1 
ATOM   1270 C CB  . SER A 1 164 ? -14.787 4.385   -16.256 1.00 41.34 ? 188  SER A CB  1 
ATOM   1271 O OG  . SER A 1 164 ? -14.047 5.194   -15.371 1.00 39.09 ? 188  SER A OG  1 
ATOM   1272 N N   . ALA A 1 165 ? -12.357 3.822   -18.222 1.00 34.07 ? 189  ALA A N   1 
ATOM   1273 C CA  . ALA A 1 165 ? -11.058 4.254   -18.719 1.00 33.64 ? 189  ALA A CA  1 
ATOM   1274 C C   . ALA A 1 165 ? -10.505 5.428   -17.943 1.00 33.05 ? 189  ALA A C   1 
ATOM   1275 O O   . ALA A 1 165 ? -9.326  5.433   -17.613 1.00 33.25 ? 189  ALA A O   1 
ATOM   1276 C CB  . ALA A 1 165 ? -11.137 4.576   -20.196 1.00 35.54 ? 189  ALA A CB  1 
ATOM   1277 N N   . ASP A 1 166 ? -11.342 6.438   -17.669 1.00 29.76 ? 190  ASP A N   1 
ATOM   1278 C CA  . ASP A 1 166 ? -10.889 7.602   -16.905 1.00 32.56 ? 190  ASP A CA  1 
ATOM   1279 C C   . ASP A 1 166 ? -10.359 7.243   -15.507 1.00 31.69 ? 190  ASP A C   1 
ATOM   1280 O O   . ASP A 1 166 ? -9.320  7.745   -15.073 1.00 31.82 ? 190  ASP A O   1 
ATOM   1281 C CB  . ASP A 1 166 ? -12.011 8.641   -16.790 1.00 36.27 ? 190  ASP A CB  1 
ATOM   1282 C CG  . ASP A 1 166 ? -11.618 9.827   -15.926 1.00 45.96 ? 190  ASP A CG  1 
ATOM   1283 O OD1 . ASP A 1 166 ? -10.715 10.590  -16.338 1.00 47.90 ? 190  ASP A OD1 1 
ATOM   1284 O OD2 . ASP A 1 166 ? -12.209 9.997   -14.835 1.00 49.81 ? 190  ASP A OD2 1 
ATOM   1285 N N   . ILE A 1 167 ? -11.090 6.388   -14.798 1.00 29.54 ? 191  ILE A N   1 
ATOM   1286 C CA  . ILE A 1 167 ? -10.638 5.889   -13.492 1.00 28.99 ? 191  ILE A CA  1 
ATOM   1287 C C   . ILE A 1 167 ? -9.302  5.121   -13.584 1.00 28.13 ? 191  ILE A C   1 
ATOM   1288 O O   . ILE A 1 167 ? -8.378  5.396   -12.822 1.00 25.90 ? 191  ILE A O   1 
ATOM   1289 C CB  . ILE A 1 167 ? -11.740 5.048   -12.810 1.00 30.74 ? 191  ILE A CB  1 
ATOM   1290 C CG1 . ILE A 1 167 ? -12.923 5.956   -12.425 1.00 35.27 ? 191  ILE A CG1 1 
ATOM   1291 C CG2 . ILE A 1 167 ? -11.194 4.297   -11.581 1.00 31.71 ? 191  ILE A CG2 1 
ATOM   1292 C CD1 . ILE A 1 167 ? -12.653 6.822   -11.225 1.00 42.53 ? 191  ILE A CD1 1 
ATOM   1293 N N   . LEU A 1 168 ? -9.188  4.183   -14.521 1.00 25.85 ? 192  LEU A N   1 
ATOM   1294 C CA  . LEU A 1 168 ? -7.926  3.454   -14.693 1.00 26.06 ? 192  LEU A CA  1 
ATOM   1295 C C   . LEU A 1 168 ? -6.774  4.407   -14.947 1.00 27.54 ? 192  LEU A C   1 
ATOM   1296 O O   . LEU A 1 168 ? -5.662  4.249   -14.412 1.00 23.90 ? 192  LEU A O   1 
ATOM   1297 C CB  . LEU A 1 168 ? -8.007  2.479   -15.864 1.00 23.99 ? 192  LEU A CB  1 
ATOM   1298 C CG  . LEU A 1 168 ? -9.039  1.372   -15.685 1.00 28.83 ? 192  LEU A CG  1 
ATOM   1299 C CD1 . LEU A 1 168 ? -9.171  0.627   -16.985 1.00 30.43 ? 192  LEU A CD1 1 
ATOM   1300 C CD2 . LEU A 1 168 ? -8.577  0.447   -14.555 1.00 31.35 ? 192  LEU A CD2 1 
ATOM   1301 N N   . GLN A 1 169 ? -7.024  5.392   -15.788 1.00 27.43 ? 193  GLN A N   1 
ATOM   1302 C CA  . GLN A 1 169 ? -5.959  6.315   -16.125 1.00 27.62 ? 193  GLN A CA  1 
ATOM   1303 C C   . GLN A 1 169 ? -5.559  7.144   -14.903 1.00 31.86 ? 193  GLN A C   1 
ATOM   1304 O O   . GLN A 1 169 ? -4.384  7.448   -14.709 1.00 32.03 ? 193  GLN A O   1 
ATOM   1305 C CB  . GLN A 1 169 ? -6.370  7.216   -17.291 1.00 26.37 ? 193  GLN A CB  1 
ATOM   1306 C CG  . GLN A 1 169 ? -5.192  8.012   -17.889 1.00 25.12 ? 193  GLN A CG  1 
ATOM   1307 C CD  . GLN A 1 169 ? -4.155  7.111   -18.554 1.00 29.33 ? 193  GLN A CD  1 
ATOM   1308 O OE1 . GLN A 1 169 ? -4.311  6.724   -19.706 1.00 29.97 ? 193  GLN A OE1 1 
ATOM   1309 N NE2 . GLN A 1 169 ? -3.092  6.781   -17.828 1.00 24.75 ? 193  GLN A NE2 1 
ATOM   1310 N N   . ARG A 1 170 ? -6.533  7.502   -14.069 1.00 26.67 ? 194  ARG A N   1 
ATOM   1311 C CA  . ARG A 1 170 ? -6.249  8.345   -12.906 1.00 25.90 ? 194  ARG A CA  1 
ATOM   1312 C C   . ARG A 1 170 ? -5.444  7.550   -11.863 1.00 26.70 ? 194  ARG A C   1 
ATOM   1313 O O   . ARG A 1 170 ? -4.638  8.122   -11.127 1.00 26.42 ? 194  ARG A O   1 
ATOM   1314 C CB  . ARG A 1 170 ? -7.549  8.876   -12.284 1.00 26.41 ? 194  ARG A CB  1 
ATOM   1315 C CG  . ARG A 1 170 ? -8.164  10.087  -12.992 1.00 30.33 ? 194  ARG A CG  1 
ATOM   1316 C CD  . ARG A 1 170 ? -9.553  10.373  -12.364 1.00 37.15 ? 194  ARG A CD  1 
ATOM   1317 N NE  . ARG A 1 170 ? -10.206 11.553  -12.929 1.00 47.89 ? 194  ARG A NE  1 
ATOM   1318 C CZ  . ARG A 1 170 ? -10.237 12.762  -12.365 1.00 47.74 ? 194  ARG A CZ  1 
ATOM   1319 N NH1 . ARG A 1 170 ? -9.632  12.991  -11.203 1.00 44.39 ? 194  ARG A NH1 1 
ATOM   1320 N NH2 . ARG A 1 170 ? -10.876 13.756  -12.974 1.00 47.75 ? 194  ARG A NH2 1 
ATOM   1321 N N   . TYR A 1 171 ? -5.681  6.238   -11.787 1.00 27.40 ? 195  TYR A N   1 
ATOM   1322 C CA  . TYR A 1 171 ? -4.887  5.389   -10.893 1.00 25.70 ? 195  TYR A CA  1 
ATOM   1323 C C   . TYR A 1 171 ? -3.475  5.219   -11.420 1.00 26.83 ? 195  TYR A C   1 
ATOM   1324 O O   . TYR A 1 171 ? -2.583  4.785   -10.691 1.00 26.21 ? 195  TYR A O   1 
ATOM   1325 C CB  . TYR A 1 171 ? -5.498  3.989   -10.734 1.00 24.56 ? 195  TYR A CB  1 
ATOM   1326 C CG  . TYR A 1 171 ? -6.645  3.949   -9.745  1.00 26.49 ? 195  TYR A CG  1 
ATOM   1327 C CD1 . TYR A 1 171 ? -6.468  4.362   -8.425  1.00 25.09 ? 195  TYR A CD1 1 
ATOM   1328 C CD2 . TYR A 1 171 ? -7.885  3.472   -10.124 1.00 28.59 ? 195  TYR A CD2 1 
ATOM   1329 C CE1 . TYR A 1 171 ? -7.523  4.324   -7.516  1.00 23.99 ? 195  TYR A CE1 1 
ATOM   1330 C CE2 . TYR A 1 171 ? -8.942  3.422   -9.229  1.00 28.54 ? 195  TYR A CE2 1 
ATOM   1331 C CZ  . TYR A 1 171 ? -8.749  3.838   -7.928  1.00 28.97 ? 195  TYR A CZ  1 
ATOM   1332 O OH  . TYR A 1 171 ? -9.796  3.775   -7.041  1.00 29.85 ? 195  TYR A OH  1 
ATOM   1333 N N   . ASN A 1 172 ? -3.280  5.509   -12.701 1.00 26.47 ? 196  ASN A N   1 
ATOM   1334 C CA  . ASN A 1 172 ? -1.985  5.240   -13.331 1.00 25.34 ? 196  ASN A CA  1 
ATOM   1335 C C   . ASN A 1 172 ? -1.570  6.470   -14.148 1.00 25.62 ? 196  ASN A C   1 
ATOM   1336 O O   . ASN A 1 172 ? -1.414  6.411   -15.367 1.00 26.00 ? 196  ASN A O   1 
ATOM   1337 C CB  . ASN A 1 172 ? -2.052  3.991   -14.206 1.00 22.10 ? 196  ASN A CB  1 
ATOM   1338 C CG  . ASN A 1 172 ? -2.415  2.726   -13.414 1.00 20.61 ? 196  ASN A CG  1 
ATOM   1339 O OD1 . ASN A 1 172 ? -1.540  2.061   -12.851 1.00 21.02 ? 196  ASN A OD1 1 
ATOM   1340 N ND2 . ASN A 1 172 ? -3.715  2.410   -13.346 1.00 20.70 ? 196  ASN A ND2 1 
ATOM   1341 N N   . PRO A 1 173 ? -1.409  7.596   -13.460 1.00 28.87 ? 197  PRO A N   1 
ATOM   1342 C CA  . PRO A 1 173 ? -1.333  8.872   -14.177 1.00 25.39 ? 197  PRO A CA  1 
ATOM   1343 C C   . PRO A 1 173 ? -0.121  8.959   -15.119 1.00 29.18 ? 197  PRO A C   1 
ATOM   1344 O O   . PRO A 1 173 ? 0.994   8.616   -14.728 1.00 27.04 ? 197  PRO A O   1 
ATOM   1345 C CB  . PRO A 1 173 ? -1.250  9.909   -13.044 1.00 30.25 ? 197  PRO A CB  1 
ATOM   1346 C CG  . PRO A 1 173 ? -0.675  9.177   -11.885 1.00 28.85 ? 197  PRO A CG  1 
ATOM   1347 C CD  . PRO A 1 173 ? -1.190  7.750   -12.008 1.00 28.09 ? 197  PRO A CD  1 
ATOM   1348 N N   . GLY A 1 174 ? -0.356  9.396   -16.358 1.00 25.82 ? 198  GLY A N   1 
ATOM   1349 C CA  . GLY A 1 174 ? 0.726   9.625   -17.301 1.00 25.15 ? 198  GLY A CA  1 
ATOM   1350 C C   . GLY A 1 174 ? 1.159   8.369   -18.038 1.00 23.03 ? 198  GLY A C   1 
ATOM   1351 O O   . GLY A 1 174 ? 1.998   8.448   -18.957 1.00 26.23 ? 198  GLY A O   1 
ATOM   1352 N N   . VAL A 1 175 ? 0.590   7.226   -17.646 1.00 23.50 ? 199  VAL A N   1 
ATOM   1353 C CA  . VAL A 1 175 ? 1.009   5.915   -18.166 1.00 23.26 ? 199  VAL A CA  1 
ATOM   1354 C C   . VAL A 1 175 ? 0.239   5.499   -19.423 1.00 24.46 ? 199  VAL A C   1 
ATOM   1355 O O   . VAL A 1 175 ? -0.998  5.416   -19.409 1.00 25.48 ? 199  VAL A O   1 
ATOM   1356 C CB  . VAL A 1 175 ? 0.848   4.805   -17.094 1.00 24.49 ? 199  VAL A CB  1 
ATOM   1357 C CG1 . VAL A 1 175 ? 1.260   3.448   -17.663 1.00 20.86 ? 199  VAL A CG1 1 
ATOM   1358 C CG2 . VAL A 1 175 ? 1.668   5.140   -15.840 1.00 28.21 ? 199  VAL A CG2 1 
ATOM   1359 N N   . ASN A 1 176 ? 0.972   5.261   -20.512 1.00 23.93 ? 200  ASN A N   1 
ATOM   1360 C CA  . ASN A 1 176 ? 0.360   4.820   -21.771 1.00 26.56 ? 200  ASN A CA  1 
ATOM   1361 C C   . ASN A 1 176 ? -0.005  3.324   -21.687 1.00 25.38 ? 200  ASN A C   1 
ATOM   1362 O O   . ASN A 1 176 ? 0.891   2.474   -21.662 1.00 25.00 ? 200  ASN A O   1 
ATOM   1363 C CB  . ASN A 1 176 ? 1.347   5.040   -22.917 1.00 31.37 ? 200  ASN A CB  1 
ATOM   1364 C CG  . ASN A 1 176 ? 0.816   4.557   -24.258 1.00 34.01 ? 200  ASN A CG  1 
ATOM   1365 O OD1 . ASN A 1 176 ? -0.353  4.204   -24.383 1.00 33.34 ? 200  ASN A OD1 1 
ATOM   1366 N ND2 . ASN A 1 176 ? 1.679   4.551   -25.271 1.00 36.60 ? 200  ASN A ND2 1 
ATOM   1367 N N   . PHE A 1 177 ? -1.296  3.002   -21.631 1.00 25.91 ? 201  PHE A N   1 
ATOM   1368 C CA  . PHE A 1 177 ? -1.714  1.591   -21.451 1.00 25.44 ? 201  PHE A CA  1 
ATOM   1369 C C   . PHE A 1 177 ? -1.466  0.744   -22.709 1.00 28.65 ? 201  PHE A C   1 
ATOM   1370 O O   . PHE A 1 177 ? -1.648  -0.491  -22.701 1.00 28.43 ? 201  PHE A O   1 
ATOM   1371 C CB  . PHE A 1 177 ? -3.195  1.479   -21.081 1.00 26.49 ? 201  PHE A CB  1 
ATOM   1372 C CG  . PHE A 1 177 ? -3.504  1.696   -19.612 1.00 24.60 ? 201  PHE A CG  1 
ATOM   1373 C CD1 . PHE A 1 177 ? -4.207  0.726   -18.888 1.00 25.09 ? 201  PHE A CD1 1 
ATOM   1374 C CD2 . PHE A 1 177 ? -3.138  2.872   -18.966 1.00 25.83 ? 201  PHE A CD2 1 
ATOM   1375 C CE1 . PHE A 1 177 ? -4.533  0.932   -17.540 1.00 27.06 ? 201  PHE A CE1 1 
ATOM   1376 C CE2 . PHE A 1 177 ? -3.469  3.092   -17.622 1.00 26.15 ? 201  PHE A CE2 1 
ATOM   1377 C CZ  . PHE A 1 177 ? -4.158  2.116   -16.906 1.00 25.94 ? 201  PHE A CZ  1 
ATOM   1378 N N   . ASN A 1 178 ? -1.063  1.407   -23.783 1.00 27.26 ? 202  ASN A N   1 
ATOM   1379 C CA  . ASN A 1 178 ? -0.754  0.722   -25.023 1.00 32.39 ? 202  ASN A CA  1 
ATOM   1380 C C   . ASN A 1 178 ? 0.758   0.535   -25.241 1.00 31.08 ? 202  ASN A C   1 
ATOM   1381 O O   . ASN A 1 178 ? 1.196   0.196   -26.339 1.00 34.70 ? 202  ASN A O   1 
ATOM   1382 C CB  . ASN A 1 178 ? -1.356  1.517   -26.186 1.00 35.60 ? 202  ASN A CB  1 
ATOM   1383 C CG  . ASN A 1 178 ? -1.221  0.804   -27.511 1.00 47.18 ? 202  ASN A CG  1 
ATOM   1384 O OD1 . ASN A 1 178 ? -1.503  -0.394  -27.621 1.00 50.25 ? 202  ASN A OD1 1 
ATOM   1385 N ND2 . ASN A 1 178 ? -0.777  1.537   -28.530 1.00 48.94 ? 202  ASN A ND2 1 
ATOM   1386 N N   . SER A 1 179 ? 1.565   0.766   -24.207 1.00 27.84 ? 203  SER A N   1 
ATOM   1387 C CA  . SER A 1 179 ? 3.011   0.778   -24.387 1.00 27.60 ? 203  SER A CA  1 
ATOM   1388 C C   . SER A 1 179 ? 3.622   -0.621  -24.459 1.00 30.82 ? 203  SER A C   1 
ATOM   1389 O O   . SER A 1 179 ? 4.740   -0.781  -24.941 1.00 37.20 ? 203  SER A O   1 
ATOM   1390 C CB  . SER A 1 179 ? 3.686   1.551   -23.262 1.00 34.70 ? 203  SER A CB  1 
ATOM   1391 O OG  . SER A 1 179 ? 3.463   0.887   -22.040 1.00 33.57 ? 203  SER A OG  1 
ATOM   1392 N N   . GLY A 1 180 ? 2.911   -1.615  -23.948 1.00 31.73 ? 204  GLY A N   1 
ATOM   1393 C CA  . GLY A 1 180 ? 3.332   -3.003  -24.104 1.00 31.90 ? 204  GLY A CA  1 
ATOM   1394 C C   . GLY A 1 180 ? 4.297   -3.503  -23.047 1.00 32.04 ? 204  GLY A C   1 
ATOM   1395 O O   . GLY A 1 180 ? 4.788   -4.621  -23.131 1.00 31.61 ? 204  GLY A O   1 
ATOM   1396 N N   . ASN A 1 181 ? 4.582   -2.684  -22.048 1.00 28.89 ? 205  ASN A N   1 
ATOM   1397 C CA  . ASN A 1 181 ? 5.480   -3.111  -20.979 1.00 34.27 ? 205  ASN A CA  1 
ATOM   1398 C C   . ASN A 1 181 ? 5.236   -2.362  -19.660 1.00 28.94 ? 205  ASN A C   1 
ATOM   1399 O O   . ASN A 1 181 ? 4.540   -1.354  -19.629 1.00 30.45 ? 205  ASN A O   1 
ATOM   1400 C CB  . ASN A 1 181 ? 6.931   -2.946  -21.435 1.00 43.06 ? 205  ASN A CB  1 
ATOM   1401 C CG  . ASN A 1 181 ? 7.191   -1.580  -21.985 1.00 50.56 ? 205  ASN A CG  1 
ATOM   1402 O OD1 . ASN A 1 181 ? 7.088   -0.597  -21.259 1.00 54.91 ? 205  ASN A OD1 1 
ATOM   1403 N ND2 . ASN A 1 181 ? 7.500   -1.496  -23.278 1.00 52.14 ? 205  ASN A ND2 1 
ATOM   1404 N N   . GLY A 1 182 ? 5.810   -2.854  -18.570 1.00 28.59 ? 206  GLY A N   1 
ATOM   1405 C CA  . GLY A 1 182 ? 5.622   -2.230  -17.273 1.00 25.27 ? 206  GLY A CA  1 
ATOM   1406 C C   . GLY A 1 182 ? 4.296   -2.628  -16.647 1.00 25.33 ? 206  GLY A C   1 
ATOM   1407 O O   . GLY A 1 182 ? 3.579   -3.454  -17.191 1.00 26.98 ? 206  GLY A O   1 
ATOM   1408 N N   . ILE A 1 183 ? 3.977   -2.076  -15.483 1.00 20.12 ? 207  ILE A N   1 
ATOM   1409 C CA  . ILE A 1 183 ? 2.753   -2.499  -14.821 1.00 18.01 ? 207  ILE A CA  1 
ATOM   1410 C C   . ILE A 1 183 ? 1.765   -1.351  -14.652 1.00 17.04 ? 207  ILE A C   1 
ATOM   1411 O O   . ILE A 1 183 ? 2.154   -0.203  -14.584 1.00 22.98 ? 207  ILE A O   1 
ATOM   1412 C CB  . ILE A 1 183 ? 2.979   -3.201  -13.473 1.00 31.85 ? 207  ILE A CB  1 
ATOM   1413 C CG1 . ILE A 1 183 ? 3.404   -2.219  -12.423 1.00 34.75 ? 207  ILE A CG1 1 
ATOM   1414 C CG2 . ILE A 1 183 ? 3.965   -4.428  -13.584 1.00 27.35 ? 207  ILE A CG2 1 
ATOM   1415 C CD1 . ILE A 1 183 ? 2.627   -2.398  -11.180 1.00 42.21 ? 207  ILE A CD1 1 
ATOM   1416 N N   . VAL A 1 184 ? 0.480   -1.696  -14.596 1.00 21.61 ? 208  VAL A N   1 
ATOM   1417 C CA  . VAL A 1 184 ? -0.546  -0.749  -14.172 1.00 22.88 ? 208  VAL A CA  1 
ATOM   1418 C C   . VAL A 1 184 ? -1.337  -1.435  -13.058 1.00 21.55 ? 208  VAL A C   1 
ATOM   1419 O O   . VAL A 1 184 ? -1.329  -2.687  -12.948 1.00 22.53 ? 208  VAL A O   1 
ATOM   1420 C CB  . VAL A 1 184 ? -1.500  -0.360  -15.336 1.00 21.83 ? 208  VAL A CB  1 
ATOM   1421 C CG1 . VAL A 1 184 ? -0.772  0.553   -16.354 1.00 22.55 ? 208  VAL A CG1 1 
ATOM   1422 C CG2 . VAL A 1 184 ? -2.067  -1.622  -16.022 1.00 19.92 ? 208  VAL A CG2 1 
ATOM   1423 N N   . TYR A 1 185 ? -1.995  -0.621  -12.233 1.00 21.14 ? 209  TYR A N   1 
ATOM   1424 C CA  . TYR A 1 185 ? -2.851  -1.148  -11.178 1.00 21.99 ? 209  TYR A CA  1 
ATOM   1425 C C   . TYR A 1 185 ? -4.296  -0.997  -11.596 1.00 20.12 ? 209  TYR A C   1 
ATOM   1426 O O   . TYR A 1 185 ? -4.726  0.121   -11.914 1.00 23.10 ? 209  TYR A O   1 
ATOM   1427 C CB  . TYR A 1 185 ? -2.624  -0.366  -9.896  1.00 19.57 ? 209  TYR A CB  1 
ATOM   1428 C CG  . TYR A 1 185 ? -1.194  -0.472  -9.432  1.00 20.37 ? 209  TYR A CG  1 
ATOM   1429 C CD1 . TYR A 1 185 ? -0.690  -1.678  -8.986  1.00 20.33 ? 209  TYR A CD1 1 
ATOM   1430 C CD2 . TYR A 1 185 ? -0.349  0.633   -9.469  1.00 27.38 ? 209  TYR A CD2 1 
ATOM   1431 C CE1 . TYR A 1 185 ? 0.629   -1.781  -8.557  1.00 25.50 ? 209  TYR A CE1 1 
ATOM   1432 C CE2 . TYR A 1 185 ? 0.964   0.544   -9.058  1.00 33.28 ? 209  TYR A CE2 1 
ATOM   1433 C CZ  . TYR A 1 185 ? 1.445   -0.670  -8.602  1.00 32.07 ? 209  TYR A CZ  1 
ATOM   1434 O OH  . TYR A 1 185 ? 2.753   -0.764  -8.185  1.00 36.05 ? 209  TYR A OH  1 
ATOM   1435 N N   . VAL A 1 186 ? -5.026  -2.111  -11.562 1.00 20.82 ? 210  VAL A N   1 
ATOM   1436 C CA  . VAL A 1 186 ? -6.412  -2.179  -12.016 1.00 22.84 ? 210  VAL A CA  1 
ATOM   1437 C C   . VAL A 1 186 ? -7.298  -2.698  -10.888 1.00 23.15 ? 210  VAL A C   1 
ATOM   1438 O O   . VAL A 1 186 ? -6.997  -3.731  -10.321 1.00 23.68 ? 210  VAL A O   1 
ATOM   1439 C CB  . VAL A 1 186 ? -6.485  -3.199  -13.165 1.00 22.79 ? 210  VAL A CB  1 
ATOM   1440 C CG1 . VAL A 1 186 ? -7.913  -3.373  -13.694 1.00 23.69 ? 210  VAL A CG1 1 
ATOM   1441 C CG2 . VAL A 1 186 ? -5.476  -2.794  -14.286 1.00 24.87 ? 210  VAL A CG2 1 
ATOM   1442 N N   . PRO A 1 187 ? -8.391  -1.990  -10.569 1.00 25.56 ? 211  PRO A N   1 
ATOM   1443 C CA  . PRO A 1 187 ? -9.238  -2.491  -9.482  1.00 27.11 ? 211  PRO A CA  1 
ATOM   1444 C C   . PRO A 1 187 ? -9.690  -3.917  -9.747  1.00 29.47 ? 211  PRO A C   1 
ATOM   1445 O O   . PRO A 1 187 ? -10.048 -4.264  -10.884 1.00 27.96 ? 211  PRO A O   1 
ATOM   1446 C CB  . PRO A 1 187 ? -10.433 -1.529  -9.499  1.00 26.25 ? 211  PRO A CB  1 
ATOM   1447 C CG  . PRO A 1 187 ? -9.893  -0.284  -10.016 1.00 25.85 ? 211  PRO A CG  1 
ATOM   1448 C CD  . PRO A 1 187 ? -8.850  -0.676  -11.060 1.00 23.74 ? 211  PRO A CD  1 
ATOM   1449 N N   . GLY A 1 188 ? -9.681  -4.744  -8.709  1.00 24.75 ? 212  GLY A N   1 
ATOM   1450 C CA  . GLY A 1 188 ? -10.072 -6.120  -8.877  1.00 22.72 ? 212  GLY A CA  1 
ATOM   1451 C C   . GLY A 1 188 ? -11.293 -6.493  -8.046  1.00 25.46 ? 212  GLY A C   1 
ATOM   1452 O O   . GLY A 1 188 ? -11.726 -5.722  -7.189  1.00 28.68 ? 212  GLY A O   1 
ATOM   1453 N N   . ARG A 1 189 ? -11.816 -7.687  -8.294  1.00 27.03 ? 213  ARG A N   1 
ATOM   1454 C CA  . ARG A 1 189 ? -13.050 -8.148  -7.659  1.00 33.67 ? 213  ARG A CA  1 
ATOM   1455 C C   . ARG A 1 189 ? -12.783 -9.194  -6.592  1.00 30.56 ? 213  ARG A C   1 
ATOM   1456 O O   . ARG A 1 189 ? -11.820 -9.960  -6.683  1.00 29.85 ? 213  ARG A O   1 
ATOM   1457 C CB  . ARG A 1 189 ? -13.981 -8.746  -8.714  1.00 31.07 ? 213  ARG A CB  1 
ATOM   1458 C CG  . ARG A 1 189 ? -14.461 -7.725  -9.765  1.00 36.30 ? 213  ARG A CG  1 
ATOM   1459 C CD  . ARG A 1 189 ? -15.029 -8.442  -10.980 1.00 39.31 ? 213  ARG A CD  1 
ATOM   1460 N NE  . ARG A 1 189 ? -15.350 -7.563  -12.104 1.00 38.30 ? 213  ARG A NE  1 
ATOM   1461 C CZ  . ARG A 1 189 ? -16.421 -6.773  -12.162 1.00 42.15 ? 213  ARG A CZ  1 
ATOM   1462 N NH1 . ARG A 1 189 ? -17.260 -6.719  -11.139 1.00 40.68 ? 213  ARG A NH1 1 
ATOM   1463 N NH2 . ARG A 1 189 ? -16.639 -6.013  -13.231 1.00 42.14 ? 213  ARG A NH2 1 
ATOM   1464 N N   . ASP A 1 190 ? -13.651 -9.244  -5.587  1.00 27.26 ? 214  ASP A N   1 
ATOM   1465 C CA  . ASP A 1 190 ? -13.638 -10.359 -4.634  1.00 29.54 ? 214  ASP A CA  1 
ATOM   1466 C C   . ASP A 1 190 ? -14.104 -11.672 -5.287  1.00 26.93 ? 214  ASP A C   1 
ATOM   1467 O O   . ASP A 1 190 ? -14.485 -11.685 -6.461  1.00 31.92 ? 214  ASP A O   1 
ATOM   1468 C CB  . ASP A 1 190 ? -14.431 -10.008 -3.368  1.00 32.30 ? 214  ASP A CB  1 
ATOM   1469 C CG  . ASP A 1 190 ? -15.946 -10.039 -3.575  1.00 38.31 ? 214  ASP A CG  1 
ATOM   1470 O OD1 . ASP A 1 190 ? -16.442 -10.437 -4.654  1.00 37.84 ? 214  ASP A OD1 1 
ATOM   1471 O OD2 . ASP A 1 190 ? -16.649 -9.689  -2.614  1.00 42.17 ? 214  ASP A OD2 1 
ATOM   1472 N N   . PRO A 1 191 ? -14.062 -12.783 -4.539  1.00 26.09 ? 215  PRO A N   1 
ATOM   1473 C CA  . PRO A 1 191 ? -14.399 -14.072 -5.163  1.00 30.38 ? 215  PRO A CA  1 
ATOM   1474 C C   . PRO A 1 191 ? -15.831 -14.121 -5.698  1.00 37.86 ? 215  PRO A C   1 
ATOM   1475 O O   . PRO A 1 191 ? -16.158 -14.955 -6.551  1.00 38.33 ? 215  PRO A O   1 
ATOM   1476 C CB  . PRO A 1 191 ? -14.230 -15.070 -4.012  1.00 30.40 ? 215  PRO A CB  1 
ATOM   1477 C CG  . PRO A 1 191 ? -13.105 -14.515 -3.211  1.00 27.31 ? 215  PRO A CG  1 
ATOM   1478 C CD  . PRO A 1 191 ? -13.433 -12.969 -3.219  1.00 28.43 ? 215  PRO A CD  1 
ATOM   1479 N N   . ASN A 1 192 ? -16.675 -13.225 -5.210  1.00 33.15 ? 216  ASN A N   1 
ATOM   1480 C CA  . ASN A 1 192 ? -18.064 -13.209 -5.673  1.00 43.22 ? 216  ASN A CA  1 
ATOM   1481 C C   . ASN A 1 192 ? -18.387 -12.185 -6.747  1.00 41.71 ? 216  ASN A C   1 
ATOM   1482 O O   . ASN A 1 192 ? -19.533 -12.052 -7.175  1.00 40.14 ? 216  ASN A O   1 
ATOM   1483 C CB  . ASN A 1 192 ? -19.024 -13.130 -4.488  1.00 46.24 ? 216  ASN A CB  1 
ATOM   1484 C CG  . ASN A 1 192 ? -19.158 -14.466 -3.797  1.00 50.04 ? 216  ASN A CG  1 
ATOM   1485 O OD1 . ASN A 1 192 ? -19.268 -15.500 -4.460  1.00 47.75 ? 216  ASN A OD1 1 
ATOM   1486 N ND2 . ASN A 1 192 ? -19.101 -14.465 -2.472  1.00 55.33 ? 216  ASN A ND2 1 
ATOM   1487 N N   . GLY A 1 193 ? -17.370 -11.469 -7.202  1.00 34.48 ? 217  GLY A N   1 
ATOM   1488 C CA  . GLY A 1 193 ? -17.555 -10.557 -8.314  1.00 38.22 ? 217  GLY A CA  1 
ATOM   1489 C C   . GLY A 1 193 ? -17.788 -9.101  -7.945  1.00 37.20 ? 217  GLY A C   1 
ATOM   1490 O O   . GLY A 1 193 ? -17.974 -8.270  -8.826  1.00 41.20 ? 217  GLY A O   1 
ATOM   1491 N N   . ALA A 1 194 ? -17.799 -8.790  -6.652  1.00 34.94 ? 218  ALA A N   1 
ATOM   1492 C CA  . ALA A 1 194 ? -18.001 -7.412  -6.197  1.00 33.23 ? 218  ALA A CA  1 
ATOM   1493 C C   . ALA A 1 194 ? -16.643 -6.724  -6.007  1.00 33.30 ? 218  ALA A C   1 
ATOM   1494 O O   . ALA A 1 194 ? -15.660 -7.396  -5.688  1.00 32.24 ? 218  ALA A O   1 
ATOM   1495 C CB  . ALA A 1 194 ? -18.772 -7.403  -4.888  1.00 35.79 ? 218  ALA A CB  1 
ATOM   1496 N N   . PHE A 1 195 ? -16.584 -5.405  -6.202  1.00 34.37 ? 219  PHE A N   1 
ATOM   1497 C CA  . PHE A 1 195 ? -15.350 -4.668  -5.906  1.00 30.33 ? 219  PHE A CA  1 
ATOM   1498 C C   . PHE A 1 195 ? -15.384 -4.285  -4.429  1.00 30.17 ? 219  PHE A C   1 
ATOM   1499 O O   . PHE A 1 195 ? -16.288 -3.554  -4.008  1.00 33.80 ? 219  PHE A O   1 
ATOM   1500 C CB  . PHE A 1 195 ? -15.255 -3.360  -6.713  1.00 30.88 ? 219  PHE A CB  1 
ATOM   1501 C CG  . PHE A 1 195 ? -15.103 -3.550  -8.192  1.00 32.12 ? 219  PHE A CG  1 
ATOM   1502 C CD1 . PHE A 1 195 ? -13.858 -3.837  -8.743  1.00 27.66 ? 219  PHE A CD1 1 
ATOM   1503 C CD2 . PHE A 1 195 ? -16.192 -3.401  -9.041  1.00 35.05 ? 219  PHE A CD2 1 
ATOM   1504 C CE1 . PHE A 1 195 ? -13.711 -4.000  -10.113 1.00 31.06 ? 219  PHE A CE1 1 
ATOM   1505 C CE2 . PHE A 1 195 ? -16.048 -3.565  -10.414 1.00 32.69 ? 219  PHE A CE2 1 
ATOM   1506 C CZ  . PHE A 1 195 ? -14.810 -3.852  -10.949 1.00 30.97 ? 219  PHE A CZ  1 
ATOM   1507 N N   . PRO A 1 196 ? -14.395 -4.744  -3.647  1.00 26.70 ? 220  PRO A N   1 
ATOM   1508 C CA  . PRO A 1 196 ? -14.246 -4.258  -2.274  1.00 30.41 ? 220  PRO A CA  1 
ATOM   1509 C C   . PRO A 1 196 ? -13.935 -2.765  -2.303  1.00 30.09 ? 220  PRO A C   1 
ATOM   1510 O O   . PRO A 1 196 ? -13.149 -2.344  -3.157  1.00 29.48 ? 220  PRO A O   1 
ATOM   1511 C CB  . PRO A 1 196 ? -13.014 -5.024  -1.765  1.00 27.14 ? 220  PRO A CB  1 
ATOM   1512 C CG  . PRO A 1 196 ? -12.919 -6.253  -2.650  1.00 29.40 ? 220  PRO A CG  1 
ATOM   1513 C CD  . PRO A 1 196 ? -13.364 -5.752  -3.996  1.00 31.04 ? 220  PRO A CD  1 
ATOM   1514 N N   . PRO A 1 197 ? -14.551 -1.977  -1.401  1.00 33.35 ? 221  PRO A N   1 
ATOM   1515 C CA  . PRO A 1 197 ? -14.359 -0.531  -1.451  1.00 31.57 ? 221  PRO A CA  1 
ATOM   1516 C C   . PRO A 1 197 ? -13.033 -0.114  -0.839  1.00 33.10 ? 221  PRO A C   1 
ATOM   1517 O O   . PRO A 1 197 ? -12.351 -0.913  -0.183  1.00 35.94 ? 221  PRO A O   1 
ATOM   1518 C CB  . PRO A 1 197 ? -15.512 0.005   -0.584  1.00 35.74 ? 221  PRO A CB  1 
ATOM   1519 C CG  . PRO A 1 197 ? -15.764 -1.087  0.380   1.00 35.63 ? 221  PRO A CG  1 
ATOM   1520 C CD  . PRO A 1 197 ? -15.570 -2.353  -0.398  1.00 36.58 ? 221  PRO A CD  1 
ATOM   1521 N N   . PHE A 1 198 ? -12.667 1.144   -1.045  1.00 31.06 ? 222  PHE A N   1 
ATOM   1522 C CA  . PHE A 1 198 ? -11.473 1.668   -0.411  1.00 33.63 ? 222  PHE A CA  1 
ATOM   1523 C C   . PHE A 1 198 ? -11.666 1.669   1.098   1.00 37.42 ? 222  PHE A C   1 
ATOM   1524 O O   . PHE A 1 198 ? -12.762 1.938   1.596   1.00 37.41 ? 222  PHE A O   1 
ATOM   1525 C CB  . PHE A 1 198 ? -11.178 3.108   -0.878  1.00 34.47 ? 222  PHE A CB  1 
ATOM   1526 C CG  . PHE A 1 198 ? -9.935  3.691   -0.256  1.00 37.01 ? 222  PHE A CG  1 
ATOM   1527 C CD1 . PHE A 1 198 ? -8.671  3.311   -0.711  1.00 38.47 ? 222  PHE A CD1 1 
ATOM   1528 C CD2 . PHE A 1 198 ? -10.023 4.587   0.799   1.00 39.35 ? 222  PHE A CD2 1 
ATOM   1529 C CE1 . PHE A 1 198 ? -7.520  3.827   -0.137  1.00 35.88 ? 222  PHE A CE1 1 
ATOM   1530 C CE2 . PHE A 1 198 ? -8.875  5.111   1.381   1.00 40.69 ? 222  PHE A CE2 1 
ATOM   1531 C CZ  . PHE A 1 198 ? -7.622  4.732   0.913   1.00 40.15 ? 222  PHE A CZ  1 
ATOM   1532 N N   . LYS A 1 199 ? -10.589 1.419   1.831   1.00 36.09 ? 223  LYS A N   1 
ATOM   1533 C CA  . LYS A 1 199 ? -10.639 1.466   3.291   1.00 48.52 ? 223  LYS A CA  1 
ATOM   1534 C C   . LYS A 1 199 ? -9.427  2.186   3.857   1.00 55.61 ? 223  LYS A C   1 
ATOM   1535 O O   . LYS A 1 199 ? -8.293  1.740   3.675   1.00 55.83 ? 223  LYS A O   1 
ATOM   1536 C CB  . LYS A 1 199 ? -10.726 0.058   3.884   1.00 56.10 ? 223  LYS A CB  1 
ATOM   1537 C CG  . LYS A 1 199 ? -12.098 -0.572  3.747   1.00 64.38 ? 223  LYS A CG  1 
ATOM   1538 C CD  . LYS A 1 199 ? -12.258 -1.789  4.639   1.00 67.94 ? 223  LYS A CD  1 
ATOM   1539 C CE  . LYS A 1 199 ? -13.597 -2.454  4.377   1.00 69.79 ? 223  LYS A CE  1 
ATOM   1540 N NZ  . LYS A 1 199 ? -14.695 -1.457  4.346   1.00 72.83 ? 223  LYS A NZ  1 
ATOM   1541 N N   . SER A 1 200 ? -9.670  3.298   4.546   1.00 61.52 ? 224  SER A N   1 
ATOM   1542 C CA  . SER A 1 200 ? -8.586  4.076   5.141   1.00 67.33 ? 224  SER A CA  1 
ATOM   1543 C C   . SER A 1 200 ? -8.115  3.450   6.452   1.00 67.67 ? 224  SER A C   1 
ATOM   1544 O O   . SER A 1 200 ? -8.806  2.605   7.026   1.00 67.17 ? 224  SER A O   1 
ATOM   1545 C CB  . SER A 1 200 ? -9.025  5.528   5.359   1.00 71.26 ? 224  SER A CB  1 
ATOM   1546 O OG  . SER A 1 200 ? -10.304 5.591   5.965   1.00 73.64 ? 224  SER A OG  1 
HETATM 1547 C C1  . NAG B 2 .   ? 4.663   -20.217 1.785   1.00 20.35 ? 801  NAG A C1  1 
HETATM 1548 C C2  . NAG B 2 .   ? 5.507   -21.294 2.484   1.00 21.35 ? 801  NAG A C2  1 
HETATM 1549 C C3  . NAG B 2 .   ? 5.257   -21.312 4.006   1.00 27.63 ? 801  NAG A C3  1 
HETATM 1550 C C4  . NAG B 2 .   ? 5.427   -19.911 4.588   1.00 28.25 ? 801  NAG A C4  1 
HETATM 1551 C C5  . NAG B 2 .   ? 4.585   -18.927 3.790   1.00 27.80 ? 801  NAG A C5  1 
HETATM 1552 C C6  . NAG B 2 .   ? 4.780   -17.507 4.319   1.00 31.00 ? 801  NAG A C6  1 
HETATM 1553 C C7  . NAG B 2 .   ? 6.300   -23.127 1.100   1.00 28.42 ? 801  NAG A C7  1 
HETATM 1554 C C8  . NAG B 2 .   ? 6.031   -24.438 0.418   1.00 32.78 ? 801  NAG A C8  1 
HETATM 1555 N N2  . NAG B 2 .   ? 5.336   -22.603 1.873   1.00 23.10 ? 801  NAG A N2  1 
HETATM 1556 O O3  . NAG B 2 .   ? 6.203   -22.184 4.597   1.00 31.77 ? 801  NAG A O3  1 
HETATM 1557 O O4  . NAG B 2 .   ? 5.040   -19.843 5.941   1.00 34.27 ? 801  NAG A O4  1 
HETATM 1558 O O5  . NAG B 2 .   ? 4.986   -19.000 2.437   1.00 23.40 ? 801  NAG A O5  1 
HETATM 1559 O O6  . NAG B 2 .   ? 6.128   -17.072 4.121   1.00 32.80 ? 801  NAG A O6  1 
HETATM 1560 O O7  . NAG B 2 .   ? 7.394   -22.592 0.938   1.00 31.37 ? 801  NAG A O7  1 
HETATM 1561 C C1  . NAG C 2 .   ? 5.638   -20.735 6.943   1.00 44.65 ? 802  NAG A C1  1 
HETATM 1562 C C2  . NAG C 2 .   ? 5.643   -19.835 8.174   1.00 53.62 ? 802  NAG A C2  1 
HETATM 1563 C C3  . NAG C 2 .   ? 6.213   -20.558 9.392   1.00 57.71 ? 802  NAG A C3  1 
HETATM 1564 C C4  . NAG C 2 .   ? 5.503   -21.890 9.580   1.00 63.63 ? 802  NAG A C4  1 
HETATM 1565 C C5  . NAG C 2 .   ? 5.637   -22.710 8.296   1.00 63.61 ? 802  NAG A C5  1 
HETATM 1566 C C6  . NAG C 2 .   ? 4.956   -24.069 8.425   1.00 69.14 ? 802  NAG A C6  1 
HETATM 1567 C C7  . NAG C 2 .   ? 5.849   -17.405 7.942   1.00 54.85 ? 802  NAG A C7  1 
HETATM 1568 C C8  . NAG C 2 .   ? 6.817   -16.260 7.890   1.00 57.13 ? 802  NAG A C8  1 
HETATM 1569 N N2  . NAG C 2 .   ? 6.399   -18.626 7.916   1.00 54.23 ? 802  NAG A N2  1 
HETATM 1570 O O3  . NAG C 2 .   ? 6.040   -19.739 10.525  1.00 58.55 ? 802  NAG A O3  1 
HETATM 1571 O O4  . NAG C 2 .   ? 6.018   -22.574 10.710  1.00 66.30 ? 802  NAG A O4  1 
HETATM 1572 O O5  . NAG C 2 .   ? 5.062   -21.997 7.207   1.00 55.92 ? 802  NAG A O5  1 
HETATM 1573 O O6  . NAG C 2 .   ? 3.558   -23.933 8.268   1.00 74.21 ? 802  NAG A O6  1 
HETATM 1574 O O7  . NAG C 2 .   ? 4.629   -17.184 8.002   1.00 54.34 ? 802  NAG A O7  1 
HETATM 1575 C C1  . NAG D 2 .   ? 7.461   -10.399 -20.257 1.00 21.85 ? 803  NAG A C1  1 
HETATM 1576 C C2  . NAG D 2 .   ? 6.628   -11.426 -21.044 1.00 25.09 ? 803  NAG A C2  1 
HETATM 1577 C C3  . NAG D 2 .   ? 7.432   -11.958 -22.232 1.00 29.64 ? 803  NAG A C3  1 
HETATM 1578 C C4  . NAG D 2 .   ? 8.096   -10.858 -23.047 1.00 33.16 ? 803  NAG A C4  1 
HETATM 1579 C C5  . NAG D 2 .   ? 8.807   -9.899  -22.097 1.00 29.36 ? 803  NAG A C5  1 
HETATM 1580 C C6  . NAG D 2 .   ? 9.429   -8.721  -22.843 1.00 32.41 ? 803  NAG A C6  1 
HETATM 1581 C C7  . NAG D 2 .   ? 4.960   -12.968 -20.098 1.00 25.51 ? 803  NAG A C7  1 
HETATM 1582 C C8  . NAG D 2 .   ? 4.721   -14.202 -19.263 1.00 22.17 ? 803  NAG A C8  1 
HETATM 1583 N N2  . NAG D 2 .   ? 6.225   -12.553 -20.210 1.00 22.71 ? 803  NAG A N2  1 
HETATM 1584 O O3  . NAG D 2 .   ? 6.640   -12.809 -23.037 1.00 33.80 ? 803  NAG A O3  1 
HETATM 1585 O O4  . NAG D 2 .   ? 9.063   -11.450 -23.894 1.00 37.62 ? 803  NAG A O4  1 
HETATM 1586 O O5  . NAG D 2 .   ? 7.834   -9.398  -21.194 1.00 26.78 ? 803  NAG A O5  1 
HETATM 1587 O O6  . NAG D 2 .   ? 8.393   -8.151  -23.616 1.00 40.10 ? 803  NAG A O6  1 
HETATM 1588 O O7  . NAG D 2 .   ? 3.996   -12.414 -20.628 1.00 25.31 ? 803  NAG A O7  1 
HETATM 1589 C C1  . NAG E 2 .   ? 9.110   -10.976 -25.271 1.00 45.44 ? 804  NAG A C1  1 
HETATM 1590 C C2  . NAG E 2 .   ? 10.456  -11.439 -25.817 1.00 49.91 ? 804  NAG A C2  1 
HETATM 1591 C C3  . NAG E 2 .   ? 10.546  -11.367 -27.347 1.00 57.49 ? 804  NAG A C3  1 
HETATM 1592 C C4  . NAG E 2 .   ? 9.276   -11.873 -28.022 1.00 57.69 ? 804  NAG A C4  1 
HETATM 1593 C C5  . NAG E 2 .   ? 8.042   -11.329 -27.298 1.00 58.96 ? 804  NAG A C5  1 
HETATM 1594 C C6  . NAG E 2 .   ? 6.733   -11.859 -27.852 1.00 65.03 ? 804  NAG A C6  1 
HETATM 1595 C C7  . NAG E 2 .   ? 12.352  -11.222 -24.339 1.00 47.45 ? 804  NAG A C7  1 
HETATM 1596 C C8  . NAG E 2 .   ? 13.216  -10.292 -23.536 1.00 50.05 ? 804  NAG A C8  1 
HETATM 1597 N N2  . NAG E 2 .   ? 11.493  -10.650 -25.188 1.00 45.44 ? 804  NAG A N2  1 
HETATM 1598 O O3  . NAG E 2 .   ? 11.633  -12.150 -27.802 1.00 58.96 ? 804  NAG A O3  1 
HETATM 1599 O O4  . NAG E 2 .   ? 9.286   -11.455 -29.371 1.00 55.72 ? 804  NAG A O4  1 
HETATM 1600 O O5  . NAG E 2 .   ? 8.076   -11.665 -25.923 1.00 50.75 ? 804  NAG A O5  1 
HETATM 1601 O O6  . NAG E 2 .   ? 5.722   -11.473 -26.944 1.00 72.62 ? 804  NAG A O6  1 
HETATM 1602 O O7  . NAG E 2 .   ? 12.453  -12.447 -24.203 1.00 45.56 ? 804  NAG A O7  1 
HETATM 1603 C C1  . NAG F 2 .   ? 8.329   -1.077  -6.717  1.00 24.26 ? 805  NAG A C1  1 
HETATM 1604 C C2  . NAG F 2 .   ? 9.292   -1.243  -7.894  1.00 26.04 ? 805  NAG A C2  1 
HETATM 1605 C C3  . NAG F 2 .   ? 10.643  -0.595  -7.610  1.00 29.64 ? 805  NAG A C3  1 
HETATM 1606 C C4  . NAG F 2 .   ? 10.508  0.836   -7.129  1.00 34.41 ? 805  NAG A C4  1 
HETATM 1607 C C5  . NAG F 2 .   ? 9.456   0.908   -6.027  1.00 34.57 ? 805  NAG A C5  1 
HETATM 1608 C C6  . NAG F 2 .   ? 9.198   2.358   -5.618  1.00 39.94 ? 805  NAG A C6  1 
HETATM 1609 C C7  . NAG F 2 .   ? 9.357   -3.336  -9.166  1.00 38.62 ? 805  NAG A C7  1 
HETATM 1610 C C8  . NAG F 2 .   ? 9.800   -4.789  -9.111  1.00 24.80 ? 805  NAG A C8  1 
HETATM 1611 N N2  . NAG F 2 .   ? 9.574   -2.662  -8.070  1.00 31.52 ? 805  NAG A N2  1 
HETATM 1612 O O3  . NAG F 2 .   ? 11.373  -0.660  -8.810  1.00 32.05 ? 805  NAG A O3  1 
HETATM 1613 O O4  . NAG F 2 .   ? 11.737  1.256   -6.571  1.00 42.66 ? 805  NAG A O4  1 
HETATM 1614 O O5  . NAG F 2 .   ? 8.246   0.312   -6.453  1.00 27.51 ? 805  NAG A O5  1 
HETATM 1615 O O6  . NAG F 2 .   ? 8.692   3.067   -6.727  1.00 43.41 ? 805  NAG A O6  1 
HETATM 1616 O O7  . NAG F 2 .   ? 8.790   -2.832  -10.140 1.00 52.53 ? 805  NAG A O7  1 
HETATM 1617 C C1  . NAG G 2 .   ? 12.371  2.196   -7.497  1.00 45.26 ? 806  NAG A C1  1 
HETATM 1618 C C2  . NAG G 2 .   ? 13.491  2.656   -6.582  1.00 48.92 ? 806  NAG A C2  1 
HETATM 1619 C C3  . NAG G 2 .   ? 14.493  3.502   -7.367  1.00 58.62 ? 806  NAG A C3  1 
HETATM 1620 C C4  . NAG G 2 .   ? 14.886  2.839   -8.687  1.00 60.98 ? 806  NAG A C4  1 
HETATM 1621 C C5  . NAG G 2 .   ? 13.644  2.371   -9.437  1.00 59.09 ? 806  NAG A C5  1 
HETATM 1622 C C6  . NAG G 2 .   ? 13.978  1.671   -10.751 1.00 65.08 ? 806  NAG A C6  1 
HETATM 1623 C C7  . NAG G 2 .   ? 12.890  2.957   -4.241  1.00 42.59 ? 806  NAG A C7  1 
HETATM 1624 C C8  . NAG G 2 .   ? 12.170  3.823   -3.251  1.00 42.88 ? 806  NAG A C8  1 
HETATM 1625 N N2  . NAG G 2 .   ? 12.942  3.430   -5.485  1.00 42.32 ? 806  NAG A N2  1 
HETATM 1626 O O3  . NAG G 2 .   ? 15.638  3.712   -6.574  1.00 59.68 ? 806  NAG A O3  1 
HETATM 1627 O O4  . NAG G 2 .   ? 15.601  3.758   -9.485  1.00 66.36 ? 806  NAG A O4  1 
HETATM 1628 O O5  . NAG G 2 .   ? 12.925  1.497   -8.595  1.00 49.31 ? 806  NAG A O5  1 
HETATM 1629 O O6  . NAG G 2 .   ? 14.789  0.540   -10.504 1.00 68.50 ? 806  NAG A O6  1 
HETATM 1630 O O7  . NAG G 2 .   ? 13.385  1.875   -3.903  1.00 38.49 ? 806  NAG A O7  1 
HETATM 1631 C C1  . NAG H 2 .   ? 11.620  -7.379  1.786   1.00 26.60 ? 807  NAG A C1  1 
HETATM 1632 C C2  . NAG H 2 .   ? 11.441  -6.862  3.226   1.00 26.15 ? 807  NAG A C2  1 
HETATM 1633 C C3  . NAG H 2 .   ? 12.481  -5.768  3.498   1.00 29.62 ? 807  NAG A C3  1 
HETATM 1634 C C4  . NAG H 2 .   ? 13.889  -6.307  3.197   1.00 29.64 ? 807  NAG A C4  1 
HETATM 1635 C C5  . NAG H 2 .   ? 13.965  -6.967  1.821   1.00 29.41 ? 807  NAG A C5  1 
HETATM 1636 C C6  . NAG H 2 .   ? 15.346  -7.637  1.656   1.00 30.24 ? 807  NAG A C6  1 
HETATM 1637 C C7  . NAG H 2 .   ? 9.405   -6.717  4.614   1.00 27.13 ? 807  NAG A C7  1 
HETATM 1638 C C8  . NAG H 2 .   ? 8.010   -6.171  4.766   1.00 26.89 ? 807  NAG A C8  1 
HETATM 1639 N N2  . NAG H 2 .   ? 10.076  -6.407  3.502   1.00 25.77 ? 807  NAG A N2  1 
HETATM 1640 O O3  . NAG H 2 .   ? 12.407  -5.430  4.866   1.00 31.19 ? 807  NAG A O3  1 
HETATM 1641 O O4  . NAG H 2 .   ? 14.888  -5.307  3.251   1.00 32.84 ? 807  NAG A O4  1 
HETATM 1642 O O5  . NAG H 2 .   ? 12.935  -7.933  1.722   1.00 28.83 ? 807  NAG A O5  1 
HETATM 1643 O O6  . NAG H 2 .   ? 15.515  -8.764  2.536   1.00 31.04 ? 807  NAG A O6  1 
HETATM 1644 O O7  . NAG H 2 .   ? 9.856   -7.409  5.509   1.00 30.23 ? 807  NAG A O7  1 
HETATM 1645 C C1  . NAG I 2 .   ? 15.545  -5.239  4.556   1.00 33.53 ? 808  NAG A C1  1 
HETATM 1646 C C2  . NAG I 2 .   ? 17.022  -4.872  4.343   1.00 39.93 ? 808  NAG A C2  1 
HETATM 1647 C C3  . NAG I 2 .   ? 17.704  -4.448  5.640   1.00 40.02 ? 808  NAG A C3  1 
HETATM 1648 C C4  . NAG I 2 .   ? 16.842  -3.451  6.400   1.00 38.56 ? 808  NAG A C4  1 
HETATM 1649 C C5  . NAG I 2 .   ? 15.402  -3.964  6.543   1.00 35.11 ? 808  NAG A C5  1 
HETATM 1650 C C6  . NAG I 2 .   ? 14.511  -2.950  7.257   1.00 41.75 ? 808  NAG A C6  1 
HETATM 1651 C C7  . NAG I 2 .   ? 18.272  -5.917  2.545   1.00 43.22 ? 808  NAG A C7  1 
HETATM 1652 C C8  . NAG I 2 .   ? 18.914  -7.161  2.006   1.00 39.89 ? 808  NAG A C8  1 
HETATM 1653 N N2  . NAG I 2 .   ? 17.755  -5.995  3.772   1.00 38.75 ? 808  NAG A N2  1 
HETATM 1654 O O3  . NAG I 2 .   ? 18.992  -3.894  5.393   1.00 36.31 ? 808  NAG A O3  1 
HETATM 1655 O O4  . NAG I 2 .   ? 17.440  -3.276  7.676   1.00 40.28 ? 808  NAG A O4  1 
HETATM 1656 O O5  . NAG I 2 .   ? 14.845  -4.226  5.260   1.00 33.61 ? 808  NAG A O5  1 
HETATM 1657 O O6  . NAG I 2 .   ? 13.376  -3.638  7.736   1.00 48.65 ? 808  NAG A O6  1 
HETATM 1658 O O7  . NAG I 2 .   ? 18.224  -4.890  1.862   1.00 39.95 ? 808  NAG A O7  1 
HETATM 1659 C C1  . BMA J 3 .   ? 17.465  -1.832  7.899   1.00 45.56 ? 809  BMA A C1  1 
HETATM 1660 C C2  . BMA J 3 .   ? 17.659  -1.778  9.411   1.00 50.32 ? 809  BMA A C2  1 
HETATM 1661 C C3  . BMA J 3 .   ? 17.814  -0.329  9.875   1.00 57.56 ? 809  BMA A C3  1 
HETATM 1662 C C4  . BMA J 3 .   ? 18.888  0.382   9.065   1.00 58.72 ? 809  BMA A C4  1 
HETATM 1663 C C5  . BMA J 3 .   ? 18.650  0.156   7.579   1.00 58.41 ? 809  BMA A C5  1 
HETATM 1664 C C6  . BMA J 3 .   ? 19.777  0.801   6.785   1.00 65.01 ? 809  BMA A C6  1 
HETATM 1665 O O2  . BMA J 3 .   ? 18.801  -2.543  9.731   1.00 47.81 ? 809  BMA A O2  1 
HETATM 1666 O O3  . BMA J 3 .   ? 18.166  -0.262  11.239  1.00 65.58 ? 809  BMA A O3  1 
HETATM 1667 O O4  . BMA J 3 .   ? 18.862  1.767   9.337   1.00 58.98 ? 809  BMA A O4  1 
HETATM 1668 O O5  . BMA J 3 .   ? 18.594  -1.236  7.308   1.00 49.78 ? 809  BMA A O5  1 
HETATM 1669 O O6  . BMA J 3 .   ? 19.329  1.121   5.487   1.00 69.30 ? 809  BMA A O6  1 
HETATM 1670 C C1  . BMA K 3 .   ? 19.302  2.154   4.455   1.00 78.58 ? 810  BMA A C1  1 
HETATM 1671 C C2  . BMA K 3 .   ? 20.760  2.562   4.642   1.00 85.11 ? 810  BMA A C2  1 
HETATM 1672 C C3  . BMA K 3 .   ? 21.274  3.341   3.443   1.00 87.42 ? 810  BMA A C3  1 
HETATM 1673 C C4  . BMA K 3 .   ? 20.874  2.674   2.131   1.00 85.67 ? 810  BMA A C4  1 
HETATM 1674 C C5  . BMA K 3 .   ? 19.404  2.267   2.119   1.00 80.47 ? 810  BMA A C5  1 
HETATM 1675 C C6  . BMA K 3 .   ? 19.076  1.531   0.821   1.00 75.29 ? 810  BMA A C6  1 
HETATM 1676 O O2  . BMA K 3 .   ? 21.580  1.428   4.807   1.00 88.75 ? 810  BMA A O2  1 
HETATM 1677 O O3  . BMA K 3 .   ? 22.680  3.385   3.523   1.00 88.50 ? 810  BMA A O3  1 
HETATM 1678 O O4  . BMA K 3 .   ? 21.109  3.568   1.066   1.00 89.25 ? 810  BMA A O4  1 
HETATM 1679 O O5  . BMA K 3 .   ? 19.147  1.452   3.239   1.00 80.39 ? 810  BMA A O5  1 
HETATM 1680 O O6  . BMA K 3 .   ? 18.035  0.598   1.008   1.00 73.18 ? 810  BMA A O6  1 
HETATM 1681 C C1  . MAN L 4 .   ? 17.008  -0.378  12.123  1.00 76.64 ? 811  MAN A C1  1 
HETATM 1682 C C2  . MAN L 4 .   ? 17.544  -0.050  13.517  1.00 83.33 ? 811  MAN A C2  1 
HETATM 1683 C C3  . MAN L 4 .   ? 17.663  -1.314  14.365  1.00 86.92 ? 811  MAN A C3  1 
HETATM 1684 C C4  . MAN L 4 .   ? 16.411  -2.173  14.265  1.00 86.36 ? 811  MAN A C4  1 
HETATM 1685 C C5  . MAN L 4 .   ? 16.036  -2.401  12.807  1.00 83.34 ? 811  MAN A C5  1 
HETATM 1686 C C6  . MAN L 4 .   ? 14.772  -3.249  12.689  1.00 85.82 ? 811  MAN A C6  1 
HETATM 1687 O O2  . MAN L 4 .   ? 16.724  0.910   14.154  1.00 83.18 ? 811  MAN A O2  1 
HETATM 1688 O O3  . MAN L 4 .   ? 17.868  -0.959  15.712  1.00 91.60 ? 811  MAN A O3  1 
HETATM 1689 O O4  . MAN L 4 .   ? 16.643  -3.411  14.899  1.00 88.45 ? 811  MAN A O4  1 
HETATM 1690 O O5  . MAN L 4 .   ? 15.827  -1.146  12.204  1.00 78.58 ? 811  MAN A O5  1 
HETATM 1691 O O6  . MAN L 4 .   ? 14.666  -3.778  11.384  1.00 88.59 ? 811  MAN A O6  1 
HETATM 1692 C C1  . NAG M 2 .   ? 22.609  -13.024 -19.257 1.00 41.52 ? 812  NAG A C1  1 
HETATM 1693 C C2  . NAG M 2 .   ? 22.298  -13.294 -17.782 1.00 35.08 ? 812  NAG A C2  1 
HETATM 1694 C C3  . NAG M 2 .   ? 23.392  -14.164 -17.147 1.00 36.17 ? 812  NAG A C3  1 
HETATM 1695 C C4  . NAG M 2 .   ? 23.653  -15.400 -18.000 1.00 36.68 ? 812  NAG A C4  1 
HETATM 1696 C C5  . NAG M 2 .   ? 23.855  -15.017 -19.466 1.00 46.25 ? 812  NAG A C5  1 
HETATM 1697 C C6  . NAG M 2 .   ? 23.982  -16.270 -20.326 1.00 52.40 ? 812  NAG A C6  1 
HETATM 1698 C C7  . NAG M 2 .   ? 21.019  -11.727 -16.439 1.00 31.06 ? 812  NAG A C7  1 
HETATM 1699 C C8  . NAG M 2 .   ? 20.970  -10.441 -15.658 1.00 31.51 ? 812  NAG A C8  1 
HETATM 1700 N N2  . NAG M 2 .   ? 22.160  -12.019 -17.076 1.00 29.76 ? 812  NAG A N2  1 
HETATM 1701 O O1  . NAG M 2 .   ? 21.560  -12.305 -19.868 1.00 41.18 ? 812  NAG A O1  1 
HETATM 1702 O O3  . NAG M 2 .   ? 23.010  -14.599 -15.849 1.00 34.89 ? 812  NAG A O3  1 
HETATM 1703 O O4  . NAG M 2 .   ? 24.827  -16.051 -17.548 1.00 36.36 ? 812  NAG A O4  1 
HETATM 1704 O O5  . NAG M 2 .   ? 22.785  -14.232 -19.957 1.00 44.04 ? 812  NAG A O5  1 
HETATM 1705 O O6  . NAG M 2 .   ? 24.507  -15.894 -21.579 1.00 59.22 ? 812  NAG A O6  1 
HETATM 1706 O O7  . NAG M 2 .   ? 20.049  -12.481 -16.486 1.00 28.58 ? 812  NAG A O7  1 
HETATM 1707 C C1  . NAG N 2 .   ? 24.563  -17.391 -17.061 1.00 31.88 ? 813  NAG A C1  1 
HETATM 1708 C C2  . NAG N 2 .   ? 25.906  -18.119 -17.023 1.00 36.02 ? 813  NAG A C2  1 
HETATM 1709 C C3  . NAG N 2 .   ? 25.731  -19.461 -16.333 1.00 35.92 ? 813  NAG A C3  1 
HETATM 1710 C C4  . NAG N 2 .   ? 25.103  -19.236 -14.965 1.00 32.38 ? 813  NAG A C4  1 
HETATM 1711 C C5  . NAG N 2 .   ? 23.830  -18.390 -15.068 1.00 30.33 ? 813  NAG A C5  1 
HETATM 1712 C C6  . NAG N 2 .   ? 23.161  -18.100 -13.712 1.00 28.74 ? 813  NAG A C6  1 
HETATM 1713 C C7  . NAG N 2 .   ? 27.438  -17.536 -18.820 1.00 44.05 ? 813  NAG A C7  1 
HETATM 1714 C C8  . NAG N 2 .   ? 27.814  -17.711 -20.265 1.00 45.83 ? 813  NAG A C8  1 
HETATM 1715 N N2  . NAG N 2 .   ? 26.462  -18.314 -18.353 1.00 38.35 ? 813  NAG A N2  1 
HETATM 1716 O O3  . NAG N 2 .   ? 26.992  -20.103 -16.201 1.00 37.21 ? 813  NAG A O3  1 
HETATM 1717 O O4  . NAG N 2 .   ? 24.791  -20.498 -14.430 1.00 32.78 ? 813  NAG A O4  1 
HETATM 1718 O O5  . NAG N 2 .   ? 24.116  -17.172 -15.726 1.00 29.09 ? 813  NAG A O5  1 
HETATM 1719 O O6  . NAG N 2 .   ? 24.065  -17.516 -12.798 1.00 26.52 ? 813  NAG A O6  1 
HETATM 1720 O O7  . NAG N 2 .   ? 28.023  -16.702 -18.129 1.00 45.44 ? 813  NAG A O7  1 
HETATM 1721 C C1  . NAG O 2 .   ? 25.434  -20.907 -13.186 1.00 32.34 ? 814  NAG A C1  1 
HETATM 1722 C C2  . NAG O 2 .   ? 24.642  -22.009 -12.482 1.00 31.95 ? 814  NAG A C2  1 
HETATM 1723 C C3  . NAG O 2 .   ? 25.460  -22.603 -11.338 1.00 31.69 ? 814  NAG A C3  1 
HETATM 1724 C C4  . NAG O 2 .   ? 26.832  -23.005 -11.856 1.00 34.99 ? 814  NAG A C4  1 
HETATM 1725 C C5  . NAG O 2 .   ? 27.521  -21.904 -12.636 1.00 30.24 ? 814  NAG A C5  1 
HETATM 1726 C C6  . NAG O 2 .   ? 28.777  -22.500 -13.274 1.00 35.32 ? 814  NAG A C6  1 
HETATM 1727 C C7  . NAG O 2 .   ? 22.245  -21.786 -12.572 1.00 36.17 ? 814  NAG A C7  1 
HETATM 1728 C C8  . NAG O 2 .   ? 21.027  -21.242 -11.879 1.00 30.25 ? 814  NAG A C8  1 
HETATM 1729 N N2  . NAG O 2 .   ? 23.396  -21.461 -11.989 1.00 28.32 ? 814  NAG A N2  1 
HETATM 1730 O O3  . NAG O 2 .   ? 24.834  -23.757 -10.826 1.00 31.87 ? 814  NAG A O3  1 
HETATM 1731 O O4  . NAG O 2 .   ? 27.692  -23.370 -10.793 1.00 40.02 ? 814  NAG A O4  1 
HETATM 1732 O O5  . NAG O 2 .   ? 26.693  -21.373 -13.648 1.00 33.93 ? 814  NAG A O5  1 
HETATM 1733 O O6  . NAG O 2 .   ? 29.575  -21.401 -13.622 1.00 43.78 ? 814  NAG A O6  1 
HETATM 1734 O O7  . NAG O 2 .   ? 22.165  -22.475 -13.604 1.00 29.89 ? 814  NAG A O7  1 
HETATM 1735 C C1  . NAG P 2 .   ? 28.167  -24.754 -10.841 1.00 43.45 ? 815  NAG A C1  1 
HETATM 1736 C C2  . NAG P 2 .   ? 29.304  -24.785 -9.825  1.00 43.54 ? 815  NAG A C2  1 
HETATM 1737 C C3  . NAG P 2 .   ? 29.875  -26.190 -9.642  1.00 49.77 ? 815  NAG A C3  1 
HETATM 1738 C C4  . NAG P 2 .   ? 28.771  -27.224 -9.476  1.00 52.14 ? 815  NAG A C4  1 
HETATM 1739 C C5  . NAG P 2 .   ? 27.735  -27.068 -10.588 1.00 48.64 ? 815  NAG A C5  1 
HETATM 1740 C C6  . NAG P 2 .   ? 26.583  -28.047 -10.426 1.00 47.94 ? 815  NAG A C6  1 
HETATM 1741 C C7  . NAG P 2 .   ? 30.768  -22.831 -9.555  1.00 47.51 ? 815  NAG A C7  1 
HETATM 1742 C C8  . NAG P 2 .   ? 31.991  -22.127 -10.067 1.00 50.05 ? 815  NAG A C8  1 
HETATM 1743 N N2  . NAG P 2 .   ? 30.356  -23.881 -10.262 1.00 44.45 ? 815  NAG A N2  1 
HETATM 1744 O O3  . NAG P 2 .   ? 30.700  -26.200 -8.505  1.00 48.53 ? 815  NAG A O3  1 
HETATM 1745 O O4  . NAG P 2 .   ? 29.341  -28.516 -9.526  1.00 60.65 ? 815  NAG A O4  1 
HETATM 1746 O O5  . NAG P 2 .   ? 27.207  -25.758 -10.593 1.00 45.90 ? 815  NAG A O5  1 
HETATM 1747 O O6  . NAG P 2 .   ? 25.806  -28.053 -11.604 1.00 51.27 ? 815  NAG A O6  1 
HETATM 1748 O O7  . NAG P 2 .   ? 30.204  -22.435 -8.534  1.00 45.52 ? 815  NAG A O7  1 
HETATM 1749 O O   . HOH Q 5 .   ? 0.487   -15.231 -2.603  1.00 19.62 ? 901  HOH A O   1 
HETATM 1750 O O   . HOH Q 5 .   ? 12.521  -8.223  -7.358  1.00 19.59 ? 902  HOH A O   1 
HETATM 1751 O O   . HOH Q 5 .   ? -5.075  -4.346  -3.389  1.00 24.35 ? 903  HOH A O   1 
HETATM 1752 O O   . HOH Q 5 .   ? -1.976  -4.290  -6.589  1.00 21.36 ? 904  HOH A O   1 
HETATM 1753 O O   . HOH Q 5 .   ? 3.088   -14.337 3.377   1.00 21.93 ? 905  HOH A O   1 
HETATM 1754 O O   . HOH Q 5 .   ? 1.772   -11.394 -16.273 1.00 17.55 ? 906  HOH A O   1 
HETATM 1755 O O   . HOH Q 5 .   ? 5.534   -14.950 0.243   1.00 22.20 ? 907  HOH A O   1 
HETATM 1756 O O   . HOH Q 5 .   ? 6.943   -8.328  2.043   1.00 25.08 ? 908  HOH A O   1 
HETATM 1757 O O   . HOH Q 5 .   ? 5.971   -4.976  -9.319  1.00 21.86 ? 909  HOH A O   1 
HETATM 1758 O O   . HOH Q 5 .   ? 0.210   -2.278  -23.558 1.00 28.45 ? 910  HOH A O   1 
HETATM 1759 O O   . HOH Q 5 .   ? -9.298  3.846   -4.443  1.00 28.89 ? 911  HOH A O   1 
HETATM 1760 O O   . HOH Q 5 .   ? 11.370  -4.205  -0.217  1.00 30.59 ? 912  HOH A O   1 
HETATM 1761 O O   . HOH Q 5 .   ? 6.112   -0.528  -14.351 1.00 28.44 ? 913  HOH A O   1 
HETATM 1762 O O   . HOH Q 5 .   ? 6.847   -17.184 -2.666  1.00 20.53 ? 914  HOH A O   1 
HETATM 1763 O O   . HOH Q 5 .   ? 10.160  -7.976  -16.193 1.00 24.53 ? 915  HOH A O   1 
HETATM 1764 O O   . HOH Q 5 .   ? 3.497   -17.961 -18.291 1.00 24.54 ? 916  HOH A O   1 
HETATM 1765 O O   . HOH Q 5 .   ? 19.970  -3.690  -10.380 1.00 28.89 ? 917  HOH A O   1 
HETATM 1766 O O   . HOH Q 5 .   ? 21.448  -13.869 -13.814 1.00 28.09 ? 918  HOH A O   1 
HETATM 1767 O O   . HOH Q 5 .   ? 15.300  -4.240  -5.472  1.00 24.16 ? 919  HOH A O   1 
HETATM 1768 O O   . HOH Q 5 .   ? -2.340  -26.697 -14.296 1.00 25.11 ? 920  HOH A O   1 
HETATM 1769 O O   . HOH Q 5 .   ? 12.937  -7.598  -16.379 1.00 24.60 ? 921  HOH A O   1 
HETATM 1770 O O   . HOH Q 5 .   ? -3.373  4.987   -21.723 1.00 27.17 ? 922  HOH A O   1 
HETATM 1771 O O   . HOH Q 5 .   ? 7.483   -18.843 -0.405  1.00 24.97 ? 923  HOH A O   1 
HETATM 1772 O O   . HOH Q 5 .   ? -11.658 -2.929  -5.602  1.00 27.34 ? 924  HOH A O   1 
HETATM 1773 O O   . HOH Q 5 .   ? -7.431  -5.177  -0.669  1.00 28.95 ? 925  HOH A O   1 
HETATM 1774 O O   . HOH Q 5 .   ? 6.102   -17.307 -18.285 1.00 24.76 ? 926  HOH A O   1 
HETATM 1775 O O   . HOH Q 5 .   ? -1.456  -25.464 -3.378  1.00 24.47 ? 927  HOH A O   1 
HETATM 1776 O O   . HOH Q 5 .   ? -5.793  -9.950  -15.234 1.00 27.31 ? 928  HOH A O   1 
HETATM 1777 O O   . HOH Q 5 .   ? 12.443  -1.707  0.219   1.00 32.16 ? 929  HOH A O   1 
HETATM 1778 O O   . HOH Q 5 .   ? -3.599  -23.079 -1.133  1.00 30.34 ? 930  HOH A O   1 
HETATM 1779 O O   . HOH Q 5 .   ? -6.513  -6.293  -23.010 1.00 37.59 ? 931  HOH A O   1 
HETATM 1780 O O   . HOH Q 5 .   ? -3.631  -27.447 -20.461 1.00 32.98 ? 932  HOH A O   1 
HETATM 1781 O O   . HOH Q 5 .   ? -8.904  -17.108 0.442   1.00 23.14 ? 933  HOH A O   1 
HETATM 1782 O O   . HOH Q 5 .   ? 7.926   -24.884 -2.840  1.00 32.20 ? 934  HOH A O   1 
HETATM 1783 O O   . HOH Q 5 .   ? 27.209  -16.411 -5.925  1.00 28.05 ? 935  HOH A O   1 
HETATM 1784 O O   . HOH Q 5 .   ? -3.518  -21.587 -3.359  1.00 29.70 ? 936  HOH A O   1 
HETATM 1785 O O   . HOH Q 5 .   ? 2.503   -20.393 -25.208 1.00 33.63 ? 937  HOH A O   1 
HETATM 1786 O O   . HOH Q 5 .   ? 13.442  -2.584  -6.706  1.00 31.29 ? 938  HOH A O   1 
HETATM 1787 O O   . HOH Q 5 .   ? 8.167   -10.037 3.894   1.00 34.40 ? 939  HOH A O   1 
HETATM 1788 O O   . HOH Q 5 .   ? -10.086 -22.538 1.394   1.00 36.01 ? 940  HOH A O   1 
HETATM 1789 O O   . HOH Q 5 .   ? -10.384 -24.725 0.539   1.00 33.17 ? 941  HOH A O   1 
HETATM 1790 O O   . HOH Q 5 .   ? 23.018  -7.946  -6.378  1.00 24.59 ? 942  HOH A O   1 
HETATM 1791 O O   . HOH Q 5 .   ? 1.774   -10.096 -18.726 1.00 28.43 ? 943  HOH A O   1 
HETATM 1792 O O   . HOH Q 5 .   ? 7.618   -12.346 2.574   1.00 34.37 ? 944  HOH A O   1 
HETATM 1793 O O   . HOH Q 5 .   ? -6.476  -16.249 1.202   1.00 30.37 ? 945  HOH A O   1 
HETATM 1794 O O   . HOH Q 5 .   ? -3.241  -9.273  -22.094 1.00 35.89 ? 946  HOH A O   1 
HETATM 1795 O O   . HOH Q 5 .   ? 18.849  -14.883 -19.430 1.00 34.18 ? 947  HOH A O   1 
HETATM 1796 O O   . HOH Q 5 .   ? 4.816   -5.911  -18.733 1.00 29.05 ? 948  HOH A O   1 
HETATM 1797 O O   . HOH Q 5 .   ? -7.307  2.524   -25.949 1.00 35.66 ? 949  HOH A O   1 
HETATM 1798 O O   . HOH Q 5 .   ? -7.377  -28.966 1.979   1.00 34.68 ? 950  HOH A O   1 
HETATM 1799 O O   . HOH Q 5 .   ? 8.470   -14.929 0.942   1.00 38.42 ? 951  HOH A O   1 
HETATM 1800 O O   . HOH Q 5 .   ? 13.343  -2.303  -2.341  1.00 29.56 ? 952  HOH A O   1 
HETATM 1801 O O   . HOH Q 5 .   ? 7.636   -2.727  -13.428 1.00 33.58 ? 953  HOH A O   1 
HETATM 1802 O O   . HOH Q 5 .   ? -17.011 -0.885  -4.389  1.00 34.48 ? 954  HOH A O   1 
HETATM 1803 O O   . HOH Q 5 .   ? 8.942   -20.938 -12.578 1.00 30.14 ? 955  HOH A O   1 
HETATM 1804 O O   . HOH Q 5 .   ? -11.017 -11.634 -9.246  1.00 46.12 ? 956  HOH A O   1 
HETATM 1805 O O   . HOH Q 5 .   ? -7.958  -27.129 -5.295  1.00 33.76 ? 957  HOH A O   1 
HETATM 1806 O O   . HOH Q 5 .   ? -2.372  2.492   -2.163  1.00 29.94 ? 958  HOH A O   1 
HETATM 1807 O O   . HOH Q 5 .   ? -13.964 6.806   -18.973 1.00 38.63 ? 959  HOH A O   1 
HETATM 1808 O O   . HOH Q 5 .   ? 11.443  -23.181 -7.815  1.00 30.40 ? 960  HOH A O   1 
HETATM 1809 O O   . HOH Q 5 .   ? 4.009   0.185   -4.867  1.00 32.27 ? 961  HOH A O   1 
HETATM 1810 O O   . HOH Q 5 .   ? -0.904  -27.534 -11.716 1.00 32.56 ? 962  HOH A O   1 
HETATM 1811 O O   . HOH Q 5 .   ? -3.340  -27.777 -10.625 1.00 38.39 ? 963  HOH A O   1 
HETATM 1812 O O   . HOH Q 5 .   ? -7.359  -21.909 -17.861 1.00 33.49 ? 964  HOH A O   1 
HETATM 1813 O O   . HOH Q 5 .   ? -11.252 -10.606 -1.574  1.00 32.67 ? 965  HOH A O   1 
HETATM 1814 O O   . HOH Q 5 .   ? -2.930  4.606   -7.940  1.00 46.08 ? 966  HOH A O   1 
HETATM 1815 O O   . HOH Q 5 .   ? -10.723 -9.211  -10.645 1.00 39.21 ? 967  HOH A O   1 
HETATM 1816 O O   . HOH Q 5 .   ? 5.365   -4.069  6.665   1.00 44.41 ? 968  HOH A O   1 
HETATM 1817 O O   . HOH Q 5 .   ? 3.008   2.451   -2.887  1.00 33.35 ? 969  HOH A O   1 
HETATM 1818 O O   . HOH Q 5 .   ? 29.832  -15.686 -5.761  1.00 35.39 ? 970  HOH A O   1 
HETATM 1819 O O   . HOH Q 5 .   ? 8.953   -5.358  -16.794 1.00 36.58 ? 971  HOH A O   1 
HETATM 1820 O O   . HOH Q 5 .   ? 5.794   1.454   -6.059  1.00 37.27 ? 972  HOH A O   1 
HETATM 1821 O O   . HOH Q 5 .   ? 6.921   -27.181 -1.489  1.00 35.91 ? 973  HOH A O   1 
HETATM 1822 O O   . HOH Q 5 .   ? 13.121  -4.499  -17.125 1.00 40.65 ? 974  HOH A O   1 
HETATM 1823 O O   . HOH Q 5 .   ? -7.115  -7.814  -14.489 1.00 32.72 ? 975  HOH A O   1 
HETATM 1824 O O   . HOH Q 5 .   ? 8.743   -20.256 -4.443  1.00 27.91 ? 976  HOH A O   1 
HETATM 1825 O O   . HOH Q 5 .   ? -11.267 -8.307  -0.310  1.00 38.93 ? 977  HOH A O   1 
HETATM 1826 O O   . HOH Q 5 .   ? 2.826   1.663   -12.673 1.00 43.13 ? 978  HOH A O   1 
HETATM 1827 O O   . HOH Q 5 .   ? 23.423  -9.306  -8.285  1.00 38.81 ? 979  HOH A O   1 
HETATM 1828 O O   . HOH Q 5 .   ? 12.032  -25.791 -7.008  1.00 41.23 ? 980  HOH A O   1 
HETATM 1829 O O   . HOH Q 5 .   ? -10.168 -14.655 -0.049  1.00 41.31 ? 981  HOH A O   1 
HETATM 1830 O O   . HOH Q 5 .   ? -1.002  -2.799  3.754   1.00 37.20 ? 982  HOH A O   1 
HETATM 1831 O O   . HOH Q 5 .   ? 0.545   -18.154 -24.676 1.00 36.38 ? 983  HOH A O   1 
HETATM 1832 O O   . HOH Q 5 .   ? 2.559   -22.986 -25.093 1.00 40.09 ? 984  HOH A O   1 
HETATM 1833 O O   . HOH Q 5 .   ? 4.051   -9.599  -19.829 1.00 37.57 ? 985  HOH A O   1 
HETATM 1834 O O   . HOH Q 5 .   ? -15.490 7.304   -14.777 1.00 50.37 ? 986  HOH A O   1 
HETATM 1835 O O   . HOH Q 5 .   ? 6.184   -20.042 -15.759 1.00 36.45 ? 987  HOH A O   1 
HETATM 1836 O O   . HOH Q 5 .   ? 22.135  -4.189  -9.145  1.00 38.59 ? 988  HOH A O   1 
HETATM 1837 O O   . HOH Q 5 .   ? 25.457  -24.046 -8.281  1.00 34.79 ? 989  HOH A O   1 
HETATM 1838 O O   . HOH Q 5 .   ? 4.416   -27.639 -0.768  1.00 34.18 ? 990  HOH A O   1 
HETATM 1839 O O   . HOH Q 5 .   ? -19.184 -10.339 -2.422  1.00 44.09 ? 991  HOH A O   1 
HETATM 1840 O O   . HOH Q 5 .   ? 21.863  -24.040 -2.365  1.00 38.60 ? 992  HOH A O   1 
HETATM 1841 O O   . HOH Q 5 .   ? -15.270 -17.691 -6.798  1.00 42.37 ? 993  HOH A O   1 
HETATM 1842 O O   . HOH Q 5 .   ? -5.819  8.186   -21.199 1.00 43.44 ? 994  HOH A O   1 
HETATM 1843 O O   . HOH Q 5 .   ? -11.039 -6.160  -12.505 1.00 36.31 ? 995  HOH A O   1 
HETATM 1844 O O   . HOH Q 5 .   ? 24.462  -10.378 -16.937 1.00 38.69 ? 996  HOH A O   1 
HETATM 1845 O O   . HOH Q 5 .   ? -7.414  -14.039 -19.359 1.00 39.82 ? 997  HOH A O   1 
HETATM 1846 O O   . HOH Q 5 .   ? 8.401   -8.173  7.657   1.00 50.17 ? 998  HOH A O   1 
HETATM 1847 O O   . HOH Q 5 .   ? -15.721 2.508   -13.144 1.00 44.27 ? 999  HOH A O   1 
HETATM 1848 O O   . HOH Q 5 .   ? -8.466  -2.274  0.988   1.00 34.80 ? 1000 HOH A O   1 
HETATM 1849 O O   . HOH Q 5 .   ? 6.603   -19.952 -19.074 1.00 36.32 ? 1001 HOH A O   1 
HETATM 1850 O O   . HOH Q 5 .   ? -7.596  -17.355 -15.219 1.00 32.90 ? 1002 HOH A O   1 
HETATM 1851 O O   . HOH Q 5 .   ? 0.923   3.260   -12.060 1.00 41.37 ? 1003 HOH A O   1 
HETATM 1852 O O   . HOH Q 5 .   ? 14.162  -21.724 -0.845  1.00 46.57 ? 1004 HOH A O   1 
HETATM 1853 O O   . HOH Q 5 .   ? 6.972   -5.137  -15.347 1.00 41.30 ? 1005 HOH A O   1 
HETATM 1854 O O   . HOH Q 5 .   ? -18.351 -4.144  -2.572  1.00 46.37 ? 1006 HOH A O   1 
HETATM 1855 O O   . HOH Q 5 .   ? 30.987  -17.277 -7.907  1.00 47.03 ? 1007 HOH A O   1 
HETATM 1856 O O   . HOH Q 5 .   ? -8.889  -7.113  -16.734 1.00 46.34 ? 1008 HOH A O   1 
HETATM 1857 O O   . HOH Q 5 .   ? -19.098 -3.977  -6.811  1.00 35.57 ? 1009 HOH A O   1 
HETATM 1858 O O   . HOH Q 5 .   ? -7.794  0.429   0.742   1.00 37.89 ? 1010 HOH A O   1 
HETATM 1859 O O   . HOH Q 5 .   ? -4.585  11.044  -11.193 1.00 35.92 ? 1011 HOH A O   1 
HETATM 1860 O O   . HOH Q 5 .   ? -6.061  7.556   -0.396  1.00 45.53 ? 1012 HOH A O   1 
HETATM 1861 O O   . HOH Q 5 .   ? -10.633 -27.700 -11.379 1.00 39.10 ? 1013 HOH A O   1 
HETATM 1862 O O   . HOH Q 5 .   ? 4.819   -7.750  -21.917 1.00 40.98 ? 1014 HOH A O   1 
HETATM 1863 O O   . HOH Q 5 .   ? 27.306  -10.054 -3.034  1.00 49.19 ? 1015 HOH A O   1 
HETATM 1864 O O   . HOH Q 5 .   ? -12.414 -11.063 -12.258 1.00 41.95 ? 1016 HOH A O   1 
HETATM 1865 O O   . HOH Q 5 .   ? -10.004 -5.787  -0.049  1.00 34.75 ? 1017 HOH A O   1 
HETATM 1866 O O   . HOH Q 5 .   ? -18.522 -1.175  -6.896  1.00 45.92 ? 1018 HOH A O   1 
HETATM 1867 O O   . HOH Q 5 .   ? -5.559  5.474   3.725   1.00 43.62 ? 1019 HOH A O   1 
HETATM 1868 O O   . HOH Q 5 .   ? 6.752   -22.377 -2.580  1.00 33.35 ? 1020 HOH A O   1 
HETATM 1869 O O   . HOH Q 5 .   ? 10.456  -21.833 -5.012  1.00 35.04 ? 1021 HOH A O   1 
HETATM 1870 O O   . HOH Q 5 .   ? -12.128 -22.107 -10.815 1.00 40.73 ? 1022 HOH A O   1 
HETATM 1871 O O   . HOH Q 5 .   ? -2.284  -27.925 3.521   1.00 51.66 ? 1023 HOH A O   1 
HETATM 1872 O O   . HOH Q 5 .   ? 27.248  -22.075 -7.857  1.00 39.16 ? 1024 HOH A O   1 
HETATM 1873 O O   . HOH Q 5 .   ? 7.161   -5.501  -18.807 1.00 42.44 ? 1025 HOH A O   1 
HETATM 1874 O O   . HOH Q 5 .   ? 1.733   -30.088 -8.107  1.00 43.01 ? 1026 HOH A O   1 
HETATM 1875 O O   . HOH Q 5 .   ? -4.400  2.907   -24.896 1.00 47.16 ? 1027 HOH A O   1 
HETATM 1876 O O   . HOH Q 5 .   ? 13.893  -10.378 4.087   1.00 39.67 ? 1028 HOH A O   1 
HETATM 1877 O O   . HOH Q 5 .   ? 2.821   -23.535 2.466   1.00 40.25 ? 1029 HOH A O   1 
HETATM 1878 O O   . HOH Q 5 .   ? -16.299 -14.906 -9.347  1.00 57.19 ? 1030 HOH A O   1 
HETATM 1879 O O   . HOH Q 5 .   ? -13.685 -15.516 -9.468  1.00 38.58 ? 1031 HOH A O   1 
HETATM 1880 O O   . HOH Q 5 .   ? 7.275   -24.865 4.084   1.00 44.25 ? 1032 HOH A O   1 
HETATM 1881 O O   . HOH Q 5 .   ? 4.929   1.049   -11.501 1.00 51.25 ? 1033 HOH A O   1 
HETATM 1882 O O   . HOH Q 5 .   ? 8.527   -2.254  5.988   1.00 46.58 ? 1034 HOH A O   1 
HETATM 1883 O O   . HOH Q 5 .   ? 4.848   -6.932  7.279   1.00 67.54 ? 1035 HOH A O   1 
HETATM 1884 O O   . HOH Q 5 .   ? 11.089  -10.606 3.574   1.00 36.88 ? 1036 HOH A O   1 
HETATM 1885 O O   . HOH Q 5 .   ? -17.970 -0.162  -9.563  1.00 42.42 ? 1037 HOH A O   1 
HETATM 1886 O O   . HOH Q 5 .   ? 10.323  -4.316  6.785   1.00 39.90 ? 1038 HOH A O   1 
HETATM 1887 O O   . HOH Q 5 .   ? 28.123  -11.930 -13.220 1.00 47.07 ? 1039 HOH A O   1 
HETATM 1888 O O   . HOH Q 5 .   ? -13.786 -22.774 -4.291  1.00 54.94 ? 1040 HOH A O   1 
HETATM 1889 O O   . HOH Q 5 .   ? 1.330   1.535   -5.043  1.00 34.98 ? 1041 HOH A O   1 
HETATM 1890 O O   . HOH Q 5 .   ? -3.057  8.006   -8.630  1.00 41.32 ? 1042 HOH A O   1 
HETATM 1891 O O   . HOH Q 5 .   ? -3.465  -24.125 -23.875 1.00 49.79 ? 1043 HOH A O   1 
HETATM 1892 O O   . HOH Q 5 .   ? -2.993  5.265   -25.440 1.00 50.04 ? 1044 HOH A O   1 
HETATM 1893 O O   . HOH Q 5 .   ? -8.363  -13.823 -15.795 1.00 54.35 ? 1045 HOH A O   1 
HETATM 1894 O O   . HOH Q 5 .   ? -1.860  -7.650  3.025   1.00 36.45 ? 1046 HOH A O   1 
HETATM 1895 O O   . HOH Q 5 .   ? -13.015 -3.010  1.506   1.00 45.28 ? 1047 HOH A O   1 
HETATM 1896 O O   . HOH Q 5 .   ? -7.027  11.954  -9.799  1.00 50.34 ? 1048 HOH A O   1 
HETATM 1897 O O   . HOH Q 5 .   ? -13.554 -12.666 -8.874  1.00 46.17 ? 1049 HOH A O   1 
HETATM 1898 O O   . HOH Q 5 .   ? 5.801   -14.417 3.060   1.00 36.85 ? 1050 HOH A O   1 
HETATM 1899 O O   . HOH Q 5 .   ? -14.601 1.095   3.254   1.00 56.29 ? 1051 HOH A O   1 
HETATM 1900 O O   . HOH Q 5 .   ? 24.675  -25.773 -12.613 1.00 38.95 ? 1052 HOH A O   1 
HETATM 1901 O O   . HOH Q 5 .   ? 8.486   -27.532 0.803   1.00 38.63 ? 1053 HOH A O   1 
HETATM 1902 O O   . HOH Q 5 .   ? 7.131   -6.500  -21.479 1.00 48.27 ? 1054 HOH A O   1 
HETATM 1903 O O   . HOH Q 5 .   ? 4.121   1.541   -7.975  1.00 51.49 ? 1055 HOH A O   1 
HETATM 1904 O O   . HOH Q 5 .   ? -10.427 -22.838 -18.413 1.00 49.99 ? 1056 HOH A O   1 
HETATM 1905 O O   . HOH Q 5 .   ? -8.028  -11.304 -15.705 1.00 42.29 ? 1057 HOH A O   1 
HETATM 1906 O O   . HOH Q 5 .   ? -9.001  -25.230 -18.024 1.00 42.74 ? 1058 HOH A O   1 
HETATM 1907 O O   . HOH Q 5 .   ? 2.043   -15.915 -25.860 1.00 44.32 ? 1059 HOH A O   1 
HETATM 1908 O O   . HOH Q 5 .   ? -9.630  -14.806 -13.758 1.00 39.25 ? 1060 HOH A O   1 
HETATM 1909 O O   . HOH Q 5 .   ? -6.551  -19.463 -16.814 1.00 39.78 ? 1061 HOH A O   1 
HETATM 1910 O O   . HOH Q 5 .   ? 12.703  -1.152  -4.672  1.00 47.41 ? 1062 HOH A O   1 
HETATM 1911 O O   . HOH Q 5 .   ? 12.321  -2.173  -11.349 1.00 42.45 ? 1063 HOH A O   1 
HETATM 1912 O O   . HOH Q 5 .   ? -8.171  -7.411  -21.458 1.00 42.91 ? 1064 HOH A O   1 
HETATM 1913 O O   . HOH Q 5 .   ? -6.050  -3.498  -27.204 1.00 43.75 ? 1065 HOH A O   1 
HETATM 1914 O O   . HOH Q 5 .   ? -15.525 5.519   -8.523  1.00 49.80 ? 1066 HOH A O   1 
HETATM 1915 O O   . HOH Q 5 .   ? 15.239  -25.752 -6.493  1.00 43.06 ? 1067 HOH A O   1 
HETATM 1916 O O   . HOH Q 5 .   ? -18.097 2.582   -9.013  1.00 57.54 ? 1068 HOH A O   1 
HETATM 1917 O O   . HOH Q 5 .   ? 20.848  -3.009  7.262   1.00 41.77 ? 1069 HOH A O   1 
HETATM 1918 O O   . HOH Q 5 .   ? -16.292 4.109   -10.674 1.00 47.66 ? 1070 HOH A O   1 
HETATM 1919 O O   . HOH Q 5 .   ? -16.399 0.074   -12.070 1.00 44.30 ? 1071 HOH A O   1 
HETATM 1920 O O   . HOH Q 5 .   ? 23.146  -23.087 -16.220 1.00 54.22 ? 1072 HOH A O   1 
HETATM 1921 O O   . HOH Q 5 .   ? -19.639 -2.193  -11.262 1.00 54.33 ? 1073 HOH A O   1 
HETATM 1922 O O   . HOH Q 5 .   ? 14.577  -1.780  -9.222  1.00 40.29 ? 1074 HOH A O   1 
HETATM 1923 O O   . HOH Q 5 .   ? -7.734  -33.060 -15.732 1.00 45.38 ? 1075 HOH A O   1 
HETATM 1924 O O   . HOH Q 5 .   ? 10.029  -1.158  -12.829 1.00 51.16 ? 1076 HOH A O   1 
HETATM 1925 O O   . HOH Q 5 .   ? -9.677  12.927  -15.529 1.00 64.95 ? 1077 HOH A O   1 
HETATM 1926 O O   . HOH Q 5 .   ? 21.865  -3.170  -4.430  1.00 41.14 ? 1078 HOH A O   1 
HETATM 1927 O O   . HOH Q 5 .   ? 10.342  -24.040 -3.404  1.00 51.62 ? 1079 HOH A O   1 
HETATM 1928 O O   . HOH Q 5 .   ? 25.962  -9.347  -11.253 1.00 33.97 ? 1080 HOH A O   1 
HETATM 1929 O O   . HOH Q 5 .   ? 20.007  -9.469  -19.454 1.00 56.78 ? 1081 HOH A O   1 
HETATM 1930 O O   . HOH Q 5 .   ? 11.877  -7.913  -25.878 1.00 58.57 ? 1082 HOH A O   1 
HETATM 1931 O O   . HOH Q 5 .   ? 7.869   0.668   -15.894 1.00 37.35 ? 1083 HOH A O   1 
HETATM 1932 O O   . HOH Q 5 .   ? 17.062  -27.626 -8.977  1.00 62.46 ? 1084 HOH A O   1 
HETATM 1933 O O   . HOH Q 5 .   ? 7.298   -16.575 -20.509 1.00 51.17 ? 1085 HOH A O   1 
HETATM 1934 O O   . HOH Q 5 .   ? 20.617  -3.862  -13.174 1.00 46.12 ? 1086 HOH A O   1 
HETATM 1935 O O   . HOH Q 5 .   ? -14.595 -19.785 -1.742  1.00 53.32 ? 1087 HOH A O   1 
HETATM 1936 O O   . HOH Q 5 .   ? -6.756  -16.855 -1.119  1.00 44.22 ? 1088 HOH A O   1 
HETATM 1937 O O   . HOH Q 5 .   ? -9.383  -8.342  -13.119 1.00 43.61 ? 1089 HOH A O   1 
HETATM 1938 O O   . HOH Q 5 .   ? -14.355 3.713   -20.227 1.00 46.35 ? 1090 HOH A O   1 
HETATM 1939 O O   . HOH Q 5 .   ? -7.942  -30.113 -4.665  1.00 49.37 ? 1091 HOH A O   1 
HETATM 1940 O O   . HOH Q 5 .   ? -7.259  -13.723 0.425   1.00 36.71 ? 1092 HOH A O   1 
HETATM 1941 O O   . HOH Q 5 .   ? 15.155  -23.898 0.328   1.00 41.50 ? 1093 HOH A O   1 
HETATM 1942 O O   . HOH Q 5 .   ? 11.184  -12.852 2.504   1.00 40.53 ? 1094 HOH A O   1 
HETATM 1943 O O   . HOH Q 5 .   ? 0.107   4.175   -9.520  1.00 43.99 ? 1095 HOH A O   1 
HETATM 1944 O O   . HOH Q 5 .   ? -13.451 0.383   -23.081 1.00 49.82 ? 1096 HOH A O   1 
HETATM 1945 O O   . HOH Q 5 .   ? 5.652   -0.558  -9.678  1.00 53.72 ? 1097 HOH A O   1 
HETATM 1946 O O   . HOH Q 5 .   ? 2.012   -12.642 5.438   1.00 44.56 ? 1098 HOH A O   1 
HETATM 1947 O O   . HOH Q 5 .   ? -13.192 -7.550  -13.816 1.00 51.52 ? 1099 HOH A O   1 
HETATM 1948 O O   . HOH Q 5 .   ? -10.519 -3.856  2.062   1.00 49.09 ? 1100 HOH A O   1 
HETATM 1949 O O   . HOH Q 5 .   ? -11.214 -6.424  -23.478 1.00 42.62 ? 1101 HOH A O   1 
HETATM 1950 O O   . HOH Q 5 .   ? 23.750  -5.893  -7.487  1.00 35.71 ? 1102 HOH A O   1 
HETATM 1951 O O   . HOH Q 5 .   ? 0.130   -23.458 -26.552 1.00 42.93 ? 1103 HOH A O   1 
HETATM 1952 O O   . HOH Q 5 .   ? 25.332  -8.387  -5.865  1.00 52.87 ? 1104 HOH A O   1 
HETATM 1953 O O   . HOH Q 5 .   ? -5.342  10.748  -20.388 1.00 42.74 ? 1105 HOH A O   1 
HETATM 1954 O O   . HOH Q 5 .   ? 12.215  -13.402 0.212   1.00 38.07 ? 1106 HOH A O   1 
HETATM 1955 O O   . HOH Q 5 .   ? 25.869  -26.445 -6.812  1.00 45.79 ? 1107 HOH A O   1 
HETATM 1956 O O   . HOH Q 5 .   ? 7.896   -17.687 2.099   1.00 42.35 ? 1108 HOH A O   1 
HETATM 1957 O O   . HOH Q 5 .   ? 17.171  -3.100  -3.892  1.00 40.25 ? 1109 HOH A O   1 
HETATM 1958 O O   . HOH Q 5 .   ? -13.214 2.872   -22.849 1.00 56.84 ? 1110 HOH A O   1 
HETATM 1959 O O   . HOH Q 5 .   ? -15.843 -21.386 -4.449  1.00 56.97 ? 1111 HOH A O   1 
HETATM 1960 O O   . HOH Q 5 .   ? 19.562  -1.045  -10.228 1.00 45.94 ? 1112 HOH A O   1 
HETATM 1961 O O   . HOH Q 5 .   ? 9.161   -25.180 -13.285 1.00 52.17 ? 1113 HOH A O   1 
HETATM 1962 O O   . HOH Q 5 .   ? 7.063   -7.813  -26.017 1.00 53.93 ? 1114 HOH A O   1 
HETATM 1963 O O   . HOH Q 5 .   ? 24.595  -25.131 -5.052  1.00 44.03 ? 1115 HOH A O   1 
HETATM 1964 O O   . HOH Q 5 .   ? 10.125  -10.844 6.132   1.00 54.32 ? 1116 HOH A O   1 
HETATM 1965 O O   . HOH Q 5 .   ? -13.394 -22.556 -8.480  1.00 57.37 ? 1117 HOH A O   1 
HETATM 1966 O O   . HOH Q 5 .   ? 5.719   3.864   -5.369  1.00 48.44 ? 1118 HOH A O   1 
HETATM 1967 O O   . HOH Q 5 .   ? -15.867 -22.057 -11.492 1.00 52.69 ? 1119 HOH A O   1 
HETATM 1968 O O   . HOH Q 5 .   ? 27.460  -23.140 -5.162  1.00 54.84 ? 1120 HOH A O   1 
HETATM 1969 O O   . HOH Q 5 .   ? 18.965  -27.591 -6.610  1.00 50.02 ? 1121 HOH A O   1 
HETATM 1970 O O   . HOH Q 5 .   ? -20.666 -4.268  -4.475  1.00 50.60 ? 1122 HOH A O   1 
HETATM 1971 O O   . HOH Q 5 .   ? -10.127 -10.217 -14.673 1.00 47.89 ? 1123 HOH A O   1 
HETATM 1972 O O   . HOH Q 5 .   ? -4.838  -21.594 -25.725 1.00 53.04 ? 1124 HOH A O   1 
HETATM 1973 O O   . HOH Q 5 .   ? 8.324   -20.999 -15.164 1.00 60.65 ? 1125 HOH A O   1 
HETATM 1974 O O   . HOH Q 5 .   ? 2.038   7.064   -12.588 1.00 49.02 ? 1126 HOH A O   1 
HETATM 1975 O O   . HOH Q 5 .   ? 11.554  -20.625 -1.638  1.00 50.69 ? 1127 HOH A O   1 
HETATM 1976 O O   . HOH Q 5 .   ? 20.099  -16.890 -20.927 1.00 57.35 ? 1128 HOH A O   1 
HETATM 1977 O O   . HOH Q 5 .   ? -0.018  7.107   -8.845  1.00 56.30 ? 1129 HOH A O   1 
HETATM 1978 O O   . HOH Q 5 .   ? -15.670 -18.238 -4.464  1.00 50.71 ? 1130 HOH A O   1 
HETATM 1979 O O   . HOH Q 5 .   ? -11.420 -13.582 -12.381 1.00 51.77 ? 1131 HOH A O   1 
HETATM 1980 O O   . HOH Q 5 .   ? -10.949 -1.734  -26.803 1.00 53.04 ? 1132 HOH A O   1 
HETATM 1981 O O   . HOH Q 5 .   ? -21.110 -9.813  -7.062  1.00 44.20 ? 1133 HOH A O   1 
HETATM 1982 O O   . HOH Q 5 .   ? 10.163  -7.630  -19.660 1.00 40.77 ? 1134 HOH A O   1 
HETATM 1983 O O   . HOH Q 5 .   ? 9.053   -20.903 -0.963  1.00 52.15 ? 1135 HOH A O   1 
HETATM 1984 O O   . HOH Q 5 .   ? 13.364  -3.796  -20.100 1.00 75.41 ? 1136 HOH A O   1 
HETATM 1985 O O   . HOH Q 5 .   ? -18.281 5.636   -11.577 1.00 89.62 ? 1137 HOH A O   1 
HETATM 1986 O O   . HOH Q 5 .   ? 2.024   -2.369  -27.761 1.00 46.66 ? 1138 HOH A O   1 
HETATM 1987 O O   . HOH Q 5 .   ? -8.613  -30.986 0.614   1.00 50.04 ? 1139 HOH A O   1 
HETATM 1988 O O   . HOH Q 5 .   ? -19.740 -4.890  -10.908 1.00 56.20 ? 1140 HOH A O   1 
HETATM 1989 O O   . HOH Q 5 .   ? 5.241   -8.796  -24.461 1.00 65.64 ? 1141 HOH A O   1 
HETATM 1990 O O   . HOH Q 5 .   ? -3.973  -11.382 -24.081 1.00 47.30 ? 1142 HOH A O   1 
HETATM 1991 O O   . HOH Q 5 .   ? -4.359  -14.484 -25.486 1.00 54.17 ? 1143 HOH A O   1 
HETATM 1992 O O   . HOH Q 5 .   ? -7.831  -9.870  -18.090 1.00 54.86 ? 1144 HOH A O   1 
HETATM 1993 O O   . HOH Q 5 .   ? 20.685  -29.471 -7.582  1.00 52.32 ? 1145 HOH A O   1 
HETATM 1994 O O   . HOH Q 5 .   ? -18.746 -12.239 -0.620  1.00 56.51 ? 1146 HOH A O   1 
HETATM 1995 O O   . HOH Q 5 .   ? -1.361  -18.866 -26.433 1.00 46.71 ? 1147 HOH A O   1 
HETATM 1996 O O   . HOH Q 5 .   ? 7.491   0.562   -18.355 1.00 47.92 ? 1148 HOH A O   1 
HETATM 1997 O O   . HOH Q 5 .   ? 8.416   -23.698 -15.303 1.00 61.61 ? 1149 HOH A O   1 
HETATM 1998 O O   . HOH Q 5 .   ? -9.026  8.217   -19.897 1.00 43.33 ? 1150 HOH A O   1 
HETATM 1999 O O   . HOH Q 5 .   ? -6.543  -7.516  -25.776 1.00 47.64 ? 1151 HOH A O   1 
HETATM 2000 O O   . HOH Q 5 .   ? -14.148 -7.864  0.329   1.00 50.77 ? 1152 HOH A O   1 
HETATM 2001 O O   . HOH Q 5 .   ? -9.881  -30.766 -19.172 1.00 53.45 ? 1153 HOH A O   1 
HETATM 2002 O O   . HOH Q 5 .   ? -0.531  3.199   -3.906  1.00 55.68 ? 1154 HOH A O   1 
HETATM 2003 O O   . HOH Q 5 .   ? -21.852 -7.410  -6.670  1.00 59.21 ? 1155 HOH A O   1 
HETATM 2004 O O   . HOH Q 5 .   ? -14.938 -12.088 -10.673 1.00 51.21 ? 1156 HOH A O   1 
HETATM 2005 O O   . HOH Q 5 .   ? -16.222 -17.480 -2.195  1.00 48.69 ? 1157 HOH A O   1 
HETATM 2006 O O   . HOH Q 5 .   ? 17.354  -4.458  -1.162  1.00 67.06 ? 1158 HOH A O   1 
HETATM 2007 O O   . HOH Q 5 .   ? -6.501  -18.283 -24.046 1.00 48.14 ? 1159 HOH A O   1 
HETATM 2008 O O   . HOH Q 5 .   ? 1.172   -25.306 3.134   1.00 51.98 ? 1160 HOH A O   1 
HETATM 2009 O O   . HOH Q 5 .   ? 7.635   -28.908 -4.089  1.00 45.00 ? 1161 HOH A O   1 
HETATM 2010 O O   . HOH Q 5 .   ? 28.328  -26.259 -5.567  1.00 67.81 ? 1162 HOH A O   1 
HETATM 2011 O O   . HOH Q 5 .   ? 12.076  -26.181 -3.702  1.00 62.87 ? 1163 HOH A O   1 
HETATM 2012 O O   . HOH Q 5 .   ? 13.945  -23.113 -25.928 1.00 63.01 ? 1164 HOH A O   1 
HETATM 2013 O O   . HOH Q 5 .   ? 17.306  -0.880  -8.811  1.00 68.09 ? 1165 HOH A O   1 
HETATM 2014 O O   . HOH Q 5 .   ? -4.728  -29.616 1.564   1.00 51.92 ? 1166 HOH A O   1 
HETATM 2015 O O   . HOH Q 5 .   ? 1.926   3.420   -6.929  1.00 54.90 ? 1167 HOH A O   1 
HETATM 2016 O O   . HOH Q 5 .   ? 10.500  -28.480 -3.731  1.00 49.10 ? 1168 HOH A O   1 
HETATM 2017 O O   . HOH Q 5 .   ? 25.345  -29.222 -6.706  1.00 52.98 ? 1169 HOH A O   1 
HETATM 2018 O O   . HOH Q 5 .   ? -3.098  -17.142 -27.479 1.00 58.44 ? 1170 HOH A O   1 
HETATM 2019 O O   . HOH Q 5 .   ? -5.962  10.374  -1.183  1.00 64.15 ? 1171 HOH A O   1 
HETATM 2020 O O   . HOH Q 5 .   ? -9.767  -8.689  -23.801 1.00 51.72 ? 1172 HOH A O   1 
HETATM 2021 O O   . HOH Q 5 .   ? -2.238  -3.470  -29.568 1.00 53.58 ? 1173 HOH A O   1 
HETATM 2022 O O   . HOH Q 5 .   ? -21.172 0.015   -6.321  1.00 60.59 ? 1174 HOH A O   1 
HETATM 2023 O O   . HOH Q 5 .   ? 23.229  -29.920 -7.601  1.00 58.43 ? 1175 HOH A O   1 
HETATM 2024 O O   . HOH Q 5 .   ? -4.979  -28.659 -22.423 1.00 55.74 ? 1176 HOH A O   1 
HETATM 2025 O O   . HOH Q 5 .   ? -11.012 -27.567 -5.670  1.00 54.51 ? 1177 HOH A O   1 
HETATM 2026 O O   . HOH Q 5 .   ? -15.691 8.034   -4.977  1.00 51.13 ? 1178 HOH A O   1 
HETATM 2027 O O   . HOH Q 5 .   ? -10.016 -30.380 -11.655 1.00 51.78 ? 1179 HOH A O   1 
HETATM 2028 O O   . HOH Q 5 .   ? 13.075  -20.059 -17.058 1.00 56.25 ? 1180 HOH A O   1 
HETATM 2029 O O   . HOH Q 5 .   ? 9.302   -5.277  -20.155 1.00 56.44 ? 1181 HOH A O   1 
HETATM 2030 O O   . HOH Q 5 .   ? -18.918 -0.019  -2.869  1.00 47.09 ? 1182 HOH A O   1 
HETATM 2031 O O   . HOH Q 5 .   ? 9.591   -1.392  -15.428 1.00 57.27 ? 1183 HOH A O   1 
HETATM 2032 O O   . HOH Q 5 .   ? -18.389 -3.430  -13.511 1.00 70.45 ? 1184 HOH A O   1 
HETATM 2033 O O   . HOH Q 5 .   ? 17.145  -23.694 -20.683 1.00 58.65 ? 1185 HOH A O   1 
HETATM 2034 O O   . HOH Q 5 .   ? 6.726   -28.834 -6.452  1.00 53.07 ? 1186 HOH A O   1 
HETATM 2035 O O   . HOH Q 5 .   ? 10.058  -23.021 -11.917 1.00 68.63 ? 1187 HOH A O   1 
HETATM 2036 O O   . HOH Q 5 .   ? 7.441   -21.948 -18.286 1.00 61.58 ? 1188 HOH A O   1 
HETATM 2037 O O   . HOH Q 5 .   ? -0.848  -31.434 -7.919  1.00 62.44 ? 1189 HOH A O   1 
HETATM 2038 O O   . HOH Q 5 .   ? 4.191   4.515   -3.527  1.00 50.50 ? 1190 HOH A O   1 
HETATM 2039 O O   . HOH Q 5 .   ? 17.662  -27.674 -11.355 1.00 53.57 ? 1191 HOH A O   1 
HETATM 2040 O O   . HOH Q 5 .   ? 22.013  -19.958 -17.966 1.00 55.53 ? 1192 HOH A O   1 
HETATM 2041 O O   . HOH Q 5 .   ? -8.688  -19.148 -22.453 1.00 61.18 ? 1193 HOH A O   1 
HETATM 2042 O O   . HOH Q 5 .   ? 9.095   2.821   -15.045 1.00 49.32 ? 1194 HOH A O   1 
HETATM 2043 O O   . HOH Q 5 .   ? 1.289   3.842   -0.397  1.00 51.33 ? 1195 HOH A O   1 
HETATM 2044 O O   . HOH Q 5 .   ? 19.677  -19.679 -19.092 1.00 60.79 ? 1196 HOH A O   1 
HETATM 2045 O O   . HOH Q 5 .   ? 6.176   -9.601  5.611   1.00 55.23 ? 1197 HOH A O   1 
HETATM 2046 O O   . HOH Q 5 .   ? -14.972 8.374   -8.512  1.00 65.37 ? 1198 HOH A O   1 
HETATM 2047 O O   . HOH Q 5 .   ? 23.550  -7.551  -15.477 1.00 58.66 ? 1199 HOH A O   1 
HETATM 2048 O O   . HOH Q 5 .   ? 23.825  -30.373 -10.361 1.00 57.94 ? 1200 HOH A O   1 
HETATM 2049 O O   . HOH Q 5 .   ? -6.281  -18.450 -26.844 1.00 64.80 ? 1201 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   . CYS A 1   ? 0.8389 0.6640 0.7018 -0.0122 0.0322  -0.0943 25   CYS A N   
2    C CA  . CYS A 1   ? 0.8081 0.6356 0.6925 -0.0066 0.0366  -0.0866 25   CYS A CA  
3    C C   . CYS A 1   ? 0.8089 0.6235 0.6919 0.0043  0.0482  -0.0910 25   CYS A C   
4    O O   . CYS A 1   ? 0.8188 0.6306 0.6868 0.0096  0.0550  -0.0969 25   CYS A O   
5    C CB  . CYS A 1   ? 0.7658 0.6173 0.6648 -0.0046 0.0368  -0.0751 25   CYS A CB  
6    S SG  . CYS A 1   ? 0.6232 0.4913 0.5267 -0.0151 0.0249  -0.0688 25   CYS A SG  
7    N N   . ARG A 2   ? 0.7310 0.5385 0.6300 0.0081  0.0506  -0.0872 26   ARG A N   
8    C CA  . ARG A 2   ? 0.7918 0.5857 0.6919 0.0192  0.0615  -0.0909 26   ARG A CA  
9    C C   . ARG A 2   ? 0.7573 0.5694 0.6699 0.0288  0.0701  -0.0828 26   ARG A C   
10   O O   . ARG A 2   ? 0.6982 0.5044 0.6122 0.0392  0.0807  -0.0848 26   ARG A O   
11   C CB  . ARG A 2   ? 0.8942 0.6730 0.8075 0.0196  0.0601  -0.0890 26   ARG A CB  
12   C CG  . ARG A 2   ? 1.0160 0.7755 0.9194 0.0093  0.0515  -0.0962 26   ARG A CG  
13   C CD  . ARG A 2   ? 1.1311 0.8790 1.0509 0.0087  0.0493  -0.0910 26   ARG A CD  
14   N NE  . ARG A 2   ? 1.1863 0.9551 1.1259 0.0060  0.0446  -0.0772 26   ARG A NE  
15   C CZ  . ARG A 2   ? 1.2468 1.0122 1.2032 0.0069  0.0434  -0.0690 26   ARG A CZ  
16   N NH1 . ARG A 2   ? 1.2969 1.0384 1.2545 0.0106  0.0466  -0.0726 26   ARG A NH1 
17   N NH2 . ARG A 2   ? 1.2296 1.0148 1.2007 0.0043  0.0391  -0.0571 26   ARG A NH2 
18   N N   . THR A 3   ? 0.6578 0.4920 0.5802 0.0252  0.0656  -0.0735 27   THR A N   
19   C CA  . THR A 3   ? 0.6321 0.4842 0.5673 0.0321  0.0720  -0.0652 27   THR A CA  
20   C C   . THR A 3   ? 0.5988 0.4678 0.5274 0.0278  0.0690  -0.0625 27   THR A C   
21   O O   . THR A 3   ? 0.5701 0.4400 0.4893 0.0194  0.0608  -0.0645 27   THR A O   
22   C CB  . THR A 3   ? 0.6451 0.5068 0.6044 0.0334  0.0694  -0.0543 27   THR A CB  
23   O OG1 . THR A 3   ? 0.5877 0.4552 0.5499 0.0240  0.0586  -0.0503 27   THR A OG1 
24   C CG2 . THR A 3   ? 0.6620 0.5079 0.6300 0.0395  0.0733  -0.0551 27   THR A CG2 
25   N N   . SER A 4   ? 0.6115 0.4939 0.5460 0.0335  0.0760  -0.0573 28   SER A N   
26   C CA  . SER A 4   ? 0.5983 0.4959 0.5281 0.0302  0.0741  -0.0535 28   SER A CA  
27   C C   . SER A 4   ? 0.5688 0.4823 0.5170 0.0350  0.0788  -0.0437 28   SER A C   
28   O O   . SER A 4   ? 0.5769 0.4895 0.5374 0.0422  0.0856  -0.0415 28   SER A O   
29   C CB  . SER A 4   ? 0.6788 0.5714 0.5860 0.0317  0.0793  -0.0609 28   SER A CB  
30   O OG  . SER A 4   ? 0.6756 0.5657 0.5826 0.0414  0.0919  -0.0624 28   SER A OG  
31   N N   . CYS A 5   ? 0.4649 0.3928 0.4161 0.0311  0.0750  -0.0375 29   CYS A N   
32   C CA  . CYS A 5   ? 0.4231 0.3660 0.3913 0.0340  0.0784  -0.0282 29   CYS A CA  
33   C C   . CYS A 5   ? 0.3975 0.3519 0.3625 0.0293  0.0748  -0.0235 29   CYS A C   
34   O O   . CYS A 5   ? 0.4244 0.3769 0.3783 0.0236  0.0677  -0.0260 29   CYS A O   
35   C CB  . CYS A 5   ? 0.3778 0.3242 0.3662 0.0340  0.0739  -0.0223 29   CYS A CB  
36   S SG  . CYS A 5   ? 0.4175 0.3636 0.4068 0.0254  0.0608  -0.0210 29   CYS A SG  
37   N N   . PRO A 6   ? 0.4170 0.3836 0.3928 0.0317  0.0797  -0.0162 30   PRO A N   
38   C CA  . PRO A 6   ? 0.4213 0.3964 0.3927 0.0277  0.0774  -0.0118 30   PRO A CA  
39   C C   . PRO A 6   ? 0.4244 0.4047 0.4047 0.0218  0.0672  -0.0071 30   PRO A C   
40   O O   . PRO A 6   ? 0.4100 0.3937 0.3843 0.0182  0.0637  -0.0049 30   PRO A O   
41   C CB  . PRO A 6   ? 0.4183 0.4040 0.4000 0.0320  0.0866  -0.0050 30   PRO A CB  
42   C CG  . PRO A 6   ? 0.4548 0.4424 0.4551 0.0366  0.0896  -0.0027 30   PRO A CG  
43   C CD  . PRO A 6   ? 0.4667 0.4397 0.4583 0.0384  0.0884  -0.0115 30   PRO A CD  
44   N N   . LEU A 7   ? 0.3460 0.3264 0.3396 0.0212  0.0628  -0.0054 31   LEU A N   
45   C CA  . LEU A 7   ? 0.3185 0.3025 0.3176 0.0161  0.0536  -0.0021 31   LEU A CA  
46   C C   . LEU A 7   ? 0.3251 0.3066 0.3332 0.0156  0.0487  -0.0020 31   LEU A C   
47   O O   . LEU A 7   ? 0.3049 0.2829 0.3186 0.0195  0.0523  -0.0029 31   LEU A O   
48   C CB  . LEU A 7   ? 0.4387 0.4328 0.4492 0.0148  0.0534  0.0055  31   LEU A CB  
49   C CG  . LEU A 7   ? 0.3928 0.3938 0.4229 0.0165  0.0543  0.0111  31   LEU A CG  
50   C CD1 . LEU A 7   ? 0.4695 0.4769 0.5094 0.0118  0.0476  0.0168  31   LEU A CD1 
51   C CD2 . LEU A 7   ? 0.4718 0.4782 0.5079 0.0215  0.0646  0.0138  31   LEU A CD2 
52   N N   . ALA A 8   ? 0.2932 0.2763 0.3019 0.0113  0.0407  -0.0005 32   ALA A N   
53   C CA  . ALA A 8   ? 0.2840 0.2670 0.3011 0.0103  0.0353  0.0014  32   ALA A CA  
54   C C   . ALA A 8   ? 0.2793 0.2688 0.3017 0.0071  0.0295  0.0059  32   ALA A C   
55   O O   . ALA A 8   ? 0.2873 0.2794 0.3064 0.0056  0.0296  0.0069  32   ALA A O   
56   C CB  . ALA A 8   ? 0.2592 0.2349 0.2673 0.0081  0.0316  -0.0029 32   ALA A CB  
57   N N   . LEU A 9   ? 0.2632 0.2545 0.2930 0.0062  0.0244  0.0086  33   LEU A N   
58   C CA  . LEU A 9   ? 0.2725 0.2679 0.3050 0.0030  0.0182  0.0116  33   LEU A CA  
59   C C   . LEU A 9   ? 0.2525 0.2449 0.2777 0.0011  0.0129  0.0098  33   LEU A C   
60   O O   . LEU A 9   ? 0.2380 0.2276 0.2632 0.0020  0.0127  0.0093  33   LEU A O   
61   C CB  . LEU A 9   ? 0.2516 0.2534 0.2989 0.0032  0.0162  0.0171  33   LEU A CB  
62   C CG  . LEU A 9   ? 0.2665 0.2745 0.3242 0.0046  0.0214  0.0205  33   LEU A CG  
63   C CD1 . LEU A 9   ? 0.2987 0.3147 0.3736 0.0053  0.0193  0.0267  33   LEU A CD1 
64   C CD2 . LEU A 9   ? 0.2568 0.2659 0.3114 0.0009  0.0197  0.0213  33   LEU A CD2 
65   N N   . ALA A 10  ? 0.2040 0.1963 0.2231 -0.0011 0.0090  0.0091  34   ALA A N   
66   C CA  . ALA A 10  ? 0.2271 0.2181 0.2395 -0.0022 0.0048  0.0080  34   ALA A CA  
67   C C   . ALA A 10  ? 0.2563 0.2492 0.2713 -0.0037 -0.0009 0.0104  34   ALA A C   
68   O O   . ALA A 10  ? 0.2766 0.2697 0.2930 -0.0051 -0.0028 0.0109  34   ALA A O   
69   C CB  . ALA A 10  ? 0.2598 0.2493 0.2622 -0.0026 0.0049  0.0052  34   ALA A CB  
70   N N   . SER A 11  ? 0.2489 0.2423 0.2629 -0.0038 -0.0040 0.0118  35   SER A N   
71   C CA  . SER A 11  ? 0.2188 0.2137 0.2322 -0.0054 -0.0101 0.0135  35   SER A CA  
72   C C   . SER A 11  ? 0.2276 0.2197 0.2281 -0.0056 -0.0122 0.0105  35   SER A C   
73   O O   . SER A 11  ? 0.2289 0.2214 0.2236 -0.0046 -0.0111 0.0104  35   SER A O   
74   C CB  . SER A 11  ? 0.2481 0.2459 0.2669 -0.0049 -0.0125 0.0178  35   SER A CB  
75   O OG  . SER A 11  ? 0.2821 0.2817 0.2987 -0.0068 -0.0194 0.0196  35   SER A OG  
76   N N   . TYR A 12  ? 0.2286 0.2176 0.2252 -0.0067 -0.0146 0.0083  36   TYR A N   
77   C CA  . TYR A 12  ? 0.2547 0.2398 0.2391 -0.0055 -0.0153 0.0047  36   TYR A CA  
78   C C   . TYR A 12  ? 0.2473 0.2298 0.2251 -0.0069 -0.0215 0.0038  36   TYR A C   
79   O O   . TYR A 12  ? 0.3042 0.2834 0.2840 -0.0097 -0.0258 0.0031  36   TYR A O   
80   C CB  . TYR A 12  ? 0.2233 0.2041 0.2066 -0.0051 -0.0133 0.0024  36   TYR A CB  
81   C CG  . TYR A 12  ? 0.2651 0.2422 0.2378 -0.0022 -0.0119 -0.0009 36   TYR A CG  
82   C CD1 . TYR A 12  ? 0.2573 0.2364 0.2294 0.0002  -0.0075 -0.0010 36   TYR A CD1 
83   C CD2 . TYR A 12  ? 0.2424 0.2142 0.2056 -0.0014 -0.0152 -0.0038 36   TYR A CD2 
84   C CE1 . TYR A 12  ? 0.2751 0.2525 0.2398 0.0037  -0.0060 -0.0029 36   TYR A CE1 
85   C CE2 . TYR A 12  ? 0.3074 0.2758 0.2613 0.0028  -0.0127 -0.0067 36   TYR A CE2 
86   C CZ  . TYR A 12  ? 0.3049 0.2768 0.2609 0.0055  -0.0080 -0.0057 36   TYR A CZ  
87   O OH  . TYR A 12  ? 0.2822 0.2521 0.2313 0.0103  -0.0055 -0.0076 36   TYR A OH  
88   N N   . TYR A 13  ? 0.2599 0.2440 0.2296 -0.0056 -0.0221 0.0041  37   TYR A N   
89   C CA  . TYR A 13  ? 0.2740 0.2556 0.2337 -0.0066 -0.0280 0.0029  37   TYR A CA  
90   C C   . TYR A 13  ? 0.2899 0.2631 0.2367 -0.0050 -0.0282 -0.0031 37   TYR A C   
91   O O   . TYR A 13  ? 0.3306 0.3030 0.2729 -0.0012 -0.0227 -0.0051 37   TYR A O   
92   C CB  . TYR A 13  ? 0.2900 0.2764 0.2437 -0.0052 -0.0275 0.0060  37   TYR A CB  
93   C CG  . TYR A 13  ? 0.3282 0.3124 0.2688 -0.0060 -0.0334 0.0049  37   TYR A CG  
94   C CD1 . TYR A 13  ? 0.3841 0.3704 0.3286 -0.0096 -0.0410 0.0078  37   TYR A CD1 
95   C CD2 . TYR A 13  ? 0.3595 0.3403 0.2834 -0.0029 -0.0315 0.0009  37   TYR A CD2 
96   C CE1 . TYR A 13  ? 0.3979 0.3820 0.3282 -0.0109 -0.0477 0.0065  37   TYR A CE1 
97   C CE2 . TYR A 13  ? 0.3667 0.3444 0.2754 -0.0034 -0.0369 -0.0009 37   TYR A CE2 
98   C CZ  . TYR A 13  ? 0.4017 0.3809 0.3130 -0.0078 -0.0454 0.0017  37   TYR A CZ  
99   O OH  . TYR A 13  ? 0.4585 0.4347 0.3531 -0.0088 -0.0517 -0.0003 37   TYR A OH  
100  N N   . LEU A 14  ? 0.3170 0.2838 0.2581 -0.0078 -0.0348 -0.0060 38   LEU A N   
101  C CA  . LEU A 14  ? 0.2980 0.2534 0.2272 -0.0065 -0.0356 -0.0125 38   LEU A CA  
102  C C   . LEU A 14  ? 0.3401 0.2915 0.2503 -0.0037 -0.0367 -0.0165 38   LEU A C   
103  O O   . LEU A 14  ? 0.3914 0.3427 0.2948 -0.0066 -0.0432 -0.0165 38   LEU A O   
104  C CB  . LEU A 14  ? 0.3043 0.2528 0.2382 -0.0122 -0.0427 -0.0139 38   LEU A CB  
105  C CG  . LEU A 14  ? 0.3018 0.2538 0.2536 -0.0147 -0.0408 -0.0099 38   LEU A CG  
106  C CD1 . LEU A 14  ? 0.3171 0.2629 0.2737 -0.0210 -0.0480 -0.0105 38   LEU A CD1 
107  C CD2 . LEU A 14  ? 0.3066 0.2556 0.2585 -0.0104 -0.0334 -0.0110 38   LEU A CD2 
108  N N   . GLU A 15  ? 0.3648 0.3136 0.2660 0.0023  -0.0302 -0.0195 39   GLU A N   
109  C CA  . GLU A 15  ? 0.3882 0.3311 0.2695 0.0060  -0.0300 -0.0245 39   GLU A CA  
110  C C   . GLU A 15  ? 0.3384 0.2735 0.2122 0.0126  -0.0238 -0.0297 39   GLU A C   
111  O O   . GLU A 15  ? 0.3718 0.3091 0.2564 0.0148  -0.0191 -0.0278 39   GLU A O   
112  C CB  . GLU A 15  ? 0.4833 0.4373 0.3600 0.0080  -0.0271 -0.0200 39   GLU A CB  
113  C CG  . GLU A 15  ? 0.4935 0.4570 0.3775 0.0123  -0.0182 -0.0161 39   GLU A CG  
114  C CD  . GLU A 15  ? 0.5624 0.5369 0.4436 0.0133  -0.0153 -0.0104 39   GLU A CD  
115  O OE1 . GLU A 15  ? 0.5438 0.5273 0.4343 0.0149  -0.0093 -0.0059 39   GLU A OE1 
116  O OE2 . GLU A 15  ? 0.5425 0.5165 0.4122 0.0121  -0.0194 -0.0100 39   GLU A OE2 
117  N N   . ASN A 16  ? 0.3807 0.3062 0.2353 0.0163  -0.0240 -0.0361 40   ASN A N   
118  C CA  . ASN A 16  ? 0.3999 0.3163 0.2456 0.0240  -0.0177 -0.0416 40   ASN A CA  
119  C C   . ASN A 16  ? 0.4148 0.3197 0.2684 0.0235  -0.0187 -0.0440 40   ASN A C   
120  O O   . ASN A 16  ? 0.4527 0.3555 0.3078 0.0302  -0.0122 -0.0446 40   ASN A O   
121  C CB  . ASN A 16  ? 0.4570 0.3872 0.3067 0.0310  -0.0077 -0.0369 40   ASN A CB  
122  C CG  . ASN A 16  ? 0.5081 0.4456 0.3442 0.0340  -0.0046 -0.0360 40   ASN A CG  
123  O OD1 . ASN A 16  ? 0.5540 0.4855 0.3754 0.0315  -0.0101 -0.0394 40   ASN A OD1 
124  N ND2 . ASN A 16  ? 0.4876 0.4389 0.3288 0.0388  0.0037  -0.0307 40   ASN A ND2 
125  N N   . GLY A 17  ? 0.4234 0.3218 0.2833 0.0156  -0.0269 -0.0443 41   GLY A N   
126  C CA  . GLY A 17  ? 0.3986 0.2826 0.2623 0.0144  -0.0288 -0.0473 41   GLY A CA  
127  C C   . GLY A 17  ? 0.4153 0.3053 0.2993 0.0115  -0.0275 -0.0407 41   GLY A C   
128  O O   . GLY A 17  ? 0.4083 0.2865 0.2959 0.0102  -0.0289 -0.0418 41   GLY A O   
129  N N   . THR A 18  ? 0.3438 0.2509 0.2399 0.0106  -0.0246 -0.0338 42   THR A N   
130  C CA  . THR A 18  ? 0.3063 0.2206 0.2191 0.0088  -0.0222 -0.0278 42   THR A CA  
131  C C   . THR A 18  ? 0.3312 0.2379 0.2523 0.0020  -0.0276 -0.0269 42   THR A C   
132  O O   . THR A 18  ? 0.3507 0.2554 0.2719 -0.0042 -0.0344 -0.0277 42   THR A O   
133  C CB  . THR A 18  ? 0.3797 0.3107 0.3023 0.0062  -0.0211 -0.0220 42   THR A CB  
134  O OG1 . THR A 18  ? 0.3709 0.3099 0.2877 0.0114  -0.0162 -0.0216 42   THR A OG1 
135  C CG2 . THR A 18  ? 0.3236 0.2617 0.2611 0.0046  -0.0184 -0.0166 42   THR A CG2 
136  N N   . THR A 19  ? 0.3743 0.2782 0.3030 0.0030  -0.0247 -0.0242 43   THR A N   
137  C CA  . THR A 19  ? 0.3379 0.2352 0.2758 -0.0035 -0.0287 -0.0219 43   THR A CA  
138  C C   . THR A 19  ? 0.3645 0.2754 0.3176 -0.0059 -0.0256 -0.0145 43   THR A C   
139  O O   . THR A 19  ? 0.2990 0.2209 0.2538 -0.0020 -0.0203 -0.0121 43   THR A O   
140  C CB  . THR A 19  ? 0.3499 0.2317 0.2847 -0.0007 -0.0275 -0.0236 43   THR A CB  
141  O OG1 . THR A 19  ? 0.3477 0.2358 0.2850 0.0061  -0.0203 -0.0200 43   THR A OG1 
142  C CG2 . THR A 19  ? 0.4019 0.2672 0.3202 0.0025  -0.0300 -0.0321 43   THR A CG2 
143  N N   . LEU A 20  ? 0.3222 0.2321 0.2860 -0.0124 -0.0286 -0.0108 44   LEU A N   
144  C CA  . LEU A 20  ? 0.3140 0.2370 0.2909 -0.0141 -0.0247 -0.0040 44   LEU A CA  
145  C C   . LEU A 20  ? 0.3043 0.2278 0.2805 -0.0090 -0.0183 -0.0014 44   LEU A C   
146  O O   . LEU A 20  ? 0.3031 0.2378 0.2833 -0.0073 -0.0137 0.0018  44   LEU A O   
147  C CB  . LEU A 20  ? 0.3516 0.2743 0.3410 -0.0216 -0.0283 0.0003  44   LEU A CB  
148  C CG  . LEU A 20  ? 0.3657 0.3026 0.3687 -0.0231 -0.0238 0.0072  44   LEU A CG  
149  C CD1 . LEU A 20  ? 0.3882 0.3366 0.3926 -0.0217 -0.0232 0.0068  44   LEU A CD1 
150  C CD2 . LEU A 20  ? 0.3672 0.3047 0.3840 -0.0307 -0.0272 0.0124  44   LEU A CD2 
151  N N   . SER A 21  ? 0.3127 0.2234 0.2834 -0.0067 -0.0186 -0.0030 45   SER A N   
152  C CA  . SER A 21  ? 0.3471 0.2583 0.3175 -0.0017 -0.0134 0.0005  45   SER A CA  
153  C C   . SER A 21  ? 0.3674 0.2886 0.3328 0.0046  -0.0094 -0.0007 45   SER A C   
154  O O   . SER A 21  ? 0.3272 0.2576 0.2955 0.0064  -0.0056 0.0034  45   SER A O   
155  C CB  . SER A 21  ? 0.4804 0.3743 0.4461 0.0004  -0.0147 -0.0008 45   SER A CB  
156  O OG  . SER A 21  ? 0.5971 0.4924 0.5631 0.0057  -0.0103 0.0036  45   SER A OG  
157  N N   . VAL A 22  ? 0.3065 0.2263 0.2638 0.0076  -0.0104 -0.0060 46   VAL A N   
158  C CA  . VAL A 22  ? 0.2871 0.2178 0.2415 0.0126  -0.0067 -0.0063 46   VAL A CA  
159  C C   . VAL A 22  ? 0.2802 0.2248 0.2407 0.0094  -0.0055 -0.0036 46   VAL A C   
160  O O   . VAL A 22  ? 0.2824 0.2364 0.2444 0.0116  -0.0024 -0.0014 46   VAL A O   
161  C CB  . VAL A 22  ? 0.3702 0.2976 0.3147 0.0164  -0.0071 -0.0118 46   VAL A CB  
162  C CG1 . VAL A 22  ? 0.4520 0.3933 0.3963 0.0195  -0.0036 -0.0107 46   VAL A CG1 
163  C CG2 . VAL A 22  ? 0.4626 0.3765 0.3999 0.0222  -0.0063 -0.0148 46   VAL A CG2 
164  N N   . ILE A 23  ? 0.2653 0.2107 0.2296 0.0042  -0.0084 -0.0039 47   ILE A N   
165  C CA  . ILE A 23  ? 0.2389 0.1952 0.2097 0.0018  -0.0070 -0.0015 47   ILE A CA  
166  C C   . ILE A 23  ? 0.2721 0.2324 0.2481 0.0013  -0.0036 0.0025  47   ILE A C   
167  O O   . ILE A 23  ? 0.2695 0.2374 0.2458 0.0024  -0.0007 0.0034  47   ILE A O   
168  C CB  . ILE A 23  ? 0.2430 0.1998 0.2191 -0.0032 -0.0108 -0.0012 47   ILE A CB  
169  C CG1 . ILE A 23  ? 0.2613 0.2158 0.2297 -0.0026 -0.0144 -0.0049 47   ILE A CG1 
170  C CG2 . ILE A 23  ? 0.2469 0.2136 0.2311 -0.0046 -0.0084 0.0018  47   ILE A CG2 
171  C CD1 . ILE A 23  ? 0.2828 0.2376 0.2555 -0.0076 -0.0200 -0.0044 47   ILE A CD1 
172  N N   . ASN A 24  ? 0.2590 0.2136 0.2385 -0.0007 -0.0040 0.0050  48   ASN A N   
173  C CA  . ASN A 24  ? 0.2365 0.1952 0.2197 -0.0011 -0.0003 0.0096  48   ASN A CA  
174  C C   . ASN A 24  ? 0.2731 0.2339 0.2505 0.0033  0.0021  0.0104  48   ASN A C   
175  O O   . ASN A 24  ? 0.2993 0.2670 0.2762 0.0036  0.0050  0.0125  48   ASN A O   
176  C CB  . ASN A 24  ? 0.2746 0.2272 0.2635 -0.0046 -0.0011 0.0133  48   ASN A CB  
177  C CG  . ASN A 24  ? 0.3008 0.2598 0.2945 -0.0059 0.0035  0.0187  48   ASN A CG  
178  O OD1 . ASN A 24  ? 0.3714 0.3378 0.3618 -0.0036 0.0072  0.0190  48   ASN A OD1 
179  N ND2 . ASN A 24  ? 0.2708 0.2270 0.2719 -0.0098 0.0033  0.0231  48   ASN A ND2 
180  N N   . GLN A 25  ? 0.2573 0.2124 0.2297 0.0071  0.0008  0.0088  49   GLN A N   
181  C CA  . GLN A 25  ? 0.2439 0.2028 0.2126 0.0119  0.0025  0.0105  49   GLN A CA  
182  C C   . GLN A 25  ? 0.2797 0.2498 0.2473 0.0124  0.0034  0.0089  49   GLN A C   
183  O O   . GLN A 25  ? 0.2668 0.2441 0.2337 0.0125  0.0046  0.0112  49   GLN A O   
184  C CB  . GLN A 25  ? 0.2811 0.2319 0.2460 0.0169  0.0016  0.0087  49   GLN A CB  
185  C CG  . GLN A 25  ? 0.3546 0.3110 0.3179 0.0227  0.0032  0.0113  49   GLN A CG  
186  C CD  . GLN A 25  ? 0.4401 0.3865 0.4007 0.0289  0.0034  0.0105  49   GLN A CD  
187  O OE1 . GLN A 25  ? 0.4313 0.3712 0.3881 0.0307  0.0030  0.0054  49   GLN A OE1 
188  N NE2 . GLN A 25  ? 0.4323 0.3764 0.3940 0.0325  0.0040  0.0155  49   GLN A NE2 
189  N N   . ASN A 26  ? 0.2490 0.2201 0.2160 0.0121  0.0024  0.0053  50   ASN A N   
190  C CA  . ASN A 26  ? 0.2564 0.2372 0.2232 0.0121  0.0031  0.0045  50   ASN A CA  
191  C C   . ASN A 26  ? 0.2767 0.2621 0.2460 0.0081  0.0040  0.0049  50   ASN A C   
192  O O   . ASN A 26  ? 0.2503 0.2424 0.2188 0.0076  0.0045  0.0052  50   ASN A O   
193  C CB  . ASN A 26  ? 0.2609 0.2418 0.2262 0.0125  0.0023  0.0015  50   ASN A CB  
194  C CG  . ASN A 26  ? 0.3143 0.2917 0.2750 0.0178  0.0027  0.0002  50   ASN A CG  
195  O OD1 . ASN A 26  ? 0.2933 0.2687 0.2534 0.0216  0.0036  0.0018  50   ASN A OD1 
196  N ND2 . ASN A 26  ? 0.3068 0.2834 0.2637 0.0186  0.0024  -0.0024 50   ASN A ND2 
197  N N   . LEU A 27  ? 0.2409 0.2225 0.2135 0.0053  0.0041  0.0049  51   LEU A N   
198  C CA  . LEU A 27  ? 0.2157 0.2006 0.1907 0.0027  0.0061  0.0050  51   LEU A CA  
199  C C   . LEU A 27  ? 0.2527 0.2370 0.2275 0.0022  0.0086  0.0078  51   LEU A C   
200  O O   . LEU A 27  ? 0.2449 0.2302 0.2226 0.0007  0.0111  0.0084  51   LEU A O   
201  C CB  . LEU A 27  ? 0.2043 0.1881 0.1849 0.0005  0.0053  0.0042  51   LEU A CB  
202  C CG  . LEU A 27  ? 0.3146 0.3008 0.2948 0.0005  0.0039  0.0023  51   LEU A CG  
203  C CD1 . LEU A 27  ? 0.3248 0.3093 0.3009 0.0023  0.0016  0.0013  51   LEU A CD1 
204  C CD2 . LEU A 27  ? 0.3354 0.3216 0.3219 -0.0014 0.0034  0.0028  51   LEU A CD2 
205  N N   . ASN A 28  ? 0.2808 0.2641 0.2522 0.0042  0.0083  0.0102  52   ASN A N   
206  C CA  . ASN A 28  ? 0.2612 0.2444 0.2310 0.0039  0.0109  0.0140  52   ASN A CA  
207  C C   . ASN A 28  ? 0.2331 0.2215 0.1985 0.0030  0.0135  0.0130  52   ASN A C   
208  O O   . ASN A 28  ? 0.2570 0.2490 0.2186 0.0030  0.0120  0.0102  52   ASN A O   
209  C CB  . ASN A 28  ? 0.2433 0.2252 0.2095 0.0067  0.0097  0.0175  52   ASN A CB  
210  C CG  . ASN A 28  ? 0.3159 0.2994 0.2784 0.0065  0.0122  0.0222  52   ASN A CG  
211  O OD1 . ASN A 28  ? 0.2866 0.2666 0.2524 0.0050  0.0143  0.0257  52   ASN A OD1 
212  N ND2 . ASN A 28  ? 0.2725 0.2619 0.2280 0.0076  0.0117  0.0229  52   ASN A ND2 
213  N N   . SER A 29  ? 0.2241 0.2127 0.1896 0.0021  0.0174  0.0153  53   SER A N   
214  C CA  . SER A 29  ? 0.2314 0.2231 0.1899 0.0019  0.0207  0.0135  53   SER A CA  
215  C C   . SER A 29  ? 0.2650 0.2573 0.2227 0.0020  0.0258  0.0181  53   SER A C   
216  O O   . SER A 29  ? 0.2755 0.2661 0.2397 0.0015  0.0262  0.0229  53   SER A O   
217  C CB  . SER A 29  ? 0.2631 0.2546 0.2244 0.0011  0.0220  0.0086  53   SER A CB  
218  O OG  . SER A 29  ? 0.2517 0.2428 0.2222 0.0009  0.0254  0.0104  53   SER A OG  
219  N N   . SER A 30  ? 0.2646 0.2588 0.2138 0.0025  0.0299  0.0165  54   SER A N   
220  C CA  . SER A 30  ? 0.2609 0.2570 0.2086 0.0032  0.0364  0.0211  54   SER A CA  
221  C C   . SER A 30  ? 0.2856 0.2827 0.2472 0.0027  0.0403  0.0232  54   SER A C   
222  O O   . SER A 30  ? 0.2951 0.2946 0.2617 0.0023  0.0445  0.0296  54   SER A O   
223  C CB  . SER A 30  ? 0.4074 0.4044 0.3414 0.0044  0.0405  0.0173  54   SER A CB  
224  O OG  . SER A 30  ? 0.5701 0.5680 0.4911 0.0042  0.0367  0.0177  54   SER A OG  
225  N N   . ILE A 31  ? 0.2798 0.2758 0.2482 0.0025  0.0387  0.0186  55   ILE A N   
226  C CA  . ILE A 31  ? 0.2592 0.2575 0.2420 0.0022  0.0412  0.0207  55   ILE A CA  
227  C C   . ILE A 31  ? 0.2776 0.2748 0.2717 -0.0008 0.0358  0.0242  55   ILE A C   
228  O O   . ILE A 31  ? 0.2958 0.2963 0.3027 -0.0024 0.0372  0.0284  55   ILE A O   
229  C CB  . ILE A 31  ? 0.3225 0.3198 0.3073 0.0036  0.0416  0.0149  55   ILE A CB  
230  C CG1 . ILE A 31  ? 0.4504 0.4487 0.4298 0.0069  0.0499  0.0130  55   ILE A CG1 
231  C CG2 . ILE A 31  ? 0.3344 0.3335 0.3346 0.0025  0.0390  0.0165  55   ILE A CG2 
232  C CD1 . ILE A 31  ? 0.4974 0.4909 0.4730 0.0086  0.0499  0.0058  55   ILE A CD1 
233  N N   . ALA A 32  ? 0.2611 0.2538 0.2510 -0.0015 0.0296  0.0223  56   ALA A N   
234  C CA  . ALA A 32  ? 0.2754 0.2642 0.2723 -0.0039 0.0245  0.0247  56   ALA A CA  
235  C C   . ALA A 32  ? 0.3104 0.2944 0.2996 -0.0031 0.0220  0.0263  56   ALA A C   
236  O O   . ALA A 32  ? 0.2794 0.2599 0.2646 -0.0019 0.0176  0.0230  56   ALA A O   
237  C CB  . ALA A 32  ? 0.2932 0.2801 0.2933 -0.0045 0.0193  0.0203  56   ALA A CB  
238  N N   . PRO A 33  ? 0.2903 0.2747 0.2779 -0.0033 0.0253  0.0321  57   PRO A N   
239  C CA  . PRO A 33  ? 0.2464 0.2267 0.2266 -0.0016 0.0231  0.0346  57   PRO A CA  
240  C C   . PRO A 33  ? 0.3315 0.3029 0.3169 -0.0027 0.0183  0.0355  57   PRO A C   
241  O O   . PRO A 33  ? 0.3978 0.3656 0.3919 -0.0062 0.0179  0.0387  57   PRO A O   
242  C CB  . PRO A 33  ? 0.3275 0.3105 0.3055 -0.0019 0.0283  0.0419  57   PRO A CB  
243  C CG  . PRO A 33  ? 0.3309 0.3202 0.3142 -0.0032 0.0341  0.0425  57   PRO A CG  
244  C CD  . PRO A 33  ? 0.3231 0.3125 0.3157 -0.0045 0.0315  0.0375  57   PRO A CD  
245  N N   . TYR A 34  ? 0.2770 0.2446 0.2569 0.0004  0.0147  0.0327  58   TYR A N   
246  C CA  . TYR A 34  ? 0.2976 0.2550 0.2798 0.0006  0.0106  0.0317  58   TYR A CA  
247  C C   . TYR A 34  ? 0.3416 0.2917 0.3237 0.0013  0.0108  0.0384  58   TYR A C   
248  O O   . TYR A 34  ? 0.3417 0.2932 0.3178 0.0052  0.0115  0.0413  58   TYR A O   
249  C CB  . TYR A 34  ? 0.2890 0.2463 0.2655 0.0048  0.0080  0.0264  58   TYR A CB  
250  C CG  . TYR A 34  ? 0.3217 0.2675 0.2980 0.0067  0.0047  0.0243  58   TYR A CG  
251  C CD1 . TYR A 34  ? 0.3437 0.2815 0.3237 0.0031  0.0018  0.0214  58   TYR A CD1 
252  C CD2 . TYR A 34  ? 0.3706 0.3136 0.3423 0.0125  0.0043  0.0248  58   TYR A CD2 
253  C CE1 . TYR A 34  ? 0.3822 0.3074 0.3592 0.0050  -0.0013 0.0180  58   TYR A CE1 
254  C CE2 . TYR A 34  ? 0.4484 0.3792 0.4185 0.0154  0.0021  0.0219  58   TYR A CE2 
255  C CZ  . TYR A 34  ? 0.4422 0.3634 0.4138 0.0117  -0.0006 0.0179  58   TYR A CZ  
256  O OH  . TYR A 34  ? 0.4747 0.3820 0.4422 0.0147  -0.0027 0.0139  58   TYR A OH  
257  N N   . ASP A 35  ? 0.3439 0.2861 0.3332 -0.0028 0.0099  0.0415  59   ASP A N   
258  C CA  . ASP A 35  ? 0.4111 0.3437 0.4009 -0.0024 0.0096  0.0481  59   ASP A CA  
259  C C   . ASP A 35  ? 0.4168 0.3333 0.4097 -0.0041 0.0049  0.0456  59   ASP A C   
260  O O   . ASP A 35  ? 0.4207 0.3261 0.4150 -0.0041 0.0042  0.0508  59   ASP A O   
261  C CB  . ASP A 35  ? 0.4708 0.4081 0.4653 -0.0062 0.0140  0.0572  59   ASP A CB  
262  C CG  . ASP A 35  ? 0.4952 0.4337 0.5013 -0.0131 0.0141  0.0583  59   ASP A CG  
263  O OD1 . ASP A 35  ? 0.4124 0.3451 0.4229 -0.0158 0.0092  0.0527  59   ASP A OD1 
264  O OD2 . ASP A 35  ? 0.5829 0.5290 0.5940 -0.0158 0.0190  0.0654  59   ASP A OD2 
265  N N   . GLN A 36  ? 0.4089 0.3232 0.4019 -0.0052 0.0014  0.0377  60   GLN A N   
266  C CA  . GLN A 36  ? 0.4368 0.3349 0.4295 -0.0067 -0.0038 0.0331  60   GLN A CA  
267  C C   . GLN A 36  ? 0.4831 0.3738 0.4856 -0.0152 -0.0067 0.0366  60   GLN A C   
268  O O   . GLN A 36  ? 0.5685 0.4449 0.5705 -0.0182 -0.0121 0.0321  60   GLN A O   
269  C CB  . GLN A 36  ? 0.4946 0.3797 0.4807 -0.0002 -0.0040 0.0330  60   GLN A CB  
270  C CG  . GLN A 36  ? 0.5763 0.4662 0.5541 0.0080  -0.0029 0.0277  60   GLN A CG  
271  C CD  . GLN A 36  ? 0.6578 0.5336 0.6308 0.0152  -0.0031 0.0272  60   GLN A CD  
272  O OE1 . GLN A 36  ? 0.6761 0.5516 0.6498 0.0191  -0.0011 0.0342  60   GLN A OE1 
273  N NE2 . GLN A 36  ? 0.5931 0.4566 0.5606 0.0175  -0.0055 0.0191  60   GLN A NE2 
274  N N   . ILE A 37  ? 0.4199 0.3202 0.4309 -0.0193 -0.0031 0.0448  61   ILE A N   
275  C CA  . ILE A 37  ? 0.4726 0.3684 0.4955 -0.0278 -0.0050 0.0506  61   ILE A CA  
276  C C   . ILE A 37  ? 0.5010 0.4117 0.5347 -0.0334 -0.0046 0.0516  61   ILE A C   
277  O O   . ILE A 37  ? 0.4971 0.4046 0.5398 -0.0406 -0.0100 0.0509  61   ILE A O   
278  C CB  . ILE A 37  ? 0.5322 0.4289 0.5588 -0.0284 -0.0001 0.0618  61   ILE A CB  
279  C CG1 . ILE A 37  ? 0.6187 0.5013 0.6364 -0.0223 -0.0004 0.0629  61   ILE A CG1 
280  C CG2 . ILE A 37  ? 0.5900 0.4837 0.6310 -0.0381 -0.0018 0.0691  61   ILE A CG2 
281  C CD1 . ILE A 37  ? 0.6496 0.5379 0.6665 -0.0200 0.0054  0.0738  61   ILE A CD1 
282  N N   . ASN A 38  ? 0.3696 0.2964 0.4024 -0.0299 0.0016  0.0533  62   ASN A N   
283  C CA  . ASN A 38  ? 0.3641 0.3062 0.4076 -0.0332 0.0043  0.0556  62   ASN A CA  
284  C C   . ASN A 38  ? 0.3673 0.3170 0.4055 -0.0290 0.0041  0.0478  62   ASN A C   
285  O O   . ASN A 38  ? 0.3334 0.2877 0.3620 -0.0231 0.0083  0.0457  62   ASN A O   
286  C CB  . ASN A 38  ? 0.3670 0.3202 0.4131 -0.0320 0.0131  0.0644  62   ASN A CB  
287  C CG  . ASN A 38  ? 0.4003 0.3692 0.4595 -0.0347 0.0174  0.0683  62   ASN A CG  
288  O OD1 . ASN A 38  ? 0.4212 0.3959 0.4841 -0.0346 0.0152  0.0631  62   ASN A OD1 
289  N ND2 . ASN A 38  ? 0.3464 0.3228 0.4125 -0.0365 0.0242  0.0780  62   ASN A ND2 
290  N N   . PHE A 39  ? 0.2993 0.2495 0.3432 -0.0326 -0.0016 0.0438  63   PHE A N   
291  C CA  . PHE A 39  ? 0.3201 0.2770 0.3603 -0.0294 -0.0024 0.0375  63   PHE A CA  
292  C C   . PHE A 39  ? 0.3062 0.2780 0.3594 -0.0311 0.0004  0.0410  63   PHE A C   
293  O O   . PHE A 39  ? 0.2865 0.2634 0.3399 -0.0296 -0.0012 0.0371  63   PHE A O   
294  C CB  . PHE A 39  ? 0.3165 0.2632 0.3517 -0.0311 -0.0109 0.0305  63   PHE A CB  
295  C CG  . PHE A 39  ? 0.3371 0.2695 0.3588 -0.0273 -0.0125 0.0260  63   PHE A CG  
296  C CD1 . PHE A 39  ? 0.3536 0.2869 0.3636 -0.0204 -0.0104 0.0210  63   PHE A CD1 
297  C CD2 . PHE A 39  ? 0.4020 0.3202 0.4238 -0.0304 -0.0158 0.0274  63   PHE A CD2 
298  C CE1 . PHE A 39  ? 0.3642 0.2863 0.3636 -0.0159 -0.0110 0.0176  63   PHE A CE1 
299  C CE2 . PHE A 39  ? 0.4446 0.3490 0.4545 -0.0255 -0.0164 0.0234  63   PHE A CE2 
300  C CZ  . PHE A 39  ? 0.3619 0.2694 0.3611 -0.0178 -0.0138 0.0186  63   PHE A CZ  
301  N N   . ASP A 40  ? 0.3079 0.2871 0.3723 -0.0336 0.0055  0.0491  64   ASP A N   
302  C CA  . ASP A 40  ? 0.2810 0.2753 0.3598 -0.0344 0.0093  0.0535  64   ASP A CA  
303  C C   . ASP A 40  ? 0.2975 0.2998 0.3718 -0.0278 0.0145  0.0496  64   ASP A C   
304  O O   . ASP A 40  ? 0.2794 0.2898 0.3636 -0.0279 0.0134  0.0498  64   ASP A O   
305  C CB  . ASP A 40  ? 0.2649 0.2668 0.3551 -0.0370 0.0159  0.0635  64   ASP A CB  
306  C CG  . ASP A 40  ? 0.4048 0.4016 0.5071 -0.0460 0.0096  0.0691  64   ASP A CG  
307  O OD1 . ASP A 40  ? 0.4247 0.4122 0.5263 -0.0501 -0.0003 0.0643  64   ASP A OD1 
308  O OD2 . ASP A 40  ? 0.3774 0.3794 0.4899 -0.0492 0.0144  0.0783  64   ASP A OD2 
309  N N   . PRO A 41  ? 0.2921 0.2919 0.3519 -0.0222 0.0197  0.0464  65   PRO A N   
310  C CA  . PRO A 41  ? 0.2841 0.2893 0.3395 -0.0169 0.0240  0.0422  65   PRO A CA  
311  C C   . PRO A 41  ? 0.2904 0.2938 0.3457 -0.0168 0.0174  0.0367  65   PRO A C   
312  O O   . PRO A 41  ? 0.2742 0.2839 0.3347 -0.0143 0.0197  0.0361  65   PRO A O   
313  C CB  . PRO A 41  ? 0.2864 0.2864 0.3244 -0.0128 0.0271  0.0388  65   PRO A CB  
314  C CG  . PRO A 41  ? 0.2870 0.2850 0.3249 -0.0149 0.0291  0.0450  65   PRO A CG  
315  C CD  . PRO A 41  ? 0.3314 0.3249 0.3800 -0.0208 0.0223  0.0478  65   PRO A CD  
316  N N   . ILE A 42  ? 0.2664 0.2607 0.3154 -0.0189 0.0099  0.0331  66   ILE A N   
317  C CA  . ILE A 42  ? 0.2192 0.2121 0.2671 -0.0192 0.0035  0.0287  66   ILE A CA  
318  C C   . ILE A 42  ? 0.2523 0.2502 0.3148 -0.0242 -0.0020 0.0323  66   ILE A C   
319  O O   . ILE A 42  ? 0.2758 0.2803 0.3445 -0.0232 -0.0033 0.0325  66   ILE A O   
320  C CB  . ILE A 42  ? 0.2335 0.2154 0.2677 -0.0187 -0.0016 0.0231  66   ILE A CB  
321  C CG1 . ILE A 42  ? 0.2782 0.2587 0.3004 -0.0137 0.0030  0.0202  66   ILE A CG1 
322  C CG2 . ILE A 42  ? 0.2777 0.2587 0.3099 -0.0193 -0.0079 0.0193  66   ILE A CG2 
323  C CD1 . ILE A 42  ? 0.2861 0.2574 0.2966 -0.0120 -0.0002 0.0163  66   ILE A CD1 
324  N N   . LEU A 43  ? 0.2243 0.2190 0.2931 -0.0297 -0.0055 0.0357  67   LEU A N   
325  C CA  . LEU A 43  ? 0.2242 0.2229 0.3063 -0.0360 -0.0129 0.0388  67   LEU A CA  
326  C C   . LEU A 43  ? 0.3085 0.3232 0.4089 -0.0356 -0.0091 0.0454  67   LEU A C   
327  O O   . LEU A 43  ? 0.2722 0.2936 0.3834 -0.0387 -0.0154 0.0475  67   LEU A O   
328  C CB  . LEU A 43  ? 0.2521 0.2435 0.3386 -0.0430 -0.0172 0.0418  67   LEU A CB  
329  C CG  . LEU A 43  ? 0.3465 0.3201 0.4167 -0.0437 -0.0224 0.0352  67   LEU A CG  
330  C CD1 . LEU A 43  ? 0.3880 0.3528 0.4637 -0.0504 -0.0254 0.0390  67   LEU A CD1 
331  C CD2 . LEU A 43  ? 0.2963 0.2646 0.3585 -0.0447 -0.0312 0.0286  67   LEU A CD2 
332  N N   . ARG A 44  ? 0.2734 0.2948 0.3775 -0.0317 0.0012  0.0491  68   ARG A N   
333  C CA  . ARG A 44  ? 0.3220 0.3583 0.4419 -0.0288 0.0073  0.0547  68   ARG A CA  
334  C C   . ARG A 44  ? 0.2600 0.2999 0.3807 -0.0248 0.0052  0.0519  68   ARG A C   
335  O O   . ARG A 44  ? 0.2604 0.3124 0.3981 -0.0242 0.0057  0.0573  68   ARG A O   
336  C CB  . ARG A 44  ? 0.4104 0.4492 0.5252 -0.0227 0.0196  0.0555  68   ARG A CB  
337  C CG  . ARG A 44  ? 0.4774 0.5235 0.6035 -0.0254 0.0253  0.0638  68   ARG A CG  
338  C CD  . ARG A 44  ? 0.4966 0.5432 0.6126 -0.0194 0.0369  0.0636  68   ARG A CD  
339  N NE  . ARG A 44  ? 0.4420 0.4895 0.5614 -0.0236 0.0396  0.0705  68   ARG A NE  
340  C CZ  . ARG A 44  ? 0.4867 0.5257 0.5909 -0.0230 0.0420  0.0695  68   ARG A CZ  
341  N NH1 . ARG A 44  ? 0.3636 0.3936 0.4478 -0.0183 0.0422  0.0616  68   ARG A NH1 
342  N NH2 . ARG A 44  ? 0.4801 0.5206 0.5905 -0.0274 0.0440  0.0776  68   ARG A NH2 
343  N N   . TYR A 45  ? 0.2422 0.2724 0.3458 -0.0217 0.0034  0.0444  69   TYR A N   
344  C CA  . TYR A 45  ? 0.2456 0.2776 0.3485 -0.0180 0.0017  0.0422  69   TYR A CA  
345  C C   . TYR A 45  ? 0.2643 0.2940 0.3660 -0.0223 -0.0099 0.0409  69   TYR A C   
346  O O   . TYR A 45  ? 0.2892 0.3196 0.3888 -0.0197 -0.0123 0.0397  69   TYR A O   
347  C CB  . TYR A 45  ? 0.2384 0.2627 0.3248 -0.0123 0.0070  0.0357  69   TYR A CB  
348  C CG  . TYR A 45  ? 0.2566 0.2837 0.3434 -0.0074 0.0181  0.0364  69   TYR A CG  
349  C CD1 . TYR A 45  ? 0.2560 0.2892 0.3516 -0.0022 0.0239  0.0381  69   TYR A CD1 
350  C CD2 . TYR A 45  ? 0.3005 0.3239 0.3784 -0.0076 0.0227  0.0356  69   TYR A CD2 
351  C CE1 . TYR A 45  ? 0.2616 0.2959 0.3551 0.0028  0.0346  0.0377  69   TYR A CE1 
352  C CE2 . TYR A 45  ? 0.2609 0.2868 0.3366 -0.0032 0.0326  0.0360  69   TYR A CE2 
353  C CZ  . TYR A 45  ? 0.3147 0.3455 0.3973 0.0020  0.0387  0.0364  69   TYR A CZ  
354  O OH  . TYR A 45  ? 0.3912 0.4230 0.4692 0.0068  0.0491  0.0358  69   TYR A OH  
355  N N   . ASN A 46  ? 0.2703 0.2960 0.3720 -0.0289 -0.0170 0.0411  70   ASN A N   
356  C CA  . ASN A 46  ? 0.3093 0.3303 0.4056 -0.0335 -0.0284 0.0385  70   ASN A CA  
357  C C   . ASN A 46  ? 0.3139 0.3386 0.4235 -0.0417 -0.0360 0.0431  70   ASN A C   
358  O O   . ASN A 46  ? 0.3016 0.3155 0.4032 -0.0471 -0.0422 0.0397  70   ASN A O   
359  C CB  . ASN A 46  ? 0.2686 0.2745 0.3435 -0.0331 -0.0303 0.0306  70   ASN A CB  
360  C CG  . ASN A 46  ? 0.2588 0.2620 0.3213 -0.0262 -0.0242 0.0264  70   ASN A CG  
361  O OD1 . ASN A 46  ? 0.3102 0.3136 0.3669 -0.0243 -0.0271 0.0245  70   ASN A OD1 
362  N ND2 . ASN A 46  ? 0.2249 0.2260 0.2837 -0.0229 -0.0161 0.0255  70   ASN A ND2 
363  N N   . SER A 47  ? 0.3465 0.3863 0.4773 -0.0429 -0.0356 0.0511  71   SER A N   
364  C CA  . SER A 47  ? 0.3843 0.4300 0.5311 -0.0516 -0.0428 0.0568  71   SER A CA  
365  C C   . SER A 47  ? 0.4124 0.4523 0.5525 -0.0584 -0.0574 0.0535  71   SER A C   
366  O O   . SER A 47  ? 0.4449 0.4843 0.5928 -0.0674 -0.0659 0.0557  71   SER A O   
367  C CB  . SER A 47  ? 0.3706 0.4365 0.5433 -0.0505 -0.0390 0.0670  71   SER A CB  
368  O OG  . SER A 47  ? 0.4088 0.4820 0.5845 -0.0462 -0.0418 0.0680  71   SER A OG  
369  N N   . ASN A 48  ? 0.3600 0.3955 0.4854 -0.0544 -0.0604 0.0483  72   ASN A N   
370  C CA  . ASN A 48  ? 0.4259 0.4543 0.5393 -0.0597 -0.0733 0.0438  72   ASN A CA  
371  C C   . ASN A 48  ? 0.4931 0.5019 0.5874 -0.0636 -0.0771 0.0353  72   ASN A C   
372  O O   . ASN A 48  ? 0.5762 0.5781 0.6637 -0.0704 -0.0886 0.0319  72   ASN A O   
373  C CB  . ASN A 48  ? 0.4684 0.4969 0.5691 -0.0533 -0.0734 0.0411  72   ASN A CB  
374  C CG  . ASN A 48  ? 0.4942 0.5126 0.5779 -0.0458 -0.0634 0.0349  72   ASN A CG  
375  O OD1 . ASN A 48  ? 0.4961 0.5178 0.5860 -0.0409 -0.0529 0.0368  72   ASN A OD1 
376  N ND2 . ASN A 48  ? 0.5048 0.5115 0.5668 -0.0448 -0.0667 0.0275  72   ASN A ND2 
377  N N   . ILE A 49  ? 0.4406 0.4398 0.5253 -0.0590 -0.0679 0.0315  73   ILE A N   
378  C CA  . ILE A 49  ? 0.4033 0.3836 0.4712 -0.0612 -0.0704 0.0240  73   ILE A CA  
379  C C   . ILE A 49  ? 0.4595 0.4353 0.5379 -0.0709 -0.0769 0.0266  73   ILE A C   
380  O O   . ILE A 49  ? 0.4519 0.4331 0.5452 -0.0724 -0.0711 0.0329  73   ILE A O   
381  C CB  . ILE A 49  ? 0.3460 0.3192 0.4038 -0.0537 -0.0591 0.0210  73   ILE A CB  
382  C CG1 . ILE A 49  ? 0.3377 0.3137 0.3841 -0.0455 -0.0542 0.0178  73   ILE A CG1 
383  C CG2 . ILE A 49  ? 0.3573 0.3114 0.4011 -0.0552 -0.0610 0.0148  73   ILE A CG2 
384  C CD1 . ILE A 49  ? 0.3399 0.3109 0.3767 -0.0385 -0.0442 0.0150  73   ILE A CD1 
385  N N   . LYS A 50  ? 0.4780 0.4433 0.5478 -0.0778 -0.0889 0.0216  74   LYS A N   
386  C CA  . LYS A 50  ? 0.5810 0.5398 0.6600 -0.0887 -0.0972 0.0233  74   LYS A CA  
387  C C   . LYS A 50  ? 0.5078 0.4469 0.5772 -0.0886 -0.0933 0.0191  74   LYS A C   
388  O O   . LYS A 50  ? 0.4658 0.4037 0.5494 -0.0948 -0.0931 0.0247  74   LYS A O   
389  C CB  . LYS A 50  ? 0.7294 0.6816 0.7995 -0.0964 -0.1125 0.0182  74   LYS A CB  
390  C CG  . LYS A 50  ? 0.8338 0.8040 0.9101 -0.0961 -0.1181 0.0222  74   LYS A CG  
391  C CD  . LYS A 50  ? 0.9120 0.9057 1.0197 -0.0994 -0.1170 0.0350  74   LYS A CD  
392  C CE  . LYS A 50  ? 0.9689 0.9801 1.0841 -0.0990 -0.1236 0.0398  74   LYS A CE  
393  N NZ  . LYS A 50  ? 0.9359 0.9506 1.0400 -0.0873 -0.1152 0.0381  74   LYS A NZ  
394  N N   . ASP A 51  ? 0.4627 0.3870 0.5090 -0.0813 -0.0900 0.0100  75   ASP A N   
395  C CA  . ASP A 51  ? 0.4483 0.3527 0.4844 -0.0800 -0.0868 0.0057  75   ASP A CA  
396  C C   . ASP A 51  ? 0.4056 0.3091 0.4297 -0.0680 -0.0752 0.0031  75   ASP A C   
397  O O   . ASP A 51  ? 0.3938 0.2938 0.4009 -0.0618 -0.0746 -0.0037 75   ASP A O   
398  C CB  . ASP A 51  ? 0.5135 0.3959 0.5317 -0.0846 -0.0974 -0.0044 75   ASP A CB  
399  C CG  . ASP A 51  ? 0.5086 0.3681 0.5174 -0.0832 -0.0947 -0.0086 75   ASP A CG  
400  O OD1 . ASP A 51  ? 0.4718 0.3338 0.4862 -0.0777 -0.0845 -0.0037 75   ASP A OD1 
401  O OD2 . ASP A 51  ? 0.5780 0.4164 0.5729 -0.0873 -0.1030 -0.0171 75   ASP A OD2 
402  N N   . LYS A 52  ? 0.3797 0.2875 0.4128 -0.0651 -0.0660 0.0092  76   LYS A N   
403  C CA  . LYS A 52  ? 0.4098 0.3197 0.4340 -0.0547 -0.0556 0.0080  76   LYS A CA  
404  C C   . LYS A 52  ? 0.3904 0.2811 0.3945 -0.0493 -0.0554 -0.0005 76   LYS A C   
405  O O   . LYS A 52  ? 0.3935 0.2859 0.3873 -0.0406 -0.0491 -0.0034 76   LYS A O   
406  C CB  . LYS A 52  ? 0.4280 0.3445 0.4642 -0.0536 -0.0471 0.0163  76   LYS A CB  
407  C CG  . LYS A 52  ? 0.4341 0.3352 0.4717 -0.0576 -0.0483 0.0182  76   LYS A CG  
408  C CD  . LYS A 52  ? 0.5467 0.4503 0.5846 -0.0518 -0.0383 0.0233  76   LYS A CD  
409  C CE  . LYS A 52  ? 0.5847 0.4911 0.6385 -0.0581 -0.0363 0.0332  76   LYS A CE  
410  N NZ  . LYS A 52  ? 0.5187 0.4067 0.5742 -0.0659 -0.0441 0.0327  76   LYS A NZ  
411  N N   . ASP A 53  ? 0.3538 0.2263 0.3533 -0.0544 -0.0622 -0.0043 77   ASP A N   
412  C CA  . ASP A 53  ? 0.4213 0.2732 0.4024 -0.0487 -0.0614 -0.0124 77   ASP A CA  
413  C C   . ASP A 53  ? 0.4397 0.2829 0.4020 -0.0470 -0.0671 -0.0227 77   ASP A C   
414  O O   . ASP A 53  ? 0.4682 0.2955 0.4140 -0.0407 -0.0654 -0.0301 77   ASP A O   
415  C CB  . ASP A 53  ? 0.4504 0.2836 0.4348 -0.0538 -0.0642 -0.0113 77   ASP A CB  
416  C CG  . ASP A 53  ? 0.5226 0.3621 0.5199 -0.0522 -0.0562 -0.0015 77   ASP A CG  
417  O OD1 . ASP A 53  ? 0.4872 0.3355 0.4816 -0.0434 -0.0476 0.0005  77   ASP A OD1 
418  O OD2 . ASP A 53  ? 0.5939 0.4299 0.6042 -0.0603 -0.0589 0.0047  77   ASP A OD2 
419  N N   . ARG A 54  ? 0.3736 0.2278 0.3387 -0.0521 -0.0734 -0.0225 78   ARG A N   
420  C CA  . ARG A 54  ? 0.4140 0.2645 0.3613 -0.0505 -0.0785 -0.0307 78   ARG A CA  
421  C C   . ARG A 54  ? 0.4584 0.3307 0.4120 -0.0505 -0.0789 -0.0262 78   ARG A C   
422  O O   . ARG A 54  ? 0.4805 0.3593 0.4409 -0.0584 -0.0878 -0.0241 78   ARG A O   
423  C CB  . ARG A 54  ? 0.4334 0.2669 0.3731 -0.0595 -0.0907 -0.0369 78   ARG A CB  
424  C CG  . ARG A 54  ? 0.4846 0.2929 0.4155 -0.0585 -0.0903 -0.0426 78   ARG A CG  
425  C CD  . ARG A 54  ? 0.5628 0.3494 0.4819 -0.0671 -0.1026 -0.0511 78   ARG A CD  
426  N NE  . ARG A 54  ? 0.5965 0.3573 0.5063 -0.0638 -0.1002 -0.0568 78   ARG A NE  
427  C CZ  . ARG A 54  ? 0.6327 0.3722 0.5181 -0.0574 -0.0999 -0.0685 78   ARG A CZ  
428  N NH1 . ARG A 54  ? 0.6632 0.4045 0.5299 -0.0545 -0.1026 -0.0760 78   ARG A NH1 
429  N NH2 . ARG A 54  ? 0.6903 0.4063 0.5702 -0.0536 -0.0969 -0.0723 78   ARG A NH2 
430  N N   . ILE A 55  ? 0.3716 0.2549 0.3236 -0.0420 -0.0697 -0.0243 79   ILE A N   
431  C CA  . ILE A 55  ? 0.3566 0.2591 0.3155 -0.0412 -0.0689 -0.0194 79   ILE A CA  
432  C C   . ILE A 55  ? 0.4363 0.3382 0.3778 -0.0389 -0.0727 -0.0247 79   ILE A C   
433  O O   . ILE A 55  ? 0.4548 0.3432 0.3770 -0.0350 -0.0724 -0.0325 79   ILE A O   
434  C CB  . ILE A 55  ? 0.4080 0.3233 0.3761 -0.0349 -0.0581 -0.0139 79   ILE A CB  
435  C CG1 . ILE A 55  ? 0.3576 0.2675 0.3115 -0.0259 -0.0507 -0.0184 79   ILE A CG1 
436  C CG2 . ILE A 55  ? 0.3631 0.2812 0.3483 -0.0380 -0.0549 -0.0076 79   ILE A CG2 
437  C CD1 . ILE A 55  ? 0.3432 0.2660 0.3053 -0.0210 -0.0418 -0.0133 79   ILE A CD1 
438  N N   . GLN A 56  ? 0.4201 0.3366 0.3681 -0.0411 -0.0762 -0.0200 80   GLN A N   
439  C CA  . GLN A 56  ? 0.4687 0.3845 0.4006 -0.0411 -0.0824 -0.0237 80   GLN A CA  
440  C C   . GLN A 56  ? 0.4402 0.3645 0.3640 -0.0330 -0.0749 -0.0227 80   GLN A C   
441  O O   . GLN A 56  ? 0.4082 0.3467 0.3454 -0.0312 -0.0705 -0.0157 80   GLN A O   
442  C CB  . GLN A 56  ? 0.5999 0.5258 0.5431 -0.0492 -0.0929 -0.0185 80   GLN A CB  
443  C CG  . GLN A 56  ? 0.7893 0.7091 0.7138 -0.0528 -0.1037 -0.0238 80   GLN A CG  
444  C CD  . GLN A 56  ? 0.9243 0.8251 0.8389 -0.0596 -0.1126 -0.0317 80   GLN A CD  
445  O OE1 . GLN A 56  ? 0.9448 0.8359 0.8660 -0.0609 -0.1098 -0.0332 80   GLN A OE1 
446  N NE2 . GLN A 56  ? 0.9765 0.8714 0.8746 -0.0642 -0.1237 -0.0367 80   GLN A NE2 
447  N N   . MET A 57  ? 0.4283 0.3435 0.3301 -0.0283 -0.0735 -0.0296 81   MET A N   
448  C CA  . MET A 57  ? 0.4115 0.3350 0.3055 -0.0213 -0.0665 -0.0280 81   MET A CA  
449  C C   . MET A 57  ? 0.4137 0.3508 0.3126 -0.0240 -0.0713 -0.0214 81   MET A C   
450  O O   . MET A 57  ? 0.4418 0.3788 0.3395 -0.0302 -0.0817 -0.0211 81   MET A O   
451  C CB  . MET A 57  ? 0.4398 0.3520 0.3085 -0.0160 -0.0646 -0.0362 81   MET A CB  
452  C CG  . MET A 57  ? 0.4389 0.3371 0.3019 -0.0111 -0.0587 -0.0425 81   MET A CG  
453  S SD  . MET A 57  ? 0.4507 0.3581 0.3303 -0.0052 -0.0468 -0.0370 81   MET A SD  
454  C CE  . MET A 57  ? 0.3897 0.2939 0.2892 -0.0119 -0.0503 -0.0338 81   MET A CE  
455  N N   . GLY A 58  ? 0.3831 0.3317 0.2880 -0.0196 -0.0642 -0.0157 82   GLY A N   
456  C CA  . GLY A 58  ? 0.4600 0.4207 0.3699 -0.0210 -0.0676 -0.0086 82   GLY A CA  
457  C C   . GLY A 58  ? 0.4471 0.4182 0.3815 -0.0238 -0.0681 -0.0010 82   GLY A C   
458  O O   . GLY A 58  ? 0.4405 0.4214 0.3820 -0.0242 -0.0704 0.0058  82   GLY A O   
459  N N   . SER A 59  ? 0.3901 0.3587 0.3371 -0.0252 -0.0656 -0.0016 83   SER A N   
460  C CA  . SER A 59  ? 0.3916 0.3703 0.3613 -0.0266 -0.0640 0.0053  83   SER A CA  
461  C C   . SER A 59  ? 0.3545 0.3349 0.3301 -0.0216 -0.0530 0.0061  83   SER A C   
462  O O   . SER A 59  ? 0.3351 0.3098 0.2993 -0.0179 -0.0477 0.0017  83   SER A O   
463  C CB  . SER A 59  ? 0.4285 0.4052 0.4094 -0.0327 -0.0692 0.0054  83   SER A CB  
464  O OG  . SER A 59  ? 0.4107 0.3763 0.3864 -0.0321 -0.0653 -0.0001 83   SER A OG  
465  N N   . ARG A 60  ? 0.2973 0.2859 0.2906 -0.0214 -0.0497 0.0116  84   ARG A N   
466  C CA  . ARG A 60  ? 0.2831 0.2727 0.2810 -0.0174 -0.0402 0.0118  84   ARG A CA  
467  C C   . ARG A 60  ? 0.2803 0.2702 0.2901 -0.0190 -0.0376 0.0127  84   ARG A C   
468  O O   . ARG A 60  ? 0.2969 0.2920 0.3197 -0.0224 -0.0412 0.0167  84   ARG A O   
469  C CB  . ARG A 60  ? 0.3085 0.3056 0.3146 -0.0147 -0.0369 0.0170  84   ARG A CB  
470  C CG  . ARG A 60  ? 0.3182 0.3152 0.3126 -0.0126 -0.0374 0.0173  84   ARG A CG  
471  C CD  . ARG A 60  ? 0.3224 0.3257 0.3269 -0.0111 -0.0365 0.0238  84   ARG A CD  
472  N NE  . ARG A 60  ? 0.3209 0.3244 0.3156 -0.0095 -0.0363 0.0256  84   ARG A NE  
473  C CZ  . ARG A 60  ? 0.3325 0.3350 0.3255 -0.0072 -0.0300 0.0257  84   ARG A CZ  
474  N NH1 . ARG A 60  ? 0.2767 0.2770 0.2751 -0.0062 -0.0240 0.0230  84   ARG A NH1 
475  N NH2 . ARG A 60  ? 0.2884 0.2921 0.2741 -0.0064 -0.0299 0.0288  84   ARG A NH2 
476  N N   . VAL A 61  ? 0.2703 0.2557 0.2762 -0.0167 -0.0313 0.0098  85   VAL A N   
477  C CA  . VAL A 61  ? 0.2934 0.2788 0.3083 -0.0178 -0.0278 0.0110  85   VAL A CA  
478  C C   . VAL A 61  ? 0.2886 0.2792 0.3094 -0.0142 -0.0199 0.0131  85   VAL A C   
479  O O   . VAL A 61  ? 0.2691 0.2582 0.2820 -0.0110 -0.0162 0.0107  85   VAL A O   
480  C CB  . VAL A 61  ? 0.2982 0.2738 0.3031 -0.0175 -0.0268 0.0067  85   VAL A CB  
481  C CG1 . VAL A 61  ? 0.2803 0.2565 0.2941 -0.0183 -0.0223 0.0094  85   VAL A CG1 
482  C CG2 . VAL A 61  ? 0.2817 0.2489 0.2788 -0.0210 -0.0347 0.0033  85   VAL A CG2 
483  N N   . LEU A 62  ? 0.2190 0.2157 0.2536 -0.0147 -0.0172 0.0173  86   LEU A N   
484  C CA  . LEU A 62  ? 0.2429 0.2429 0.2816 -0.0110 -0.0093 0.0183  86   LEU A CA  
485  C C   . LEU A 62  ? 0.2396 0.2367 0.2747 -0.0103 -0.0039 0.0170  86   LEU A C   
486  O O   . LEU A 62  ? 0.2589 0.2561 0.2988 -0.0130 -0.0045 0.0191  86   LEU A O   
487  C CB  . LEU A 62  ? 0.2417 0.2502 0.2969 -0.0104 -0.0077 0.0237  86   LEU A CB  
488  C CG  . LEU A 62  ? 0.2494 0.2619 0.3097 -0.0099 -0.0123 0.0265  86   LEU A CG  
489  C CD1 . LEU A 62  ? 0.3061 0.3288 0.3858 -0.0093 -0.0116 0.0331  86   LEU A CD1 
490  C CD2 . LEU A 62  ? 0.2850 0.2939 0.3380 -0.0060 -0.0088 0.0242  86   LEU A CD2 
491  N N   . VAL A 63  ? 0.2386 0.2334 0.2653 -0.0074 0.0007  0.0140  87   VAL A N   
492  C CA  . VAL A 63  ? 0.2512 0.2436 0.2724 -0.0066 0.0049  0.0131  87   VAL A CA  
493  C C   . VAL A 63  ? 0.2348 0.2295 0.2561 -0.0039 0.0118  0.0128  87   VAL A C   
494  O O   . VAL A 63  ? 0.2245 0.2179 0.2413 -0.0022 0.0128  0.0100  87   VAL A O   
495  C CB  . VAL A 63  ? 0.2894 0.2767 0.2980 -0.0058 0.0032  0.0094  87   VAL A CB  
496  C CG1 . VAL A 63  ? 0.2703 0.2557 0.2740 -0.0050 0.0064  0.0098  87   VAL A CG1 
497  C CG2 . VAL A 63  ? 0.2975 0.2808 0.3032 -0.0074 -0.0030 0.0082  87   VAL A CG2 
498  N N   . PRO A 64  ? 0.2483 0.2456 0.2738 -0.0035 0.0168  0.0155  88   PRO A N   
499  C CA  . PRO A 64  ? 0.2315 0.2297 0.2540 -0.0004 0.0239  0.0141  88   PRO A CA  
500  C C   . PRO A 64  ? 0.2541 0.2481 0.2621 0.0002  0.0244  0.0102  88   PRO A C   
501  O O   . PRO A 64  ? 0.2749 0.2674 0.2778 -0.0011 0.0220  0.0109  88   PRO A O   
502  C CB  . PRO A 64  ? 0.2114 0.2146 0.2411 -0.0003 0.0291  0.0189  88   PRO A CB  
503  C CG  . PRO A 64  ? 0.2395 0.2415 0.2706 -0.0042 0.0244  0.0219  88   PRO A CG  
504  C CD  . PRO A 64  ? 0.2322 0.2312 0.2639 -0.0062 0.0163  0.0198  88   PRO A CD  
505  N N   . PHE A 65  ? 0.2568 0.2486 0.2588 0.0021  0.0275  0.0065  89   PHE A N   
506  C CA  . PHE A 65  ? 0.2685 0.2575 0.2574 0.0019  0.0272  0.0030  89   PHE A CA  
507  C C   . PHE A 65  ? 0.2588 0.2448 0.2414 0.0037  0.0322  -0.0010 89   PHE A C   
508  O O   . PHE A 65  ? 0.2589 0.2436 0.2477 0.0059  0.0357  -0.0017 89   PHE A O   
509  C CB  . PHE A 65  ? 0.2312 0.2189 0.2168 0.0002  0.0212  0.0011  89   PHE A CB  
510  C CG  . PHE A 65  ? 0.2448 0.2303 0.2327 0.0000  0.0200  -0.0013 89   PHE A CG  
511  C CD1 . PHE A 65  ? 0.2615 0.2439 0.2422 -0.0009 0.0198  -0.0051 89   PHE A CD1 
512  C CD2 . PHE A 65  ? 0.2421 0.2284 0.2392 0.0001  0.0181  0.0008  89   PHE A CD2 
513  C CE1 . PHE A 65  ? 0.3056 0.2850 0.2890 -0.0017 0.0185  -0.0065 89   PHE A CE1 
514  C CE2 . PHE A 65  ? 0.2363 0.2203 0.2354 0.0000  0.0169  -0.0001 89   PHE A CE2 
515  C CZ  . PHE A 65  ? 0.2567 0.2367 0.2494 -0.0010 0.0173  -0.0036 89   PHE A CZ  
516  N N   . PRO A 66  ? 0.2874 0.2719 0.2573 0.0033  0.0327  -0.0036 90   PRO A N   
517  C CA  . PRO A 66  ? 0.3169 0.2966 0.2775 0.0047  0.0371  -0.0086 90   PRO A CA  
518  C C   . PRO A 66  ? 0.3227 0.2964 0.2827 0.0035  0.0343  -0.0134 90   PRO A C   
519  O O   . PRO A 66  ? 0.3236 0.2983 0.2854 0.0007  0.0284  -0.0130 90   PRO A O   
520  C CB  . PRO A 66  ? 0.3597 0.3403 0.3060 0.0033  0.0358  -0.0095 90   PRO A CB  
521  C CG  . PRO A 66  ? 0.2778 0.2641 0.2287 0.0026  0.0331  -0.0031 90   PRO A CG  
522  C CD  . PRO A 66  ? 0.2820 0.2688 0.2451 0.0017  0.0290  -0.0019 90   PRO A CD  
523  N N   . CYS A 67  ? 0.3063 0.2733 0.2642 0.0059  0.0391  -0.0175 91   CYS A N   
524  C CA  . CYS A 67  ? 0.3012 0.2604 0.2594 0.0045  0.0366  -0.0216 91   CYS A CA  
525  C C   . CYS A 67  ? 0.3521 0.3021 0.2948 0.0039  0.0384  -0.0292 91   CYS A C   
526  O O   . CYS A 67  ? 0.3931 0.3380 0.3314 0.0081  0.0454  -0.0323 91   CYS A O   
527  C CB  . CYS A 67  ? 0.3507 0.3082 0.3224 0.0083  0.0400  -0.0195 91   CYS A CB  
528  S SG  . CYS A 67  ? 0.4040 0.3508 0.3791 0.0070  0.0372  -0.0224 91   CYS A SG  
529  N N   . GLU A 68  ? 0.3476 0.2958 0.2822 -0.0013 0.0319  -0.0321 92   GLU A N   
530  C CA  . GLU A 68  ? 0.3715 0.3130 0.2888 -0.0034 0.0313  -0.0389 92   GLU A CA  
531  C C   . GLU A 68  ? 0.3861 0.3177 0.3010 -0.0083 0.0263  -0.0442 92   GLU A C   
532  O O   . GLU A 68  ? 0.3636 0.2979 0.2891 -0.0115 0.0215  -0.0408 92   GLU A O   
533  C CB  . GLU A 68  ? 0.3847 0.3355 0.2943 -0.0064 0.0265  -0.0363 92   GLU A CB  
534  C CG  . GLU A 68  ? 0.4997 0.4587 0.4105 -0.0023 0.0315  -0.0307 92   GLU A CG  
535  C CD  . GLU A 68  ? 0.5649 0.5341 0.4778 -0.0041 0.0263  -0.0247 92   GLU A CD  
536  O OE1 . GLU A 68  ? 0.5111 0.4839 0.4315 -0.0069 0.0204  -0.0227 92   GLU A OE1 
537  O OE2 . GLU A 68  ? 0.6783 0.6520 0.5856 -0.0023 0.0288  -0.0213 92   GLU A OE2 
538  N N   . CYS A 69  ? 0.3772 0.2969 0.2774 -0.0092 0.0274  -0.0524 93   CYS A N   
539  C CA  . CYS A 69  ? 0.4196 0.3285 0.3165 -0.0152 0.0216  -0.0578 93   CYS A CA  
540  C C   . CYS A 69  ? 0.4747 0.3932 0.3698 -0.0229 0.0120  -0.0555 93   CYS A C   
541  O O   . CYS A 69  ? 0.5024 0.4281 0.3874 -0.0237 0.0100  -0.0553 93   CYS A O   
542  C CB  . CYS A 69  ? 0.5168 0.4085 0.3963 -0.0144 0.0250  -0.0683 93   CYS A CB  
543  S SG  . CYS A 69  ? 0.6773 0.5504 0.5565 -0.0210 0.0194  -0.0751 93   CYS A SG  
544  N N   . GLN A 70  ? 0.4702 0.3898 0.3760 -0.0281 0.0063  -0.0529 94   GLN A N   
545  C CA  . GLN A 70  ? 0.4043 0.3355 0.3127 -0.0348 -0.0022 -0.0492 94   GLN A CA  
546  C C   . GLN A 70  ? 0.4357 0.3567 0.3374 -0.0432 -0.0088 -0.0554 94   GLN A C   
547  O O   . GLN A 70  ? 0.4327 0.3374 0.3331 -0.0437 -0.0068 -0.0606 94   GLN A O   
548  C CB  . GLN A 70  ? 0.3773 0.3184 0.3035 -0.0348 -0.0033 -0.0409 94   GLN A CB  
549  C CG  . GLN A 70  ? 0.3509 0.3010 0.2838 -0.0275 0.0020  -0.0351 94   GLN A CG  
550  C CD  . GLN A 70  ? 0.3742 0.3360 0.3022 -0.0263 0.0005  -0.0323 94   GLN A CD  
551  O OE1 . GLN A 70  ? 0.3584 0.3270 0.2833 -0.0308 -0.0056 -0.0316 94   GLN A OE1 
552  N NE2 . GLN A 70  ? 0.3524 0.3168 0.2805 -0.0204 0.0057  -0.0300 94   GLN A NE2 
553  N N   . PRO A 71  ? 0.4474 0.3779 0.3460 -0.0499 -0.0170 -0.0543 95   PRO A N   
554  C CA  . PRO A 71  ? 0.4406 0.3628 0.3356 -0.0597 -0.0249 -0.0591 95   PRO A CA  
555  C C   . PRO A 71  ? 0.4705 0.3877 0.3811 -0.0624 -0.0248 -0.0559 95   PRO A C   
556  O O   . PRO A 71  ? 0.4458 0.3757 0.3715 -0.0604 -0.0236 -0.0472 95   PRO A O   
557  C CB  . PRO A 71  ? 0.4899 0.4305 0.3874 -0.0654 -0.0336 -0.0539 95   PRO A CB  
558  C CG  . PRO A 71  ? 0.5001 0.4523 0.3927 -0.0579 -0.0298 -0.0503 95   PRO A CG  
559  C CD  . PRO A 71  ? 0.4686 0.4176 0.3682 -0.0489 -0.0199 -0.0480 95   PRO A CD  
560  N N   . GLY A 72  ? 0.5397 0.4374 0.4460 -0.0667 -0.0259 -0.0628 96   GLY A N   
561  C CA  . GLY A 72  ? 0.5064 0.3979 0.4274 -0.0684 -0.0248 -0.0588 96   GLY A CA  
562  C C   . GLY A 72  ? 0.5651 0.4402 0.4846 -0.0599 -0.0159 -0.0623 96   GLY A C   
563  O O   . GLY A 72  ? 0.5800 0.4470 0.5103 -0.0597 -0.0141 -0.0593 96   GLY A O   
564  N N   . ASP A 73  ? 0.5182 0.3896 0.4249 -0.0526 -0.0101 -0.0678 97   ASP A N   
565  C CA  . ASP A 73  ? 0.5395 0.3973 0.4448 -0.0435 -0.0008 -0.0713 97   ASP A CA  
566  C C   . ASP A 73  ? 0.5317 0.3966 0.4550 -0.0372 0.0043  -0.0621 97   ASP A C   
567  O O   . ASP A 73  ? 0.5257 0.3780 0.4559 -0.0346 0.0075  -0.0619 97   ASP A O   
568  C CB  . ASP A 73  ? 0.7312 0.5631 0.6278 -0.0463 -0.0010 -0.0809 97   ASP A CB  
569  C CG  . ASP A 73  ? 0.8566 0.6791 0.7310 -0.0509 -0.0049 -0.0919 97   ASP A CG  
570  O OD1 . ASP A 73  ? 0.9521 0.7547 0.8185 -0.0571 -0.0090 -0.1000 97   ASP A OD1 
571  O OD2 . ASP A 73  ? 0.8751 0.7096 0.7394 -0.0486 -0.0043 -0.0923 97   ASP A OD2 
572  N N   . PHE A 74  ? 0.4100 0.2946 0.3406 -0.0347 0.0046  -0.0544 98   PHE A N   
573  C CA  . PHE A 74  ? 0.4491 0.3405 0.3939 -0.0285 0.0090  -0.0466 98   PHE A CA  
574  C C   . PHE A 74  ? 0.4277 0.3325 0.3708 -0.0228 0.0126  -0.0442 98   PHE A C   
575  O O   . PHE A 74  ? 0.3973 0.3077 0.3301 -0.0245 0.0108  -0.0467 98   PHE A O   
576  C CB  . PHE A 74  ? 0.4330 0.3341 0.3910 -0.0332 0.0041  -0.0381 98   PHE A CB  
577  C CG  . PHE A 74  ? 0.4569 0.3755 0.4151 -0.0373 -0.0009 -0.0343 98   PHE A CG  
578  C CD1 . PHE A 74  ? 0.3844 0.3177 0.3461 -0.0325 0.0010  -0.0291 98   PHE A CD1 
579  C CD2 . PHE A 74  ? 0.4608 0.3808 0.4165 -0.0459 -0.0076 -0.0356 98   PHE A CD2 
580  C CE1 . PHE A 74  ? 0.3744 0.3224 0.3366 -0.0351 -0.0029 -0.0256 98   PHE A CE1 
581  C CE2 . PHE A 74  ? 0.4188 0.3559 0.3766 -0.0488 -0.0118 -0.0313 98   PHE A CE2 
582  C CZ  . PHE A 74  ? 0.3806 0.3313 0.3414 -0.0428 -0.0091 -0.0263 98   PHE A CZ  
583  N N   . LEU A 75  ? 0.3583 0.2680 0.3116 -0.0164 0.0173  -0.0389 99   LEU A N   
584  C CA  . LEU A 75  ? 0.3271 0.2483 0.2802 -0.0116 0.0207  -0.0362 99   LEU A CA  
585  C C   . LEU A 75  ? 0.2739 0.2101 0.2341 -0.0129 0.0170  -0.0291 99   LEU A C   
586  O O   . LEU A 75  ? 0.2962 0.2357 0.2664 -0.0139 0.0148  -0.0240 99   LEU A O   
587  C CB  . LEU A 75  ? 0.3448 0.2634 0.3055 -0.0040 0.0278  -0.0346 99   LEU A CB  
588  C CG  . LEU A 75  ? 0.3650 0.2688 0.3181 0.0001  0.0340  -0.0418 99   LEU A CG  
589  C CD1 . LEU A 75  ? 0.3623 0.2660 0.3281 0.0078  0.0404  -0.0379 99   LEU A CD1 
590  C CD2 . LEU A 75  ? 0.3912 0.2953 0.3287 0.0011  0.0372  -0.0473 99   LEU A CD2 
591  N N   . GLY A 76  ? 0.3007 0.2457 0.2554 -0.0125 0.0167  -0.0286 100  GLY A N   
592  C CA  . GLY A 76  ? 0.2792 0.2367 0.2398 -0.0127 0.0139  -0.0225 100  GLY A CA  
593  C C   . GLY A 76  ? 0.3093 0.2736 0.2632 -0.0114 0.0143  -0.0220 100  GLY A C   
594  O O   . GLY A 76  ? 0.2983 0.2588 0.2432 -0.0100 0.0175  -0.0256 100  GLY A O   
595  N N   . HIS A 77  ? 0.2502 0.2240 0.2079 -0.0116 0.0114  -0.0174 101  HIS A N   
596  C CA  . HIS A 77  ? 0.2583 0.2379 0.2106 -0.0103 0.0113  -0.0158 101  HIS A CA  
597  C C   . HIS A 77  ? 0.2633 0.2516 0.2173 -0.0119 0.0065  -0.0125 101  HIS A C   
598  O O   . HIS A 77  ? 0.2442 0.2357 0.2056 -0.0119 0.0050  -0.0098 101  HIS A O   
599  C CB  . HIS A 77  ? 0.2319 0.2130 0.1891 -0.0063 0.0151  -0.0126 101  HIS A CB  
600  C CG  . HIS A 77  ? 0.2667 0.2524 0.2194 -0.0050 0.0153  -0.0099 101  HIS A CG  
601  N ND1 . HIS A 77  ? 0.2905 0.2752 0.2331 -0.0047 0.0175  -0.0114 101  HIS A ND1 
602  C CD2 . HIS A 77  ? 0.2746 0.2648 0.2308 -0.0037 0.0138  -0.0056 101  HIS A CD2 
603  C CE1 . HIS A 77  ? 0.3035 0.2928 0.2446 -0.0034 0.0171  -0.0071 101  HIS A CE1 
604  N NE2 . HIS A 77  ? 0.2879 0.2797 0.2376 -0.0027 0.0149  -0.0038 101  HIS A NE2 
605  N N   . ASN A 78  ? 0.2532 0.2457 0.2000 -0.0127 0.0043  -0.0122 102  ASN A N   
606  C CA  . ASN A 78  ? 0.2243 0.2263 0.1739 -0.0126 0.0004  -0.0081 102  ASN A CA  
607  C C   . ASN A 78  ? 0.3010 0.3053 0.2522 -0.0079 0.0024  -0.0040 102  ASN A C   
608  O O   . ASN A 78  ? 0.2736 0.2775 0.2186 -0.0066 0.0036  -0.0031 102  ASN A O   
609  C CB  . ASN A 78  ? 0.2549 0.2614 0.1968 -0.0156 -0.0039 -0.0088 102  ASN A CB  
610  C CG  . ASN A 78  ? 0.2843 0.2881 0.2242 -0.0216 -0.0074 -0.0129 102  ASN A CG  
611  O OD1 . ASN A 78  ? 0.2808 0.2824 0.2279 -0.0237 -0.0075 -0.0134 102  ASN A OD1 
612  N ND2 . ASN A 78  ? 0.3216 0.3249 0.2507 -0.0249 -0.0108 -0.0158 102  ASN A ND2 
613  N N   . PHE A 79  ? 0.2362 0.2419 0.1946 -0.0057 0.0028  -0.0017 103  PHE A N   
614  C CA  . PHE A 79  ? 0.2196 0.2263 0.1794 -0.0018 0.0034  0.0018  103  PHE A CA  
615  C C   . PHE A 79  ? 0.2322 0.2468 0.1920 -0.0003 0.0004  0.0049  103  PHE A C   
616  O O   . PHE A 79  ? 0.2794 0.3004 0.2403 -0.0029 -0.0023 0.0047  103  PHE A O   
617  C CB  . PHE A 79  ? 0.1994 0.2032 0.1649 0.0000  0.0043  0.0021  103  PHE A CB  
618  C CG  . PHE A 79  ? 0.2199 0.2176 0.1876 -0.0009 0.0066  0.0005  103  PHE A CG  
619  C CD1 . PHE A 79  ? 0.2446 0.2388 0.2123 0.0000  0.0088  0.0018  103  PHE A CD1 
620  C CD2 . PHE A 79  ? 0.2394 0.2357 0.2105 -0.0027 0.0067  -0.0012 103  PHE A CD2 
621  C CE1 . PHE A 79  ? 0.2315 0.2225 0.2038 -0.0006 0.0111  0.0014  103  PHE A CE1 
622  C CE2 . PHE A 79  ? 0.2678 0.2598 0.2427 -0.0028 0.0088  -0.0017 103  PHE A CE2 
623  C CZ  . PHE A 79  ? 0.2667 0.2569 0.2428 -0.0016 0.0110  -0.0004 103  PHE A CZ  
624  N N   . SER A 80  ? 0.2248 0.2391 0.1845 0.0036  0.0009  0.0082  104  SER A N   
625  C CA  . SER A 80  ? 0.2544 0.2763 0.2159 0.0067  -0.0013 0.0120  104  SER A CA  
626  C C   . SER A 80  ? 0.3185 0.3372 0.2839 0.0117  0.0004  0.0131  104  SER A C   
627  O O   . SER A 80  ? 0.3665 0.3761 0.3309 0.0128  0.0022  0.0124  104  SER A O   
628  C CB  . SER A 80  ? 0.3114 0.3346 0.2679 0.0079  -0.0023 0.0156  104  SER A CB  
629  O OG  . SER A 80  ? 0.3726 0.3981 0.3227 0.0034  -0.0042 0.0137  104  SER A OG  
630  N N   . TYR A 81  ? 0.2466 0.2725 0.2163 0.0145  -0.0001 0.0147  105  TYR A N   
631  C CA  . TYR A 81  ? 0.2579 0.2799 0.2292 0.0200  0.0022  0.0146  105  TYR A CA  
632  C C   . TYR A 81  ? 0.2690 0.2978 0.2435 0.0262  0.0022  0.0191  105  TYR A C   
633  O O   . TYR A 81  ? 0.2535 0.2950 0.2328 0.0260  0.0008  0.0219  105  TYR A O   
634  C CB  . TYR A 81  ? 0.2498 0.2736 0.2228 0.0188  0.0034  0.0121  105  TYR A CB  
635  C CG  . TYR A 81  ? 0.2773 0.2975 0.2493 0.0248  0.0059  0.0113  105  TYR A CG  
636  C CD1 . TYR A 81  ? 0.2843 0.2913 0.2517 0.0261  0.0064  0.0083  105  TYR A CD1 
637  C CD2 . TYR A 81  ? 0.3131 0.3429 0.2886 0.0293  0.0078  0.0136  105  TYR A CD2 
638  C CE1 . TYR A 81  ? 0.3103 0.3115 0.2742 0.0316  0.0083  0.0064  105  TYR A CE1 
639  C CE2 . TYR A 81  ? 0.2890 0.3144 0.2616 0.0360  0.0111  0.0122  105  TYR A CE2 
640  C CZ  . TYR A 81  ? 0.3335 0.3434 0.2991 0.0370  0.0111  0.0080  105  TYR A CZ  
641  O OH  . TYR A 81  ? 0.3677 0.3707 0.3278 0.0435  0.0140  0.0053  105  TYR A OH  
642  N N   . SER A 82  ? 0.2995 0.3196 0.2725 0.0318  0.0036  0.0201  106  SER A N   
643  C CA  . SER A 82  ? 0.2732 0.2979 0.2500 0.0394  0.0045  0.0244  106  SER A CA  
644  C C   . SER A 82  ? 0.2848 0.3099 0.2630 0.0450  0.0081  0.0223  106  SER A C   
645  O O   . SER A 82  ? 0.2859 0.2986 0.2588 0.0461  0.0100  0.0176  106  SER A O   
646  C CB  . SER A 82  ? 0.4069 0.4194 0.3810 0.0432  0.0047  0.0265  106  SER A CB  
647  O OG  . SER A 82  ? 0.4495 0.4630 0.4214 0.0385  0.0022  0.0294  106  SER A OG  
648  N N   . VAL A 83  ? 0.2977 0.3381 0.2828 0.0481  0.0090  0.0259  107  VAL A N   
649  C CA  . VAL A 83  ? 0.3321 0.3765 0.3188 0.0533  0.0134  0.0248  107  VAL A CA  
650  C C   . VAL A 83  ? 0.4117 0.4451 0.3952 0.0635  0.0175  0.0237  107  VAL A C   
651  O O   . VAL A 83  ? 0.3899 0.4208 0.3759 0.0686  0.0170  0.0274  107  VAL A O   
652  C CB  . VAL A 83  ? 0.2488 0.3150 0.2464 0.0535  0.0134  0.0307  107  VAL A CB  
653  C CG1 . VAL A 83  ? 0.3310 0.4041 0.3318 0.0612  0.0195  0.0314  107  VAL A CG1 
654  C CG2 . VAL A 83  ? 0.2262 0.2992 0.2251 0.0426  0.0095  0.0300  107  VAL A CG2 
655  N N   . ARG A 84  ? 0.3506 0.3762 0.3276 0.0665  0.0213  0.0184  108  ARG A N   
656  C CA  . ARG A 84  ? 0.3973 0.4104 0.3689 0.0764  0.0256  0.0156  108  ARG A CA  
657  C C   . ARG A 84  ? 0.3787 0.4021 0.3514 0.0836  0.0319  0.0158  108  ARG A C   
658  O O   . ARG A 84  ? 0.3459 0.3828 0.3213 0.0793  0.0327  0.0171  108  ARG A O   
659  C CB  . ARG A 84  ? 0.4414 0.4328 0.4008 0.0734  0.0242  0.0078  108  ARG A CB  
660  C CG  . ARG A 84  ? 0.5187 0.4996 0.4775 0.0662  0.0189  0.0079  108  ARG A CG  
661  C CD  . ARG A 84  ? 0.6747 0.6399 0.6243 0.0607  0.0166  0.0011  108  ARG A CD  
662  N NE  . ARG A 84  ? 0.7945 0.7676 0.7418 0.0562  0.0167  -0.0013 108  ARG A NE  
663  C CZ  . ARG A 84  ? 0.8297 0.8005 0.7692 0.0596  0.0195  -0.0055 108  ARG A CZ  
664  N NH1 . ARG A 84  ? 0.6830 0.6622 0.6212 0.0551  0.0193  -0.0060 108  ARG A NH1 
665  N NH2 . ARG A 84  ? 0.9064 0.8660 0.8386 0.0680  0.0227  -0.0092 108  ARG A NH2 
666  N N   . GLN A 85  ? 0.4072 0.4240 0.3778 0.0950  0.0370  0.0149  109  GLN A N   
667  C CA  . GLN A 85  ? 0.4341 0.4599 0.4046 0.1037  0.0447  0.0149  109  GLN A CA  
668  C C   . GLN A 85  ? 0.4132 0.4401 0.3747 0.0987  0.0462  0.0104  109  GLN A C   
669  O O   . GLN A 85  ? 0.4626 0.4725 0.4115 0.0939  0.0433  0.0034  109  GLN A O   
670  C CB  . GLN A 85  ? 0.5400 0.5492 0.5030 0.1164  0.0502  0.0108  109  GLN A CB  
671  C CG  . GLN A 85  ? 0.6845 0.7023 0.6461 0.1273  0.0597  0.0104  109  GLN A CG  
672  C CD  . GLN A 85  ? 0.7494 0.7926 0.7298 0.1338  0.0634  0.0208  109  GLN A CD  
673  O OE1 . GLN A 85  ? 0.7827 0.8432 0.7677 0.1383  0.0701  0.0239  109  GLN A OE1 
674  N NE2 . GLN A 85  ? 0.7741 0.8206 0.7658 0.1342  0.0589  0.0271  109  GLN A NE2 
675  N N   . GLU A 86  ? 0.4106 0.4583 0.3797 0.0995  0.0504  0.0155  110  GLU A N   
676  C CA  . GLU A 86  ? 0.4641 0.5156 0.4257 0.0960  0.0530  0.0133  110  GLU A CA  
677  C C   . GLU A 86  ? 0.4284 0.4824 0.3913 0.0823  0.0462  0.0138  110  GLU A C   
678  O O   . GLU A 86  ? 0.4045 0.4616 0.3621 0.0785  0.0475  0.0132  110  GLU A O   
679  C CB  . GLU A 86  ? 0.5846 0.6164 0.5268 0.1019  0.0567  0.0042  110  GLU A CB  
680  C CG  . GLU A 86  ? 0.6945 0.7194 0.6341 0.1163  0.0636  0.0023  110  GLU A CG  
681  C CD  . GLU A 86  ? 0.8330 0.8545 0.7583 0.1252  0.0723  -0.0025 110  GLU A CD  
682  O OE1 . GLU A 86  ? 0.8789 0.8857 0.7866 0.1213  0.0703  -0.0102 110  GLU A OE1 
683  O OE2 . GLU A 86  ? 0.8939 0.9284 0.8255 0.1362  0.0812  0.0016  110  GLU A OE2 
684  N N   . ASP A 87  ? 0.3689 0.4214 0.3383 0.0755  0.0394  0.0154  111  ASP A N   
685  C CA  . ASP A 87  ? 0.3265 0.3819 0.2983 0.0637  0.0339  0.0161  111  ASP A CA  
686  C C   . ASP A 87  ? 0.3051 0.3820 0.2882 0.0603  0.0354  0.0229  111  ASP A C   
687  O O   . ASP A 87  ? 0.2936 0.3863 0.2880 0.0646  0.0380  0.0290  111  ASP A O   
688  C CB  . ASP A 87  ? 0.2945 0.3456 0.2706 0.0581  0.0274  0.0167  111  ASP A CB  
689  C CG  . ASP A 87  ? 0.3731 0.4032 0.3392 0.0570  0.0245  0.0106  111  ASP A CG  
690  O OD1 . ASP A 87  ? 0.3640 0.3824 0.3194 0.0583  0.0258  0.0052  111  ASP A OD1 
691  O OD2 . ASP A 87  ? 0.3692 0.3952 0.3380 0.0543  0.0207  0.0116  111  ASP A OD2 
692  N N   . THR A 88  ? 0.2860 0.3637 0.2672 0.0523  0.0337  0.0228  112  THR A N   
693  C CA  . THR A 88  ? 0.2493 0.3448 0.2420 0.0464  0.0337  0.0295  112  THR A CA  
694  C C   . THR A 88  ? 0.2430 0.3327 0.2359 0.0353  0.0272  0.0282  112  THR A C   
695  O O   . THR A 88  ? 0.2593 0.3333 0.2431 0.0333  0.0244  0.0226  112  THR A O   
696  C CB  . THR A 88  ? 0.3346 0.4381 0.3247 0.0490  0.0402  0.0321  112  THR A CB  
697  O OG1 . THR A 88  ? 0.3242 0.4136 0.3006 0.0465  0.0393  0.0271  112  THR A OG1 
698  C CG2 . THR A 88  ? 0.3488 0.4578 0.3372 0.0615  0.0483  0.0329  112  THR A CG2 
699  N N   . TYR A 89  ? 0.2506 0.3523 0.2543 0.0280  0.0249  0.0332  113  TYR A N   
700  C CA  . TYR A 89  ? 0.2438 0.3376 0.2467 0.0184  0.0194  0.0312  113  TYR A CA  
701  C C   . TYR A 89  ? 0.2810 0.3647 0.2750 0.0170  0.0207  0.0287  113  TYR A C   
702  O O   . TYR A 89  ? 0.2716 0.3427 0.2607 0.0131  0.0171  0.0247  113  TYR A O   
703  C CB  . TYR A 89  ? 0.2639 0.3704 0.2791 0.0102  0.0165  0.0366  113  TYR A CB  
704  C CG  . TYR A 89  ? 0.2747 0.3901 0.2982 0.0088  0.0124  0.0386  113  TYR A CG  
705  C CD1 . TYR A 89  ? 0.2136 0.3188 0.2318 0.0076  0.0078  0.0340  113  TYR A CD1 
706  C CD2 . TYR A 89  ? 0.2411 0.3762 0.2780 0.0079  0.0127  0.0459  113  TYR A CD2 
707  C CE1 . TYR A 89  ? 0.2278 0.3410 0.2516 0.0058  0.0033  0.0362  113  TYR A CE1 
708  C CE2 . TYR A 89  ? 0.2817 0.4260 0.3263 0.0058  0.0075  0.0482  113  TYR A CE2 
709  C CZ  . TYR A 89  ? 0.2440 0.3765 0.2808 0.0047  0.0026  0.0431  113  TYR A CZ  
710  O OH  . TYR A 89  ? 0.2293 0.3708 0.2716 0.0027  -0.0031 0.0457  113  TYR A OH  
711  N N   . GLU A 90  ? 0.2921 0.3822 0.2839 0.0205  0.0259  0.0318  114  GLU A N   
712  C CA  . GLU A 90  ? 0.3070 0.3884 0.2888 0.0198  0.0266  0.0302  114  GLU A CA  
713  C C   . GLU A 90  ? 0.3143 0.3794 0.2836 0.0236  0.0249  0.0227  114  GLU A C   
714  O O   . GLU A 90  ? 0.3060 0.3605 0.2710 0.0196  0.0210  0.0200  114  GLU A O   
715  C CB  . GLU A 90  ? 0.3219 0.4136 0.3009 0.0241  0.0333  0.0348  114  GLU A CB  
716  C CG  . GLU A 90  ? 0.4586 0.5414 0.4255 0.0231  0.0332  0.0337  114  GLU A CG  
717  C CD  . GLU A 90  ? 0.6182 0.7077 0.5762 0.0293  0.0403  0.0363  114  GLU A CD  
718  O OE1 . GLU A 90  ? 0.6751 0.7713 0.6324 0.0372  0.0460  0.0360  114  GLU A OE1 
719  O OE2 . GLU A 90  ? 0.6815 0.7696 0.6327 0.0269  0.0405  0.0389  114  GLU A OE2 
720  N N   . ARG A 91  ? 0.2694 0.3324 0.2339 0.0315  0.0277  0.0197  115  ARG A N   
721  C CA  . ARG A 91  ? 0.2771 0.3236 0.2300 0.0345  0.0258  0.0127  115  ARG A CA  
722  C C   . ARG A 91  ? 0.3082 0.3459 0.2646 0.0296  0.0201  0.0101  115  ARG A C   
723  O O   . ARG A 91  ? 0.3118 0.3378 0.2621 0.0274  0.0167  0.0062  115  ARG A O   
724  C CB  . ARG A 91  ? 0.3635 0.4074 0.3108 0.0442  0.0301  0.0099  115  ARG A CB  
725  C CG  . ARG A 91  ? 0.5541 0.6007 0.4912 0.0505  0.0363  0.0096  115  ARG A CG  
726  C CD  . ARG A 91  ? 0.7626 0.8022 0.6917 0.0611  0.0410  0.0051  115  ARG A CD  
727  N NE  . ARG A 91  ? 0.8745 0.9017 0.8048 0.0619  0.0370  0.0013  115  ARG A NE  
728  C CZ  . ARG A 91  ? 0.9772 0.9953 0.9022 0.0706  0.0400  -0.0026 115  ARG A CZ  
729  N NH1 . ARG A 91  ? 0.9940 1.0136 0.9111 0.0799  0.0474  -0.0040 115  ARG A NH1 
730  N NH2 . ARG A 91  ? 1.0109 1.0179 0.9382 0.0704  0.0361  -0.0047 115  ARG A NH2 
731  N N   . VAL A 92  ? 0.2315 0.2755 0.1975 0.0280  0.0189  0.0125  116  VAL A N   
732  C CA  . VAL A 92  ? 0.2380 0.2743 0.2060 0.0234  0.0143  0.0104  116  VAL A CA  
733  C C   . VAL A 92  ? 0.2514 0.2834 0.2197 0.0165  0.0114  0.0099  116  VAL A C   
734  O O   . VAL A 92  ? 0.2685 0.2906 0.2344 0.0145  0.0088  0.0068  116  VAL A O   
735  C CB  . VAL A 92  ? 0.2608 0.3053 0.2372 0.0224  0.0131  0.0133  116  VAL A CB  
736  C CG1 . VAL A 92  ? 0.2455 0.2826 0.2220 0.0175  0.0092  0.0112  116  VAL A CG1 
737  C CG2 . VAL A 92  ? 0.2262 0.2729 0.2026 0.0307  0.0157  0.0141  116  VAL A CG2 
738  N N   . ALA A 93  ? 0.2265 0.2660 0.1988 0.0129  0.0121  0.0135  117  ALA A N   
739  C CA  . ALA A 93  ? 0.2058 0.2401 0.1792 0.0072  0.0095  0.0135  117  ALA A CA  
740  C C   . ALA A 93  ? 0.2734 0.3005 0.2392 0.0084  0.0089  0.0120  117  ALA A C   
741  O O   . ALA A 93  ? 0.2812 0.3007 0.2472 0.0057  0.0060  0.0104  117  ALA A O   
742  C CB  . ALA A 93  ? 0.1813 0.2239 0.1618 0.0025  0.0099  0.0183  117  ALA A CB  
743  N N   . ILE A 94  ? 0.2747 0.3052 0.2341 0.0123  0.0117  0.0130  118  ILE A N   
744  C CA  . ILE A 94  ? 0.2893 0.3139 0.2400 0.0125  0.0102  0.0122  118  ILE A CA  
745  C C   . ILE A 94  ? 0.3117 0.3255 0.2536 0.0154  0.0079  0.0063  118  ILE A C   
746  O O   . ILE A 94  ? 0.3266 0.3343 0.2635 0.0136  0.0042  0.0051  118  ILE A O   
747  C CB  . ILE A 94  ? 0.3430 0.3751 0.2877 0.0149  0.0140  0.0160  118  ILE A CB  
748  C CG1 . ILE A 94  ? 0.4028 0.4362 0.3389 0.0222  0.0184  0.0133  118  ILE A CG1 
749  C CG2 . ILE A 94  ? 0.3356 0.3788 0.2907 0.0110  0.0162  0.0230  118  ILE A CG2 
750  C CD1 . ILE A 94  ? 0.5137 0.5544 0.4416 0.0254  0.0232  0.0168  118  ILE A CD1 
751  N N   . SER A 95  ? 0.2700 0.2815 0.2108 0.0194  0.0095  0.0033  119  SER A N   
752  C CA  . SER A 95  ? 0.2938 0.2935 0.2264 0.0219  0.0074  -0.0022 119  SER A CA  
753  C C   . SER A 95  ? 0.2690 0.2631 0.2084 0.0201  0.0051  -0.0036 119  SER A C   
754  O O   . SER A 95  ? 0.2902 0.2772 0.2303 0.0164  0.0011  -0.0051 119  SER A O   
755  C CB  . SER A 95  ? 0.3695 0.3683 0.2931 0.0295  0.0119  -0.0046 119  SER A CB  
756  O OG  . SER A 95  ? 0.4513 0.4360 0.3659 0.0317  0.0096  -0.0106 119  SER A OG  
757  N N   . ASN A 96  ? 0.2772 0.2758 0.2220 0.0224  0.0076  -0.0022 120  ASN A N   
758  C CA  . ASN A 96  ? 0.2593 0.2527 0.2086 0.0211  0.0058  -0.0028 120  ASN A CA  
759  C C   . ASN A 96  ? 0.2167 0.2100 0.1724 0.0149  0.0032  -0.0017 120  ASN A C   
760  O O   . ASN A 96  ? 0.2650 0.2516 0.2222 0.0130  0.0012  -0.0027 120  ASN A O   
761  C CB  . ASN A 96  ? 0.2513 0.2512 0.2054 0.0245  0.0083  -0.0004 120  ASN A CB  
762  C CG  . ASN A 96  ? 0.4003 0.4009 0.3498 0.0321  0.0119  -0.0010 120  ASN A CG  
763  O OD1 . ASN A 96  ? 0.4535 0.4580 0.3987 0.0345  0.0145  -0.0013 120  ASN A OD1 
764  N ND2 . ASN A 96  ? 0.4667 0.4634 0.4170 0.0365  0.0127  -0.0010 120  ASN A ND2 
765  N N   . TYR A 97  ? 0.2390 0.2396 0.1989 0.0118  0.0035  0.0008  121  TYR A N   
766  C CA  . TYR A 97  ? 0.2301 0.2296 0.1956 0.0071  0.0019  0.0015  121  TYR A CA  
767  C C   . TYR A 97  ? 0.2228 0.2212 0.1883 0.0048  0.0001  0.0024  121  TYR A C   
768  O O   . TYR A 97  ? 0.2267 0.2247 0.1978 0.0018  -0.0006 0.0036  121  TYR A O   
769  C CB  . TYR A 97  ? 0.2209 0.2267 0.1917 0.0049  0.0031  0.0032  121  TYR A CB  
770  C CG  . TYR A 97  ? 0.2382 0.2436 0.2091 0.0062  0.0034  0.0027  121  TYR A CG  
771  C CD1 . TYR A 97  ? 0.2636 0.2648 0.2359 0.0042  0.0031  0.0019  121  TYR A CD1 
772  C CD2 . TYR A 97  ? 0.2152 0.2247 0.1848 0.0101  0.0045  0.0037  121  TYR A CD2 
773  C CE1 . TYR A 97  ? 0.2655 0.2665 0.2367 0.0054  0.0034  0.0024  121  TYR A CE1 
774  C CE2 . TYR A 97  ? 0.2347 0.2438 0.2043 0.0117  0.0043  0.0043  121  TYR A CE2 
775  C CZ  . TYR A 97  ? 0.2500 0.2548 0.2198 0.0090  0.0036  0.0038  121  TYR A CZ  
776  O OH  . TYR A 97  ? 0.2510 0.2558 0.2199 0.0105  0.0036  0.0054  121  TYR A OH  
777  N N   . ALA A 98  ? 0.2564 0.2540 0.2149 0.0067  -0.0005 0.0019  122  ALA A N   
778  C CA  . ALA A 98  ? 0.2737 0.2697 0.2307 0.0047  -0.0035 0.0030  122  ALA A CA  
779  C C   . ALA A 98  ? 0.2482 0.2486 0.2118 0.0019  -0.0032 0.0072  122  ALA A C   
780  O O   . ALA A 98  ? 0.2307 0.2292 0.1988 -0.0003 -0.0057 0.0088  122  ALA A O   
781  C CB  . ALA A 98  ? 0.2616 0.2506 0.2201 0.0029  -0.0076 0.0011  122  ALA A CB  
782  N N   . ASN A 99  ? 0.2506 0.2571 0.2160 0.0019  -0.0001 0.0094  123  ASN A N   
783  C CA  . ASN A 99  ? 0.2210 0.2303 0.1926 -0.0013 0.0004  0.0134  123  ASN A CA  
784  C C   . ASN A 99  ? 0.2447 0.2499 0.2241 -0.0039 -0.0001 0.0126  123  ASN A C   
785  O O   . ASN A 99  ? 0.2367 0.2406 0.2212 -0.0063 -0.0002 0.0153  123  ASN A O   
786  C CB  . ASN A 99  ? 0.2723 0.2821 0.2411 -0.0017 -0.0012 0.0173  123  ASN A CB  
787  C CG  . ASN A 99  ? 0.3155 0.3301 0.2748 0.0010  0.0006  0.0185  123  ASN A CG  
788  O OD1 . ASN A 99  ? 0.2785 0.2996 0.2383 0.0020  0.0043  0.0197  123  ASN A OD1 
789  N ND2 . ASN A 99  ? 0.2653 0.2774 0.2157 0.0024  -0.0020 0.0181  123  ASN A ND2 
790  N N   . LEU A 100 ? 0.2522 0.2546 0.2320 -0.0032 0.0001  0.0090  124  LEU A N   
791  C CA  . LEU A 100 ? 0.2551 0.2540 0.2400 -0.0049 0.0009  0.0075  124  LEU A CA  
792  C C   . LEU A 100 ? 0.2577 0.2592 0.2436 -0.0072 0.0021  0.0072  124  LEU A C   
793  O O   . LEU A 100 ? 0.2770 0.2745 0.2653 -0.0092 0.0026  0.0056  124  LEU A O   
794  C CB  . LEU A 100 ? 0.2268 0.2232 0.2108 -0.0035 0.0011  0.0047  124  LEU A CB  
795  C CG  . LEU A 100 ? 0.2239 0.2174 0.2099 -0.0029 -0.0007 0.0052  124  LEU A CG  
796  C CD1 . LEU A 100 ? 0.2441 0.2354 0.2287 -0.0020 -0.0008 0.0033  124  LEU A CD1 
797  C CD2 . LEU A 100 ? 0.2518 0.2435 0.2454 -0.0037 -0.0002 0.0067  124  LEU A CD2 
798  N N   . THR A 101 ? 0.2390 0.2472 0.2230 -0.0068 0.0024  0.0086  125  THR A N   
799  C CA  . THR A 101 ? 0.2314 0.2446 0.2179 -0.0098 0.0024  0.0096  125  THR A CA  
800  C C   . THR A 101 ? 0.2659 0.2867 0.2539 -0.0102 0.0033  0.0143  125  THR A C   
801  O O   . THR A 101 ? 0.2545 0.2757 0.2392 -0.0075 0.0040  0.0160  125  THR A O   
802  C CB  . THR A 101 ? 0.2627 0.2800 0.2475 -0.0086 0.0022  0.0078  125  THR A CB  
803  O OG1 . THR A 101 ? 0.2668 0.2877 0.2544 -0.0130 0.0007  0.0081  125  THR A OG1 
804  C CG2 . THR A 101 ? 0.2431 0.2674 0.2259 -0.0041 0.0035  0.0095  125  THR A CG2 
805  N N   . THR A 102 ? 0.2420 0.2689 0.2346 -0.0139 0.0030  0.0167  126  THR A N   
806  C CA  . THR A 102 ? 0.2370 0.2731 0.2328 -0.0147 0.0046  0.0224  126  THR A CA  
807  C C   . THR A 102 ? 0.2599 0.3083 0.2589 -0.0139 0.0054  0.0243  126  THR A C   
808  O O   . THR A 102 ? 0.2390 0.2885 0.2395 -0.0152 0.0033  0.0219  126  THR A O   
809  C CB  . THR A 102 ? 0.2882 0.3221 0.2903 -0.0212 0.0034  0.0259  126  THR A CB  
810  O OG1 . THR A 102 ? 0.2668 0.3005 0.2731 -0.0264 0.0008  0.0240  126  THR A OG1 
811  C CG2 . THR A 102 ? 0.3152 0.3368 0.3159 -0.0213 0.0027  0.0249  126  THR A CG2 
812  N N   . MET A 103 ? 0.2278 0.2863 0.2279 -0.0114 0.0087  0.0291  127  MET A N   
813  C CA  . MET A 103 ? 0.2311 0.3036 0.2368 -0.0098 0.0102  0.0321  127  MET A CA  
814  C C   . MET A 103 ? 0.2563 0.3351 0.2722 -0.0177 0.0068  0.0350  127  MET A C   
815  O O   . MET A 103 ? 0.2779 0.3652 0.2985 -0.0179 0.0050  0.0354  127  MET A O   
816  C CB  . MET A 103 ? 0.2720 0.3548 0.2766 -0.0045 0.0157  0.0368  127  MET A CB  
817  C CG  . MET A 103 ? 0.3440 0.4305 0.3507 -0.0079 0.0178  0.0429  127  MET A CG  
818  S SD  . MET A 103 ? 0.6212 0.7241 0.6271 -0.0005 0.0258  0.0487  127  MET A SD  
819  C CE  . MET A 103 ? 0.7679 0.8897 0.7921 -0.0058 0.0255  0.0560  127  MET A CE  
820  N N   . GLU A 104 ? 0.2454 0.3194 0.2648 -0.0244 0.0053  0.0371  128  GLU A N   
821  C CA  . GLU A 104 ? 0.2767 0.3547 0.3053 -0.0331 0.0013  0.0393  128  GLU A CA  
822  C C   . GLU A 104 ? 0.2471 0.3174 0.2725 -0.0356 -0.0037 0.0325  128  GLU A C   
823  O O   . GLU A 104 ? 0.2493 0.3274 0.2803 -0.0404 -0.0076 0.0334  128  GLU A O   
824  C CB  . GLU A 104 ? 0.3153 0.3862 0.3476 -0.0397 0.0006  0.0425  128  GLU A CB  
825  C CG  . GLU A 104 ? 0.4101 0.4914 0.4467 -0.0389 0.0052  0.0513  128  GLU A CG  
826  C CD  . GLU A 104 ? 0.5102 0.5865 0.5366 -0.0314 0.0094  0.0509  128  GLU A CD  
827  O OE1 . GLU A 104 ? 0.4005 0.4656 0.4179 -0.0270 0.0084  0.0441  128  GLU A OE1 
828  O OE2 . GLU A 104 ? 0.5237 0.6083 0.5511 -0.0303 0.0135  0.0580  128  GLU A OE2 
829  N N   . SER A 105 ? 0.2512 0.3072 0.2674 -0.0325 -0.0035 0.0263  129  SER A N   
830  C CA  . SER A 105 ? 0.2524 0.3001 0.2634 -0.0342 -0.0070 0.0198  129  SER A CA  
831  C C   . SER A 105 ? 0.2382 0.2955 0.2480 -0.0302 -0.0078 0.0196  129  SER A C   
832  O O   . SER A 105 ? 0.2450 0.3048 0.2546 -0.0339 -0.0120 0.0179  129  SER A O   
833  C CB  . SER A 105 ? 0.2647 0.2972 0.2679 -0.0308 -0.0053 0.0146  129  SER A CB  
834  O OG  . SER A 105 ? 0.2503 0.2767 0.2473 -0.0309 -0.0072 0.0089  129  SER A OG  
835  N N   . LEU A 106 ? 0.2194 0.2815 0.2277 -0.0226 -0.0039 0.0213  130  LEU A N   
836  C CA  . LEU A 106 ? 0.2114 0.2818 0.2194 -0.0175 -0.0039 0.0220  130  LEU A CA  
837  C C   . LEU A 106 ? 0.2686 0.3558 0.2867 -0.0203 -0.0062 0.0275  130  LEU A C   
838  O O   . LEU A 106 ? 0.2343 0.3272 0.2533 -0.0210 -0.0099 0.0277  130  LEU A O   
839  C CB  . LEU A 106 ? 0.2199 0.2908 0.2248 -0.0090 0.0010  0.0228  130  LEU A CB  
840  C CG  . LEU A 106 ? 0.2587 0.3152 0.2545 -0.0055 0.0023  0.0178  130  LEU A CG  
841  C CD1 . LEU A 106 ? 0.2578 0.3152 0.2503 0.0018  0.0063  0.0185  130  LEU A CD1 
842  C CD2 . LEU A 106 ? 0.2428 0.2942 0.2343 -0.0046 0.0000  0.0146  130  LEU A CD2 
843  N N   . GLN A 107 ? 0.2563 0.3528 0.2826 -0.0223 -0.0041 0.0330  131  GLN A N   
844  C CA  . GLN A 107 ? 0.2521 0.3671 0.2908 -0.0255 -0.0061 0.0395  131  GLN A CA  
845  C C   . GLN A 107 ? 0.2508 0.3653 0.2923 -0.0355 -0.0140 0.0381  131  GLN A C   
846  O O   . GLN A 107 ? 0.2734 0.4013 0.3219 -0.0375 -0.0182 0.0413  131  GLN A O   
847  C CB  . GLN A 107 ? 0.3254 0.4503 0.3729 -0.0271 -0.0020 0.0464  131  GLN A CB  
848  C CG  . GLN A 107 ? 0.4016 0.5321 0.4471 -0.0170 0.0057  0.0490  131  GLN A CG  
849  C CD  . GLN A 107 ? 0.4612 0.6141 0.5205 -0.0159 0.0092  0.0582  131  GLN A CD  
850  O OE1 . GLN A 107 ? 0.4980 0.6563 0.5588 -0.0138 0.0152  0.0627  131  GLN A OE1 
851  N NE2 . GLN A 107 ? 0.5544 0.7214 0.6241 -0.0172 0.0056  0.0616  131  GLN A NE2 
852  N N   . ALA A 108 ? 0.2384 0.3376 0.2746 -0.0419 -0.0162 0.0334  132  ALA A N   
853  C CA  . ALA A 108 ? 0.2540 0.3502 0.2912 -0.0520 -0.0237 0.0310  132  ALA A CA  
854  C C   . ALA A 108 ? 0.2730 0.3659 0.3011 -0.0513 -0.0283 0.0258  132  ALA A C   
855  O O   . ALA A 108 ? 0.3027 0.4018 0.3332 -0.0582 -0.0354 0.0260  132  ALA A O   
856  C CB  . ALA A 108 ? 0.2864 0.3646 0.3195 -0.0578 -0.0241 0.0268  132  ALA A CB  
857  N N   . ARG A 109 ? 0.2170 0.3013 0.2348 -0.0433 -0.0246 0.0217  133  ARG A N   
858  C CA  . ARG A 109 ? 0.1911 0.2695 0.1982 -0.0428 -0.0279 0.0167  133  ARG A CA  
859  C C   . ARG A 109 ? 0.3025 0.3928 0.3107 -0.0355 -0.0276 0.0207  133  ARG A C   
860  O O   . ARG A 109 ? 0.2990 0.3859 0.2983 -0.0341 -0.0300 0.0181  133  ARG A O   
861  C CB  . ARG A 109 ? 0.2146 0.2740 0.2097 -0.0398 -0.0241 0.0098  133  ARG A CB  
862  C CG  . ARG A 109 ? 0.2609 0.3185 0.2547 -0.0305 -0.0177 0.0109  133  ARG A CG  
863  C CD  . ARG A 109 ? 0.2848 0.3261 0.2722 -0.0292 -0.0141 0.0059  133  ARG A CD  
864  N NE  . ARG A 109 ? 0.2844 0.3158 0.2614 -0.0298 -0.0150 0.0003  133  ARG A NE  
865  C CZ  . ARG A 109 ? 0.3266 0.3479 0.2985 -0.0351 -0.0168 -0.0048 133  ARG A CZ  
866  N NH1 . ARG A 109 ? 0.3707 0.3837 0.3316 -0.0344 -0.0164 -0.0099 133  ARG A NH1 
867  N NH2 . ARG A 109 ? 0.2672 0.2861 0.2447 -0.0408 -0.0186 -0.0046 133  ARG A NH2 
868  N N   . ASN A 110 ? 0.1978 0.3018 0.2166 -0.0304 -0.0243 0.0273  134  ASN A N   
869  C CA  . ASN A 110 ? 0.1870 0.3028 0.2090 -0.0229 -0.0238 0.0320  134  ASN A CA  
870  C C   . ASN A 110 ? 0.2293 0.3670 0.2669 -0.0249 -0.0265 0.0401  134  ASN A C   
871  O O   . ASN A 110 ? 0.2468 0.3912 0.2938 -0.0284 -0.0248 0.0433  134  ASN A O   
872  C CB  . ASN A 110 ? 0.1848 0.2954 0.2043 -0.0127 -0.0161 0.0319  134  ASN A CB  
873  C CG  . ASN A 110 ? 0.2409 0.3323 0.2471 -0.0107 -0.0141 0.0252  134  ASN A CG  
874  O OD1 . ASN A 110 ? 0.2463 0.3267 0.2488 -0.0117 -0.0111 0.0215  134  ASN A OD1 
875  N ND2 . ASN A 110 ? 0.1687 0.2571 0.1686 -0.0083 -0.0160 0.0244  134  ASN A ND2 
876  N N   . PRO A 111 ? 0.1854 0.3355 0.2267 -0.0227 -0.0307 0.0444  135  PRO A N   
877  C CA  . PRO A 111 ? 0.1745 0.3476 0.2325 -0.0261 -0.0349 0.0527  135  PRO A CA  
878  C C   . PRO A 111 ? 0.2675 0.4566 0.3390 -0.0162 -0.0279 0.0605  135  PRO A C   
879  O O   . PRO A 111 ? 0.2194 0.4298 0.3074 -0.0185 -0.0300 0.0685  135  PRO A O   
880  C CB  . PRO A 111 ? 0.2349 0.4135 0.2896 -0.0277 -0.0433 0.0538  135  PRO A CB  
881  C CG  . PRO A 111 ? 0.2644 0.4298 0.3064 -0.0180 -0.0388 0.0507  135  PRO A CG  
882  C CD  . PRO A 111 ? 0.2824 0.4264 0.3132 -0.0185 -0.0330 0.0424  135  PRO A CD  
883  N N   . PHE A 112 ? 0.2174 0.3967 0.2821 -0.0056 -0.0197 0.0583  136  PHE A N   
884  C CA  . PHE A 112 ? 0.2524 0.4446 0.3271 0.0052  -0.0124 0.0644  136  PHE A CA  
885  C C   . PHE A 112 ? 0.2326 0.4315 0.3149 0.0037  -0.0065 0.0671  136  PHE A C   
886  O O   . PHE A 112 ? 0.2420 0.4268 0.3156 -0.0001 -0.0043 0.0619  136  PHE A O   
887  C CB  . PHE A 112 ? 0.2664 0.4430 0.3294 0.0167  -0.0063 0.0601  136  PHE A CB  
888  C CG  . PHE A 112 ? 0.2261 0.3915 0.2789 0.0168  -0.0113 0.0569  136  PHE A CG  
889  C CD1 . PHE A 112 ? 0.2208 0.3979 0.2797 0.0206  -0.0154 0.0630  136  PHE A CD1 
890  C CD2 . PHE A 112 ? 0.2438 0.3881 0.2814 0.0135  -0.0117 0.0488  136  PHE A CD2 
891  C CE1 . PHE A 112 ? 0.2543 0.4219 0.3031 0.0205  -0.0199 0.0611  136  PHE A CE1 
892  C CE2 . PHE A 112 ? 0.2518 0.3871 0.2801 0.0135  -0.0156 0.0468  136  PHE A CE2 
893  C CZ  . PHE A 112 ? 0.2256 0.3722 0.2587 0.0169  -0.0196 0.0530  136  PHE A CZ  
894  N N   . PRO A 113 ? 0.2747 0.4963 0.3737 0.0070  -0.0034 0.0760  137  PRO A N   
895  C CA  . PRO A 113 ? 0.2481 0.4772 0.3537 0.0065  0.0036  0.0796  137  PRO A CA  
896  C C   . PRO A 113 ? 0.2552 0.4683 0.3464 0.0163  0.0128  0.0740  137  PRO A C   
897  O O   . PRO A 113 ? 0.2595 0.4647 0.3434 0.0264  0.0155  0.0709  137  PRO A O   
898  C CB  . PRO A 113 ? 0.2348 0.4923 0.3608 0.0120  0.0067  0.0907  137  PRO A CB  
899  C CG  . PRO A 113 ? 0.3445 0.6106 0.4766 0.0118  -0.0015 0.0935  137  PRO A CG  
900  C CD  . PRO A 113 ? 0.2926 0.5341 0.4051 0.0132  -0.0050 0.0839  137  PRO A CD  
901  N N   . ALA A 114 ? 0.2219 0.4297 0.3089 0.0132  0.0171  0.0729  138  ALA A N   
902  C CA  . ALA A 114 ? 0.2520 0.4439 0.3235 0.0215  0.0244  0.0671  138  ALA A CA  
903  C C   . ALA A 114 ? 0.2727 0.4700 0.3438 0.0360  0.0326  0.0685  138  ALA A C   
904  O O   . ALA A 114 ? 0.2544 0.4345 0.3111 0.0435  0.0354  0.0615  138  ALA A O   
905  C CB  . ALA A 114 ? 0.2678 0.4583 0.3370 0.0168  0.0281  0.0684  138  ALA A CB  
906  N N   . THR A 115 ? 0.2888 0.5096 0.3761 0.0402  0.0367  0.0775  139  THR A N   
907  C CA  . THR A 115 ? 0.2751 0.5010 0.3621 0.0553  0.0462  0.0788  139  THR A CA  
908  C C   . THR A 115 ? 0.2724 0.5003 0.3645 0.0630  0.0438  0.0797  139  THR A C   
909  O O   . THR A 115 ? 0.3091 0.5419 0.4034 0.0763  0.0515  0.0816  139  THR A O   
910  C CB  . THR A 115 ? 0.2818 0.5325 0.3834 0.0587  0.0545  0.0886  139  THR A CB  
911  O OG1 . THR A 115 ? 0.2862 0.5607 0.4104 0.0520  0.0489  0.0983  139  THR A OG1 
912  C CG2 . THR A 115 ? 0.2919 0.5389 0.3863 0.0522  0.0579  0.0883  139  THR A CG2 
913  N N   . ASN A 116 ? 0.2693 0.4928 0.3623 0.0552  0.0335  0.0785  140  ASN A N   
914  C CA  . ASN A 116 ? 0.2621 0.4821 0.3553 0.0624  0.0307  0.0784  140  ASN A CA  
915  C C   . ASN A 116 ? 0.2395 0.4413 0.3211 0.0549  0.0217  0.0721  140  ASN A C   
916  O O   . ASN A 116 ? 0.2537 0.4631 0.3418 0.0492  0.0134  0.0754  140  ASN A O   
917  C CB  . ASN A 116 ? 0.3095 0.5563 0.4240 0.0655  0.0289  0.0894  140  ASN A CB  
918  C CG  . ASN A 116 ? 0.3255 0.5680 0.4397 0.0767  0.0285  0.0904  140  ASN A CG  
919  O OD1 . ASN A 116 ? 0.3607 0.5803 0.4593 0.0836  0.0317  0.0830  140  ASN A OD1 
920  N ND2 . ASN A 116 ? 0.3346 0.5987 0.4665 0.0781  0.0242  0.0999  140  ASN A ND2 
921  N N   . ILE A 117 ? 0.2194 0.3976 0.2836 0.0551  0.0234  0.0631  141  ILE A N   
922  C CA  . ILE A 117 ? 0.2457 0.4056 0.2985 0.0513  0.0173  0.0573  141  ILE A CA  
923  C C   . ILE A 117 ? 0.3172 0.4706 0.3678 0.0629  0.0196  0.0578  141  ILE A C   
924  O O   . ILE A 117 ? 0.3249 0.4678 0.3687 0.0720  0.0266  0.0543  141  ILE A O   
925  C CB  . ILE A 117 ? 0.2349 0.3738 0.2722 0.0474  0.0184  0.0486  141  ILE A CB  
926  C CG1 . ILE A 117 ? 0.2348 0.3795 0.2749 0.0374  0.0173  0.0490  141  ILE A CG1 
927  C CG2 . ILE A 117 ? 0.2188 0.3408 0.2461 0.0431  0.0127  0.0436  141  ILE A CG2 
928  C CD1 . ILE A 117 ? 0.2810 0.4076 0.3077 0.0347  0.0190  0.0420  141  ILE A CD1 
929  N N   . PRO A 118 ? 0.2469 0.4057 0.3025 0.0625  0.0135  0.0621  142  PRO A N   
930  C CA  . PRO A 118 ? 0.2674 0.4209 0.3231 0.0739  0.0155  0.0644  142  PRO A CA  
931  C C   . PRO A 118 ? 0.3090 0.4353 0.3486 0.0762  0.0166  0.0569  142  PRO A C   
932  O O   . PRO A 118 ? 0.3080 0.4215 0.3372 0.0674  0.0132  0.0511  142  PRO A O   
933  C CB  . PRO A 118 ? 0.3404 0.5072 0.4043 0.0703  0.0070  0.0717  142  PRO A CB  
934  C CG  . PRO A 118 ? 0.2968 0.4729 0.3627 0.0563  0.0003  0.0713  142  PRO A CG  
935  C CD  . PRO A 118 ? 0.2539 0.4208 0.3129 0.0511  0.0042  0.0644  142  PRO A CD  
936  N N   . LEU A 119 ? 0.3112 0.4285 0.3494 0.0881  0.0215  0.0572  143  LEU A N   
937  C CA  . LEU A 119 ? 0.3374 0.4291 0.3621 0.0898  0.0219  0.0510  143  LEU A CA  
938  C C   . LEU A 119 ? 0.3487 0.4364 0.3709 0.0832  0.0144  0.0533  143  LEU A C   
939  O O   . LEU A 119 ? 0.3909 0.4930 0.4218 0.0836  0.0102  0.0610  143  LEU A O   
940  C CB  . LEU A 119 ? 0.4290 0.5115 0.4540 0.1041  0.0280  0.0517  143  LEU A CB  
941  C CG  . LEU A 119 ? 0.4832 0.5497 0.4978 0.1105  0.0354  0.0435  143  LEU A CG  
942  C CD1 . LEU A 119 ? 0.4740 0.5457 0.4843 0.1041  0.0374  0.0388  143  LEU A CD1 
943  C CD2 . LEU A 119 ? 0.4691 0.5380 0.4895 0.1260  0.0429  0.0465  143  LEU A CD2 
944  N N   . SER A 120 ? 0.4475 0.5172 0.4580 0.0769  0.0127  0.0471  144  SER A N   
945  C CA  . SER A 120 ? 0.5520 0.6179 0.5586 0.0704  0.0068  0.0491  144  SER A CA  
946  C C   . SER A 120 ? 0.4431 0.5240 0.4519 0.0603  0.0010  0.0508  144  SER A C   
947  O O   . SER A 120 ? 0.4038 0.4826 0.4077 0.0552  -0.0036 0.0522  144  SER A O   
948  C CB  . SER A 120 ? 0.6113 0.6751 0.6210 0.0782  0.0059  0.0561  144  SER A CB  
949  O OG  . SER A 120 ? 0.6480 0.6902 0.6515 0.0840  0.0097  0.0528  144  SER A OG  
950  N N   . ALA A 121 ? 0.3284 0.4232 0.3434 0.0570  0.0012  0.0505  145  ALA A N   
951  C CA  . ALA A 121 ? 0.2727 0.3742 0.2865 0.0457  -0.0040 0.0489  145  ALA A CA  
952  C C   . ALA A 121 ? 0.2797 0.3633 0.2813 0.0395  -0.0038 0.0415  145  ALA A C   
953  O O   . ALA A 121 ? 0.2764 0.3457 0.2729 0.0427  0.0005  0.0371  145  ALA A O   
954  C CB  . ALA A 121 ? 0.2667 0.3820 0.2888 0.0425  -0.0029 0.0492  145  ALA A CB  
955  N N   . THR A 122 ? 0.2415 0.3261 0.2386 0.0309  -0.0085 0.0401  146  THR A N   
956  C CA  . THR A 122 ? 0.2312 0.3020 0.2189 0.0248  -0.0078 0.0334  146  THR A CA  
957  C C   . THR A 122 ? 0.2517 0.3277 0.2418 0.0176  -0.0090 0.0303  146  THR A C   
958  O O   . THR A 122 ? 0.2676 0.3561 0.2622 0.0132  -0.0134 0.0328  146  THR A O   
959  C CB  . THR A 122 ? 0.3028 0.3695 0.2823 0.0209  -0.0112 0.0336  146  THR A CB  
960  O OG1 . THR A 122 ? 0.3097 0.3721 0.2879 0.0273  -0.0104 0.0381  146  THR A OG1 
961  C CG2 . THR A 122 ? 0.3043 0.3578 0.2758 0.0161  -0.0093 0.0273  146  THR A CG2 
962  N N   . LEU A 123 ? 0.2233 0.2895 0.2106 0.0161  -0.0057 0.0253  147  LEU A N   
963  C CA  . LEU A 123 ? 0.2325 0.3002 0.2210 0.0090  -0.0067 0.0224  147  LEU A CA  
964  C C   . LEU A 123 ? 0.2571 0.3138 0.2374 0.0034  -0.0079 0.0176  147  LEU A C   
965  O O   . LEU A 123 ? 0.2553 0.3011 0.2300 0.0054  -0.0057 0.0153  147  LEU A O   
966  C CB  . LEU A 123 ? 0.2188 0.2838 0.2094 0.0110  -0.0024 0.0210  147  LEU A CB  
967  C CG  . LEU A 123 ? 0.2527 0.3280 0.2501 0.0176  0.0007  0.0251  147  LEU A CG  
968  C CD1 . LEU A 123 ? 0.2291 0.3015 0.2257 0.0184  0.0048  0.0233  147  LEU A CD1 
969  C CD2 . LEU A 123 ? 0.2056 0.2996 0.2134 0.0159  -0.0022 0.0311  147  LEU A CD2 
970  N N   . ASN A 124 ? 0.2162 0.2757 0.1966 -0.0036 -0.0112 0.0159  148  ASN A N   
971  C CA  . ASN A 124 ? 0.2596 0.3082 0.2331 -0.0086 -0.0113 0.0105  148  ASN A CA  
972  C C   . ASN A 124 ? 0.2475 0.2905 0.2243 -0.0096 -0.0082 0.0084  148  ASN A C   
973  O O   . ASN A 124 ? 0.2352 0.2845 0.2186 -0.0121 -0.0089 0.0103  148  ASN A O   
974  C CB  . ASN A 124 ? 0.2534 0.3064 0.2249 -0.0157 -0.0168 0.0094  148  ASN A CB  
975  C CG  . ASN A 124 ? 0.3438 0.3842 0.3062 -0.0200 -0.0165 0.0030  148  ASN A CG  
976  O OD1 . ASN A 124 ? 0.3206 0.3527 0.2842 -0.0207 -0.0135 0.0001  148  ASN A OD1 
977  N ND2 . ASN A 124 ? 0.3971 0.4361 0.3498 -0.0223 -0.0196 0.0010  148  ASN A ND2 
978  N N   . VAL A 125 ? 0.2343 0.2663 0.2073 -0.0077 -0.0050 0.0056  149  VAL A N   
979  C CA  . VAL A 125 ? 0.2270 0.2543 0.2029 -0.0075 -0.0025 0.0047  149  VAL A CA  
980  C C   . VAL A 125 ? 0.2380 0.2554 0.2111 -0.0108 -0.0018 0.0007  149  VAL A C   
981  O O   . VAL A 125 ? 0.2321 0.2431 0.2012 -0.0092 0.0000  -0.0012 149  VAL A O   
982  C CB  . VAL A 125 ? 0.2515 0.2750 0.2268 -0.0019 0.0001  0.0053  149  VAL A CB  
983  C CG1 . VAL A 125 ? 0.2851 0.3042 0.2620 -0.0021 0.0016  0.0045  149  VAL A CG1 
984  C CG2 . VAL A 125 ? 0.2315 0.2625 0.2086 0.0030  0.0004  0.0085  149  VAL A CG2 
985  N N   . LEU A 126 ? 0.2356 0.2517 0.2116 -0.0151 -0.0028 0.0000  150  LEU A N   
986  C CA  . LEU A 126 ? 0.2080 0.2135 0.1818 -0.0175 -0.0017 -0.0038 150  LEU A CA  
987  C C   . LEU A 126 ? 0.2423 0.2429 0.2200 -0.0151 0.0009  -0.0029 150  LEU A C   
988  O O   . LEU A 126 ? 0.2395 0.2437 0.2216 -0.0151 0.0007  0.0002  150  LEU A O   
989  C CB  . LEU A 126 ? 0.2326 0.2367 0.2076 -0.0237 -0.0046 -0.0051 150  LEU A CB  
990  C CG  . LEU A 126 ? 0.2841 0.2752 0.2574 -0.0258 -0.0033 -0.0093 150  LEU A CG  
991  C CD1 . LEU A 126 ? 0.2605 0.2443 0.2249 -0.0239 -0.0012 -0.0144 150  LEU A CD1 
992  C CD2 . LEU A 126 ? 0.2684 0.2572 0.2436 -0.0329 -0.0071 -0.0101 150  LEU A CD2 
993  N N   . VAL A 127 ? 0.2333 0.2267 0.2093 -0.0131 0.0034  -0.0052 151  VAL A N   
994  C CA  . VAL A 127 ? 0.2140 0.2033 0.1949 -0.0112 0.0051  -0.0039 151  VAL A CA  
995  C C   . VAL A 127 ? 0.2584 0.2390 0.2390 -0.0118 0.0072  -0.0071 151  VAL A C   
996  O O   . VAL A 127 ? 0.2585 0.2360 0.2339 -0.0111 0.0092  -0.0104 151  VAL A O   
997  C CB  . VAL A 127 ? 0.2356 0.2260 0.2172 -0.0076 0.0062  -0.0026 151  VAL A CB  
998  C CG1 . VAL A 127 ? 0.2585 0.2459 0.2461 -0.0063 0.0069  -0.0010 151  VAL A CG1 
999  C CG2 . VAL A 127 ? 0.2281 0.2247 0.2083 -0.0062 0.0044  -0.0005 151  VAL A CG2 
1000 N N   . ASN A 128 ? 0.2254 0.2017 0.2110 -0.0128 0.0072  -0.0059 152  ASN A N   
1001 C CA  . ASN A 128 ? 0.2302 0.1962 0.2160 -0.0126 0.0095  -0.0091 152  ASN A CA  
1002 C C   . ASN A 128 ? 0.2645 0.2285 0.2549 -0.0078 0.0132  -0.0082 152  ASN A C   
1003 O O   . ASN A 128 ? 0.2664 0.2365 0.2613 -0.0059 0.0125  -0.0044 152  ASN A O   
1004 C CB  . ASN A 128 ? 0.2520 0.2127 0.2419 -0.0159 0.0078  -0.0075 152  ASN A CB  
1005 C CG  . ASN A 128 ? 0.2962 0.2581 0.2827 -0.0218 0.0044  -0.0089 152  ASN A CG  
1006 O OD1 . ASN A 128 ? 0.2865 0.2502 0.2660 -0.0233 0.0033  -0.0126 152  ASN A OD1 
1007 N ND2 . ASN A 128 ? 0.3181 0.2795 0.3098 -0.0255 0.0023  -0.0052 152  ASN A ND2 
1008 N N   . CYS A 129 ? 0.3197 0.2751 0.3091 -0.0058 0.0170  -0.0118 153  CYS A N   
1009 C CA  . CYS A 129 ? 0.2947 0.2497 0.2910 -0.0007 0.0212  -0.0101 153  CYS A CA  
1010 C C   . CYS A 129 ? 0.2719 0.2156 0.2702 0.0019  0.0251  -0.0128 153  CYS A C   
1011 O O   . CYS A 129 ? 0.3040 0.2381 0.2973 -0.0010 0.0241  -0.0165 153  CYS A O   
1012 C CB  . CYS A 129 ? 0.3104 0.2700 0.3029 0.0015  0.0246  -0.0114 153  CYS A CB  
1013 S SG  . CYS A 129 ? 0.3448 0.2982 0.3218 0.0000  0.0268  -0.0188 153  CYS A SG  
1014 N N   . SER A 130 ? 0.2594 0.2039 0.2659 0.0074  0.0296  -0.0106 154  SER A N   
1015 C CA  . SER A 130 ? 0.3074 0.2407 0.3166 0.0117  0.0346  -0.0130 154  SER A CA  
1016 C C   . SER A 130 ? 0.3258 0.2617 0.3372 0.0179  0.0421  -0.0138 154  SER A C   
1017 O O   . SER A 130 ? 0.2790 0.2268 0.2967 0.0188  0.0422  -0.0092 154  SER A O   
1018 C CB  . SER A 130 ? 0.3696 0.3021 0.3917 0.0136  0.0327  -0.0066 154  SER A CB  
1019 O OG  . SER A 130 ? 0.3579 0.2800 0.3847 0.0195  0.0384  -0.0081 154  SER A OG  
1020 N N   . CYS A 131 ? 0.3722 0.2966 0.3783 0.0220  0.0484  -0.0196 155  CYS A N   
1021 C CA  . CYS A 131 ? 0.3825 0.3093 0.3915 0.0292  0.0573  -0.0199 155  CYS A CA  
1022 C C   . CYS A 131 ? 0.3994 0.3217 0.4223 0.0365  0.0620  -0.0169 155  CYS A C   
1023 O O   . CYS A 131 ? 0.4267 0.3503 0.4541 0.0438  0.0706  -0.0169 155  CYS A O   
1024 C CB  . CYS A 131 ? 0.3536 0.2706 0.3443 0.0301  0.0626  -0.0292 155  CYS A CB  
1025 S SG  . CYS A 131 ? 0.4529 0.3778 0.4286 0.0232  0.0581  -0.0311 155  CYS A SG  
1026 N N   . GLY A 132 ? 0.4191 0.3367 0.4492 0.0348  0.0566  -0.0136 156  GLY A N   
1027 C CA  . GLY A 132 ? 0.3972 0.3098 0.4410 0.0417  0.0600  -0.0096 156  GLY A CA  
1028 C C   . GLY A 132 ? 0.4325 0.3236 0.4694 0.0438  0.0627  -0.0163 156  GLY A C   
1029 O O   . GLY A 132 ? 0.4365 0.3161 0.4577 0.0383  0.0605  -0.0242 156  GLY A O   
1030 N N   . ASP A 133 ? 0.3962 0.2813 0.4456 0.0518  0.0673  -0.0130 157  ASP A N   
1031 C CA  . ASP A 133 ? 0.4463 0.3087 0.4916 0.0543  0.0696  -0.0182 157  ASP A CA  
1032 C C   . ASP A 133 ? 0.4377 0.2975 0.4968 0.0668  0.0788  -0.0153 157  ASP A C   
1033 O O   . ASP A 133 ? 0.4425 0.3130 0.5206 0.0707  0.0773  -0.0046 157  ASP A O   
1034 C CB  . ASP A 133 ? 0.5024 0.3602 0.5525 0.0480  0.0607  -0.0126 157  ASP A CB  
1035 C CG  . ASP A 133 ? 0.6069 0.4392 0.6531 0.0491  0.0620  -0.0176 157  ASP A CG  
1036 O OD1 . ASP A 133 ? 0.6290 0.4469 0.6712 0.0568  0.0705  -0.0247 157  ASP A OD1 
1037 O OD2 . ASP A 133 ? 0.6036 0.4300 0.6505 0.0421  0.0549  -0.0143 157  ASP A OD2 
1038 N N   . GLU A 134 ? 0.4801 0.3270 0.5289 0.0732  0.0883  -0.0247 158  GLU A N   
1039 C CA  . GLU A 134 ? 0.5582 0.4028 0.6188 0.0868  0.0994  -0.0231 158  GLU A CA  
1040 C C   . GLU A 134 ? 0.6051 0.4376 0.6802 0.0922  0.0987  -0.0175 158  GLU A C   
1041 O O   . GLU A 134 ? 0.5644 0.4036 0.6582 0.1029  0.1047  -0.0102 158  GLU A O   
1042 C CB  . GLU A 134 ? 0.6921 0.5202 0.7337 0.0922  0.1098  -0.0364 158  GLU A CB  
1043 C CG  . GLU A 134 ? 0.8575 0.6893 0.9094 0.1068  0.1237  -0.0350 158  GLU A CG  
1044 C CD  . GLU A 134 ? 0.9756 0.7935 1.0048 0.1116  0.1342  -0.0486 158  GLU A CD  
1045 O OE1 . GLU A 134 ? 1.0080 0.8077 1.0138 0.1041  0.1300  -0.0600 158  GLU A OE1 
1046 O OE2 . GLU A 134 ? 1.0162 0.8459 1.0502 0.1202  0.1435  -0.0467 158  GLU A OE2 
1047 N N   . SER A 135 ? 0.5603 0.3757 0.6280 0.0849  0.0914  -0.0200 159  SER A N   
1048 C CA  . SER A 135 ? 0.6361 0.4377 0.7164 0.0892  0.0901  -0.0142 159  SER A CA  
1049 C C   . SER A 135 ? 0.5998 0.4217 0.7001 0.0874  0.0823  0.0014  159  SER A C   
1050 O O   . SER A 135 ? 0.5905 0.4061 0.7044 0.0918  0.0809  0.0095  159  SER A O   
1051 C CB  . SER A 135 ? 0.6593 0.4349 0.7251 0.0811  0.0850  -0.0218 159  SER A CB  
1052 O OG  . SER A 135 ? 0.6532 0.4378 0.7155 0.0678  0.0736  -0.0178 159  SER A OG  
1053 N N   . VAL A 136 ? 0.4939 0.3391 0.5948 0.0809  0.0768  0.0057  160  VAL A N   
1054 C CA  . VAL A 136 ? 0.4951 0.3598 0.6125 0.0793  0.0693  0.0194  160  VAL A CA  
1055 C C   . VAL A 136 ? 0.5175 0.4021 0.6515 0.0878  0.0745  0.0257  160  VAL A C   
1056 O O   . VAL A 136 ? 0.5162 0.4101 0.6698 0.0936  0.0731  0.0370  160  VAL A O   
1057 C CB  . VAL A 136 ? 0.4935 0.3711 0.6023 0.0669  0.0594  0.0208  160  VAL A CB  
1058 C CG1 . VAL A 136 ? 0.4295 0.3287 0.5537 0.0662  0.0524  0.0339  160  VAL A CG1 
1059 C CG2 . VAL A 136 ? 0.4821 0.3434 0.5784 0.0582  0.0538  0.0171  160  VAL A CG2 
1060 N N   . SER A 137 ? 0.4607 0.3525 0.5874 0.0883  0.0804  0.0192  161  SER A N   
1061 C CA  . SER A 137 ? 0.4496 0.3613 0.5926 0.0956  0.0862  0.0253  161  SER A CA  
1062 C C   . SER A 137 ? 0.4697 0.3844 0.6013 0.0968  0.0949  0.0168  161  SER A C   
1063 O O   . SER A 137 ? 0.4862 0.3985 0.5992 0.0882  0.0919  0.0095  161  SER A O   
1064 C CB  . SER A 137 ? 0.4109 0.3465 0.5667 0.0895  0.0761  0.0366  161  SER A CB  
1065 O OG  . SER A 137 ? 0.4671 0.4228 0.6412 0.0956  0.0808  0.0436  161  SER A OG  
1066 N N   . LYS A 138 ? 0.4257 0.3471 0.5693 0.1078  0.1059  0.0189  162  LYS A N   
1067 C CA  . LYS A 138 ? 0.4817 0.4103 0.6169 0.1093  0.1147  0.0135  162  LYS A CA  
1068 C C   . LYS A 138 ? 0.4417 0.3972 0.5880 0.1035  0.1101  0.0221  162  LYS A C   
1069 O O   . LYS A 138 ? 0.4459 0.4093 0.5856 0.1028  0.1159  0.0194  162  LYS A O   
1070 C CB  . LYS A 138 ? 0.5594 0.4850 0.7026 0.1242  0.1300  0.0124  162  LYS A CB  
1071 C CG  . LYS A 138 ? 0.7027 0.5993 0.8275 0.1292  0.1361  0.0001  162  LYS A CG  
1072 C CD  . LYS A 138 ? 0.8213 0.7200 0.9519 0.1402  0.1462  0.0003  162  LYS A CD  
1073 C CE  . LYS A 138 ? 0.8793 0.7997 1.0134 0.1428  0.1544  0.0031  162  LYS A CE  
1074 N NZ  . LYS A 138 ? 0.9288 0.8551 1.0730 0.1538  0.1642  0.0059  162  LYS A NZ  
1075 N N   . ASP A 139 ? 0.3752 0.3441 0.5380 0.0993  0.0997  0.0328  163  ASP A N   
1076 C CA  . ASP A 139 ? 0.3972 0.3912 0.5742 0.0948  0.0955  0.0418  163  ASP A CA  
1077 C C   . ASP A 139 ? 0.3625 0.3597 0.5242 0.0821  0.0866  0.0385  163  ASP A C   
1078 O O   . ASP A 139 ? 0.3751 0.3903 0.5454 0.0775  0.0835  0.0442  163  ASP A O   
1079 C CB  . ASP A 139 ? 0.3485 0.3568 0.5500 0.0960  0.0877  0.0548  163  ASP A CB  
1080 C CG  . ASP A 139 ? 0.5050 0.5176 0.7282 0.1097  0.0971  0.0613  163  ASP A CG  
1081 O OD1 . ASP A 139 ? 0.5122 0.5226 0.7348 0.1183  0.1108  0.0570  163  ASP A OD1 
1082 O OD2 . ASP A 139 ? 0.5276 0.5461 0.7683 0.1122  0.0909  0.0710  163  ASP A OD2 
1083 N N   . PHE A 140 ? 0.3447 0.3249 0.4850 0.0763  0.0824  0.0297  164  PHE A N   
1084 C CA  . PHE A 140 ? 0.3390 0.3224 0.4663 0.0650  0.0734  0.0275  164  PHE A CA  
1085 C C   . PHE A 140 ? 0.3007 0.2704 0.4036 0.0617  0.0763  0.0162  164  PHE A C   
1086 O O   . PHE A 140 ? 0.3598 0.3116 0.4506 0.0626  0.0776  0.0090  164  PHE A O   
1087 C CB  . PHE A 140 ? 0.3270 0.3089 0.4550 0.0589  0.0614  0.0313  164  PHE A CB  
1088 C CG  . PHE A 140 ? 0.2995 0.2940 0.4494 0.0617  0.0568  0.0427  164  PHE A CG  
1089 C CD1 . PHE A 140 ? 0.2670 0.2807 0.4295 0.0582  0.0517  0.0502  164  PHE A CD1 
1090 C CD2 . PHE A 140 ? 0.3726 0.3593 0.5309 0.0677  0.0572  0.0463  164  PHE A CD2 
1091 C CE1 . PHE A 140 ? 0.3001 0.3265 0.4826 0.0600  0.0461  0.0609  164  PHE A CE1 
1092 C CE2 . PHE A 140 ? 0.3501 0.3495 0.5287 0.0705  0.0522  0.0578  164  PHE A CE2 
1093 C CZ  . PHE A 140 ? 0.3038 0.3238 0.4946 0.0666  0.0464  0.0651  164  PHE A CZ  
1094 N N   . GLY A 141 ? 0.3252 0.3033 0.4213 0.0570  0.0763  0.0151  165  GLY A N   
1095 C CA  . GLY A 141 ? 0.3442 0.3122 0.4177 0.0536  0.0783  0.0057  165  GLY A CA  
1096 C C   . GLY A 141 ? 0.3166 0.2916 0.3828 0.0445  0.0704  0.0064  165  GLY A C   
1097 O O   . GLY A 141 ? 0.3786 0.3486 0.4277 0.0413  0.0712  0.0003  165  GLY A O   
1098 N N   . LEU A 142 ? 0.2854 0.2716 0.3640 0.0405  0.0626  0.0138  166  LEU A N   
1099 C CA  . LEU A 142 ? 0.2697 0.2606 0.3414 0.0325  0.0548  0.0142  166  LEU A CA  
1100 C C   . LEU A 142 ? 0.2842 0.2740 0.3580 0.0283  0.0449  0.0166  166  LEU A C   
1101 O O   . LEU A 142 ? 0.2820 0.2779 0.3705 0.0301  0.0421  0.0230  166  LEU A O   
1102 C CB  . LEU A 142 ? 0.2392 0.2450 0.3225 0.0310  0.0551  0.0208  166  LEU A CB  
1103 C CG  . LEU A 142 ? 0.2471 0.2569 0.3258 0.0232  0.0468  0.0221  166  LEU A CG  
1104 C CD1 . LEU A 142 ? 0.2581 0.2594 0.3168 0.0203  0.0467  0.0152  166  LEU A CD1 
1105 C CD2 . LEU A 142 ? 0.2778 0.3005 0.3693 0.0210  0.0469  0.0289  166  LEU A CD2 
1106 N N   . PHE A 143 ? 0.2440 0.2275 0.3036 0.0231  0.0398  0.0121  167  PHE A N   
1107 C CA  . PHE A 143 ? 0.2533 0.2348 0.3125 0.0198  0.0320  0.0140  167  PHE A CA  
1108 C C   . PHE A 143 ? 0.2724 0.2578 0.3241 0.0138  0.0253  0.0139  167  PHE A C   
1109 O O   . PHE A 143 ? 0.2744 0.2587 0.3159 0.0116  0.0263  0.0098  167  PHE A O   
1110 C CB  . PHE A 143 ? 0.2717 0.2402 0.3226 0.0200  0.0329  0.0093  167  PHE A CB  
1111 C CG  . PHE A 143 ? 0.2650 0.2275 0.3248 0.0262  0.0378  0.0105  167  PHE A CG  
1112 C CD1 . PHE A 143 ? 0.2379 0.1995 0.3069 0.0273  0.0340  0.0161  167  PHE A CD1 
1113 C CD2 . PHE A 143 ? 0.2480 0.2069 0.3077 0.0318  0.0467  0.0069  167  PHE A CD2 
1114 C CE1 . PHE A 143 ? 0.2977 0.2538 0.3771 0.0342  0.0389  0.0184  167  PHE A CE1 
1115 C CE2 . PHE A 143 ? 0.2854 0.2383 0.3547 0.0393  0.0524  0.0082  167  PHE A CE2 
1116 C CZ  . PHE A 143 ? 0.3385 0.2899 0.4183 0.0405  0.0483  0.0140  167  PHE A CZ  
1117 N N   . VAL A 144 ? 0.2266 0.2163 0.2831 0.0118  0.0186  0.0184  168  VAL A N   
1118 C CA  . VAL A 144 ? 0.2480 0.2398 0.2965 0.0071  0.0122  0.0180  168  VAL A CA  
1119 C C   . VAL A 144 ? 0.2392 0.2250 0.2786 0.0054  0.0103  0.0160  168  VAL A C   
1120 O O   . VAL A 144 ? 0.2421 0.2251 0.2855 0.0065  0.0094  0.0188  168  VAL A O   
1121 C CB  . VAL A 144 ? 0.2690 0.2684 0.3253 0.0056  0.0055  0.0237  168  VAL A CB  
1122 C CG1 . VAL A 144 ? 0.2497 0.2491 0.2953 0.0015  -0.0003 0.0222  168  VAL A CG1 
1123 C CG2 . VAL A 144 ? 0.2410 0.2484 0.3101 0.0063  0.0066  0.0273  168  VAL A CG2 
1124 N N   . THR A 145 ? 0.2023 0.1867 0.2308 0.0026  0.0096  0.0120  169  THR A N   
1125 C CA  . THR A 145 ? 0.2186 0.2006 0.2396 0.0002  0.0072  0.0112  169  THR A CA  
1126 C C   . THR A 145 ? 0.2004 0.1876 0.2202 -0.0011 0.0018  0.0146  169  THR A C   
1127 O O   . THR A 145 ? 0.2346 0.2246 0.2500 -0.0021 -0.0001 0.0134  169  THR A O   
1128 C CB  . THR A 145 ? 0.2618 0.2425 0.2733 -0.0016 0.0086  0.0065  169  THR A CB  
1129 O OG1 . THR A 145 ? 0.2613 0.2364 0.2717 -0.0006 0.0130  0.0028  169  THR A OG1 
1130 C CG2 . THR A 145 ? 0.2497 0.2307 0.2558 -0.0043 0.0061  0.0067  169  THR A CG2 
1131 N N   . TYR A 146 ? 0.2217 0.2091 0.2445 -0.0010 -0.0006 0.0190  170  TYR A N   
1132 C CA  . TYR A 146 ? 0.2458 0.2380 0.2672 -0.0018 -0.0060 0.0228  170  TYR A CA  
1133 C C   . TYR A 146 ? 0.2342 0.2267 0.2476 -0.0033 -0.0075 0.0246  170  TYR A C   
1134 O O   . TYR A 146 ? 0.2520 0.2427 0.2683 -0.0033 -0.0073 0.0287  170  TYR A O   
1135 C CB  . TYR A 146 ? 0.2464 0.2409 0.2791 0.0001  -0.0080 0.0284  170  TYR A CB  
1136 C CG  . TYR A 146 ? 0.2793 0.2794 0.3109 -0.0011 -0.0150 0.0325  170  TYR A CG  
1137 C CD1 . TYR A 146 ? 0.2698 0.2747 0.3069 -0.0019 -0.0186 0.0333  170  TYR A CD1 
1138 C CD2 . TYR A 146 ? 0.2718 0.2727 0.2966 -0.0020 -0.0181 0.0361  170  TYR A CD2 
1139 C CE1 . TYR A 146 ? 0.2695 0.2790 0.3046 -0.0038 -0.0261 0.0365  170  TYR A CE1 
1140 C CE2 . TYR A 146 ? 0.2786 0.2841 0.2997 -0.0031 -0.0249 0.0395  170  TYR A CE2 
1141 C CZ  . TYR A 146 ? 0.2930 0.3024 0.3190 -0.0042 -0.0293 0.0393  170  TYR A CZ  
1142 O OH  . TYR A 146 ? 0.3430 0.3565 0.3643 -0.0062 -0.0372 0.0421  170  TYR A OH  
1143 N N   . PRO A 147 ? 0.2481 0.2429 0.2517 -0.0042 -0.0085 0.0220  171  PRO A N   
1144 C CA  . PRO A 147 ? 0.2438 0.2408 0.2401 -0.0050 -0.0089 0.0244  171  PRO A CA  
1145 C C   . PRO A 147 ? 0.2257 0.2254 0.2195 -0.0048 -0.0133 0.0294  171  PRO A C   
1146 O O   . PRO A 147 ? 0.2310 0.2319 0.2216 -0.0046 -0.0172 0.0282  171  PRO A O   
1147 C CB  . PRO A 147 ? 0.2355 0.2342 0.2227 -0.0046 -0.0078 0.0199  171  PRO A CB  
1148 C CG  . PRO A 147 ? 0.2489 0.2450 0.2397 -0.0044 -0.0062 0.0153  171  PRO A CG  
1149 C CD  . PRO A 147 ? 0.2367 0.2314 0.2359 -0.0041 -0.0079 0.0170  171  PRO A CD  
1150 N N   . LEU A 148 ? 0.2843 0.2846 0.2797 -0.0052 -0.0132 0.0352  172  LEU A N   
1151 C CA  . LEU A 148 ? 0.2799 0.2832 0.2727 -0.0050 -0.0176 0.0415  172  LEU A CA  
1152 C C   . LEU A 148 ? 0.3046 0.3116 0.2824 -0.0049 -0.0191 0.0405  172  LEU A C   
1153 O O   . LEU A 148 ? 0.3273 0.3355 0.2987 -0.0048 -0.0151 0.0382  172  LEU A O   
1154 C CB  . LEU A 148 ? 0.2767 0.2786 0.2749 -0.0054 -0.0163 0.0489  172  LEU A CB  
1155 C CG  . LEU A 148 ? 0.2237 0.2201 0.2360 -0.0043 -0.0152 0.0508  172  LEU A CG  
1156 C CD1 . LEU A 148 ? 0.3294 0.3219 0.3457 -0.0053 -0.0136 0.0579  172  LEU A CD1 
1157 C CD2 . LEU A 148 ? 0.2743 0.2734 0.2935 -0.0022 -0.0199 0.0537  172  LEU A CD2 
1158 N N   . ARG A 149 ? 0.3132 0.3222 0.2852 -0.0048 -0.0248 0.0425  173  ARG A N   
1159 C CA  . ARG A 149 ? 0.3399 0.3511 0.2949 -0.0043 -0.0265 0.0414  173  ARG A CA  
1160 C C   . ARG A 149 ? 0.3572 0.3721 0.3077 -0.0046 -0.0307 0.0498  173  ARG A C   
1161 O O   . ARG A 149 ? 0.3513 0.3670 0.3131 -0.0050 -0.0340 0.0557  173  ARG A O   
1162 C CB  . ARG A 149 ? 0.2686 0.2768 0.2164 -0.0046 -0.0307 0.0340  173  ARG A CB  
1163 C CG  . ARG A 149 ? 0.3307 0.3352 0.2801 -0.0037 -0.0261 0.0267  173  ARG A CG  
1164 C CD  . ARG A 149 ? 0.4313 0.4309 0.3737 -0.0044 -0.0305 0.0200  173  ARG A CD  
1165 N NE  . ARG A 149 ? 0.4111 0.4097 0.3363 -0.0040 -0.0346 0.0190  173  ARG A NE  
1166 C CZ  . ARG A 149 ? 0.4451 0.4419 0.3549 -0.0011 -0.0310 0.0152  173  ARG A CZ  
1167 N NH1 . ARG A 149 ? 0.4504 0.4472 0.3618 0.0017  -0.0237 0.0126  173  ARG A NH1 
1168 N NH2 . ARG A 149 ? 0.4671 0.4625 0.3596 -0.0006 -0.0347 0.0140  173  ARG A NH2 
1169 N N   . PRO A 150 ? 0.4358 0.4534 0.3695 -0.0037 -0.0302 0.0508  174  PRO A N   
1170 C CA  . PRO A 150 ? 0.4463 0.4681 0.3732 -0.0039 -0.0336 0.0597  174  PRO A CA  
1171 C C   . PRO A 150 ? 0.4598 0.4825 0.3897 -0.0051 -0.0430 0.0627  174  PRO A C   
1172 O O   . PRO A 150 ? 0.4670 0.4931 0.4010 -0.0052 -0.0461 0.0724  174  PRO A O   
1173 C CB  . PRO A 150 ? 0.5008 0.5244 0.4056 -0.0022 -0.0317 0.0568  174  PRO A CB  
1174 C CG  . PRO A 150 ? 0.4811 0.5031 0.3863 -0.0006 -0.0242 0.0496  174  PRO A CG  
1175 C CD  . PRO A 150 ? 0.4327 0.4497 0.3527 -0.0018 -0.0258 0.0440  174  PRO A CD  
1176 N N   . GLU A 151 ? 0.3780 0.3981 0.3077 -0.0062 -0.0479 0.0555  175  GLU A N   
1177 C CA  . GLU A 151 ? 0.4802 0.5029 0.4145 -0.0082 -0.0577 0.0587  175  GLU A CA  
1178 C C   . GLU A 151 ? 0.4991 0.5239 0.4579 -0.0080 -0.0584 0.0640  175  GLU A C   
1179 O O   . GLU A 151 ? 0.4747 0.5042 0.4408 -0.0090 -0.0662 0.0691  175  GLU A O   
1180 C CB  . GLU A 151 ? 0.5211 0.5404 0.4456 -0.0105 -0.0639 0.0498  175  GLU A CB  
1181 C CG  . GLU A 151 ? 0.4941 0.5085 0.4291 -0.0112 -0.0608 0.0420  175  GLU A CG  
1182 C CD  . GLU A 151 ? 0.4954 0.5042 0.4207 -0.0089 -0.0525 0.0343  175  GLU A CD  
1183 O OE1 . GLU A 151 ? 0.4933 0.5032 0.4078 -0.0065 -0.0472 0.0359  175  GLU A OE1 
1184 O OE2 . GLU A 151 ? 0.5317 0.5356 0.4609 -0.0095 -0.0512 0.0276  175  GLU A OE2 
1185 N N   . ASP A 152 ? 0.4315 0.4530 0.4025 -0.0065 -0.0503 0.0627  176  ASP A N   
1186 C CA  . ASP A 152 ? 0.3644 0.3862 0.3570 -0.0052 -0.0494 0.0666  176  ASP A CA  
1187 C C   . ASP A 152 ? 0.3587 0.3817 0.3584 -0.0033 -0.0490 0.0773  176  ASP A C   
1188 O O   . ASP A 152 ? 0.3423 0.3643 0.3329 -0.0033 -0.0461 0.0807  176  ASP A O   
1189 C CB  . ASP A 152 ? 0.3625 0.3787 0.3626 -0.0043 -0.0408 0.0603  176  ASP A CB  
1190 C CG  . ASP A 152 ? 0.3893 0.4037 0.3859 -0.0056 -0.0405 0.0510  176  ASP A CG  
1191 O OD1 . ASP A 152 ? 0.3938 0.4111 0.3949 -0.0070 -0.0462 0.0504  176  ASP A OD1 
1192 O OD2 . ASP A 152 ? 0.3735 0.3841 0.3645 -0.0055 -0.0347 0.0451  176  ASP A OD2 
1193 N N   . SER A 153 ? 0.3559 0.3812 0.3731 -0.0013 -0.0513 0.0832  177  SER A N   
1194 C CA  . SER A 153 ? 0.3585 0.3821 0.3860 0.0015  -0.0496 0.0929  177  SER A CA  
1195 C C   . SER A 153 ? 0.2818 0.3030 0.3299 0.0049  -0.0461 0.0927  177  SER A C   
1196 O O   . SER A 153 ? 0.3292 0.3524 0.3828 0.0047  -0.0458 0.0866  177  SER A O   
1197 C CB  . SER A 153 ? 0.3632 0.3942 0.3892 0.0019  -0.0583 0.1039  177  SER A CB  
1198 O OG  . SER A 153 ? 0.3779 0.4168 0.4122 0.0015  -0.0657 0.1043  177  SER A OG  
1199 N N   . LEU A 154 ? 0.3447 0.3609 0.4039 0.0083  -0.0428 0.0995  178  LEU A N   
1200 C CA  . LEU A 154 ? 0.3500 0.3634 0.4281 0.0129  -0.0388 0.0993  178  LEU A CA  
1201 C C   . LEU A 154 ? 0.3644 0.3893 0.4550 0.0147  -0.0450 0.1035  178  LEU A C   
1202 O O   . LEU A 154 ? 0.3263 0.3531 0.4278 0.0164  -0.0419 0.0991  178  LEU A O   
1203 C CB  . LEU A 154 ? 0.3097 0.3138 0.3970 0.0168  -0.0347 0.1063  178  LEU A CB  
1204 C CG  . LEU A 154 ? 0.3689 0.3685 0.4753 0.0231  -0.0297 0.1065  178  LEU A CG  
1205 C CD1 . LEU A 154 ? 0.3477 0.3396 0.4522 0.0228  -0.0218 0.0942  178  LEU A CD1 
1206 C CD2 . LEU A 154 ? 0.4078 0.3971 0.5226 0.0273  -0.0272 0.1148  178  LEU A CD2 
1207 N N   . SER A 155 ? 0.3749 0.4085 0.4643 0.0140  -0.0540 0.1127  179  SER A N   
1208 C CA  . SER A 155 ? 0.3580 0.4043 0.4615 0.0150  -0.0611 0.1179  179  SER A CA  
1209 C C   . SER A 155 ? 0.3760 0.4280 0.4737 0.0099  -0.0647 0.1093  179  SER A C   
1210 O O   . SER A 155 ? 0.3541 0.4137 0.4672 0.0105  -0.0659 0.1096  179  SER A O   
1211 C CB  . SER A 155 ? 0.4540 0.5090 0.5570 0.0151  -0.0713 0.1304  179  SER A CB  
1212 O OG  . SER A 155 ? 0.5362 0.5906 0.6156 0.0100  -0.0759 0.1289  179  SER A OG  
1213 N N   . SER A 156 ? 0.3994 0.4473 0.4755 0.0049  -0.0659 0.1020  180  SER A N   
1214 C CA  . SER A 156 ? 0.4053 0.4560 0.4746 0.0000  -0.0697 0.0937  180  SER A CA  
1215 C C   . SER A 156 ? 0.4141 0.4606 0.4919 0.0009  -0.0612 0.0858  180  SER A C   
1216 O O   . SER A 156 ? 0.3461 0.3983 0.4321 -0.0013 -0.0637 0.0836  180  SER A O   
1217 C CB  . SER A 156 ? 0.3514 0.3978 0.3949 -0.0043 -0.0724 0.0879  180  SER A CB  
1218 O OG  . SER A 156 ? 0.3865 0.4232 0.4202 -0.0036 -0.0630 0.0804  180  SER A OG  
1219 N N   . ILE A 157 ? 0.3363 0.3733 0.4124 0.0038  -0.0514 0.0820  181  ILE A N   
1220 C CA  . ILE A 157 ? 0.3106 0.3434 0.3936 0.0052  -0.0431 0.0751  181  ILE A CA  
1221 C C   . ILE A 157 ? 0.3374 0.3754 0.4433 0.0102  -0.0399 0.0801  181  ILE A C   
1222 O O   . ILE A 157 ? 0.3507 0.3916 0.4648 0.0104  -0.0365 0.0766  181  ILE A O   
1223 C CB  . ILE A 157 ? 0.3472 0.3685 0.4203 0.0061  -0.0347 0.0693  181  ILE A CB  
1224 C CG1 . ILE A 157 ? 0.2763 0.2952 0.3291 0.0017  -0.0368 0.0638  181  ILE A CG1 
1225 C CG2 . ILE A 157 ? 0.3378 0.3545 0.4179 0.0083  -0.0263 0.0630  181  ILE A CG2 
1226 C CD1 . ILE A 157 ? 0.3074 0.3177 0.3511 0.0018  -0.0302 0.0604  181  ILE A CD1 
1227 N N   . ALA A 158 ? 0.3289 0.3683 0.4454 0.0148  -0.0406 0.0890  182  ALA A N   
1228 C CA  . ALA A 158 ? 0.3349 0.3801 0.4741 0.0207  -0.0372 0.0944  182  ALA A CA  
1229 C C   . ALA A 158 ? 0.3797 0.4401 0.5297 0.0178  -0.0446 0.0979  182  ALA A C   
1230 O O   . ALA A 158 ? 0.3785 0.4452 0.5439 0.0200  -0.0402 0.0978  182  ALA A O   
1231 C CB  . ALA A 158 ? 0.3401 0.3842 0.4895 0.0266  -0.0378 0.1046  182  ALA A CB  
1232 N N   . ARG A 159 ? 0.4136 0.4801 0.5550 0.0123  -0.0559 0.1009  183  ARG A N   
1233 C CA  . ARG A 159 ? 0.5144 0.5952 0.6658 0.0080  -0.0652 0.1047  183  ARG A CA  
1234 C C   . ARG A 159 ? 0.4601 0.5402 0.6091 0.0033  -0.0627 0.0959  183  ARG A C   
1235 O O   . ARG A 159 ? 0.5154 0.6057 0.6829 0.0033  -0.0622 0.0988  183  ARG A O   
1236 C CB  . ARG A 159 ? 0.5749 0.6601 0.7134 0.0026  -0.0785 0.1084  183  ARG A CB  
1237 C CG  . ARG A 159 ? 0.6709 0.7708 0.8199 -0.0028 -0.0904 0.1131  183  ARG A CG  
1238 C CD  . ARG A 159 ? 0.7940 0.8987 0.9311 -0.0066 -0.1038 0.1188  183  ARG A CD  
1239 N NE  . ARG A 159 ? 0.9534 1.0452 1.0612 -0.0088 -0.1032 0.1116  183  ARG A NE  
1240 C CZ  . ARG A 159 ? 1.0315 1.1176 1.1188 -0.0153 -0.1076 0.1023  183  ARG A CZ  
1241 N NH1 . ARG A 159 ? 1.0510 1.1417 1.1435 -0.0214 -0.1138 0.0988  183  ARG A NH1 
1242 N NH2 . ARG A 159 ? 1.0202 1.0958 1.0825 -0.0157 -0.1055 0.0968  183  ARG A NH2 
1243 N N   . SER A 160 ? 0.4452 0.5139 0.5728 -0.0003 -0.0607 0.0861  184  SER A N   
1244 C CA  . SER A 160 ? 0.4614 0.5280 0.5848 -0.0049 -0.0592 0.0783  184  SER A CA  
1245 C C   . SER A 160 ? 0.5124 0.5770 0.6462 -0.0008 -0.0473 0.0754  184  SER A C   
1246 O O   . SER A 160 ? 0.4798 0.5484 0.6206 -0.0036 -0.0461 0.0736  184  SER A O   
1247 C CB  . SER A 160 ? 0.4564 0.5114 0.5542 -0.0088 -0.0602 0.0693  184  SER A CB  
1248 O OG  . SER A 160 ? 0.4119 0.4569 0.5005 -0.0047 -0.0511 0.0652  184  SER A OG  
1249 N N   . SER A 161 ? 0.4155 0.4732 0.5496 0.0056  -0.0384 0.0749  185  SER A N   
1250 C CA  . SER A 161 ? 0.3289 0.3825 0.4683 0.0098  -0.0268 0.0708  185  SER A CA  
1251 C C   . SER A 161 ? 0.3406 0.4052 0.5044 0.0152  -0.0228 0.0781  185  SER A C   
1252 O O   . SER A 161 ? 0.3931 0.4585 0.5634 0.0179  -0.0141 0.0757  185  SER A O   
1253 C CB  . SER A 161 ? 0.3432 0.3832 0.4716 0.0139  -0.0195 0.0664  185  SER A CB  
1254 O OG  . SER A 161 ? 0.3108 0.3510 0.4483 0.0190  -0.0198 0.0735  185  SER A OG  
1255 N N   . GLY A 162 ? 0.3546 0.4286 0.5319 0.0172  -0.0290 0.0875  186  GLY A N   
1256 C CA  . GLY A 162 ? 0.4013 0.4864 0.6036 0.0240  -0.0247 0.0957  186  GLY A CA  
1257 C C   . GLY A 162 ? 0.3878 0.4629 0.5930 0.0336  -0.0131 0.0946  186  GLY A C   
1258 O O   . GLY A 162 ? 0.3684 0.4495 0.5916 0.0408  -0.0052 0.0983  186  GLY A O   
1259 N N   . VAL A 163 ? 0.3101 0.3695 0.4977 0.0338  -0.0117 0.0894  187  VAL A N   
1260 C CA  . VAL A 163 ? 0.3118 0.3580 0.4994 0.0416  -0.0020 0.0874  187  VAL A CA  
1261 C C   . VAL A 163 ? 0.3002 0.3427 0.4895 0.0440  -0.0074 0.0948  187  VAL A C   
1262 O O   . VAL A 163 ? 0.3436 0.3873 0.5221 0.0379  -0.0166 0.0967  187  VAL A O   
1263 C CB  . VAL A 163 ? 0.3485 0.3782 0.5147 0.0391  0.0041  0.0753  187  VAL A CB  
1264 C CG1 . VAL A 163 ? 0.2814 0.2956 0.4463 0.0459  0.0127  0.0724  187  VAL A CG1 
1265 C CG2 . VAL A 163 ? 0.4093 0.4425 0.5731 0.0371  0.0093  0.0690  187  VAL A CG2 
1266 N N   . SER A 164 ? 0.3435 0.3818 0.5463 0.0530  -0.0015 0.0997  188  SER A N   
1267 C CA  . SER A 164 ? 0.3672 0.4018 0.5727 0.0555  -0.0067 0.1083  188  SER A CA  
1268 C C   . SER A 164 ? 0.3731 0.3915 0.5571 0.0506  -0.0078 0.1031  188  SER A C   
1269 O O   . SER A 164 ? 0.3402 0.3459 0.5110 0.0487  -0.0012 0.0925  188  SER A O   
1270 C CB  . SER A 164 ? 0.4387 0.4692 0.6629 0.0670  0.0006  0.1144  188  SER A CB  
1271 O OG  . SER A 164 ? 0.4204 0.4297 0.6351 0.0706  0.0105  0.1057  188  SER A OG  
1272 N N   . ALA A 165 ? 0.3645 0.3847 0.5455 0.0483  -0.0162 0.1112  189  ALA A N   
1273 C CA  . ALA A 165 ? 0.3691 0.3766 0.5324 0.0438  -0.0175 0.1092  189  ALA A CA  
1274 C C   . ALA A 165 ? 0.3684 0.3563 0.5311 0.0481  -0.0084 0.1052  189  ALA A C   
1275 O O   . ALA A 165 ? 0.3799 0.3564 0.5271 0.0432  -0.0058 0.0973  189  ALA A O   
1276 C CB  . ALA A 165 ? 0.3913 0.4051 0.5540 0.0423  -0.0271 0.1210  189  ALA A CB  
1277 N N   . ASP A 166 ? 0.3225 0.3060 0.5021 0.0571  -0.0039 0.1108  190  ASP A N   
1278 C CA  . ASP A 166 ? 0.3655 0.3275 0.5442 0.0616  0.0047  0.1061  190  ASP A CA  
1279 C C   . ASP A 166 ? 0.3612 0.3136 0.5294 0.0602  0.0130  0.0914  190  ASP A C   
1280 O O   . ASP A 166 ? 0.3727 0.3080 0.5285 0.0570  0.0162  0.0842  190  ASP A O   
1281 C CB  . ASP A 166 ? 0.4065 0.3656 0.6061 0.0732  0.0090  0.1141  190  ASP A CB  
1282 C CG  . ASP A 166 ? 0.5380 0.4722 0.7360 0.0783  0.0184  0.1078  190  ASP A CG  
1283 O OD1 . ASP A 166 ? 0.5704 0.4893 0.7601 0.0746  0.0166  0.1090  190  ASP A OD1 
1284 O OD2 . ASP A 166 ? 0.5863 0.5156 0.7907 0.0859  0.0276  0.1017  190  ASP A OD2 
1285 N N   . ILE A 167 ? 0.3284 0.2922 0.5019 0.0623  0.0163  0.0875  191  ILE A N   
1286 C CA  . ILE A 167 ? 0.3273 0.2846 0.4895 0.0607  0.0235  0.0745  191  ILE A CA  
1287 C C   . ILE A 167 ? 0.3238 0.2793 0.4657 0.0501  0.0192  0.0674  191  ILE A C   
1288 O O   . ILE A 167 ? 0.3045 0.2458 0.4338 0.0476  0.0233  0.0583  191  ILE A O   
1289 C CB  . ILE A 167 ? 0.3409 0.3132 0.5139 0.0646  0.0276  0.0740  191  ILE A CB  
1290 C CG1 . ILE A 167 ? 0.3920 0.3635 0.5845 0.0767  0.0352  0.0790  191  ILE A CG1 
1291 C CG2 . ILE A 167 ? 0.3592 0.3276 0.5179 0.0613  0.0335  0.0617  191  ILE A CG2 
1292 C CD1 . ILE A 167 ? 0.4932 0.4439 0.6791 0.0828  0.0465  0.0693  191  ILE A CD1 
1293 N N   . LEU A 168 ? 0.2913 0.2608 0.4300 0.0440  0.0108  0.0716  192  LEU A N   
1294 C CA  . LEU A 168 ? 0.3004 0.2689 0.4210 0.0353  0.0072  0.0658  192  LEU A CA  
1295 C C   . LEU A 168 ? 0.3270 0.2810 0.4386 0.0324  0.0073  0.0651  192  LEU A C   
1296 O O   . LEU A 168 ? 0.2876 0.2342 0.3863 0.0274  0.0090  0.0572  192  LEU A O   
1297 C CB  . LEU A 168 ? 0.2701 0.2534 0.3880 0.0304  -0.0020 0.0711  192  LEU A CB  
1298 C CG  . LEU A 168 ? 0.3239 0.3218 0.4498 0.0308  -0.0037 0.0717  192  LEU A CG  
1299 C CD1 . LEU A 168 ? 0.3412 0.3509 0.4641 0.0260  -0.0140 0.0774  192  LEU A CD1 
1300 C CD2 . LEU A 168 ? 0.3595 0.3555 0.4761 0.0280  0.0011  0.0612  192  LEU A CD2 
1301 N N   . GLN A 169 ? 0.3241 0.2747 0.4435 0.0351  0.0049  0.0744  193  GLN A N   
1302 C CA  . GLN A 169 ? 0.3331 0.2705 0.4457 0.0315  0.0045  0.0756  193  GLN A CA  
1303 C C   . GLN A 169 ? 0.3940 0.3122 0.5045 0.0331  0.0119  0.0668  193  GLN A C   
1304 O O   . GLN A 169 ? 0.4029 0.3111 0.5031 0.0270  0.0120  0.0624  193  GLN A O   
1305 C CB  . GLN A 169 ? 0.3142 0.2516 0.4361 0.0343  0.0003  0.0888  193  GLN A CB  
1306 C CG  . GLN A 169 ? 0.3043 0.2313 0.4186 0.0289  -0.0013 0.0925  193  GLN A CG  
1307 C CD  . GLN A 169 ? 0.3592 0.2964 0.4589 0.0207  -0.0057 0.0916  193  GLN A CD  
1308 O OE1 . GLN A 169 ? 0.3640 0.3133 0.4615 0.0195  -0.0115 0.0996  193  GLN A OE1 
1309 N NE2 . GLN A 169 ? 0.3062 0.2386 0.3956 0.0153  -0.0029 0.0820  193  GLN A NE2 
1310 N N   . ARG A 170 ? 0.3267 0.2400 0.4465 0.0411  0.0180  0.0642  194  ARG A N   
1311 C CA  . ARG A 170 ? 0.3250 0.2180 0.4410 0.0434  0.0252  0.0551  194  ARG A CA  
1312 C C   . ARG A 170 ? 0.3405 0.2328 0.4413 0.0378  0.0273  0.0427  194  ARG A C   
1313 O O   . ARG A 170 ? 0.3456 0.2215 0.4368 0.0348  0.0297  0.0346  194  ARG A O   
1314 C CB  . ARG A 170 ? 0.3284 0.2173 0.4577 0.0549  0.0325  0.0553  194  ARG A CB  
1315 C CG  . ARG A 170 ? 0.3759 0.2568 0.5197 0.0618  0.0324  0.0658  194  ARG A CG  
1316 C CD  . ARG A 170 ? 0.4570 0.3389 0.6158 0.0744  0.0403  0.0665  194  ARG A CD  
1317 N NE  . ARG A 170 ? 0.5906 0.4642 0.7649 0.0828  0.0411  0.0765  194  ARG A NE  
1318 C CZ  . ARG A 170 ? 0.5962 0.4458 0.7720 0.0894  0.0479  0.0727  194  ARG A CZ  
1319 N NH1 . ARG A 170 ? 0.5648 0.3958 0.7261 0.0879  0.0541  0.0584  194  ARG A NH1 
1320 N NH2 . ARG A 170 ? 0.5933 0.4391 0.7819 0.0960  0.0474  0.0822  194  ARG A NH2 
1321 N N   . TYR A 171 ? 0.3444 0.2537 0.4429 0.0362  0.0258  0.0414  195  TYR A N   
1322 C CA  . TYR A 171 ? 0.3273 0.2376 0.4117 0.0309  0.0270  0.0314  195  TYR A CA  
1323 C C   . TYR A 171 ? 0.3453 0.2553 0.4189 0.0217  0.0213  0.0311  195  TYR A C   
1324 O O   . TYR A 171 ? 0.3420 0.2500 0.4041 0.0168  0.0217  0.0233  195  TYR A O   
1325 C CB  . TYR A 171 ? 0.3065 0.2344 0.3922 0.0314  0.0266  0.0313  195  TYR A CB  
1326 C CG  . TYR A 171 ? 0.3283 0.2571 0.4212 0.0392  0.0343  0.0287  195  TYR A CG  
1327 C CD1 . TYR A 171 ? 0.3177 0.2334 0.4023 0.0416  0.0417  0.0191  195  TYR A CD1 
1328 C CD2 . TYR A 171 ? 0.3450 0.2886 0.4525 0.0437  0.0341  0.0359  195  TYR A CD2 
1329 C CE1 . TYR A 171 ? 0.3013 0.2186 0.3915 0.0495  0.0500  0.0169  195  TYR A CE1 
1330 C CE2 . TYR A 171 ? 0.3406 0.2873 0.4565 0.0510  0.0420  0.0347  195  TYR A CE2 
1331 C CZ  . TYR A 171 ? 0.3534 0.2871 0.4602 0.0543  0.0505  0.0252  195  TYR A CZ  
1332 O OH  . TYR A 171 ? 0.3608 0.2984 0.4750 0.0622  0.0596  0.0243  195  TYR A OH  
1333 N N   . ASN A 172 ? 0.3380 0.2520 0.4158 0.0196  0.0161  0.0403  196  ASN A N   
1334 C CA  . ASN A 172 ? 0.3256 0.2430 0.3943 0.0115  0.0114  0.0415  196  ASN A CA  
1335 C C   . ASN A 172 ? 0.3309 0.2390 0.4036 0.0097  0.0095  0.0491  196  ASN A C   
1336 O O   . ASN A 172 ? 0.3325 0.2489 0.4063 0.0079  0.0051  0.0581  196  ASN A O   
1337 C CB  . ASN A 172 ? 0.2793 0.2147 0.3455 0.0098  0.0067  0.0454  196  ASN A CB  
1338 C CG  . ASN A 172 ? 0.2589 0.2025 0.3216 0.0107  0.0083  0.0386  196  ASN A CG  
1339 O OD1 . ASN A 172 ? 0.2670 0.2117 0.3199 0.0067  0.0087  0.0322  196  ASN A OD1 
1340 N ND2 . ASN A 172 ? 0.2549 0.2047 0.3268 0.0160  0.0092  0.0409  196  ASN A ND2 
1341 N N   . PRO A 173 ? 0.3777 0.2674 0.4519 0.0103  0.0128  0.0455  197  PRO A N   
1342 C CA  . PRO A 173 ? 0.3351 0.2133 0.4163 0.0103  0.0117  0.0538  197  PRO A CA  
1343 C C   . PRO A 173 ? 0.3830 0.2657 0.4599 0.0018  0.0072  0.0603  197  PRO A C   
1344 O O   . PRO A 173 ? 0.3584 0.2423 0.4269 -0.0053 0.0064  0.0547  197  PRO A O   
1345 C CB  . PRO A 173 ? 0.4045 0.2598 0.4849 0.0114  0.0163  0.0455  197  PRO A CB  
1346 C CG  . PRO A 173 ? 0.3904 0.2466 0.4591 0.0077  0.0178  0.0331  197  PRO A CG  
1347 C CD  . PRO A 173 ? 0.3741 0.2514 0.4416 0.0101  0.0173  0.0333  197  PRO A CD  
1348 N N   . GLY A 174 ? 0.3373 0.2237 0.4202 0.0028  0.0043  0.0727  198  GLY A N   
1349 C CA  . GLY A 174 ? 0.3286 0.2188 0.4083 -0.0044 0.0012  0.0806  198  GLY A CA  
1350 C C   . GLY A 174 ? 0.2976 0.2087 0.3689 -0.0071 -0.0016 0.0823  198  GLY A C   
1351 O O   . GLY A 174 ? 0.3372 0.2545 0.4050 -0.0121 -0.0035 0.0899  198  GLY A O   
1352 N N   . VAL A 175 ? 0.3014 0.2223 0.3691 -0.0038 -0.0015 0.0756  199  VAL A N   
1353 C CA  . VAL A 175 ? 0.2959 0.2337 0.3541 -0.0060 -0.0038 0.0747  199  VAL A CA  
1354 C C   . VAL A 175 ? 0.3072 0.2569 0.3653 -0.0028 -0.0079 0.0834  199  VAL A C   
1355 O O   . VAL A 175 ? 0.3172 0.2686 0.3822 0.0027  -0.0092 0.0847  199  VAL A O   
1356 C CB  . VAL A 175 ? 0.3116 0.2533 0.3654 -0.0050 -0.0021 0.0631  199  VAL A CB  
1357 C CG1 . VAL A 175 ? 0.2638 0.2205 0.3081 -0.0067 -0.0044 0.0621  199  VAL A CG1 
1358 C CG2 . VAL A 175 ? 0.3631 0.2942 0.4145 -0.0087 0.0010  0.0543  199  VAL A CG2 
1359 N N   . ASN A 176 ? 0.3001 0.2587 0.3503 -0.0062 -0.0101 0.0896  200  ASN A N   
1360 C CA  . ASN A 176 ? 0.3310 0.3008 0.3772 -0.0039 -0.0147 0.0972  200  ASN A CA  
1361 C C   . ASN A 176 ? 0.3152 0.2952 0.3538 -0.0029 -0.0168 0.0896  200  ASN A C   
1362 O O   . ASN A 176 ? 0.3121 0.2972 0.3405 -0.0057 -0.0155 0.0842  200  ASN A O   
1363 C CB  . ASN A 176 ? 0.3929 0.3682 0.4307 -0.0077 -0.0152 0.1057  200  ASN A CB  
1364 C CG  . ASN A 176 ? 0.4254 0.4120 0.4550 -0.0058 -0.0203 0.1130  200  ASN A CG  
1365 O OD1 . ASN A 176 ? 0.4148 0.4047 0.4473 -0.0021 -0.0246 0.1131  200  ASN A OD1 
1366 N ND2 . ASN A 176 ? 0.4594 0.4526 0.4785 -0.0085 -0.0200 0.1194  200  ASN A ND2 
1367 N N   . PHE A 177 ? 0.3189 0.3019 0.3637 0.0012  -0.0199 0.0896  201  PHE A N   
1368 C CA  . PHE A 177 ? 0.3121 0.3031 0.3515 0.0014  -0.0221 0.0824  201  PHE A CA  
1369 C C   . PHE A 177 ? 0.3543 0.3549 0.3795 -0.0005 -0.0270 0.0848  201  PHE A C   
1370 O O   . PHE A 177 ? 0.3522 0.3578 0.3703 -0.0011 -0.0293 0.0785  201  PHE A O   
1371 C CB  . PHE A 177 ? 0.3206 0.3137 0.3723 0.0054  -0.0244 0.0829  201  PHE A CB  
1372 C CG  . PHE A 177 ? 0.2958 0.2815 0.3573 0.0079  -0.0185 0.0760  201  PHE A CG  
1373 C CD1 . PHE A 177 ? 0.2996 0.2898 0.3641 0.0089  -0.0182 0.0699  201  PHE A CD1 
1374 C CD2 . PHE A 177 ? 0.3137 0.2872 0.3806 0.0090  -0.0134 0.0759  201  PHE A CD2 
1375 C CE1 . PHE A 177 ? 0.3240 0.3081 0.3960 0.0117  -0.0121 0.0641  201  PHE A CE1 
1376 C CE2 . PHE A 177 ? 0.3182 0.2839 0.3916 0.0117  -0.0078 0.0689  201  PHE A CE2 
1377 C CZ  . PHE A 177 ? 0.3128 0.2845 0.3883 0.0134  -0.0068 0.0631  201  PHE A CZ  
1378 N N   . ASN A 178 ? 0.3377 0.3400 0.3580 -0.0013 -0.0285 0.0939  202  ASN A N   
1379 C CA  . ASN A 178 ? 0.4054 0.4160 0.4095 -0.0026 -0.0322 0.0963  202  ASN A CA  
1380 C C   . ASN A 178 ? 0.3924 0.4040 0.3846 -0.0053 -0.0271 0.0944  202  ASN A C   
1381 O O   . ASN A 178 ? 0.4409 0.4588 0.4188 -0.0057 -0.0283 0.0977  202  ASN A O   
1382 C CB  . ASN A 178 ? 0.4446 0.4586 0.4494 -0.0014 -0.0375 0.1091  202  ASN A CB  
1383 C CG  . ASN A 178 ? 0.5947 0.6172 0.5807 -0.0024 -0.0423 0.1115  202  ASN A CG  
1384 O OD1 . ASN A 178 ? 0.6356 0.6616 0.6122 -0.0030 -0.0459 0.1038  202  ASN A OD1 
1385 N ND2 . ASN A 178 ? 0.6185 0.6434 0.5977 -0.0029 -0.0424 0.1220  202  ASN A ND2 
1386 N N   . SER A 179 ? 0.3511 0.3575 0.3491 -0.0068 -0.0212 0.0894  203  SER A N   
1387 C CA  . SER A 179 ? 0.3495 0.3586 0.3404 -0.0095 -0.0163 0.0897  203  SER A CA  
1388 C C   . SER A 179 ? 0.3926 0.4078 0.3705 -0.0090 -0.0149 0.0815  203  SER A C   
1389 O O   . SER A 179 ? 0.4743 0.4950 0.4441 -0.0099 -0.0111 0.0831  203  SER A O   
1390 C CB  . SER A 179 ? 0.4382 0.4399 0.4403 -0.0122 -0.0118 0.0876  203  SER A CB  
1391 O OG  . SER A 179 ? 0.4239 0.4223 0.4293 -0.0115 -0.0109 0.0769  203  SER A OG  
1392 N N   . GLY A 180 ? 0.4050 0.4190 0.3818 -0.0074 -0.0175 0.0732  204  GLY A N   
1393 C CA  . GLY A 180 ? 0.4102 0.4278 0.3742 -0.0063 -0.0171 0.0656  204  GLY A CA  
1394 C C   . GLY A 180 ? 0.4116 0.4284 0.3776 -0.0068 -0.0119 0.0583  204  GLY A C   
1395 O O   . GLY A 180 ? 0.4085 0.4276 0.3649 -0.0052 -0.0106 0.0525  204  GLY A O   
1396 N N   . ASN A 181 ? 0.3688 0.3818 0.3470 -0.0088 -0.0092 0.0586  205  ASN A N   
1397 C CA  . ASN A 181 ? 0.4362 0.4491 0.4166 -0.0097 -0.0054 0.0522  205  ASN A CA  
1398 C C   . ASN A 181 ? 0.3672 0.3727 0.3598 -0.0116 -0.0047 0.0498  205  ASN A C   
1399 O O   . ASN A 181 ? 0.3857 0.3854 0.3858 -0.0120 -0.0060 0.0538  205  ASN A O   
1400 C CB  . ASN A 181 ? 0.5462 0.5665 0.5233 -0.0111 -0.0011 0.0560  205  ASN A CB  
1401 C CG  . ASN A 181 ? 0.6395 0.6598 0.6220 -0.0141 -0.0005 0.0657  205  ASN A CG  
1402 O OD1 . ASN A 181 ? 0.6931 0.7067 0.6865 -0.0171 -0.0007 0.0669  205  ASN A OD1 
1403 N ND2 . ASN A 181 ? 0.6600 0.6869 0.6342 -0.0133 0.0005  0.0727  205  ASN A ND2 
1404 N N   . GLY A 182 ? 0.3624 0.3675 0.3562 -0.0123 -0.0026 0.0433  206  GLY A N   
1405 C CA  . GLY A 182 ? 0.3203 0.3178 0.3222 -0.0141 -0.0019 0.0398  206  GLY A CA  
1406 C C   . GLY A 182 ? 0.3218 0.3144 0.3262 -0.0112 -0.0032 0.0354  206  GLY A C   
1407 O O   . GLY A 182 ? 0.3428 0.3385 0.3436 -0.0088 -0.0054 0.0352  206  GLY A O   
1408 N N   . ILE A 183 ? 0.2563 0.2416 0.2665 -0.0116 -0.0017 0.0318  207  ILE A N   
1409 C CA  . ILE A 183 ? 0.2296 0.2120 0.2428 -0.0085 -0.0016 0.0282  207  ILE A CA  
1410 C C   . ILE A 183 ? 0.2168 0.1918 0.2390 -0.0067 -0.0009 0.0308  207  ILE A C   
1411 O O   . ILE A 183 ? 0.2931 0.2614 0.3184 -0.0083 0.0001  0.0327  207  ILE A O   
1412 C CB  . ILE A 183 ? 0.4061 0.3874 0.4167 -0.0086 0.0005  0.0210  207  ILE A CB  
1413 C CG1 . ILE A 183 ? 0.4449 0.4183 0.4572 -0.0106 0.0028  0.0179  207  ILE A CG1 
1414 C CG2 . ILE A 183 ? 0.3493 0.3378 0.3520 -0.0094 0.0000  0.0188  207  ILE A CG2 
1415 C CD1 . ILE A 183 ? 0.5408 0.5095 0.5537 -0.0083 0.0054  0.0125  207  ILE A CD1 
1416 N N   . VAL A 184 ? 0.2725 0.2488 0.2998 -0.0032 -0.0015 0.0312  208  VAL A N   
1417 C CA  . VAL A 184 ? 0.2874 0.2573 0.3245 0.0002  0.0006  0.0327  208  VAL A CA  
1418 C C   . VAL A 184 ? 0.2695 0.2402 0.3090 0.0028  0.0035  0.0274  208  VAL A C   
1419 O O   . VAL A 184 ? 0.2813 0.2585 0.3164 0.0018  0.0023  0.0249  208  VAL A O   
1420 C CB  . VAL A 184 ? 0.2703 0.2441 0.3149 0.0026  -0.0030 0.0412  208  VAL A CB  
1421 C CG1 . VAL A 184 ? 0.2808 0.2524 0.3236 0.0005  -0.0049 0.0477  208  VAL A CG1 
1422 C CG2 . VAL A 184 ? 0.2434 0.2278 0.2857 0.0025  -0.0076 0.0423  208  VAL A CG2 
1423 N N   . TYR A 185 ? 0.2646 0.2280 0.3106 0.0063  0.0079  0.0260  209  TYR A N   
1424 C CA  . TYR A 185 ? 0.2738 0.2387 0.3229 0.0095  0.0120  0.0222  209  TYR A CA  
1425 C C   . TYR A 185 ? 0.2438 0.2142 0.3066 0.0142  0.0119  0.0283  209  TYR A C   
1426 O O   . TYR A 185 ? 0.2805 0.2459 0.3512 0.0175  0.0128  0.0324  209  TYR A O   
1427 C CB  . TYR A 185 ? 0.2481 0.2016 0.2939 0.0110  0.0179  0.0158  209  TYR A CB  
1428 C CG  . TYR A 185 ? 0.2637 0.2131 0.2972 0.0057  0.0169  0.0103  209  TYR A CG  
1429 C CD1 . TYR A 185 ? 0.2636 0.2195 0.2894 0.0033  0.0160  0.0070  209  TYR A CD1 
1430 C CD2 . TYR A 185 ? 0.3567 0.2960 0.3875 0.0029  0.0163  0.0092  209  TYR A CD2 
1431 C CE1 . TYR A 185 ? 0.3328 0.2869 0.3491 -0.0012 0.0147  0.0030  209  TYR A CE1 
1432 C CE2 . TYR A 185 ? 0.4351 0.3727 0.4567 -0.0026 0.0146  0.0050  209  TYR A CE2 
1433 C CZ  . TYR A 185 ? 0.4194 0.3652 0.4340 -0.0044 0.0138  0.0021  209  TYR A CZ  
1434 O OH  . TYR A 185 ? 0.4722 0.4181 0.4793 -0.0095 0.0117  -0.0011 209  TYR A OH  
1435 N N   . VAL A 186 ? 0.2481 0.2285 0.3145 0.0142  0.0106  0.0293  210  VAL A N   
1436 C CA  . VAL A 186 ? 0.2659 0.2550 0.3469 0.0174  0.0091  0.0360  210  VAL A CA  
1437 C C   . VAL A 186 ? 0.2661 0.2596 0.3539 0.0204  0.0149  0.0341  210  VAL A C   
1438 O O   . VAL A 186 ? 0.2745 0.2700 0.3554 0.0174  0.0155  0.0301  210  VAL A O   
1439 C CB  . VAL A 186 ? 0.2627 0.2613 0.3420 0.0131  0.0007  0.0396  210  VAL A CB  
1440 C CG1 . VAL A 186 ? 0.2653 0.2748 0.3602 0.0148  -0.0030 0.0470  210  VAL A CG1 
1441 C CG2 . VAL A 186 ? 0.2934 0.2886 0.3630 0.0102  -0.0041 0.0413  210  VAL A CG2 
1442 N N   . PRO A 187 ? 0.2914 0.2866 0.3933 0.0266  0.0196  0.0378  211  PRO A N   
1443 C CA  . PRO A 187 ? 0.3069 0.3078 0.4155 0.0297  0.0264  0.0368  211  PRO A CA  
1444 C C   . PRO A 187 ? 0.3313 0.3447 0.4437 0.0249  0.0215  0.0397  211  PRO A C   
1445 O O   . PRO A 187 ? 0.3075 0.3286 0.4261 0.0219  0.0132  0.0454  211  PRO A O   
1446 C CB  . PRO A 187 ? 0.2889 0.2929 0.4155 0.0375  0.0307  0.0429  211  PRO A CB  
1447 C CG  . PRO A 187 ? 0.2887 0.2810 0.4123 0.0394  0.0296  0.0429  211  PRO A CG  
1448 C CD  . PRO A 187 ? 0.2662 0.2576 0.3783 0.0318  0.0203  0.0430  211  PRO A CD  
1449 N N   . GLY A 188 ? 0.2724 0.2873 0.3806 0.0238  0.0262  0.0361  212  GLY A N   
1450 C CA  . GLY A 188 ? 0.2424 0.2668 0.3540 0.0188  0.0218  0.0387  212  GLY A CA  
1451 C C   . GLY A 188 ? 0.2687 0.3035 0.3951 0.0215  0.0281  0.0430  212  GLY A C   
1452 O O   . GLY A 188 ? 0.3083 0.3422 0.4393 0.0282  0.0375  0.0426  212  GLY A O   
1453 N N   . ARG A 189 ? 0.2832 0.3274 0.4164 0.0162  0.0233  0.0469  213  ARG A N   
1454 C CA  . ARG A 189 ? 0.3573 0.4143 0.5078 0.0173  0.0282  0.0531  213  ARG A CA  
1455 C C   . ARG A 189 ? 0.3210 0.3768 0.4634 0.0145  0.0330  0.0505  213  ARG A C   
1456 O O   . ARG A 189 ? 0.3197 0.3676 0.4469 0.0095  0.0285  0.0457  213  ARG A O   
1457 C CB  . ARG A 189 ? 0.3145 0.3842 0.4817 0.0122  0.0184  0.0610  213  ARG A CB  
1458 C CG  . ARG A 189 ? 0.3756 0.4498 0.5538 0.0154  0.0134  0.0661  213  ARG A CG  
1459 C CD  . ARG A 189 ? 0.4076 0.4913 0.5948 0.0082  0.0003  0.0718  213  ARG A CD  
1460 N NE  . ARG A 189 ? 0.3911 0.4787 0.5855 0.0103  -0.0065 0.0770  213  ARG A NE  
1461 C CZ  . ARG A 189 ? 0.4288 0.5282 0.6447 0.0161  -0.0043 0.0854  213  ARG A CZ  
1462 N NH1 . ARG A 189 ? 0.4016 0.5103 0.6337 0.0209  0.0056  0.0891  213  ARG A NH1 
1463 N NH2 . ARG A 189 ? 0.4259 0.5283 0.6471 0.0179  -0.0114 0.0907  213  ARG A NH2 
1464 N N   . ASP A 190 ? 0.2728 0.3369 0.4259 0.0182  0.0424  0.0544  214  ASP A N   
1465 C CA  . ASP A 190 ? 0.3023 0.3684 0.4515 0.0149  0.0465  0.0549  214  ASP A CA  
1466 C C   . ASP A 190 ? 0.2635 0.3370 0.4228 0.0060  0.0373  0.0606  214  ASP A C   
1467 O O   . ASP A 190 ? 0.3221 0.3999 0.4910 0.0025  0.0277  0.0637  214  ASP A O   
1468 C CB  . ASP A 190 ? 0.3324 0.4058 0.4890 0.0217  0.0602  0.0579  214  ASP A CB  
1469 C CG  . ASP A 190 ? 0.3929 0.4850 0.5776 0.0229  0.0621  0.0686  214  ASP A CG  
1470 O OD1 . ASP A 190 ? 0.3797 0.4796 0.5786 0.0173  0.0517  0.0742  214  ASP A OD1 
1471 O OD2 . ASP A 190 ? 0.4368 0.5363 0.6291 0.0296  0.0743  0.0718  214  ASP A OD2 
1472 N N   . PRO A 191 ? 0.2538 0.3277 0.4100 0.0019  0.0397  0.0619  215  PRO A N   
1473 C CA  . PRO A 191 ? 0.3044 0.3816 0.4683 -0.0073 0.0302  0.0663  215  PRO A CA  
1474 C C   . PRO A 191 ? 0.3846 0.4785 0.5752 -0.0099 0.0268  0.0759  215  PRO A C   
1475 O O   . PRO A 191 ? 0.3875 0.4835 0.5853 -0.0182 0.0158  0.0788  215  PRO A O   
1476 C CB  . PRO A 191 ? 0.3073 0.3826 0.4654 -0.0095 0.0363  0.0676  215  PRO A CB  
1477 C CG  . PRO A 191 ? 0.2791 0.3433 0.4154 -0.0036 0.0431  0.0597  215  PRO A CG  
1478 C CD  . PRO A 191 ? 0.2907 0.3582 0.4314 0.0046  0.0489  0.0582  215  PRO A CD  
1479 N N   . ASN A 192 ? 0.3162 0.4218 0.5216 -0.0028 0.0358  0.0809  216  ASN A N   
1480 C CA  . ASN A 192 ? 0.4280 0.5524 0.6617 -0.0045 0.0331  0.0914  216  ASN A CA  
1481 C C   . ASN A 192 ? 0.4045 0.5332 0.6472 -0.0010 0.0269  0.0928  216  ASN A C   
1482 O O   . ASN A 192 ? 0.3707 0.5164 0.6380 -0.0016 0.0240  0.1021  216  ASN A O   
1483 C CB  . ASN A 192 ? 0.4560 0.5951 0.7061 0.0005  0.0469  0.0991  216  ASN A CB  
1484 C CG  . ASN A 192 ? 0.5028 0.6442 0.7541 -0.0069 0.0484  0.1032  216  ASN A CG  
1485 O OD1 . ASN A 192 ? 0.4724 0.6135 0.7285 -0.0173 0.0370  0.1057  216  ASN A OD1 
1486 N ND2 . ASN A 192 ? 0.5717 0.7136 0.8168 -0.0017 0.0622  0.1035  216  ASN A ND2 
1487 N N   . GLY A 193 ? 0.3241 0.4383 0.5478 0.0022  0.0245  0.0844  217  GLY A N   
1488 C CA  . GLY A 193 ? 0.3687 0.4851 0.5983 0.0047  0.0175  0.0861  217  GLY A CA  
1489 C C   . GLY A 193 ? 0.3536 0.4710 0.5888 0.0162  0.0273  0.0867  217  GLY A C   
1490 O O   . GLY A 193 ? 0.4017 0.5208 0.6430 0.0191  0.0222  0.0893  217  GLY A O   
1491 N N   . ALA A 194 ? 0.3265 0.4422 0.5589 0.0230  0.0414  0.0846  218  ALA A N   
1492 C CA  . ALA A 194 ? 0.3045 0.4181 0.5400 0.0347  0.0519  0.0837  218  ALA A CA  
1493 C C   . ALA A 194 ? 0.3216 0.4135 0.5303 0.0373  0.0538  0.0722  218  ALA A C   
1494 O O   . ALA A 194 ? 0.3181 0.3997 0.5071 0.0320  0.0521  0.0653  218  ALA A O   
1495 C CB  . ALA A 194 ? 0.3305 0.4534 0.5758 0.0413  0.0668  0.0870  218  ALA A CB  
1496 N N   . PHE A 195 ? 0.3372 0.4223 0.5464 0.0452  0.0569  0.0706  219  PHE A N   
1497 C CA  . PHE A 195 ? 0.3007 0.3654 0.4863 0.0473  0.0594  0.0601  219  PHE A CA  
1498 C C   . PHE A 195 ? 0.3032 0.3622 0.4811 0.0546  0.0739  0.0548  219  PHE A C   
1499 O O   . PHE A 195 ? 0.3429 0.4070 0.5344 0.0639  0.0834  0.0583  219  PHE A O   
1500 C CB  . PHE A 195 ? 0.3091 0.3665 0.4979 0.0524  0.0567  0.0608  219  PHE A CB  
1501 C CG  . PHE A 195 ? 0.3225 0.3834 0.5146 0.0460  0.0427  0.0654  219  PHE A CG  
1502 C CD1 . PHE A 195 ? 0.2763 0.3260 0.4486 0.0391  0.0349  0.0593  219  PHE A CD1 
1503 C CD2 . PHE A 195 ? 0.3471 0.4229 0.5618 0.0474  0.0374  0.0759  219  PHE A CD2 
1504 C CE1 . PHE A 195 ? 0.3181 0.3708 0.4912 0.0339  0.0228  0.0633  219  PHE A CE1 
1505 C CE2 . PHE A 195 ? 0.3160 0.3947 0.5312 0.0415  0.0240  0.0800  219  PHE A CE2 
1506 C CZ  . PHE A 195 ? 0.3055 0.3721 0.4989 0.0350  0.0172  0.0733  219  PHE A CZ  
1507 N N   . PRO A 196 ? 0.2702 0.3186 0.4259 0.0511  0.0759  0.0465  220  PRO A N   
1508 C CA  . PRO A 196 ? 0.3242 0.3641 0.4671 0.0577  0.0887  0.0398  220  PRO A CA  
1509 C C   . PRO A 196 ? 0.3273 0.3517 0.4643 0.0649  0.0921  0.0339  220  PRO A C   
1510 O O   . PRO A 196 ? 0.3247 0.3396 0.4557 0.0612  0.0832  0.0314  220  PRO A O   
1511 C CB  . PRO A 196 ? 0.2938 0.3245 0.4130 0.0506  0.0854  0.0325  220  PRO A CB  
1512 C CG  . PRO A 196 ? 0.3175 0.3570 0.4427 0.0412  0.0741  0.0378  220  PRO A CG  
1513 C CD  . PRO A 196 ? 0.3315 0.3754 0.4725 0.0412  0.0664  0.0431  220  PRO A CD  
1514 N N   . PRO A 197 ? 0.3689 0.3904 0.5077 0.0751  0.1050  0.0319  221  PRO A N   
1515 C CA  . PRO A 197 ? 0.3533 0.3583 0.4880 0.0824  0.1084  0.0265  221  PRO A CA  
1516 C C   . PRO A 197 ? 0.3892 0.3726 0.4957 0.0794  0.1080  0.0138  221  PRO A C   
1517 O O   . PRO A 197 ? 0.4310 0.4136 0.5208 0.0736  0.1071  0.0092  221  PRO A O   
1518 C CB  . PRO A 197 ? 0.4010 0.4106 0.5462 0.0948  0.1236  0.0283  221  PRO A CB  
1519 C CG  . PRO A 197 ? 0.3973 0.4185 0.5380 0.0927  0.1298  0.0293  221  PRO A CG  
1520 C CD  . PRO A 197 ? 0.4028 0.4370 0.5500 0.0810  0.1174  0.0358  221  PRO A CD  
1521 N N   . PHE A 198 ? 0.3709 0.3368 0.4726 0.0833  0.1082  0.0086  222  PHE A N   
1522 C CA  . PHE A 198 ? 0.4188 0.3638 0.4951 0.0804  0.1079  -0.0035 222  PHE A CA  
1523 C C   . PHE A 198 ? 0.4737 0.4135 0.5347 0.0860  0.1201  -0.0111 222  PHE A C   
1524 O O   . PHE A 198 ? 0.4685 0.4135 0.5393 0.0961  0.1316  -0.0087 222  PHE A O   
1525 C CB  . PHE A 198 ? 0.4360 0.3617 0.5120 0.0839  0.1066  -0.0071 222  PHE A CB  
1526 C CG  . PHE A 198 ? 0.4838 0.3874 0.5348 0.0796  0.1051  -0.0195 222  PHE A CG  
1527 C CD1 . PHE A 198 ? 0.5067 0.4080 0.5471 0.0682  0.0937  -0.0213 222  PHE A CD1 
1528 C CD2 . PHE A 198 ? 0.5240 0.4095 0.5617 0.0867  0.1148  -0.0294 222  PHE A CD2 
1529 C CE1 . PHE A 198 ? 0.4869 0.3701 0.5063 0.0633  0.0913  -0.0319 222  PHE A CE1 
1530 C CE2 . PHE A 198 ? 0.5557 0.4206 0.5699 0.0815  0.1119  -0.0412 222  PHE A CE2 
1531 C CZ  . PHE A 198 ? 0.5516 0.4162 0.5576 0.0693  0.0998  -0.0419 222  PHE A CZ  
1532 N N   . LYS A 199 ? 0.4683 0.3981 0.5049 0.0799  0.1178  -0.0202 223  LYS A N   
1533 C CA  . LYS A 199 ? 0.6343 0.5574 0.6517 0.0845  0.1284  -0.0284 223  LYS A CA  
1534 C C   . LYS A 199 ? 0.7405 0.6406 0.7317 0.0806  0.1251  -0.0415 223  LYS A C   
1535 O O   . LYS A 199 ? 0.7472 0.6459 0.7279 0.0704  0.1147  -0.0435 223  LYS A O   
1536 C CB  . LYS A 199 ? 0.7261 0.6660 0.7397 0.0804  0.1296  -0.0242 223  LYS A CB  
1537 C CG  . LYS A 199 ? 0.8158 0.7772 0.8530 0.0857  0.1365  -0.0126 223  LYS A CG  
1538 C CD  . LYS A 199 ? 0.8589 0.8333 0.8893 0.0832  0.1410  -0.0095 223  LYS A CD  
1539 C CE  . LYS A 199 ? 0.8658 0.8628 0.9229 0.0865  0.1462  0.0034  223  LYS A CE  
1540 N NZ  . LYS A 199 ? 0.8986 0.8969 0.9717 0.0984  0.1567  0.0055  223  LYS A NZ  
1541 N N   . SER A 200 ? 0.8247 0.7069 0.8058 0.0888  0.1340  -0.0503 224  SER A N   
1542 C CA  . SER A 200 ? 0.9148 0.7730 0.8704 0.0848  0.1308  -0.0636 224  SER A CA  
1543 C C   . SER A 200 ? 0.9279 0.7858 0.8576 0.0820  0.1335  -0.0708 224  SER A C   
1544 O O   . SER A 200 ? 0.9158 0.7894 0.8468 0.0859  0.1412  -0.0660 224  SER A O   
1545 C CB  . SER A 200 ? 0.9727 0.8086 0.9261 0.0945  0.1389  -0.0711 224  SER A CB  
1546 O OG  . SER A 200 ? 0.9984 0.8416 0.9582 0.1068  0.1528  -0.0691 224  SER A OG  
1547 C C1  . NAG B .   ? 0.2774 0.2686 0.2272 0.0070  0.0146  0.0271  801  NAG A C1  
1548 C C2  . NAG B .   ? 0.2911 0.2830 0.2370 0.0098  0.0127  0.0333  801  NAG A C2  
1549 C C3  . NAG B .   ? 0.3725 0.3680 0.3093 0.0092  0.0153  0.0378  801  NAG A C3  
1550 C C4  . NAG B .   ? 0.3815 0.3824 0.3096 0.0073  0.0157  0.0323  801  NAG A C4  
1551 C C5  . NAG B .   ? 0.3747 0.3731 0.3084 0.0053  0.0182  0.0258  801  NAG A C5  
1552 C C6  . NAG B .   ? 0.4173 0.4182 0.3424 0.0036  0.0186  0.0196  801  NAG A C6  
1553 C C7  . NAG B .   ? 0.3810 0.3631 0.3358 0.0151  0.0089  0.0363  801  NAG A C7  
1554 C C8  . NAG B .   ? 0.4383 0.4090 0.3983 0.0170  0.0084  0.0385  801  NAG A C8  
1555 N N2  . NAG B .   ? 0.3138 0.2979 0.2661 0.0116  0.0120  0.0369  801  NAG A N2  
1556 O O3  . NAG B .   ? 0.4255 0.4229 0.3585 0.0120  0.0123  0.0440  801  NAG A O3  
1557 O O4  . NAG B .   ? 0.4606 0.4637 0.3780 0.0068  0.0190  0.0351  801  NAG A O4  
1558 O O5  . NAG B .   ? 0.3168 0.3133 0.2592 0.0058  0.0149  0.0233  801  NAG A O5  
1559 O O6  . NAG B .   ? 0.4396 0.4443 0.3623 0.0030  0.0128  0.0171  801  NAG A O6  
1560 O O7  . NAG B .   ? 0.4166 0.4054 0.3698 0.0170  0.0066  0.0342  801  NAG A O7  
1561 C C1  . NAG C .   ? 0.5934 0.5996 0.5033 0.0085  0.0172  0.0428  802  NAG A C1  
1562 C C2  . NAG C .   ? 0.7111 0.7213 0.6051 0.0071  0.0186  0.0402  802  NAG A C2  
1563 C C3  . NAG C .   ? 0.7652 0.7799 0.6478 0.0083  0.0165  0.0480  802  NAG A C3  
1564 C C4  . NAG C .   ? 0.8393 0.8509 0.7273 0.0101  0.0206  0.0580  802  NAG A C4  
1565 C C5  . NAG C .   ? 0.8354 0.8414 0.7401 0.0115  0.0183  0.0594  802  NAG A C5  
1566 C C6  . NAG C .   ? 0.9052 0.9056 0.8162 0.0124  0.0213  0.0690  802  NAG A C6  
1567 C C7  . NAG C .   ? 0.7293 0.7390 0.6157 0.0032  0.0175  0.0239  802  NAG A C7  
1568 C C8  . NAG C .   ? 0.7594 0.7706 0.6405 0.0003  0.0118  0.0167  802  NAG A C8  
1569 N N2  . NAG C .   ? 0.7191 0.7315 0.6097 0.0051  0.0144  0.0318  802  NAG A N2  
1570 O O3  . NAG C .   ? 0.7806 0.7977 0.6461 0.0069  0.0186  0.0448  802  NAG A O3  
1571 O O4  . NAG C .   ? 0.8754 0.8910 0.7527 0.0116  0.0187  0.0666  802  NAG A O4  
1572 O O5  . NAG C .   ? 0.7361 0.7388 0.6497 0.0097  0.0199  0.0514  802  NAG A O5  
1573 O O6  . NAG C .   ? 0.9686 0.9659 0.8851 0.0097  0.0277  0.0684  802  NAG A O6  
1574 O O7  . NAG C .   ? 0.7236 0.7296 0.6113 0.0036  0.0245  0.0228  802  NAG A O7  
1575 C C1  . NAG D .   ? 0.2919 0.3076 0.2307 0.0060  0.0007  0.0180  803  NAG A C1  
1576 C C2  . NAG D .   ? 0.3393 0.3479 0.2660 0.0078  -0.0033 0.0134  803  NAG A C2  
1577 C C3  . NAG D .   ? 0.4014 0.4121 0.3128 0.0122  -0.0001 0.0125  803  NAG A C3  
1578 C C4  . NAG D .   ? 0.4431 0.4631 0.3535 0.0119  0.0033  0.0200  803  NAG A C4  
1579 C C5  . NAG D .   ? 0.3874 0.4143 0.3137 0.0092  0.0066  0.0249  803  NAG A C5  
1580 C C6  . NAG D .   ? 0.4227 0.4583 0.3505 0.0075  0.0096  0.0337  803  NAG A C6  
1581 C C7  . NAG D .   ? 0.3486 0.3434 0.2774 0.0060  -0.0105 0.0049  803  NAG A C7  
1582 C C8  . NAG D .   ? 0.3083 0.2958 0.2380 0.0067  -0.0112 -0.0005 803  NAG A C8  
1583 N N2  . NAG D .   ? 0.3113 0.3127 0.2390 0.0085  -0.0049 0.0073  803  NAG A N2  
1584 O O3  . NAG D .   ? 0.4613 0.4639 0.3592 0.0130  -0.0047 0.0076  803  NAG A O3  
1585 O O4  . NAG D .   ? 0.5027 0.5264 0.4003 0.0172  0.0087  0.0190  803  NAG A O4  
1586 O O5  . NAG D .   ? 0.3529 0.3746 0.2901 0.0050  0.0021  0.0246  803  NAG A O5  
1587 O O6  . NAG D .   ? 0.5226 0.5547 0.4462 0.0055  0.0048  0.0369  803  NAG A O6  
1588 O O7  . NAG D .   ? 0.3456 0.3404 0.2755 0.0032  -0.0151 0.0076  803  NAG A O7  
1589 C C1  . NAG E .   ? 0.6047 0.6322 0.4898 0.0179  0.0095  0.0235  804  NAG A C1  
1590 C C2  . NAG E .   ? 0.6617 0.6964 0.5384 0.0242  0.0183  0.0236  804  NAG A C2  
1591 C C3  . NAG E .   ? 0.7633 0.8004 0.6206 0.0271  0.0203  0.0259  804  NAG A C3  
1592 C C4  . NAG E .   ? 0.7751 0.8003 0.6167 0.0259  0.0119  0.0203  804  NAG A C4  
1593 C C5  . NAG E .   ? 0.7879 0.8086 0.6437 0.0190  0.0031  0.0217  804  NAG A C5  
1594 C C6  . NAG E .   ? 0.8719 0.8828 0.7162 0.0169  -0.0064 0.0168  804  NAG A C6  
1595 C C7  . NAG E .   ? 0.6173 0.6673 0.5183 0.0256  0.0276  0.0281  804  NAG A C7  
1596 C C8  . NAG E .   ? 0.6402 0.7016 0.5599 0.0217  0.0301  0.0352  804  NAG A C8  
1597 N N2  . NAG E .   ? 0.5958 0.6422 0.4886 0.0228  0.0236  0.0305  804  NAG A N2  
1598 O O3  . NAG E .   ? 0.7843 0.8250 0.6311 0.0347  0.0288  0.0232  804  NAG A O3  
1599 O O4  . NAG E .   ? 0.7543 0.7834 0.5795 0.0269  0.0126  0.0248  804  NAG A O4  
1600 O O5  . NAG E .   ? 0.6796 0.6975 0.5509 0.0181  0.0032  0.0181  804  NAG A O5  
1601 O O6  . NAG E .   ? 0.9630 0.9715 0.8245 0.0117  -0.0126 0.0181  804  NAG A O6  
1602 O O7  . NAG E .   ? 0.5977 0.6417 0.4916 0.0310  0.0288  0.0208  804  NAG A O7  
1603 C C1  . NAG F .   ? 0.3234 0.2846 0.3137 -0.0323 -0.0013 -0.0066 805  NAG A C1  
1604 C C2  . NAG F .   ? 0.3398 0.3127 0.3367 -0.0347 -0.0031 0.0007  805  NAG A C2  
1605 C C3  . NAG F .   ? 0.3837 0.3592 0.3831 -0.0427 -0.0072 0.0015  805  NAG A C3  
1606 C C4  . NAG F .   ? 0.4496 0.4090 0.4488 -0.0477 -0.0086 -0.0021 805  NAG A C4  
1607 C C5  . NAG F .   ? 0.4590 0.4053 0.4493 -0.0439 -0.0064 -0.0104 805  NAG A C5  
1608 C C6  . NAG F .   ? 0.5337 0.4610 0.5228 -0.0473 -0.0068 -0.0149 805  NAG A C6  
1609 C C7  . NAG F .   ? 0.4927 0.4851 0.4898 -0.0272 -0.0012 0.0066  805  NAG A C7  
1610 C C8  . NAG F .   ? 0.3152 0.3180 0.3092 -0.0238 -0.0010 0.0069  805  NAG A C8  
1611 N N2  . NAG F .   ? 0.4056 0.3913 0.4007 -0.0311 -0.0027 0.0023  805  NAG A N2  
1612 O O3  . NAG F .   ? 0.4081 0.3947 0.4147 -0.0439 -0.0072 0.0094  805  NAG A O3  
1613 O O4  . NAG F .   ? 0.5531 0.5149 0.5531 -0.0560 -0.0137 -0.0029 805  NAG A O4  
1614 O O5  . NAG F .   ? 0.3690 0.3162 0.3599 -0.0359 -0.0018 -0.0092 805  NAG A O5  
1615 O O6  . NAG F .   ? 0.5765 0.4988 0.5742 -0.0456 -0.0048 -0.0091 805  NAG A O6  
1616 O O7  . NAG F .   ? 0.6687 0.6581 0.6691 -0.0261 -0.0002 0.0101  805  NAG A O7  
1617 C C1  . NAG G .   ? 0.5827 0.5446 0.5925 -0.0619 -0.0151 0.0039  806  NAG A C1  
1618 C C2  . NAG G .   ? 0.6291 0.5910 0.6386 -0.0714 -0.0213 0.0009  806  NAG A C2  
1619 C C3  . NAG G .   ? 0.7464 0.7128 0.7680 -0.0798 -0.0241 0.0089  806  NAG A C3  
1620 C C4  . NAG G .   ? 0.7671 0.7524 0.7973 -0.0762 -0.0205 0.0193  806  NAG A C4  
1621 C C5  . NAG G .   ? 0.7457 0.7277 0.7719 -0.0661 -0.0146 0.0199  806  NAG A C5  
1622 C C6  . NAG G .   ? 0.8143 0.8131 0.8453 -0.0621 -0.0111 0.0288  806  NAG A C6  
1623 C C7  . NAG G .   ? 0.5631 0.5032 0.5519 -0.0727 -0.0246 -0.0166 806  NAG A C7  
1624 C C8  . NAG G .   ? 0.5781 0.4954 0.5556 -0.0731 -0.0243 -0.0269 806  NAG A C8  
1625 N N2  . NAG G .   ? 0.5553 0.4971 0.5555 -0.0733 -0.0228 -0.0088 806  NAG A N2  
1626 O O3  . NAG G .   ? 0.7576 0.7289 0.7809 -0.0891 -0.0308 0.0074  806  NAG A O3  
1627 O O4  . NAG G .   ? 0.8308 0.8183 0.8721 -0.0834 -0.0215 0.0275  806  NAG A O4  
1628 O O5  . NAG G .   ? 0.6259 0.6054 0.6424 -0.0600 -0.0136 0.0123  806  NAG A O5  
1629 O O6  . NAG G .   ? 0.8522 0.8676 0.8830 -0.0604 -0.0114 0.0291  806  NAG A O6  
1630 O O7  . NAG G .   ? 0.5067 0.4621 0.4935 -0.0713 -0.0259 -0.0155 806  NAG A O7  
1631 C C1  . NAG H .   ? 0.3595 0.3632 0.2882 -0.0319 -0.0167 -0.0184 807  NAG A C1  
1632 C C2  . NAG H .   ? 0.3619 0.3576 0.2739 -0.0347 -0.0183 -0.0249 807  NAG A C2  
1633 C C3  . NAG H .   ? 0.4069 0.4015 0.3171 -0.0435 -0.0260 -0.0285 807  NAG A C3  
1634 C C4  . NAG H .   ? 0.3979 0.4100 0.3184 -0.0464 -0.0329 -0.0213 807  NAG A C4  
1635 C C5  . NAG H .   ? 0.3866 0.4075 0.3233 -0.0415 -0.0291 -0.0142 807  NAG A C5  
1636 C C6  . NAG H .   ? 0.3877 0.4271 0.3341 -0.0425 -0.0345 -0.0067 807  NAG A C6  
1637 C C7  . NAG H .   ? 0.3872 0.3651 0.2785 -0.0285 -0.0078 -0.0331 807  NAG A C7  
1638 C C8  . NAG H .   ? 0.3898 0.3552 0.2768 -0.0243 0.0006  -0.0379 807  NAG A C8  
1639 N N2  . NAG H .   ? 0.3641 0.3461 0.2690 -0.0314 -0.0112 -0.0304 807  NAG A N2  
1640 O O3  . NAG H .   ? 0.4351 0.4226 0.3273 -0.0461 -0.0285 -0.0348 807  NAG A O3  
1641 O O4  . NAG H .   ? 0.4370 0.4505 0.3603 -0.0554 -0.0404 -0.0229 807  NAG A O4  
1642 O O5  . NAG H .   ? 0.3809 0.3990 0.3154 -0.0337 -0.0224 -0.0130 807  NAG A O5  
1643 O O6  . NAG H .   ? 0.3976 0.4440 0.3377 -0.0386 -0.0360 -0.0036 807  NAG A O6  
1644 O O7  . NAG H .   ? 0.4273 0.4116 0.3096 -0.0288 -0.0107 -0.0312 807  NAG A O7  
1645 C C1  . NAG I .   ? 0.4491 0.4651 0.3599 -0.0608 -0.0483 -0.0256 808  NAG A C1  
1646 C C2  . NAG I .   ? 0.5216 0.5513 0.4441 -0.0692 -0.0578 -0.0211 808  NAG A C2  
1647 C C3  . NAG I .   ? 0.5272 0.5569 0.4365 -0.0776 -0.0681 -0.0254 808  NAG A C3  
1648 C C4  . NAG I .   ? 0.5230 0.5296 0.4125 -0.0803 -0.0668 -0.0375 808  NAG A C4  
1649 C C5  . NAG I .   ? 0.4862 0.4821 0.3656 -0.0700 -0.0556 -0.0404 808  NAG A C5  
1650 C C6  . NAG I .   ? 0.5842 0.5574 0.4448 -0.0711 -0.0526 -0.0523 808  NAG A C6  
1651 C C7  . NAG I .   ? 0.5427 0.6015 0.4979 -0.0646 -0.0562 -0.0049 808  NAG A C7  
1652 C C8  . NAG I .   ? 0.4902 0.5677 0.4580 -0.0577 -0.0546 0.0048  808  NAG A C8  
1653 N N2  . NAG I .   ? 0.4952 0.5450 0.4322 -0.0646 -0.0579 -0.0107 808  NAG A N2  
1654 O O3  . NAG I .   ? 0.4722 0.5133 0.3942 -0.0871 -0.0773 -0.0217 808  NAG A O3  
1655 O O4  . NAG I .   ? 0.5499 0.5571 0.4236 -0.0871 -0.0764 -0.0416 808  NAG A O4  
1656 O O5  . NAG I .   ? 0.4616 0.4587 0.3568 -0.0637 -0.0475 -0.0357 808  NAG A O5  
1657 O O6  . NAG I .   ? 0.6766 0.6456 0.5263 -0.0620 -0.0437 -0.0534 808  NAG A O6  
1658 O O7  . NAG I .   ? 0.5017 0.5534 0.4628 -0.0693 -0.0555 -0.0069 808  NAG A O7  
1659 C C1  . BMA J .   ? 0.6254 0.6145 0.4913 -0.0962 -0.0807 -0.0516 809  BMA A C1  
1660 C C2  . BMA J .   ? 0.6953 0.6800 0.5366 -0.1006 -0.0883 -0.0585 809  BMA A C2  
1661 C C3  . BMA J .   ? 0.7980 0.7624 0.6267 -0.1112 -0.0949 -0.0704 809  BMA A C3  
1662 C C4  . BMA J .   ? 0.8033 0.7744 0.6535 -0.1220 -0.1032 -0.0660 809  BMA A C4  
1663 C C5  . BMA J .   ? 0.7887 0.7670 0.6636 -0.1158 -0.0941 -0.0572 809  BMA A C5  
1664 C C6  . BMA J .   ? 0.8619 0.8497 0.7586 -0.1264 -0.1017 -0.0511 809  BMA A C6  
1665 O O2  . BMA J .   ? 0.6537 0.6613 0.5013 -0.1039 -0.0979 -0.0498 809  BMA A O2  
1666 O O3  . BMA J .   ? 0.9084 0.8699 0.7136 -0.1168 -0.1039 -0.0768 809  BMA A O3  
1667 O O4  . BMA J .   ? 0.8176 0.7657 0.6578 -0.1313 -0.1077 -0.0772 809  BMA A O4  
1668 O O5  . BMA J .   ? 0.6703 0.6680 0.5532 -0.1060 -0.0890 -0.0475 809  BMA A O5  
1669 O O6  . BMA J .   ? 0.9122 0.8959 0.8250 -0.1225 -0.0929 -0.0474 809  BMA A O6  
1670 C C1  . BMA K .   ? 1.0283 1.0022 0.9550 -0.1269 -0.0906 -0.0464 810  BMA A C1  
1671 C C2  . BMA K .   ? 1.1031 1.0902 1.0403 -0.1409 -0.1039 -0.0423 810  BMA A C2  
1672 C C3  . BMA K .   ? 1.1240 1.1138 1.0837 -0.1474 -0.1038 -0.0351 810  BMA A C3  
1673 C C4  . BMA K .   ? 1.0931 1.0942 1.0680 -0.1362 -0.0921 -0.0255 810  BMA A C4  
1674 C C5  . BMA K .   ? 1.0366 1.0230 0.9977 -0.1231 -0.0810 -0.0313 810  BMA A C5  
1675 C C6  . BMA K .   ? 0.9622 0.9609 0.9376 -0.1130 -0.0711 -0.0219 810  BMA A C6  
1676 O O2  . BMA K .   ? 1.1374 1.1521 1.0826 -0.1389 -0.1078 -0.0331 810  BMA A O2  
1677 O O3  . BMA K .   ? 1.1261 1.1363 1.1003 -0.1586 -0.1149 -0.0277 810  BMA A O3  
1678 O O4  . BMA K .   ? 1.1340 1.1319 1.1251 -0.1417 -0.0907 -0.0204 810  BMA A O4  
1679 O O5  . BMA K .   ? 1.0408 1.0289 0.9849 -0.1184 -0.0822 -0.0362 810  BMA A O5  
1680 O O6  . BMA K .   ? 0.9399 0.9359 0.9046 -0.1009 -0.0633 -0.0245 810  BMA A O6  
1681 C C1  . MAN L .   ? 1.0624 1.0080 0.8415 -0.1088 -0.0954 -0.0854 811  MAN A C1  
1682 C C2  . MAN L .   ? 1.1548 1.0974 0.9139 -0.1136 -0.1047 -0.0920 811  MAN A C2  
1683 C C3  . MAN L .   ? 1.1979 1.1578 0.9470 -0.1080 -0.1059 -0.0850 811  MAN A C3  
1684 C C4  . MAN L .   ? 1.1945 1.1519 0.9350 -0.0969 -0.0923 -0.0832 811  MAN A C4  
1685 C C5  . MAN L .   ? 1.1457 1.1074 0.9136 -0.0915 -0.0835 -0.0761 811  MAN A C5  
1686 C C6  . MAN L .   ? 1.1778 1.1385 0.9446 -0.0784 -0.0689 -0.0728 811  MAN A C6  
1687 O O2  . MAN L .   ? 1.1679 1.0851 0.9074 -0.1111 -0.0991 -0.1057 811  MAN A O2  
1688 O O3  . MAN L .   ? 1.2659 1.2199 0.9946 -0.1092 -0.1112 -0.0923 811  MAN A O3  
1689 O O4  . MAN L .   ? 1.2165 1.1918 0.9523 -0.0923 -0.0940 -0.0741 811  MAN A O4  
1690 O O5  . MAN L .   ? 1.0897 1.0334 0.8626 -0.0959 -0.0821 -0.0841 811  MAN A O5  
1691 O O6  . MAN L .   ? 1.2005 1.1713 0.9942 -0.0735 -0.0634 -0.0635 811  MAN A O6  
1692 C C1  . NAG M .   ? 0.4661 0.6324 0.4790 0.0477  0.0620  0.0601  812  NAG A C1  
1693 C C2  . NAG M .   ? 0.3848 0.5442 0.4039 0.0438  0.0533  0.0564  812  NAG A C2  
1694 C C3  . NAG M .   ? 0.3899 0.5631 0.4212 0.0511  0.0557  0.0598  812  NAG A C3  
1695 C C4  . NAG M .   ? 0.4005 0.5711 0.4219 0.0656  0.0649  0.0569  812  NAG A C4  
1696 C C5  . NAG M .   ? 0.5225 0.6986 0.5361 0.0687  0.0735  0.0595  812  NAG A C5  
1697 C C6  . NAG M .   ? 0.6075 0.7768 0.6068 0.0833  0.0826  0.0543  812  NAG A C6  
1698 C C7  . NAG M .   ? 0.3378 0.4823 0.3601 0.0246  0.0386  0.0533  812  NAG A C7  
1699 C C8  . NAG M .   ? 0.3398 0.4855 0.3718 0.0123  0.0317  0.0559  812  NAG A C8  
1700 N N2  . NAG M .   ? 0.3134 0.4751 0.3424 0.0308  0.0459  0.0596  812  NAG A N2  
1701 O O1  . NAG M .   ? 0.4701 0.6234 0.4711 0.0418  0.0593  0.0575  812  NAG A O1  
1702 O O3  . NAG M .   ? 0.3759 0.5406 0.4089 0.0490  0.0481  0.0559  812  NAG A O3  
1703 O O4  . NAG M .   ? 0.3861 0.5734 0.4220 0.0732  0.0685  0.0625  812  NAG A O4  
1704 O O5  . NAG M .   ? 0.5030 0.6659 0.5045 0.0607  0.0696  0.0562  812  NAG A O5  
1705 O O6  . NAG M .   ? 0.6914 0.8721 0.6866 0.0871  0.0921  0.0590  812  NAG A O6  
1706 O O7  . NAG M .   ? 0.3164 0.4442 0.3253 0.0287  0.0377  0.0457  812  NAG A O7  
1707 C C1  . NAG N .   ? 0.3361 0.5099 0.3654 0.0822  0.0681  0.0564  813  NAG A C1  
1708 C C2  . NAG N .   ? 0.3775 0.5702 0.4209 0.0938  0.0753  0.0633  813  NAG A C2  
1709 C C3  . NAG N .   ? 0.3818 0.5613 0.4217 0.1026  0.0738  0.0587  813  NAG A C3  
1710 C C4  . NAG N .   ? 0.3384 0.5105 0.3813 0.0923  0.0619  0.0574  813  NAG A C4  
1711 C C5  . NAG N .   ? 0.3221 0.4781 0.3522 0.0804  0.0559  0.0510  813  NAG A C5  
1712 C C6  . NAG N .   ? 0.3038 0.4524 0.3356 0.0706  0.0452  0.0494  813  NAG A C6  
1713 C C7  . NAG N .   ? 0.4654 0.6903 0.5180 0.1021  0.0928  0.0748  813  NAG A C7  
1714 C C8  . NAG N .   ? 0.4896 0.7192 0.5325 0.1121  0.1060  0.0753  813  NAG A C8  
1715 N N2  . NAG N .   ? 0.4062 0.6062 0.4446 0.1036  0.0874  0.0648  813  NAG A N2  
1716 O O3  . NAG N .   ? 0.3868 0.5849 0.4421 0.1137  0.0799  0.0661  813  NAG A O3  
1717 O O4  . NAG N .   ? 0.3504 0.5074 0.3876 0.1002  0.0609  0.0532  813  NAG A O4  
1718 O O5  . NAG N .   ? 0.3006 0.4693 0.3353 0.0735  0.0576  0.0555  813  NAG A O5  
1719 O O6  . NAG N .   ? 0.2632 0.4318 0.3126 0.0650  0.0405  0.0574  813  NAG A O6  
1720 O O7  . NAG N .   ? 0.4702 0.7138 0.5425 0.0928  0.0876  0.0833  813  NAG A O7  
1721 C C1  . NAG O .   ? 0.3364 0.5041 0.3884 0.1016  0.0561  0.0596  814  NAG A C1  
1722 C C2  . NAG O .   ? 0.3422 0.4876 0.3843 0.1052  0.0523  0.0541  814  NAG A C2  
1723 C C3  . NAG O .   ? 0.3298 0.4875 0.3868 0.1097  0.0489  0.0621  814  NAG A C3  
1724 C C4  . NAG O .   ? 0.3599 0.5381 0.4314 0.1221  0.0574  0.0697  814  NAG A C4  
1725 C C5  . NAG O .   ? 0.2894 0.4893 0.3700 0.1180  0.0616  0.0743  814  NAG A C5  
1726 C C6  . NAG O .   ? 0.3436 0.5617 0.4369 0.1329  0.0724  0.0812  814  NAG A C6  
1727 C C7  . NAG O .   ? 0.4176 0.5245 0.4323 0.0928  0.0451  0.0392  814  NAG A C7  
1728 C C8  . NAG O .   ? 0.3489 0.4436 0.3569 0.0809  0.0370  0.0351  814  NAG A C8  
1729 N N2  . NAG O .   ? 0.3048 0.4348 0.3366 0.0931  0.0444  0.0483  814  NAG A N2  
1730 O O3  . NAG O .   ? 0.3419 0.4788 0.3902 0.1151  0.0473  0.0583  814  NAG A O3  
1731 O O4  . NAG O .   ? 0.4125 0.6071 0.5010 0.1252  0.0533  0.0792  814  NAG A O4  
1732 O O5  . NAG O .   ? 0.3463 0.5324 0.4106 0.1135  0.0646  0.0665  814  NAG A O5  
1733 O O6  . NAG O .   ? 0.4370 0.6814 0.5450 0.1268  0.0741  0.0891  814  NAG A O6  
1734 O O7  . NAG O .   ? 0.3449 0.4413 0.3496 0.1015  0.0519  0.0344  814  NAG A O7  
1735 C C1  . NAG P .   ? 0.4565 0.6465 0.5479 0.1417  0.0594  0.0812  815  NAG A C1  
1736 C C2  . NAG P .   ? 0.4411 0.6578 0.5554 0.1434  0.0546  0.0942  815  NAG A C2  
1737 C C3  . NAG P .   ? 0.5187 0.7329 0.6394 0.1605  0.0595  0.0987  815  NAG A C3  
1738 C C4  . NAG P .   ? 0.5666 0.7462 0.6681 0.1642  0.0588  0.0899  815  NAG A C4  
1739 C C5  . NAG P .   ? 0.5374 0.6932 0.6173 0.1614  0.0637  0.0766  815  NAG A C5  
1740 C C6  . NAG P .   ? 0.5459 0.6676 0.6079 0.1629  0.0619  0.0680  815  NAG A C6  
1741 C C7  . NAG P .   ? 0.4643 0.7320 0.6090 0.1280  0.0485  0.1087  815  NAG A C7  
1742 C C8  . NAG P .   ? 0.4803 0.7772 0.6440 0.1264  0.0523  0.1176  815  NAG A C8  
1743 N N2  . NAG P .   ? 0.4367 0.6836 0.5685 0.1410  0.0575  0.1020  815  NAG A N2  
1744 O O3  . NAG P .   ? 0.4905 0.7248 0.6286 0.1582  0.0517  0.1099  815  NAG A O3  
1745 O O4  . NAG P .   ? 0.6751 0.8486 0.7808 0.1798  0.0647  0.0928  815  NAG A O4  
1746 O O5  . NAG P .   ? 0.5025 0.6632 0.5783 0.1454  0.0580  0.0739  815  NAG A O5  
1747 O O6  . NAG P .   ? 0.6010 0.7026 0.6444 0.1629  0.0672  0.0564  815  NAG A O6  
1748 O O7  . NAG P .   ? 0.4427 0.7042 0.5824 0.1163  0.0374  0.1071  815  NAG A O7  
1749 O O   . HOH Q .   ? 0.2578 0.2468 0.2409 -0.0005 0.0187  0.0083  901  HOH A O   
1750 O O   . HOH Q .   ? 0.2409 0.2732 0.2303 -0.0184 -0.0039 0.0080  902  HOH A O   
1751 O O   . HOH Q .   ? 0.3089 0.2786 0.3376 0.0214  0.0466  -0.0016 903  HOH A O   
1752 O O   . HOH Q .   ? 0.2745 0.2420 0.2951 0.0072  0.0238  0.0009  904  HOH A O   
1753 O O   . HOH Q .   ? 0.3029 0.2967 0.2337 0.0012  0.0257  0.0044  905  HOH A O   
1754 O O   . HOH Q .   ? 0.2330 0.2261 0.2078 -0.0031 -0.0135 0.0095  906  HOH A O   
1755 O O   . HOH Q .   ? 0.2990 0.2970 0.2473 0.0003  0.0117  0.0049  907  HOH A O   
1756 O O   . HOH Q .   ? 0.3496 0.3310 0.2721 -0.0146 0.0070  -0.0215 908  HOH A O   
1757 O O   . HOH Q .   ? 0.2841 0.2687 0.2778 -0.0142 0.0037  0.0034  909  HOH A O   
1758 O O   . HOH Q .   ? 0.3605 0.3723 0.3482 -0.0046 -0.0278 0.0697  910  HOH A O   
1759 O O   . HOH Q .   ? 0.3640 0.2828 0.4509 0.0655  0.0747  0.0046  911  HOH A O   
1760 O O   . HOH Q .   ? 0.4114 0.3948 0.3559 -0.0408 -0.0159 -0.0240 912  HOH A O   
1761 O O   . HOH Q .   ? 0.3627 0.3417 0.3762 -0.0203 0.0005  0.0306  913  HOH A O   
1762 O O   . HOH Q .   ? 0.2735 0.2712 0.2353 0.0061  0.0060  0.0092  914  HOH A O   
1763 O O   . HOH Q .   ? 0.3081 0.3379 0.2860 -0.0044 0.0069  0.0235  915  HOH A O   
1764 O O   . HOH Q .   ? 0.3500 0.3094 0.2728 0.0067  -0.0178 -0.0141 916  HOH A O   
1765 O O   . HOH Q .   ? 0.3117 0.4183 0.3676 -0.0523 -0.0103 0.0477  917  HOH A O   
1766 O O   . HOH Q .   ? 0.2983 0.4411 0.3279 0.0328  0.0313  0.0483  918  HOH A O   
1767 O O   . HOH Q .   ? 0.2938 0.3295 0.2947 -0.0471 -0.0193 0.0075  919  HOH A O   
1768 O O   . HOH Q .   ? 0.3717 0.2513 0.3312 -0.0250 -0.0444 -0.0173 920  HOH A O   
1769 O O   . HOH Q .   ? 0.2985 0.3509 0.2854 -0.0058 0.0125  0.0318  921  HOH A O   
1770 O O   . HOH Q .   ? 0.3284 0.3025 0.4013 0.0106  -0.0217 0.1044  922  HOH A O   
1771 O O   . HOH Q .   ? 0.3315 0.3318 0.2853 0.0093  0.0058  0.0177  923  HOH A O   
1772 O O   . HOH Q .   ? 0.3007 0.3129 0.4253 0.0454  0.0575  0.0337  924  HOH A O   
1773 O O   . HOH Q .   ? 0.3617 0.3435 0.3946 0.0325  0.0690  0.0006  925  HOH A O   
1774 O O   . HOH Q .   ? 0.3496 0.3222 0.2688 0.0160  -0.0057 -0.0115 926  HOH A O   
1775 O O   . HOH Q .   ? 0.3285 0.2696 0.3316 -0.0118 0.0040  0.0335  927  HOH A O   
1776 O O   . HOH Q .   ? 0.3277 0.3385 0.3714 -0.0079 -0.0246 0.0290  928  HOH A O   
1777 O O   . HOH Q .   ? 0.4375 0.4048 0.3796 -0.0562 -0.0250 -0.0316 929  HOH A O   
1778 O O   . HOH Q .   ? 0.3876 0.3612 0.4041 -0.0142 0.0190  0.0426  930  HOH A O   
1779 O O   . HOH Q .   ? 0.4590 0.4891 0.4801 -0.0086 -0.0604 0.0617  931  HOH A O   
1780 O O   . HOH Q .   ? 0.5044 0.3467 0.4021 -0.0388 -0.0810 -0.0487 932  HOH A O   
1781 O O   . HOH Q .   ? 0.2634 0.2923 0.3237 -0.0045 0.0523  0.0479  933  HOH A O   
1782 O O   . HOH Q .   ? 0.4321 0.3949 0.3963 0.0268  0.0046  0.0270  934  HOH A O   
1783 O O   . HOH Q .   ? 0.2406 0.4777 0.3474 0.0347  -0.0059 0.0860  935  HOH A O   
1784 O O   . HOH Q .   ? 0.3785 0.3531 0.3969 -0.0140 0.0115  0.0308  936  HOH A O   
1785 O O   . HOH Q .   ? 0.5101 0.4289 0.3387 0.0074  -0.0406 -0.0403 937  HOH A O   
1786 O O   . HOH Q .   ? 0.3926 0.4029 0.3931 -0.0467 -0.0136 0.0051  938  HOH A O   
1787 O O   . HOH Q .   ? 0.4689 0.4631 0.3752 -0.0148 0.0015  -0.0163 939  HOH A O   
1788 O O   . HOH Q .   ? 0.4201 0.4449 0.5033 -0.0258 0.0466  0.0775  940  HOH A O   
1789 O O   . HOH Q .   ? 0.3844 0.3956 0.4802 -0.0380 0.0344  0.0842  941  HOH A O   
1790 O O   . HOH Q .   ? 0.2359 0.3960 0.3026 -0.0387 -0.0245 0.0513  942  HOH A O   
1791 O O   . HOH Q .   ? 0.3718 0.3701 0.3382 -0.0034 -0.0181 0.0167  943  HOH A O   
1792 O O   . HOH Q .   ? 0.4599 0.4620 0.3840 -0.0074 0.0050  -0.0048 944  HOH A O   
1793 O O   . HOH Q .   ? 0.3717 0.3863 0.3960 0.0008  0.0517  0.0347  945  HOH A O   
1794 O O   . HOH Q .   ? 0.4588 0.4681 0.4369 -0.0105 -0.0478 0.0340  946  HOH A O   
1795 O O   . HOH Q .   ? 0.4115 0.5116 0.3755 0.0518  0.0508  0.0315  947  HOH A O   
1796 O O   . HOH Q .   ? 0.3726 0.3804 0.3506 -0.0061 -0.0060 0.0318  948  HOH A O   
1797 O O   . HOH Q .   ? 0.4187 0.4487 0.4874 0.0127  -0.0590 0.1305  949  HOH A O   
1798 O O   . HOH Q .   ? 0.4317 0.3931 0.4929 -0.0388 0.0275  0.0938  950  HOH A O   
1799 O O   . HOH Q .   ? 0.5026 0.5135 0.4437 -0.0008 0.0024  0.0066  951  HOH A O   
1800 O O   . HOH Q .   ? 0.3873 0.3780 0.3578 -0.0544 -0.0233 -0.0154 952  HOH A O   
1801 O O   . HOH Q .   ? 0.4259 0.4203 0.4298 -0.0203 0.0011  0.0230  953  HOH A O   
1802 O O   . HOH Q .   ? 0.3500 0.4025 0.5576 0.0832  0.0924  0.0598  954  HOH A O   
1803 O O   . HOH Q .   ? 0.4107 0.3796 0.3548 0.0302  0.0057  -0.0070 955  HOH A O   
1804 O O   . HOH Q .   ? 0.5310 0.5736 0.6477 -0.0048 0.0036  0.0444  956  HOH A O   
1805 O O   . HOH Q .   ? 0.4234 0.3676 0.4917 -0.0490 -0.0132 0.0496  957  HOH A O   
1806 O O   . HOH Q .   ? 0.4184 0.3065 0.4125 0.0223  0.0504  -0.0318 958  HOH A O   
1807 O O   . HOH Q .   ? 0.4110 0.4251 0.6317 0.0690  -0.0137 0.1368  959  HOH A O   
1808 O O   . HOH Q .   ? 0.4038 0.3849 0.3663 0.0418  0.0084  0.0106  960  HOH A O   
1809 O O   . HOH Q .   ? 0.4387 0.3641 0.4232 -0.0156 0.0136  -0.0198 961  HOH A O   
1810 O O   . HOH Q .   ? 0.4639 0.3425 0.4307 -0.0152 -0.0300 -0.0084 962  HOH A O   
1811 O O   . HOH Q .   ? 0.5260 0.4126 0.5200 -0.0305 -0.0343 0.0035  963  HOH A O   
1812 O O   . HOH Q .   ? 0.4444 0.3887 0.4393 -0.0486 -0.0751 -0.0025 964  HOH A O   
1813 O O   . HOH Q .   ? 0.3681 0.4093 0.4640 0.0190  0.0635  0.0381  965  HOH A O   
1814 O O   . HOH Q .   ? 0.6023 0.4972 0.6514 0.0216  0.0331  0.0046  966  HOH A O   
1815 O O   . HOH Q .   ? 0.4443 0.4843 0.5611 0.0025  0.0008  0.0451  967  HOH A O   
1816 O O   . HOH Q .   ? 0.6334 0.5633 0.4907 -0.0160 0.0189  -0.0573 968  HOH A O   
1817 O O   . HOH Q .   ? 0.4687 0.3577 0.4406 -0.0117 0.0214  -0.0353 969  HOH A O   
1818 O O   . HOH Q .   ? 0.3012 0.5937 0.4499 0.0298  -0.0114 0.1062  970  HOH A O   
1819 O O   . HOH Q .   ? 0.4607 0.4817 0.4473 -0.0116 0.0039  0.0311  971  HOH A O   
1820 O O   . HOH Q .   ? 0.5007 0.4238 0.4916 -0.0264 0.0060  -0.0145 972  HOH A O   
1821 O O   . HOH Q .   ? 0.4847 0.4289 0.4506 0.0268  0.0053  0.0385  973  HOH A O   
1822 O O   . HOH Q .   ? 0.4973 0.5495 0.4977 -0.0186 0.0112  0.0446  974  HOH A O   
1823 O O   . HOH Q .   ? 0.3857 0.4032 0.4544 -0.0012 -0.0177 0.0375  975  HOH A O   
1824 O O   . HOH Q .   ? 0.3677 0.3602 0.3324 0.0186  0.0039  0.0135  976  HOH A O   
1825 O O   . HOH Q .   ? 0.4546 0.4855 0.5389 0.0331  0.0797  0.0290  977  HOH A O   
1826 O O   . HOH Q .   ? 0.5547 0.5011 0.5828 -0.0118 0.0046  0.0251  978  HOH A O   
1827 O O   . HOH Q .   ? 0.4092 0.5829 0.4826 -0.0216 -0.0099 0.0587  979  HOH A O   
1828 O O   . HOH Q .   ? 0.5463 0.5109 0.5093 0.0536  0.0097  0.0163  980  HOH A O   
1829 O O   . HOH Q .   ? 0.4848 0.5239 0.5609 0.0040  0.0595  0.0450  981  HOH A O   
1830 O O   . HOH Q .   ? 0.5234 0.4451 0.4449 0.0156  0.0578  -0.0458 982  HOH A O   
1831 O O   . HOH Q .   ? 0.5254 0.4692 0.3878 -0.0047 -0.0504 -0.0233 983  HOH A O   
1832 O O   . HOH Q .   ? 0.6088 0.4937 0.4207 0.0097  -0.0431 -0.0565 984  HOH A O   
1833 O O   . HOH Q .   ? 0.4902 0.4947 0.4427 -0.0006 -0.0118 0.0192  985  HOH A O   
1834 O O   . HOH Q .   ? 0.5560 0.5552 0.8026 0.0925  0.0239  0.1152  986  HOH A O   
1835 O O   . HOH Q .   ? 0.5007 0.4557 0.4284 0.0195  -0.0045 -0.0156 987  HOH A O   
1836 O O   . HOH Q .   ? 0.4184 0.5557 0.4922 -0.0579 -0.0178 0.0544  988  HOH A O   
1837 O O   . HOH Q .   ? 0.3672 0.5208 0.4338 0.1106  0.0331  0.0714  989  HOH A O   
1838 O O   . HOH Q .   ? 0.4640 0.3991 0.4355 0.0156  0.0071  0.0438  990  HOH A O   
1839 O O   . HOH Q .   ? 0.4318 0.5692 0.6741 0.0297  0.0809  0.0931  991  HOH A O   
1840 O O   . HOH Q .   ? 0.4407 0.5538 0.4721 0.0748  -0.0033 0.0709  992  HOH A O   
1841 O O   . HOH Q .   ? 0.4510 0.5274 0.6315 -0.0347 0.0026  0.0750  993  HOH A O   
1842 O O   . HOH Q .   ? 0.5272 0.4784 0.6449 0.0284  -0.0175 0.1227  994  HOH A O   
1843 O O   . HOH Q .   ? 0.4037 0.4439 0.5319 0.0119  -0.0035 0.0536  995  HOH A O   
1844 O O   . HOH Q .   ? 0.4000 0.6045 0.4656 0.0196  0.0474  0.0797  996  HOH A O   
1845 O O   . HOH Q .   ? 0.4960 0.5027 0.5142 -0.0273 -0.0629 0.0242  997  HOH A O   
1846 O O   . HOH Q .   ? 0.6913 0.6694 0.5454 -0.0220 -0.0014 -0.0336 998  HOH A O   
1847 O O   . HOH Q .   ? 0.4698 0.5121 0.7001 0.0695  0.0215  0.0967  999  HOH A O   
1848 O O   . HOH Q .   ? 0.4461 0.4050 0.4711 0.0506  0.0906  -0.0114 1000 HOH A O   
1849 O O   . HOH Q .   ? 0.5108 0.4609 0.4082 0.0245  -0.0051 -0.0229 1001 HOH A O   
1850 O O   . HOH Q .   ? 0.4068 0.3990 0.4441 -0.0320 -0.0475 0.0182  1002 HOH A O   
1851 O O   . HOH Q .   ? 0.5347 0.4621 0.5751 -0.0037 0.0092  0.0251  1003 HOH A O   
1852 O O   . HOH Q .   ? 0.5877 0.6235 0.5584 0.0330  -0.0047 0.0374  1004 HOH A O   
1853 O O   . HOH Q .   ? 0.5239 0.5299 0.5156 -0.0116 0.0007  0.0245  1005 HOH A O   
1854 O O   . HOH Q .   ? 0.4826 0.5757 0.7037 0.0728  0.1024  0.0702  1006 HOH A O   
1855 O O   . HOH Q .   ? 0.4365 0.7479 0.6025 0.0590  0.0130  0.1155  1007 HOH A O   
1856 O O   . HOH Q .   ? 0.5477 0.5801 0.6331 -0.0022 -0.0326 0.0518  1008 HOH A O   
1857 O O   . HOH Q .   ? 0.3253 0.4389 0.5875 0.0602  0.0623  0.0903  1009 HOH A O   
1858 O O   . HOH Q .   ? 0.4995 0.4248 0.5154 0.0558  0.0911  -0.0236 1010 HOH A O   
1859 O O   . HOH Q .   ? 0.4772 0.3103 0.5774 0.0403  0.0338  0.0375  1011 HOH A O   
1860 O O   . HOH Q .   ? 0.6360 0.4540 0.6400 0.0625  0.0873  -0.0484 1012 HOH A O   
1861 O O   . HOH Q .   ? 0.4940 0.4205 0.5710 -0.0784 -0.0632 0.0298  1013 HOH A O   
1862 O O   . HOH Q .   ? 0.5326 0.5464 0.4779 -0.0012 -0.0105 0.0322  1014 HOH A O   
1863 O O   . HOH Q .   ? 0.5085 0.7458 0.6145 -0.0387 -0.0494 0.0761  1015 HOH A O   
1864 O O   . HOH Q .   ? 0.4670 0.5239 0.6031 -0.0099 -0.0181 0.0547  1016 HOH A O   
1865 O O   . HOH Q .   ? 0.4186 0.4225 0.4793 0.0410  0.0830  0.0129  1017 HOH A O   
1866 O O   . HOH Q .   ? 0.4689 0.5540 0.7220 0.0784  0.0716  0.0833  1018 HOH A O   
1867 O O   . HOH Q .   ? 0.6305 0.4548 0.5721 0.0610  0.1010  -0.0734 1019 HOH A O   
1868 O O   . HOH Q .   ? 0.4425 0.4184 0.4062 0.0168  0.0056  0.0215  1020 HOH A O   
1869 O O   . HOH Q .   ? 0.4576 0.4502 0.4235 0.0291  0.0044  0.0168  1021 HOH A O   
1870 O O   . HOH Q .   ? 0.4772 0.4804 0.5901 -0.0598 -0.0440 0.0449  1022 HOH A O   
1871 O O   . HOH Q .   ? 0.6691 0.6249 0.6688 -0.0118 0.0286  0.0793  1023 HOH A O   
1872 O O   . HOH Q .   ? 0.3955 0.6007 0.4917 0.0979  0.0268  0.0855  1024 HOH A O   
1873 O O   . HOH Q .   ? 0.5396 0.5565 0.5163 -0.0078 0.0002  0.0350  1025 HOH A O   
1874 O O   . HOH Q .   ? 0.6009 0.4640 0.5694 0.0026  -0.0140 0.0073  1026 HOH A O   
1875 O O   . HOH Q .   ? 0.5778 0.5867 0.6276 0.0078  -0.0419 0.1169  1027 HOH A O   
1876 O O   . HOH Q .   ? 0.5173 0.5543 0.4358 -0.0287 -0.0291 -0.0042 1028 HOH A O   
1877 O O   . HOH Q .   ? 0.5310 0.5073 0.4909 0.0063  0.0187  0.0445  1029 HOH A O   
1878 O O   . HOH Q .   ? 0.6260 0.7208 0.8263 -0.0271 -0.0102 0.0777  1030 HOH A O   
1879 O O   . HOH Q .   ? 0.4170 0.4789 0.5698 -0.0271 -0.0120 0.0598  1031 HOH A O   
1880 O O   . HOH Q .   ? 0.5837 0.5713 0.5263 0.0200  0.0083  0.0559  1032 HOH A O   
1881 O O   . HOH Q .   ? 0.6597 0.6102 0.6772 -0.0201 0.0036  0.0171  1033 HOH A O   
1882 O O   . HOH Q .   ? 0.6616 0.5864 0.5220 -0.0374 -0.0056 -0.0633 1034 HOH A O   
1883 O O   . HOH Q .   ? 0.9175 0.8723 0.7762 -0.0095 0.0235  -0.0418 1035 HOH A O   
1884 O O   . HOH Q .   ? 0.4904 0.5058 0.4051 -0.0202 -0.0132 -0.0090 1036 HOH A O   
1885 O O   . HOH Q .   ? 0.4257 0.5046 0.6814 0.0735  0.0480  0.0912  1037 HOH A O   
1886 O O   . HOH Q .   ? 0.5679 0.5237 0.4246 -0.0418 -0.0178 -0.0521 1038 HOH A O   
1887 O O   . HOH Q .   ? 0.4654 0.7320 0.5910 0.0224  0.0340  0.0973  1039 HOH A O   
1888 O O   . HOH Q .   ? 0.6313 0.6699 0.7862 -0.0527 0.0055  0.0793  1040 HOH A O   
1889 O O   . HOH Q .   ? 0.4744 0.3834 0.4714 -0.0025 0.0240  -0.0190 1041 HOH A O   
1890 O O   . HOH Q .   ? 0.5511 0.4057 0.6130 0.0267  0.0352  0.0094  1042 HOH A O   
1891 O O   . HOH Q .   ? 0.7165 0.5938 0.5815 -0.0342 -0.0881 -0.0484 1043 HOH A O   
1892 O O   . HOH Q .   ? 0.6185 0.6121 0.6708 0.0069  -0.0353 0.1320  1044 HOH A O   
1893 O O   . HOH Q .   ? 0.6644 0.6800 0.7206 -0.0235 -0.0437 0.0298  1045 HOH A O   
1894 O O   . HOH Q .   ? 0.4902 0.4576 0.4372 0.0135  0.0550  -0.0184 1046 HOH A O   
1895 O O   . HOH Q .   ? 0.5434 0.5486 0.6283 0.0712  0.1177  0.0139  1047 HOH A O   
1896 O O   . HOH Q .   ? 0.6588 0.4778 0.7761 0.0649  0.0507  0.0328  1048 HOH A O   
1897 O O   . HOH Q .   ? 0.5108 0.5778 0.6657 -0.0098 0.0032  0.0591  1049 HOH A O   
1898 O O   . HOH Q .   ? 0.4914 0.4914 0.4174 -0.0012 0.0134  0.0036  1050 HOH A O   
1899 O O   . HOH Q .   ? 0.6965 0.6658 0.7766 0.1092  0.1549  -0.0026 1051 HOH A O   
1900 O O   . HOH Q .   ? 0.4485 0.5542 0.4773 0.1392  0.0633  0.0474  1052 HOH A O   
1901 O O   . HOH Q .   ? 0.5155 0.4751 0.4770 0.0331  0.0049  0.0526  1053 HOH A O   
1902 O O   . HOH Q .   ? 0.6189 0.6425 0.5725 -0.0026 -0.0006 0.0387  1054 HOH A O   
1903 O O   . HOH Q .   ? 0.6744 0.6012 0.6807 -0.0177 0.0093  -0.0034 1055 HOH A O   
1904 O O   . HOH Q .   ? 0.6399 0.5936 0.6660 -0.0702 -0.0976 0.0066  1056 HOH A O   
1905 O O   . HOH Q .   ? 0.5077 0.5293 0.5698 -0.0144 -0.0355 0.0348  1057 HOH A O   
1906 O O   . HOH Q .   ? 0.5699 0.4840 0.5702 -0.0699 -0.0948 -0.0072 1058 HOH A O   
1907 O O   . HOH Q .   ? 0.6217 0.5868 0.4755 0.0023  -0.0400 -0.0120 1059 HOH A O   
1908 O O   . HOH Q .   ? 0.4631 0.4852 0.5430 -0.0261 -0.0364 0.0344  1060 HOH A O   
1909 O O   . HOH Q .   ? 0.5133 0.4799 0.5184 -0.0363 -0.0586 0.0052  1061 HOH A O   
1910 O O   . HOH Q .   ? 0.6101 0.5941 0.5970 -0.0533 -0.0175 -0.0082 1062 HOH A O   
1911 O O   . HOH Q .   ? 0.5284 0.5436 0.5411 -0.0374 -0.0029 0.0233  1063 HOH A O   
1912 O O   . HOH Q .   ? 0.5161 0.5517 0.5625 -0.0108 -0.0610 0.0586  1064 HOH A O   
1913 O O   . HOH Q .   ? 0.5421 0.5829 0.5374 -0.0060 -0.0741 0.0914  1065 HOH A O   
1914 O O   . HOH Q .   ? 0.5648 0.5476 0.7798 0.1019  0.0726  0.0667  1066 HOH A O   
1915 O O   . HOH Q .   ? 0.5540 0.5511 0.5308 0.0685  0.0132  0.0274  1067 HOH A O   
1916 O O   . HOH Q .   ? 0.6242 0.6773 0.8848 0.0955  0.0646  0.0891  1068 HOH A O   
1917 O O   . HOH Q .   ? 0.5424 0.5928 0.4519 -0.1078 -0.1022 -0.0256 1069 HOH A O   
1918 O O   . HOH Q .   ? 0.5174 0.5385 0.7548 0.0904  0.0504  0.0867  1070 HOH A O   
1919 O O   . HOH Q .   ? 0.4613 0.5271 0.6947 0.0604  0.0229  0.0924  1071 HOH A O   
1920 O O   . HOH Q .   ? 0.6567 0.7550 0.6484 0.1213  0.0715  0.0304  1072 HOH A O   
1921 O O   . HOH Q .   ? 0.5501 0.6738 0.8402 0.0582  0.0245  0.1113  1073 HOH A O   
1922 O O   . HOH Q .   ? 0.4956 0.5209 0.5142 -0.0502 -0.0110 0.0203  1074 HOH A O   
1923 O O   . HOH Q .   ? 0.6496 0.4433 0.6315 -0.0829 -0.0967 -0.0226 1075 HOH A O   
1924 O O   . HOH Q .   ? 0.6449 0.6424 0.6568 -0.0322 -0.0003 0.0266  1076 HOH A O   
1925 O O   . HOH Q .   ? 0.8047 0.6740 0.9890 0.0783  0.0263  0.1024  1077 HOH A O   
1926 O O   . HOH Q .   ? 0.4674 0.5773 0.5183 -0.0796 -0.0459 0.0324  1078 HOH A O   
1927 O O   . HOH Q .   ? 0.6715 0.6530 0.6367 0.0343  0.0041  0.0259  1079 HOH A O   
1928 O O   . HOH Q .   ? 0.3199 0.5436 0.4274 -0.0117 0.0088  0.0819  1080 HOH A O   
1929 O O   . HOH Q .   ? 0.6707 0.8097 0.6769 0.0166  0.0451  0.0608  1081 HOH A O   
1930 O O   . HOH Q .   ? 0.7520 0.8140 0.6595 0.0136  0.0252  0.0508  1082 HOH A O   
1931 O O   . HOH Q .   ? 0.4718 0.4583 0.4892 -0.0275 0.0005  0.0436  1083 HOH A O   
1932 O O   . HOH Q .   ? 0.8040 0.7901 0.7791 0.0950  0.0262  0.0226  1084 HOH A O   
1933 O O   . HOH Q .   ? 0.6877 0.6685 0.5882 0.0213  -0.0011 -0.0102 1085 HOH A O   
1934 O O   . HOH Q .   ? 0.5207 0.6473 0.5845 -0.0442 0.0034  0.0625  1086 HOH A O   
1935 O O   . HOH Q .   ? 0.5972 0.6694 0.7592 -0.0303 0.0394  0.0856  1087 HOH A O   
1936 O O   . HOH Q .   ? 0.5423 0.5545 0.5836 -0.0054 0.0378  0.0351  1088 HOH A O   
1937 O O   . HOH Q .   ? 0.5092 0.5404 0.6073 0.0002  -0.0131 0.0436  1089 HOH A O   
1938 O O   . HOH Q .   ? 0.5003 0.5530 0.7078 0.0502  -0.0350 0.1356  1090 HOH A O   
1939 O O   . HOH Q .   ? 0.6307 0.5439 0.7014 -0.0578 -0.0177 0.0580  1091 HOH A O   
1940 O O   . HOH Q .   ? 0.4479 0.4650 0.4818 0.0071  0.0555  0.0278  1092 HOH A O   
1941 O O   . HOH Q .   ? 0.5218 0.5590 0.4958 0.0444  -0.0064 0.0513  1093 HOH A O   
1942 O O   . HOH Q .   ? 0.5285 0.5535 0.4578 -0.0111 -0.0104 0.0022  1094 HOH A O   
1943 O O   . HOH Q .   ? 0.5769 0.4807 0.6139 0.0020  0.0183  0.0097  1095 HOH A O   
1944 O O   . HOH Q .   ? 0.5530 0.6283 0.7115 0.0224  -0.0677 0.1309  1096 HOH A O   
1945 O O   . HOH Q .   ? 0.6926 0.6501 0.6986 -0.0210 0.0040  0.0062  1097 HOH A O   
1946 O O   . HOH Q .   ? 0.5981 0.5865 0.5084 0.0029  0.0365  -0.0034 1098 HOH A O   
1947 O O   . HOH Q .   ? 0.5787 0.6446 0.7341 0.0040  -0.0195 0.0668  1099 HOH A O   
1948 O O   . HOH Q .   ? 0.6116 0.5990 0.6545 0.0569  0.1053  0.0011  1100 HOH A O   
1949 O O   . HOH Q .   ? 0.4930 0.5569 0.5694 -0.0126 -0.0847 0.0829  1101 HOH A O   
1950 O O   . HOH Q .   ? 0.3688 0.5356 0.4522 -0.0535 -0.0251 0.0582  1102 HOH A O   
1951 O O   . HOH Q .   ? 0.6540 0.5255 0.4516 -0.0073 -0.0679 -0.0624 1103 HOH A O   
1952 O O   . HOH Q .   ? 0.5719 0.7720 0.6649 -0.0405 -0.0306 0.0655  1104 HOH A O   
1953 O O   . HOH Q .   ? 0.5266 0.4402 0.6571 0.0326  -0.0083 0.1258  1105 HOH A O   
1954 O O   . HOH Q .   ? 0.4871 0.5214 0.4377 -0.0073 -0.0107 0.0074  1106 HOH A O   
1955 O O   . HOH Q .   ? 0.5081 0.6509 0.5807 0.1288  0.0311  0.0808  1107 HOH A O   
1956 O O   . HOH Q .   ? 0.5542 0.5630 0.4920 0.0055  0.0051  0.0180  1108 HOH A O   
1957 O O   . HOH Q .   ? 0.4938 0.5371 0.4984 -0.0634 -0.0324 0.0066  1109 HOH A O   
1958 O O   . HOH Q .   ? 0.6425 0.7022 0.8149 0.0352  -0.0567 0.1414  1110 HOH A O   
1959 O O   . HOH Q .   ? 0.6341 0.7054 0.8250 -0.0516 0.0097  0.0902  1111 HOH A O   
1960 O O   . HOH Q .   ? 0.5337 0.6177 0.5939 -0.0699 -0.0167 0.0469  1112 HOH A O   
1961 O O   . HOH Q .   ? 0.7102 0.6352 0.6367 0.0452  0.0067  -0.0163 1113 HOH A O   
1962 O O   . HOH Q .   ? 0.7059 0.7364 0.6067 0.0057  -0.0024 0.0429  1114 HOH A O   
1963 O O   . HOH Q .   ? 0.4905 0.6302 0.5522 0.1040  0.0148  0.0787  1115 HOH A O   
1964 O O   . HOH Q .   ? 0.7238 0.7317 0.6084 -0.0192 -0.0102 -0.0128 1116 HOH A O   
1965 O O   . HOH Q .   ? 0.6725 0.6930 0.8145 -0.0615 -0.0290 0.0609  1117 HOH A O   
1966 O O   . HOH Q .   ? 0.6533 0.5448 0.6423 -0.0303 0.0064  -0.0217 1118 HOH A O   
1967 O O   . HOH Q .   ? 0.5950 0.6378 0.7693 -0.0777 -0.0589 0.0669  1119 HOH A O   
1968 O O   . HOH Q .   ? 0.5910 0.7997 0.6929 0.0978  0.0109  0.0960  1120 HOH A O   
1969 O O   . HOH Q .   ? 0.6267 0.6482 0.6255 0.0995  0.0217  0.0428  1121 HOH A O   
1970 O O   . HOH Q .   ? 0.5019 0.6360 0.7847 0.0724  0.0901  0.0960  1122 HOH A O   
1971 O O   . HOH Q .   ? 0.5611 0.5995 0.6591 -0.0103 -0.0301 0.0461  1123 HOH A O   
1972 O O   . HOH Q .   ? 0.7460 0.6572 0.6122 -0.0404 -0.1019 -0.0356 1124 HOH A O   
1973 O O   . HOH Q .   ? 0.8066 0.7646 0.7332 0.0309  0.0038  -0.0149 1125 HOH A O   
1974 O O   . HOH Q .   ? 0.6411 0.5300 0.6917 -0.0109 0.0085  0.0331  1126 HOH A O   
1975 O O   . HOH Q .   ? 0.6488 0.6651 0.6122 0.0233  -0.0004 0.0257  1127 HOH A O   
1976 O O   . HOH Q .   ? 0.7096 0.8118 0.6576 0.0752  0.0671  0.0278  1128 HOH A O   
1977 O O   . HOH Q .   ? 0.7451 0.6080 0.7859 0.0043  0.0230  0.0052  1129 HOH A O   
1978 O O   . HOH Q .   ? 0.5521 0.6363 0.7383 -0.0315 0.0219  0.0830  1130 HOH A O   
1979 O O   . HOH Q .   ? 0.6034 0.6460 0.7175 -0.0212 -0.0260 0.0461  1131 HOH A O   
1980 O O   . HOH Q .   ? 0.6231 0.6946 0.6975 0.0012  -0.0926 0.1223  1132 HOH A O   
1981 O O   . HOH Q .   ? 0.4026 0.5713 0.7053 0.0173  0.0370  0.1135  1133 HOH A O   
1982 O O   . HOH Q .   ? 0.5170 0.5538 0.4784 -0.0004 0.0098  0.0332  1134 HOH A O   
1983 O O   . HOH Q .   ? 0.6746 0.6744 0.6324 0.0179  0.0031  0.0243  1135 HOH A O   
1984 O O   . HOH Q .   ? 0.9369 0.9996 0.9287 -0.0162 0.0173  0.0597  1136 HOH A O   
1985 O O   . HOH Q .   ? 1.0288 1.0647 1.3116 0.1088  0.0519  0.1085  1137 HOH A O   
1986 O O   . HOH Q .   ? 0.6022 0.6303 0.5406 -0.0049 -0.0299 0.0860  1138 HOH A O   
1987 O O   . HOH Q .   ? 0.6252 0.5658 0.7101 -0.0548 0.0142  0.0990  1139 HOH A O   
1988 O O   . HOH Q .   ? 0.5706 0.7084 0.8565 0.0391  0.0165  0.1091  1140 HOH A O   
1989 O O   . HOH Q .   ? 0.8547 0.8715 0.7677 0.0031  -0.0118 0.0319  1141 HOH A O   
1990 O O   . HOH Q .   ? 0.6139 0.6186 0.5647 -0.0166 -0.0646 0.0269  1142 HOH A O   
1991 O O   . HOH Q .   ? 0.7191 0.7046 0.6345 -0.0242 -0.0803 0.0092  1143 HOH A O   
1992 O O   . HOH Q .   ? 0.6689 0.6938 0.7217 -0.0133 -0.0458 0.0409  1144 HOH A O   
1993 O O   . HOH Q .   ? 0.6543 0.6722 0.6615 0.1260  0.0327  0.0468  1145 HOH A O   
1994 O O   . HOH Q .   ? 0.5957 0.7313 0.8203 0.0220  0.0901  0.0942  1146 HOH A O   
1995 O O   . HOH Q .   ? 0.6656 0.5996 0.5096 -0.0154 -0.0716 -0.0281 1147 HOH A O   
1996 O O   . HOH Q .   ? 0.6039 0.6008 0.6162 -0.0237 0.0003  0.0567  1148 HOH A O   
1997 O O   . HOH Q .   ? 0.8319 0.7621 0.7469 0.0391  0.0039  -0.0222 1149 HOH A O   
1998 O O   . HOH Q .   ? 0.5097 0.4707 0.6661 0.0475  -0.0131 0.1241  1150 HOH A O   
1999 O O   . HOH Q .   ? 0.5972 0.6304 0.5825 -0.0150 -0.0788 0.0615  1151 HOH A O   
2000 O O   . HOH Q .   ? 0.5826 0.6402 0.7064 0.0451  0.0982  0.0437  1152 HOH A O   
2001 O O   . HOH Q .   ? 0.7428 0.5706 0.7173 -0.0994 -0.1266 -0.0299 1153 HOH A O   
2002 O O   . HOH Q .   ? 0.7440 0.6288 0.7427 0.0096  0.0362  -0.0262 1154 HOH A O   
2003 O O   . HOH Q .   ? 0.5853 0.7596 0.9048 0.0401  0.0539  0.1171  1155 HOH A O   
2004 O O   . HOH Q .   ? 0.5614 0.6443 0.7399 -0.0124 -0.0105 0.0687  1156 HOH A O   
2005 O O   . HOH Q .   ? 0.5205 0.6188 0.7107 -0.0201 0.0468  0.0896  1157 HOH A O   
2006 O O   . HOH Q .   ? 0.8392 0.8860 0.8229 -0.0619 -0.0404 -0.0007 1158 HOH A O   
2007 O O   . HOH Q .   ? 0.6452 0.6072 0.5765 -0.0412 -0.0965 -0.0053 1159 HOH A O   
2008 O O   . HOH Q .   ? 0.6793 0.6472 0.6487 0.0022  0.0229  0.0574  1160 HOH A O   
2009 O O   . HOH Q .   ? 0.6096 0.5259 0.5743 0.0364  0.0037  0.0286  1161 HOH A O   
2010 O O   . HOH Q .   ? 0.7560 0.9534 0.8670 0.1344  0.0249  0.1043  1162 HOH A O   
2011 O O   . HOH Q .   ? 0.8149 0.7901 0.7838 0.0501  0.0056  0.0320  1163 HOH A O   
2012 O O   . HOH Q .   ? 0.8843 0.8304 0.6795 0.0930  0.0497  -0.0457 1164 HOH A O   
2013 O O   . HOH Q .   ? 0.8343 0.8816 0.8712 -0.0662 -0.0190 0.0290  1165 HOH A O   
2014 O O   . HOH Q .   ? 0.6669 0.6051 0.7007 -0.0283 0.0201  0.0832  1166 HOH A O   
2015 O O   . HOH Q .   ? 0.7258 0.6237 0.7366 -0.0071 0.0186  -0.0098 1167 HOH A O   
2016 O O   . HOH Q .   ? 0.6532 0.5931 0.6192 0.0508  0.0059  0.0332  1168 HOH A O   
2017 O O   . HOH Q .   ? 0.6163 0.7180 0.6788 0.1507  0.0374  0.0793  1169 HOH A O   
2018 O O   . HOH Q .   ? 0.8036 0.7585 0.6585 -0.0235 -0.0860 -0.0140 1170 HOH A O   
2019 O O   . HOH Q .   ? 0.8842 0.6570 0.8964 0.0676  0.0873  -0.0509 1171 HOH A O   
2020 O O   . HOH Q .   ? 0.6266 0.6741 0.6645 -0.0209 -0.0870 0.0637  1172 HOH A O   
2021 O O   . HOH Q .   ? 0.6892 0.7247 0.6220 -0.0060 -0.0621 0.0905  1173 HOH A O   
2022 O O   . HOH Q .   ? 0.6279 0.7411 0.9331 0.1011  0.0902  0.1010  1174 HOH A O   
2023 O O   . HOH Q .   ? 0.7121 0.7636 0.7444 0.1464  0.0399  0.0609  1175 HOH A O   
2024 O O   . HOH Q .   ? 0.8086 0.6254 0.6840 -0.0535 -0.1039 -0.0615 1176 HOH A O   
2025 O O   . HOH Q .   ? 0.6664 0.6280 0.7766 -0.0678 -0.0208 0.0638  1177 HOH A O   
2026 O O   . HOH Q .   ? 0.6084 0.5360 0.7984 0.1295  0.1121  0.0379  1178 HOH A O   
2027 O O   . HOH Q .   ? 0.6748 0.5569 0.7359 -0.0858 -0.0719 0.0223  1179 HOH A O   
2028 O O   . HOH Q .   ? 0.7388 0.7362 0.6623 0.0526  0.0247  -0.0075 1180 HOH A O   
2029 O O   . HOH Q .   ? 0.7136 0.7461 0.6847 -0.0077 0.0065  0.0434  1181 HOH A O   
2030 O O   . HOH Q .   ? 0.4971 0.5625 0.7296 0.1045  0.1185  0.0653  1182 HOH A O   
2031 O O   . HOH Q .   ? 0.7199 0.7266 0.7296 -0.0269 0.0020  0.0381  1183 HOH A O   
2032 O O   . HOH Q .   ? 0.7653 0.8835 1.0279 0.0375  -0.0042 0.1087  1184 HOH A O   
2033 O O   . HOH Q .   ? 0.7841 0.7745 0.6700 0.1041  0.0596  -0.0186 1185 HOH A O   
2034 O O   . HOH Q .   ? 0.7189 0.6193 0.6783 0.0328  0.0010  0.0143  1186 HOH A O   
2035 O O   . HOH Q .   ? 0.9020 0.8610 0.8447 0.0411  0.0089  -0.0063 1187 HOH A O   
2036 O O   . HOH Q .   ? 0.8366 0.7717 0.7313 0.0327  -0.0010 -0.0279 1188 HOH A O   
2037 O O   . HOH Q .   ? 0.8470 0.6933 0.8320 -0.0159 -0.0225 0.0134  1189 HOH A O   
2038 O O   . HOH Q .   ? 0.6917 0.5596 0.6673 -0.0214 0.0150  -0.0359 1190 HOH A O   
2039 O O   . HOH Q .   ? 0.6964 0.6781 0.6610 0.1054  0.0360  0.0127  1191 HOH A O   
2040 O O   . HOH Q .   ? 0.6744 0.7825 0.6531 0.0965  0.0686  0.0296  1192 HOH A O   
2041 O O   . HOH Q .   ? 0.7937 0.7634 0.7673 -0.0532 -0.1036 0.0023  1193 HOH A O   
2042 O O   . HOH Q .   ? 0.6240 0.5971 0.6527 -0.0391 -0.0007 0.0459  1194 HOH A O   
2043 O O   . HOH Q .   ? 0.7143 0.5703 0.6658 0.0004  0.0364  -0.0539 1195 HOH A O   
2044 O O   . HOH Q .   ? 0.7630 0.8368 0.7098 0.0871  0.0619  0.0156  1196 HOH A O   
2045 O O   . HOH Q .   ? 0.7435 0.7248 0.6302 -0.0106 0.0133  -0.0225 1197 HOH A O   
2046 O O   . HOH Q .   ? 0.7788 0.7158 0.9892 0.1154  0.0804  0.0621  1198 HOH A O   
2047 O O   . HOH Q .   ? 0.6551 0.8433 0.7303 -0.0107 0.0283  0.0792  1199 HOH A O   
2048 O O   . HOH Q .   ? 0.7133 0.7534 0.7348 0.1646  0.0584  0.0478  1200 HOH A O   
2049 O O   . HOH Q .   ? 0.8739 0.8276 0.7605 -0.0431 -0.1112 -0.0125 1201 HOH A O   
# 
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   CYS 1   25  25  CYS CYS A . n 
A 1 2   ARG 2   26  26  ARG ARG A . n 
A 1 3   THR 3   27  27  THR THR A . n 
A 1 4   SER 4   28  28  SER SER A . n 
A 1 5   CYS 5   29  29  CYS CYS A . n 
A 1 6   PRO 6   30  30  PRO PRO A . n 
A 1 7   LEU 7   31  31  LEU LEU A . n 
A 1 8   ALA 8   32  32  ALA ALA A . n 
A 1 9   LEU 9   33  33  LEU LEU A . n 
A 1 10  ALA 10  34  34  ALA ALA A . n 
A 1 11  SER 11  35  35  SER SER A . n 
A 1 12  TYR 12  36  36  TYR TYR A . n 
A 1 13  TYR 13  37  37  TYR TYR A . n 
A 1 14  LEU 14  38  38  LEU LEU A . n 
A 1 15  GLU 15  39  39  GLU GLU A . n 
A 1 16  ASN 16  40  40  ASN ASN A . n 
A 1 17  GLY 17  41  41  GLY GLY A . n 
A 1 18  THR 18  42  42  THR THR A . n 
A 1 19  THR 19  43  43  THR THR A . n 
A 1 20  LEU 20  44  44  LEU LEU A . n 
A 1 21  SER 21  45  45  SER SER A . n 
A 1 22  VAL 22  46  46  VAL VAL A . n 
A 1 23  ILE 23  47  47  ILE ILE A . n 
A 1 24  ASN 24  48  48  ASN ASN A . n 
A 1 25  GLN 25  49  49  GLN GLN A . n 
A 1 26  ASN 26  50  50  ASN ASN A . n 
A 1 27  LEU 27  51  51  LEU LEU A . n 
A 1 28  ASN 28  52  52  ASN ASN A . n 
A 1 29  SER 29  53  53  SER SER A . n 
A 1 30  SER 30  54  54  SER SER A . n 
A 1 31  ILE 31  55  55  ILE ILE A . n 
A 1 32  ALA 32  56  56  ALA ALA A . n 
A 1 33  PRO 33  57  57  PRO PRO A . n 
A 1 34  TYR 34  58  58  TYR TYR A . n 
A 1 35  ASP 35  59  59  ASP ASP A . n 
A 1 36  GLN 36  60  60  GLN GLN A . n 
A 1 37  ILE 37  61  61  ILE ILE A . n 
A 1 38  ASN 38  62  62  ASN ASN A . n 
A 1 39  PHE 39  63  63  PHE PHE A . n 
A 1 40  ASP 40  64  64  ASP ASP A . n 
A 1 41  PRO 41  65  65  PRO PRO A . n 
A 1 42  ILE 42  66  66  ILE ILE A . n 
A 1 43  LEU 43  67  67  LEU LEU A . n 
A 1 44  ARG 44  68  68  ARG ARG A . n 
A 1 45  TYR 45  69  69  TYR TYR A . n 
A 1 46  ASN 46  70  70  ASN ASN A . n 
A 1 47  SER 47  71  71  SER SER A . n 
A 1 48  ASN 48  72  72  ASN ASN A . n 
A 1 49  ILE 49  73  73  ILE ILE A . n 
A 1 50  LYS 50  74  74  LYS LYS A . n 
A 1 51  ASP 51  75  75  ASP ASP A . n 
A 1 52  LYS 52  76  76  LYS LYS A . n 
A 1 53  ASP 53  77  77  ASP ASP A . n 
A 1 54  ARG 54  78  78  ARG ARG A . n 
A 1 55  ILE 55  79  79  ILE ILE A . n 
A 1 56  GLN 56  80  80  GLN GLN A . n 
A 1 57  MET 57  81  81  MET MET A . n 
A 1 58  GLY 58  82  82  GLY GLY A . n 
A 1 59  SER 59  83  83  SER SER A . n 
A 1 60  ARG 60  84  84  ARG ARG A . n 
A 1 61  VAL 61  85  85  VAL VAL A . n 
A 1 62  LEU 62  86  86  LEU LEU A . n 
A 1 63  VAL 63  87  87  VAL VAL A . n 
A 1 64  PRO 64  88  88  PRO PRO A . n 
A 1 65  PHE 65  89  89  PHE PHE A . n 
A 1 66  PRO 66  90  90  PRO PRO A . n 
A 1 67  CYS 67  91  91  CYS CYS A . n 
A 1 68  GLU 68  92  92  GLU GLU A . n 
A 1 69  CYS 69  93  93  CYS CYS A . n 
A 1 70  GLN 70  94  94  GLN GLN A . n 
A 1 71  PRO 71  95  95  PRO PRO A . n 
A 1 72  GLY 72  96  96  GLY GLY A . n 
A 1 73  ASP 73  97  97  ASP ASP A . n 
A 1 74  PHE 74  98  98  PHE PHE A . n 
A 1 75  LEU 75  99  99  LEU LEU A . n 
A 1 76  GLY 76  100 100 GLY GLY A . n 
A 1 77  HIS 77  101 101 HIS HIS A . n 
A 1 78  ASN 78  102 102 ASN ASN A . n 
A 1 79  PHE 79  103 103 PHE PHE A . n 
A 1 80  SER 80  104 104 SER SER A . n 
A 1 81  TYR 81  105 105 TYR TYR A . n 
A 1 82  SER 82  106 106 SER SER A . n 
A 1 83  VAL 83  107 107 VAL VAL A . n 
A 1 84  ARG 84  108 108 ARG ARG A . n 
A 1 85  GLN 85  109 109 GLN GLN A . n 
A 1 86  GLU 86  110 110 GLU GLU A . n 
A 1 87  ASP 87  111 111 ASP ASP A . n 
A 1 88  THR 88  112 112 THR THR A . n 
A 1 89  TYR 89  113 113 TYR TYR A . n 
A 1 90  GLU 90  114 114 GLU GLU A . n 
A 1 91  ARG 91  115 115 ARG ARG A . n 
A 1 92  VAL 92  116 116 VAL VAL A . n 
A 1 93  ALA 93  117 117 ALA ALA A . n 
A 1 94  ILE 94  118 118 ILE ILE A . n 
A 1 95  SER 95  119 119 SER SER A . n 
A 1 96  ASN 96  120 120 ASN ASN A . n 
A 1 97  TYR 97  121 121 TYR TYR A . n 
A 1 98  ALA 98  122 122 ALA ALA A . n 
A 1 99  ASN 99  123 123 ASN ASN A . n 
A 1 100 LEU 100 124 124 LEU LEU A . n 
A 1 101 THR 101 125 125 THR THR A . n 
A 1 102 THR 102 126 126 THR THR A . n 
A 1 103 MET 103 127 127 MET MET A . n 
A 1 104 GLU 104 128 128 GLU GLU A . n 
A 1 105 SER 105 129 129 SER SER A . n 
A 1 106 LEU 106 130 130 LEU LEU A . n 
A 1 107 GLN 107 131 131 GLN GLN A . n 
A 1 108 ALA 108 132 132 ALA ALA A . n 
A 1 109 ARG 109 133 133 ARG ARG A . n 
A 1 110 ASN 110 134 134 ASN ASN A . n 
A 1 111 PRO 111 135 135 PRO PRO A . n 
A 1 112 PHE 112 136 136 PHE PHE A . n 
A 1 113 PRO 113 137 137 PRO PRO A . n 
A 1 114 ALA 114 138 138 ALA ALA A . n 
A 1 115 THR 115 139 139 THR THR A . n 
A 1 116 ASN 116 140 140 ASN ASN A . n 
A 1 117 ILE 117 141 141 ILE ILE A . n 
A 1 118 PRO 118 142 142 PRO PRO A . n 
A 1 119 LEU 119 143 143 LEU LEU A . n 
A 1 120 SER 120 144 144 SER SER A . n 
A 1 121 ALA 121 145 145 ALA ALA A . n 
A 1 122 THR 122 146 146 THR THR A . n 
A 1 123 LEU 123 147 147 LEU LEU A . n 
A 1 124 ASN 124 148 148 ASN ASN A . n 
A 1 125 VAL 125 149 149 VAL VAL A . n 
A 1 126 LEU 126 150 150 LEU LEU A . n 
A 1 127 VAL 127 151 151 VAL VAL A . n 
A 1 128 ASN 128 152 152 ASN ASN A . n 
A 1 129 CYS 129 153 153 CYS CYS A . n 
A 1 130 SER 130 154 154 SER SER A . n 
A 1 131 CYS 131 155 155 CYS CYS A . n 
A 1 132 GLY 132 156 156 GLY GLY A . n 
A 1 133 ASP 133 157 157 ASP ASP A . n 
A 1 134 GLU 134 158 158 GLU GLU A . n 
A 1 135 SER 135 159 159 SER SER A . n 
A 1 136 VAL 136 160 160 VAL VAL A . n 
A 1 137 SER 137 161 161 SER SER A . n 
A 1 138 LYS 138 162 162 LYS LYS A . n 
A 1 139 ASP 139 163 163 ASP ASP A . n 
A 1 140 PHE 140 164 164 PHE PHE A . n 
A 1 141 GLY 141 165 165 GLY GLY A . n 
A 1 142 LEU 142 166 166 LEU LEU A . n 
A 1 143 PHE 143 167 167 PHE PHE A . n 
A 1 144 VAL 144 168 168 VAL VAL A . n 
A 1 145 THR 145 169 169 THR THR A . n 
A 1 146 TYR 146 170 170 TYR TYR A . n 
A 1 147 PRO 147 171 171 PRO PRO A . n 
A 1 148 LEU 148 172 172 LEU LEU A . n 
A 1 149 ARG 149 173 173 ARG ARG A . n 
A 1 150 PRO 150 174 174 PRO PRO A . n 
A 1 151 GLU 151 175 175 GLU GLU A . n 
A 1 152 ASP 152 176 176 ASP ASP A . n 
A 1 153 SER 153 177 177 SER SER A . n 
A 1 154 LEU 154 178 178 LEU LEU A . n 
A 1 155 SER 155 179 179 SER SER A . n 
A 1 156 SER 156 180 180 SER SER A . n 
A 1 157 ILE 157 181 181 ILE ILE A . n 
A 1 158 ALA 158 182 182 ALA ALA A . n 
A 1 159 ARG 159 183 183 ARG ARG A . n 
A 1 160 SER 160 184 184 SER SER A . n 
A 1 161 SER 161 185 185 SER SER A . n 
A 1 162 GLY 162 186 186 GLY GLY A . n 
A 1 163 VAL 163 187 187 VAL VAL A . n 
A 1 164 SER 164 188 188 SER SER A . n 
A 1 165 ALA 165 189 189 ALA ALA A . n 
A 1 166 ASP 166 190 190 ASP ASP A . n 
A 1 167 ILE 167 191 191 ILE ILE A . n 
A 1 168 LEU 168 192 192 LEU LEU A . n 
A 1 169 GLN 169 193 193 GLN GLN A . n 
A 1 170 ARG 170 194 194 ARG ARG A . n 
A 1 171 TYR 171 195 195 TYR TYR A . n 
A 1 172 ASN 172 196 196 ASN ASN A . n 
A 1 173 PRO 173 197 197 PRO PRO A . n 
A 1 174 GLY 174 198 198 GLY GLY A . n 
A 1 175 VAL 175 199 199 VAL VAL A . n 
A 1 176 ASN 176 200 200 ASN ASN A . n 
A 1 177 PHE 177 201 201 PHE PHE A . n 
A 1 178 ASN 178 202 202 ASN ASN A . n 
A 1 179 SER 179 203 203 SER SER A . n 
A 1 180 GLY 180 204 204 GLY GLY A . n 
A 1 181 ASN 181 205 205 ASN ASN A . n 
A 1 182 GLY 182 206 206 GLY GLY A . n 
A 1 183 ILE 183 207 207 ILE ILE A . n 
A 1 184 VAL 184 208 208 VAL VAL A . n 
A 1 185 TYR 185 209 209 TYR TYR A . n 
A 1 186 VAL 186 210 210 VAL VAL A . n 
A 1 187 PRO 187 211 211 PRO PRO A . n 
A 1 188 GLY 188 212 212 GLY GLY A . n 
A 1 189 ARG 189 213 213 ARG ARG A . n 
A 1 190 ASP 190 214 214 ASP ASP A . n 
A 1 191 PRO 191 215 215 PRO PRO A . n 
A 1 192 ASN 192 216 216 ASN ASN A . n 
A 1 193 GLY 193 217 217 GLY GLY A . n 
A 1 194 ALA 194 218 218 ALA ALA A . n 
A 1 195 PHE 195 219 219 PHE PHE A . n 
A 1 196 PRO 196 220 220 PRO PRO A . n 
A 1 197 PRO 197 221 221 PRO PRO A . n 
A 1 198 PHE 198 222 222 PHE PHE A . n 
A 1 199 LYS 199 223 223 LYS LYS A . n 
A 1 200 SER 200 224 224 SER SER A . n 
A 1 201 SER 201 225 ?   ?   ?   A . n 
A 1 202 LYS 202 226 ?   ?   ?   A . n 
A 1 203 GLN 203 227 ?   ?   ?   A . n 
A 1 204 ASP 204 228 ?   ?   ?   A . n 
A 1 205 GLY 205 229 ?   ?   ?   A . n 
A 1 206 VAL 206 230 ?   ?   ?   A . n 
A 1 207 HIS 207 231 ?   ?   ?   A . n 
A 1 208 HIS 208 232 ?   ?   ?   A . n 
A 1 209 HIS 209 233 ?   ?   ?   A . n 
A 1 210 HIS 210 234 ?   ?   ?   A . n 
A 1 211 HIS 211 235 ?   ?   ?   A . n 
A 1 212 HIS 212 236 ?   ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 NAG 1   801  801  NAG NAG A . 
C 2 NAG 2   802  802  NAG NAG A . 
D 2 NAG 1   803  852  NAG NAG A . 
E 2 NAG 2   804  851  NAG NAG A . 
F 2 NAG 1   805  1121 NAG NAG A . 
G 2 NAG 2   806  1122 NAG NAG A . 
H 2 NAG 1   807  3511 NAG NAG A . 
I 2 NAG 2   808  3512 NAG NAG A . 
J 3 BMA 3   809  1    BMA MAN A . 
K 3 BMA 4   810  2    BMA MAN A . 
L 4 MAN 5   811  3    MAN MAN A . 
M 2 NAG 1   812  366  NAG NAG A . 
N 2 NAG 2   813  367  NAG NAG A . 
O 2 NAG 3   814  368  NAG NAG A . 
P 2 NAG 4   815  369  NAG NAG A . 
Q 5 HOH 1   901  1    HOH HOH A . 
Q 5 HOH 2   902  2    HOH HOH A . 
Q 5 HOH 3   903  3    HOH HOH A . 
Q 5 HOH 4   904  4    HOH HOH A . 
Q 5 HOH 5   905  5    HOH HOH A . 
Q 5 HOH 6   906  6    HOH HOH A . 
Q 5 HOH 7   907  7    HOH HOH A . 
Q 5 HOH 8   908  8    HOH HOH A . 
Q 5 HOH 9   909  9    HOH HOH A . 
Q 5 HOH 10  910  10   HOH HOH A . 
Q 5 HOH 11  911  11   HOH HOH A . 
Q 5 HOH 12  912  12   HOH HOH A . 
Q 5 HOH 13  913  13   HOH HOH A . 
Q 5 HOH 14  914  14   HOH HOH A . 
Q 5 HOH 15  915  15   HOH HOH A . 
Q 5 HOH 16  916  16   HOH HOH A . 
Q 5 HOH 17  917  17   HOH HOH A . 
Q 5 HOH 18  918  18   HOH HOH A . 
Q 5 HOH 19  919  19   HOH HOH A . 
Q 5 HOH 20  920  20   HOH HOH A . 
Q 5 HOH 21  921  21   HOH HOH A . 
Q 5 HOH 22  922  22   HOH HOH A . 
Q 5 HOH 23  923  23   HOH HOH A . 
Q 5 HOH 24  924  24   HOH HOH A . 
Q 5 HOH 25  925  25   HOH HOH A . 
Q 5 HOH 26  926  26   HOH HOH A . 
Q 5 HOH 27  927  27   HOH HOH A . 
Q 5 HOH 28  928  28   HOH HOH A . 
Q 5 HOH 29  929  29   HOH HOH A . 
Q 5 HOH 30  930  30   HOH HOH A . 
Q 5 HOH 31  931  31   HOH HOH A . 
Q 5 HOH 32  932  32   HOH HOH A . 
Q 5 HOH 33  933  33   HOH HOH A . 
Q 5 HOH 34  934  34   HOH HOH A . 
Q 5 HOH 35  935  35   HOH HOH A . 
Q 5 HOH 36  936  36   HOH HOH A . 
Q 5 HOH 37  937  37   HOH HOH A . 
Q 5 HOH 38  938  38   HOH HOH A . 
Q 5 HOH 39  939  39   HOH HOH A . 
Q 5 HOH 40  940  40   HOH HOH A . 
Q 5 HOH 41  941  41   HOH HOH A . 
Q 5 HOH 42  942  42   HOH HOH A . 
Q 5 HOH 43  943  43   HOH HOH A . 
Q 5 HOH 44  944  44   HOH HOH A . 
Q 5 HOH 45  945  45   HOH HOH A . 
Q 5 HOH 46  946  46   HOH HOH A . 
Q 5 HOH 47  947  47   HOH HOH A . 
Q 5 HOH 48  948  48   HOH HOH A . 
Q 5 HOH 49  949  49   HOH HOH A . 
Q 5 HOH 50  950  50   HOH HOH A . 
Q 5 HOH 51  951  51   HOH HOH A . 
Q 5 HOH 52  952  52   HOH HOH A . 
Q 5 HOH 53  953  53   HOH HOH A . 
Q 5 HOH 54  954  54   HOH HOH A . 
Q 5 HOH 55  955  55   HOH HOH A . 
Q 5 HOH 56  956  56   HOH HOH A . 
Q 5 HOH 57  957  57   HOH HOH A . 
Q 5 HOH 58  958  58   HOH HOH A . 
Q 5 HOH 59  959  59   HOH HOH A . 
Q 5 HOH 60  960  60   HOH HOH A . 
Q 5 HOH 61  961  61   HOH HOH A . 
Q 5 HOH 62  962  62   HOH HOH A . 
Q 5 HOH 63  963  63   HOH HOH A . 
Q 5 HOH 64  964  64   HOH HOH A . 
Q 5 HOH 65  965  65   HOH HOH A . 
Q 5 HOH 66  966  66   HOH HOH A . 
Q 5 HOH 67  967  67   HOH HOH A . 
Q 5 HOH 68  968  68   HOH HOH A . 
Q 5 HOH 69  969  69   HOH HOH A . 
Q 5 HOH 70  970  70   HOH HOH A . 
Q 5 HOH 71  971  71   HOH HOH A . 
Q 5 HOH 72  972  72   HOH HOH A . 
Q 5 HOH 73  973  73   HOH HOH A . 
Q 5 HOH 74  974  74   HOH HOH A . 
Q 5 HOH 75  975  75   HOH HOH A . 
Q 5 HOH 76  976  76   HOH HOH A . 
Q 5 HOH 77  977  77   HOH HOH A . 
Q 5 HOH 78  978  78   HOH HOH A . 
Q 5 HOH 79  979  79   HOH HOH A . 
Q 5 HOH 80  980  80   HOH HOH A . 
Q 5 HOH 81  981  81   HOH HOH A . 
Q 5 HOH 82  982  82   HOH HOH A . 
Q 5 HOH 83  983  83   HOH HOH A . 
Q 5 HOH 84  984  84   HOH HOH A . 
Q 5 HOH 85  985  85   HOH HOH A . 
Q 5 HOH 86  986  86   HOH HOH A . 
Q 5 HOH 87  987  87   HOH HOH A . 
Q 5 HOH 88  988  88   HOH HOH A . 
Q 5 HOH 89  989  89   HOH HOH A . 
Q 5 HOH 90  990  90   HOH HOH A . 
Q 5 HOH 91  991  91   HOH HOH A . 
Q 5 HOH 92  992  92   HOH HOH A . 
Q 5 HOH 93  993  93   HOH HOH A . 
Q 5 HOH 94  994  94   HOH HOH A . 
Q 5 HOH 95  995  95   HOH HOH A . 
Q 5 HOH 96  996  96   HOH HOH A . 
Q 5 HOH 97  997  97   HOH HOH A . 
Q 5 HOH 98  998  98   HOH HOH A . 
Q 5 HOH 99  999  99   HOH HOH A . 
Q 5 HOH 100 1000 101  HOH HOH A . 
Q 5 HOH 101 1001 102  HOH HOH A . 
Q 5 HOH 102 1002 103  HOH HOH A . 
Q 5 HOH 103 1003 104  HOH HOH A . 
Q 5 HOH 104 1004 105  HOH HOH A . 
Q 5 HOH 105 1005 106  HOH HOH A . 
Q 5 HOH 106 1006 107  HOH HOH A . 
Q 5 HOH 107 1007 108  HOH HOH A . 
Q 5 HOH 108 1008 109  HOH HOH A . 
Q 5 HOH 109 1009 110  HOH HOH A . 
Q 5 HOH 110 1010 111  HOH HOH A . 
Q 5 HOH 111 1011 112  HOH HOH A . 
Q 5 HOH 112 1012 113  HOH HOH A . 
Q 5 HOH 113 1013 114  HOH HOH A . 
Q 5 HOH 114 1014 115  HOH HOH A . 
Q 5 HOH 115 1015 116  HOH HOH A . 
Q 5 HOH 116 1016 117  HOH HOH A . 
Q 5 HOH 117 1017 118  HOH HOH A . 
Q 5 HOH 118 1018 119  HOH HOH A . 
Q 5 HOH 119 1019 120  HOH HOH A . 
Q 5 HOH 120 1020 121  HOH HOH A . 
Q 5 HOH 121 1021 122  HOH HOH A . 
Q 5 HOH 122 1022 123  HOH HOH A . 
Q 5 HOH 123 1023 124  HOH HOH A . 
Q 5 HOH 124 1024 125  HOH HOH A . 
Q 5 HOH 125 1025 126  HOH HOH A . 
Q 5 HOH 126 1026 127  HOH HOH A . 
Q 5 HOH 127 1027 128  HOH HOH A . 
Q 5 HOH 128 1028 129  HOH HOH A . 
Q 5 HOH 129 1029 130  HOH HOH A . 
Q 5 HOH 130 1030 131  HOH HOH A . 
Q 5 HOH 131 1031 132  HOH HOH A . 
Q 5 HOH 132 1032 133  HOH HOH A . 
Q 5 HOH 133 1033 134  HOH HOH A . 
Q 5 HOH 134 1034 135  HOH HOH A . 
Q 5 HOH 135 1035 136  HOH HOH A . 
Q 5 HOH 136 1036 137  HOH HOH A . 
Q 5 HOH 137 1037 138  HOH HOH A . 
Q 5 HOH 138 1038 139  HOH HOH A . 
Q 5 HOH 139 1039 140  HOH HOH A . 
Q 5 HOH 140 1040 141  HOH HOH A . 
Q 5 HOH 141 1041 142  HOH HOH A . 
Q 5 HOH 142 1042 143  HOH HOH A . 
Q 5 HOH 143 1043 144  HOH HOH A . 
Q 5 HOH 144 1044 145  HOH HOH A . 
Q 5 HOH 145 1045 146  HOH HOH A . 
Q 5 HOH 146 1046 147  HOH HOH A . 
Q 5 HOH 147 1047 148  HOH HOH A . 
Q 5 HOH 148 1048 149  HOH HOH A . 
Q 5 HOH 149 1049 150  HOH HOH A . 
Q 5 HOH 150 1050 151  HOH HOH A . 
Q 5 HOH 151 1051 152  HOH HOH A . 
Q 5 HOH 152 1052 153  HOH HOH A . 
Q 5 HOH 153 1053 154  HOH HOH A . 
Q 5 HOH 154 1054 155  HOH HOH A . 
Q 5 HOH 155 1055 156  HOH HOH A . 
Q 5 HOH 156 1056 157  HOH HOH A . 
Q 5 HOH 157 1057 158  HOH HOH A . 
Q 5 HOH 158 1058 159  HOH HOH A . 
Q 5 HOH 159 1059 160  HOH HOH A . 
Q 5 HOH 160 1060 161  HOH HOH A . 
Q 5 HOH 161 1061 162  HOH HOH A . 
Q 5 HOH 162 1062 163  HOH HOH A . 
Q 5 HOH 163 1063 164  HOH HOH A . 
Q 5 HOH 164 1064 165  HOH HOH A . 
Q 5 HOH 165 1065 166  HOH HOH A . 
Q 5 HOH 166 1066 167  HOH HOH A . 
Q 5 HOH 167 1067 168  HOH HOH A . 
Q 5 HOH 168 1068 169  HOH HOH A . 
Q 5 HOH 169 1069 170  HOH HOH A . 
Q 5 HOH 170 1070 171  HOH HOH A . 
Q 5 HOH 171 1071 172  HOH HOH A . 
Q 5 HOH 172 1072 173  HOH HOH A . 
Q 5 HOH 173 1073 174  HOH HOH A . 
Q 5 HOH 174 1074 175  HOH HOH A . 
Q 5 HOH 175 1075 176  HOH HOH A . 
Q 5 HOH 176 1076 177  HOH HOH A . 
Q 5 HOH 177 1077 178  HOH HOH A . 
Q 5 HOH 178 1078 179  HOH HOH A . 
Q 5 HOH 179 1079 180  HOH HOH A . 
Q 5 HOH 180 1080 181  HOH HOH A . 
Q 5 HOH 181 1081 182  HOH HOH A . 
Q 5 HOH 182 1082 183  HOH HOH A . 
Q 5 HOH 183 1083 184  HOH HOH A . 
Q 5 HOH 184 1084 185  HOH HOH A . 
Q 5 HOH 185 1085 186  HOH HOH A . 
Q 5 HOH 186 1086 187  HOH HOH A . 
Q 5 HOH 187 1087 188  HOH HOH A . 
Q 5 HOH 188 1088 189  HOH HOH A . 
Q 5 HOH 189 1089 190  HOH HOH A . 
Q 5 HOH 190 1090 191  HOH HOH A . 
Q 5 HOH 191 1091 192  HOH HOH A . 
Q 5 HOH 192 1092 193  HOH HOH A . 
Q 5 HOH 193 1093 194  HOH HOH A . 
Q 5 HOH 194 1094 195  HOH HOH A . 
Q 5 HOH 195 1095 196  HOH HOH A . 
Q 5 HOH 196 1096 197  HOH HOH A . 
Q 5 HOH 197 1097 198  HOH HOH A . 
Q 5 HOH 198 1098 199  HOH HOH A . 
Q 5 HOH 199 1099 200  HOH HOH A . 
Q 5 HOH 200 1100 201  HOH HOH A . 
Q 5 HOH 201 1101 202  HOH HOH A . 
Q 5 HOH 202 1102 203  HOH HOH A . 
Q 5 HOH 203 1103 204  HOH HOH A . 
Q 5 HOH 204 1104 205  HOH HOH A . 
Q 5 HOH 205 1105 206  HOH HOH A . 
Q 5 HOH 206 1106 207  HOH HOH A . 
Q 5 HOH 207 1107 208  HOH HOH A . 
Q 5 HOH 208 1108 209  HOH HOH A . 
Q 5 HOH 209 1109 210  HOH HOH A . 
Q 5 HOH 210 1110 211  HOH HOH A . 
Q 5 HOH 211 1111 212  HOH HOH A . 
Q 5 HOH 212 1112 213  HOH HOH A . 
Q 5 HOH 213 1113 214  HOH HOH A . 
Q 5 HOH 214 1114 215  HOH HOH A . 
Q 5 HOH 215 1115 216  HOH HOH A . 
Q 5 HOH 216 1116 217  HOH HOH A . 
Q 5 HOH 217 1117 218  HOH HOH A . 
Q 5 HOH 218 1118 219  HOH HOH A . 
Q 5 HOH 219 1119 220  HOH HOH A . 
Q 5 HOH 220 1120 221  HOH HOH A . 
Q 5 HOH 221 1121 222  HOH HOH A . 
Q 5 HOH 222 1122 223  HOH HOH A . 
Q 5 HOH 223 1123 224  HOH HOH A . 
Q 5 HOH 224 1124 225  HOH HOH A . 
Q 5 HOH 225 1125 226  HOH HOH A . 
Q 5 HOH 226 1126 227  HOH HOH A . 
Q 5 HOH 227 1127 228  HOH HOH A . 
Q 5 HOH 228 1128 229  HOH HOH A . 
Q 5 HOH 229 1129 230  HOH HOH A . 
Q 5 HOH 230 1130 231  HOH HOH A . 
Q 5 HOH 231 1131 232  HOH HOH A . 
Q 5 HOH 232 1132 233  HOH HOH A . 
Q 5 HOH 233 1133 234  HOH HOH A . 
Q 5 HOH 234 1134 235  HOH HOH A . 
Q 5 HOH 235 1135 236  HOH HOH A . 
Q 5 HOH 236 1136 237  HOH HOH A . 
Q 5 HOH 237 1137 238  HOH HOH A . 
Q 5 HOH 238 1138 239  HOH HOH A . 
Q 5 HOH 239 1139 240  HOH HOH A . 
Q 5 HOH 240 1140 241  HOH HOH A . 
Q 5 HOH 241 1141 242  HOH HOH A . 
Q 5 HOH 242 1142 243  HOH HOH A . 
Q 5 HOH 243 1143 244  HOH HOH A . 
Q 5 HOH 244 1144 245  HOH HOH A . 
Q 5 HOH 245 1145 246  HOH HOH A . 
Q 5 HOH 246 1146 247  HOH HOH A . 
Q 5 HOH 247 1147 248  HOH HOH A . 
Q 5 HOH 248 1148 249  HOH HOH A . 
Q 5 HOH 249 1149 250  HOH HOH A . 
Q 5 HOH 250 1150 251  HOH HOH A . 
Q 5 HOH 251 1151 252  HOH HOH A . 
Q 5 HOH 252 1152 253  HOH HOH A . 
Q 5 HOH 253 1153 254  HOH HOH A . 
Q 5 HOH 254 1154 255  HOH HOH A . 
Q 5 HOH 255 1155 256  HOH HOH A . 
Q 5 HOH 256 1156 257  HOH HOH A . 
Q 5 HOH 257 1157 258  HOH HOH A . 
Q 5 HOH 258 1158 259  HOH HOH A . 
Q 5 HOH 259 1159 260  HOH HOH A . 
Q 5 HOH 260 1160 261  HOH HOH A . 
Q 5 HOH 261 1161 262  HOH HOH A . 
Q 5 HOH 262 1162 263  HOH HOH A . 
Q 5 HOH 263 1163 264  HOH HOH A . 
Q 5 HOH 264 1164 265  HOH HOH A . 
Q 5 HOH 265 1165 266  HOH HOH A . 
Q 5 HOH 266 1166 267  HOH HOH A . 
Q 5 HOH 267 1167 268  HOH HOH A . 
Q 5 HOH 268 1168 269  HOH HOH A . 
Q 5 HOH 269 1169 270  HOH HOH A . 
Q 5 HOH 270 1170 271  HOH HOH A . 
Q 5 HOH 271 1171 272  HOH HOH A . 
Q 5 HOH 272 1172 273  HOH HOH A . 
Q 5 HOH 273 1173 274  HOH HOH A . 
Q 5 HOH 274 1174 275  HOH HOH A . 
Q 5 HOH 275 1175 276  HOH HOH A . 
Q 5 HOH 276 1176 277  HOH HOH A . 
Q 5 HOH 277 1177 278  HOH HOH A . 
Q 5 HOH 278 1178 279  HOH HOH A . 
Q 5 HOH 279 1179 280  HOH HOH A . 
Q 5 HOH 280 1180 281  HOH HOH A . 
Q 5 HOH 281 1181 282  HOH HOH A . 
Q 5 HOH 282 1182 283  HOH HOH A . 
Q 5 HOH 283 1183 284  HOH HOH A . 
Q 5 HOH 284 1184 285  HOH HOH A . 
Q 5 HOH 285 1185 286  HOH HOH A . 
Q 5 HOH 286 1186 287  HOH HOH A . 
Q 5 HOH 287 1187 288  HOH HOH A . 
Q 5 HOH 288 1188 289  HOH HOH A . 
Q 5 HOH 289 1189 290  HOH HOH A . 
Q 5 HOH 290 1190 291  HOH HOH A . 
Q 5 HOH 291 1191 292  HOH HOH A . 
Q 5 HOH 292 1192 293  HOH HOH A . 
Q 5 HOH 293 1193 294  HOH HOH A . 
Q 5 HOH 294 1194 295  HOH HOH A . 
Q 5 HOH 295 1195 296  HOH HOH A . 
Q 5 HOH 296 1196 297  HOH HOH A . 
Q 5 HOH 297 1197 298  HOH HOH A . 
Q 5 HOH 298 1198 299  HOH HOH A . 
Q 5 HOH 299 1199 300  HOH HOH A . 
Q 5 HOH 300 1200 301  HOH HOH A . 
Q 5 HOH 301 1201 302  HOH HOH A . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A ASN 78  A ASN 102 ? ASN 'GLYCOSYLATION SITE' 
2 A ASN 99  A ASN 123 ? ASN 'GLYCOSYLATION SITE' 
3 A ASN 28  A ASN 52  ? ASN 'GLYCOSYLATION SITE' 
4 A ASN 128 A ASN 152 ? ASN 'GLYCOSYLATION SITE' 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_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,G,H,I,J,K,L,M,N,O,P,Q 
# 
_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 
# 
_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       2012-06-27 
# 
_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_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         2.5195 
_pdbx_refine_tls.origin_y         -10.3461 
_pdbx_refine_tls.origin_z         -9.3712 
_pdbx_refine_tls.T[1][1]          0.1499 
_pdbx_refine_tls.T[2][2]          0.1399 
_pdbx_refine_tls.T[3][3]          0.1414 
_pdbx_refine_tls.T[1][2]          -0.0032 
_pdbx_refine_tls.T[1][3]          0.0038 
_pdbx_refine_tls.T[2][3]          0.0028 
_pdbx_refine_tls.L[1][1]          1.2729 
_pdbx_refine_tls.L[2][2]          1.2623 
_pdbx_refine_tls.L[3][3]          1.2198 
_pdbx_refine_tls.L[1][2]          -0.0522 
_pdbx_refine_tls.L[1][3]          0.0355 
_pdbx_refine_tls.L[2][3]          -0.5569 
_pdbx_refine_tls.S[1][1]          0.0132 
_pdbx_refine_tls.S[1][2]          0.0131 
_pdbx_refine_tls.S[1][3]          0.0753 
_pdbx_refine_tls.S[2][1]          0.0118 
_pdbx_refine_tls.S[2][2]          0.0160 
_pdbx_refine_tls.S[2][3]          0.1202 
_pdbx_refine_tls.S[3][1]          -0.0162 
_pdbx_refine_tls.S[3][2]          0.0330 
_pdbx_refine_tls.S[3][3]          -0.0195 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_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   ALL 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
HKL-2000 'data collection' .                          ? 1 
DM       'model building'  .                          ? 2 
PHENIX   refinement        '(phenix.refine: dev_596)' ? 3 
HKL-2000 'data reduction'  .                          ? 4 
HKL-2000 'data scaling'    .                          ? 5 
DM       phasing           .                          ? 6 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              68 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              68 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              68 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                117.19 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            -3.11 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    GLN 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     60 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             72.45 
_pdbx_validate_torsion.psi             -7.17 
# 
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 SER 225 ? A SER 201 
2  1 Y 1 A LYS 226 ? A LYS 202 
3  1 Y 1 A GLN 227 ? A GLN 203 
4  1 Y 1 A ASP 228 ? A ASP 204 
5  1 Y 1 A GLY 229 ? A GLY 205 
6  1 Y 1 A VAL 230 ? A VAL 206 
7  1 Y 1 A HIS 231 ? A HIS 207 
8  1 Y 1 A HIS 232 ? A HIS 208 
9  1 Y 1 A HIS 233 ? A HIS 209 
10 1 Y 1 A HIS 234 ? A HIS 210 
11 1 Y 1 A HIS 235 ? A HIS 211 
12 1 Y 1 A HIS 236 ? A HIS 212 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE NAG 
3 BETA-D-MANNOSE         BMA 
4 ALPHA-D-MANNOSE        MAN 
5 water                  HOH 
# 



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.