HEADER VIRAL PROTEIN/IMMUNE SYSTEM 19-JUN-24 9CBN TITLE HASTV1 SPIKE IN COMPLEX WITH NEUTRALIZING FABS 3H4 AND 3B4 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HASTV1 NEUTRALIZING FAB 3B4 HEAVY CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HASTV1 NEUTRALIZING FAB 3B4 KAPPA CHAIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: STRUCTURAL PROTEIN; COMPND 11 CHAIN: C, D; COMPND 12 SYNONYM: SPIKE; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: HASTV1 NEUTRALIZING FAB 3H4 HEAVY CHAIN; COMPND 16 CHAIN: E, G; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 5; COMPND 19 MOLECULE: HASTV1 NEUTRALIZING FAB 3H4 LAMBDA CHAIN; COMPND 20 CHAIN: F, H; COMPND 21 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 STRAIN: BALB/C; SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: CHO-S; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 12 ORGANISM_COMMON: MOUSE; SOURCE 13 ORGANISM_TAXID: 10090; SOURCE 14 STRAIN: BALB/C; SOURCE 15 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 16 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: CHO-S; SOURCE 19 MOL_ID: 3; SOURCE 20 ORGANISM_SCIENTIFIC: HUMAN ASTROVIRUS 1; SOURCE 21 ORGANISM_TAXID: 12456; SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 23 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 24 MOL_ID: 4; SOURCE 25 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 26 ORGANISM_COMMON: MOUSE; SOURCE 27 ORGANISM_TAXID: 10090; SOURCE 28 STRAIN: BALB/C; SOURCE 29 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 30 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 31 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 32 EXPRESSION_SYSTEM_CELL_LINE: CHO-S; SOURCE 33 MOL_ID: 5; SOURCE 34 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 35 ORGANISM_COMMON: MOUSE; SOURCE 36 ORGANISM_TAXID: 10090; SOURCE 37 STRAIN: BALB/C; SOURCE 38 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 39 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 40 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 41 EXPRESSION_SYSTEM_CELL_LINE: CHO-S KEYWDS ANTIBODY, VIRUS, SPIKE, HOMODIMER, VIRAL PROTEIN-IMMUNE SYSTEM KEYWDS 2 COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR S.LANNING,R.M.DUBOIS,V.H.BALASCO SERRAO REVDAT 1 25-DEC-24 9CBN 0 JRNL AUTH S.LANNING,R.M.DUBOIS,V.H.BALASCO SERRAO,C.F.ARIAS JRNL TITL STRUCTURAL TECHNIQUES REVEAL 3 NOVEL NEUTRALIZING ANTIBODY JRNL TITL 2 EPITOPES ON THE HUMAN ASTROVIRUS SPIKE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.33 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 5EWO REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : 112.000 REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.330 REMARK 3 NUMBER OF PARTICLES : 163237 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9CBN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-24. REMARK 100 THE DEPOSITION ID IS D_1000284956. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : HUMAN ASTROVIRUS 1 SPIKE IN REMARK 245 COMPLEX WITH FAB 3B4 AND FAB REMARK 245 3H4; HASTV1 NEUTRALIZING FAB REMARK 245 3B4; RECOMBINANT HUMAN REMARK 245 ASTROVIRUS SEROTYPE 1 SPIKE REMARK 245 PROTEIN; HASTV1 NEUTRALIZING REMARK 245 FAB 3H4 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.86 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 8.00 REMARK 245 SAMPLE DETAILS : RECOMBINANT FAB EXPRESSED IN REMARK 245 CHO-S CELLS REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 7235 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOCONTINUUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 3226.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLN A 1 REMARK 465 LEU A 11 REMARK 465 VAL A 12 REMARK 465 LYS A 13 REMARK 465 PRO A 41 REMARK 465 GLY A 42 REMARK 465 GLN A 43 REMARK 465 GLU A 89 REMARK 465 ASP A 90 REMARK 465 VAL A 114 REMARK 465 SER A 115 REMARK 465 SER A 116 REMARK 465 ALA A 117 REMARK 465 SER A 118 REMARK 465 THR A 119 REMARK 465 LYS A 120 REMARK 465 GLY A 121 REMARK 465 PRO A 122 REMARK 465 SER A 123 REMARK 465 VAL A 124 REMARK 465 PHE A 125 REMARK 465 PRO A 126 REMARK 465 LEU A 127 REMARK 465 ALA A 128 REMARK 465 PRO A 129 REMARK 465 SER A 130 REMARK 465 SER A 131 REMARK 465 LYS A 132 REMARK 465 SER A 133 REMARK 465 THR A 134 REMARK 465 SER A 135 REMARK 465 GLY A 136 REMARK 465 GLY A 137 REMARK 465 THR A 138 REMARK 465 ALA A 139 REMARK 465 ALA A 140 REMARK 465 LEU A 141 REMARK 465 GLY A 142 REMARK 465 CYS A 143 REMARK 465 LEU A 144 REMARK 465 VAL A 145 REMARK 465 LYS A 146 REMARK 465 ASP A 147 REMARK 465 TYR A 148 REMARK 465 PHE A 149 REMARK 465 PRO A 150 REMARK 465 GLU A 151 REMARK 465 PRO A 152 REMARK 465 VAL A 153 REMARK 465 THR A 154 REMARK 465 VAL A 155 REMARK 465 SER A 156 REMARK 465 TRP A 157 REMARK 465 ASN A 158 REMARK 465 SER A 159 REMARK 465 GLY A 160 REMARK 465 ALA A 161 REMARK 465 LEU A 162 REMARK 465 THR A 163 REMARK 465 SER A 164 REMARK 465 GLY A 165 REMARK 465 VAL A 166 REMARK 465 HIS A 167 REMARK 465 THR A 168 REMARK 465 PHE A 169 REMARK 465 PRO A 170 REMARK 465 ALA A 171 REMARK 465 VAL A 172 REMARK 465 LEU A 173 REMARK 465 GLN A 174 REMARK 465 SER A 175 REMARK 465 SER A 176 REMARK 465 GLY A 177 REMARK 465 LEU A 178 REMARK 465 TYR A 179 REMARK 465 SER A 180 REMARK 465 LEU A 181 REMARK 465 SER A 182 REMARK 465 SER A 183 REMARK 465 VAL A 184 REMARK 465 VAL A 185 REMARK 465 THR A 186 REMARK 465 VAL A 187 REMARK 465 PRO A 188 REMARK 465 SER A 189 REMARK 465 SER A 190 REMARK 465 SER A 191 REMARK 465 LEU A 192 REMARK 465 GLY A 193 REMARK 465 THR A 194 REMARK 465 GLN A 195 REMARK 465 THR A 196 REMARK 465 TYR A 197 REMARK 465 ILE A 198 REMARK 465 CYS A 199 REMARK 465 ASN A 200 REMARK 465 VAL A 201 REMARK 465 ASN A 202 REMARK 465 HIS A 203 REMARK 465 LYS A 204 REMARK 465 PRO A 205 REMARK 465 SER A 206 REMARK 465 ASN A 207 REMARK 465 THR A 208 REMARK 465 LYS A 209 REMARK 465 VAL A 210 REMARK 465 ASP A 211 REMARK 465 LYS A 212 REMARK 465 LYS A 213 REMARK 465 VAL A 214 REMARK 465 GLU A 215 REMARK 465 PRO A 216 REMARK 465 LYS A 217 REMARK 465 SER A 218 REMARK 465 CYS A 219 REMARK 465 ALA A 220 REMARK 465 SER A 221 REMARK 465 LEU A 222 REMARK 465 VAL A 223 REMARK 465 PRO A 224 REMARK 465 ARG A 225 REMARK 465 ASP B 1 REMARK 465 PRO B 8 REMARK 465 ALA B 9 REMARK 465 THR B 10 REMARK 465 LEU B 11 REMARK 465 SER B 12 REMARK 465 VAL B 13 REMARK 465 THR B 14 REMARK 465 PRO B 15 REMARK 465 GLY B 16 REMARK 465 ASP B 17 REMARK 465 SER B 18 REMARK 465 GLN B 38 REMARK 465 LYS B 39 REMARK 465 SER B 40 REMARK 465 HIS B 41 REMARK 465 SER B 77 REMARK 465 VAL B 78 REMARK 465 GLU B 79 REMARK 465 THR B 80 REMARK 465 GLU B 81 REMARK 465 ASP B 82 REMARK 465 PHE B 83 REMARK 465 GLY B 101 REMARK 465 THR B 102 REMARK 465 LYS B 103 REMARK 465 LEU B 104 REMARK 465 ASP B 105 REMARK 465 LEU B 106 REMARK 465 LYS B 107 REMARK 465 ARG B 108 REMARK 465 ARG B 109 REMARK 465 THR B 110 REMARK 465 VAL B 111 REMARK 465 ALA B 112 REMARK 465 ALA B 113 REMARK 465 PRO B 114 REMARK 465 SER B 115 REMARK 465 VAL B 116 REMARK 465 PHE B 117 REMARK 465 ILE B 118 REMARK 465 PHE B 119 REMARK 465 PRO B 120 REMARK 465 PRO B 121 REMARK 465 SER B 122 REMARK 465 ASP B 123 REMARK 465 GLU B 124 REMARK 465 GLN B 125 REMARK 465 LEU B 126 REMARK 465 LYS B 127 REMARK 465 SER B 128 REMARK 465 GLY B 129 REMARK 465 THR B 130 REMARK 465 ALA B 131 REMARK 465 SER B 132 REMARK 465 VAL B 133 REMARK 465 VAL B 134 REMARK 465 CYS B 135 REMARK 465 LEU B 136 REMARK 465 LEU B 137 REMARK 465 ASN B 138 REMARK 465 ASN B 139 REMARK 465 PHE B 140 REMARK 465 TYR B 141 REMARK 465 PRO B 142 REMARK 465 ARG B 143 REMARK 465 GLU B 144 REMARK 465 ALA B 145 REMARK 465 LYS B 146 REMARK 465 VAL B 147 REMARK 465 GLN B 148 REMARK 465 TRP B 149 REMARK 465 LYS B 150 REMARK 465 VAL B 151 REMARK 465 ASP B 152 REMARK 465 ASN B 153 REMARK 465 ALA B 154 REMARK 465 LEU B 155 REMARK 465 GLN B 156 REMARK 465 SER B 157 REMARK 465 GLY B 158 REMARK 465 ASN B 159 REMARK 465 SER B 160 REMARK 465 GLN B 161 REMARK 465 GLU B 162 REMARK 465 SER B 163 REMARK 465 VAL B 164 REMARK 465 THR B 165 REMARK 465 GLU B 166 REMARK 465 GLN B 167 REMARK 465 ASP B 168 REMARK 465 SER B 169 REMARK 465 LYS B 170 REMARK 465 ASP B 171 REMARK 465 SER B 172 REMARK 465 THR B 173 REMARK 465 TYR B 174 REMARK 465 SER B 175 REMARK 465 LEU B 176 REMARK 465 SER B 177 REMARK 465 SER B 178 REMARK 465 THR B 179 REMARK 465 LEU B 180 REMARK 465 THR B 181 REMARK 465 LEU B 182 REMARK 465 SER B 183 REMARK 465 LYS B 184 REMARK 465 ALA B 185 REMARK 465 ASP B 186 REMARK 465 TYR B 187 REMARK 465 GLU B 188 REMARK 465 LYS B 189 REMARK 465 HIS B 190 REMARK 465 LYS B 191 REMARK 465 VAL B 192 REMARK 465 TYR B 193 REMARK 465 ALA B 194 REMARK 465 CYS B 195 REMARK 465 GLU B 196 REMARK 465 VAL B 197 REMARK 465 THR B 198 REMARK 465 HIS B 199 REMARK 465 GLN B 200 REMARK 465 GLY B 201 REMARK 465 LEU B 202 REMARK 465 SER B 203 REMARK 465 SER B 204 REMARK 465 PRO B 205 REMARK 465 VAL B 206 REMARK 465 THR B 207 REMARK 465 LYS B 208 REMARK 465 SER B 209 REMARK 465 PHE B 210 REMARK 465 ASN B 211 REMARK 465 ARG B 212 REMARK 465 GLY B 213 REMARK 465 GLU B 214 REMARK 465 MET C 428 REMARK 465 GLY C 429 REMARK 465 GLU C 430 REMARK 465 ALA C 599 REMARK 465 GLY C 603 REMARK 465 PRO C 645 REMARK 465 ALA C 646 REMARK 465 ALA C 647 REMARK 465 ALA C 648 REMARK 465 GLU C 649 REMARK 465 LEU C 650 REMARK 465 ALA C 651 REMARK 465 LEU C 652 REMARK 465 VAL C 653 REMARK 465 PRO C 654 REMARK 465 ARG C 655 REMARK 465 MET D 428 REMARK 465 GLY D 429 REMARK 465 GLU D 430 REMARK 465 PRO D 602 REMARK 465 GLY D 603 REMARK 465 PRO D 645 REMARK 465 ALA D 646 REMARK 465 ALA D 647 REMARK 465 ALA D 648 REMARK 465 GLU D 649 REMARK 465 LEU D 650 REMARK 465 ALA D 651 REMARK 465 LEU D 652 REMARK 465 VAL D 653 REMARK 465 PRO D 654 REMARK 465 ARG D 655 REMARK 465 GLY E 42 REMARK 465 LYS E 43 REMARK 465 SER E 118 REMARK 465 SER E 119 REMARK 465 ALA E 120 REMARK 465 SER E 121 REMARK 465 THR E 122 REMARK 465 LYS E 123 REMARK 465 GLY E 124 REMARK 465 PRO E 125 REMARK 465 SER E 126 REMARK 465 VAL E 127 REMARK 465 PHE E 128 REMARK 465 PRO E 129 REMARK 465 LEU E 130 REMARK 465 ALA E 131 REMARK 465 PRO E 132 REMARK 465 SER E 133 REMARK 465 SER E 134 REMARK 465 LYS E 135 REMARK 465 SER E 136 REMARK 465 THR E 137 REMARK 465 SER E 138 REMARK 465 GLY E 139 REMARK 465 GLY E 140 REMARK 465 THR E 141 REMARK 465 ALA E 142 REMARK 465 ALA E 143 REMARK 465 LEU E 144 REMARK 465 GLY E 145 REMARK 465 CYS E 146 REMARK 465 LEU E 147 REMARK 465 VAL E 148 REMARK 465 LYS E 149 REMARK 465 ASP E 150 REMARK 465 TYR E 151 REMARK 465 PHE E 152 REMARK 465 PRO E 153 REMARK 465 GLU E 154 REMARK 465 PRO E 155 REMARK 465 VAL E 156 REMARK 465 THR E 157 REMARK 465 VAL E 158 REMARK 465 SER E 159 REMARK 465 TRP E 160 REMARK 465 ASN E 161 REMARK 465 SER E 162 REMARK 465 GLY E 163 REMARK 465 ALA E 164 REMARK 465 LEU E 165 REMARK 465 THR E 166 REMARK 465 SER E 167 REMARK 465 GLY E 168 REMARK 465 VAL E 169 REMARK 465 HIS E 170 REMARK 465 THR E 171 REMARK 465 PHE E 172 REMARK 465 PRO E 173 REMARK 465 ALA E 174 REMARK 465 VAL E 175 REMARK 465 LEU E 176 REMARK 465 GLN E 177 REMARK 465 SER E 178 REMARK 465 SER E 179 REMARK 465 GLY E 180 REMARK 465 LEU E 181 REMARK 465 TYR E 182 REMARK 465 SER E 183 REMARK 465 LEU E 184 REMARK 465 SER E 185 REMARK 465 SER E 186 REMARK 465 VAL E 187 REMARK 465 VAL E 188 REMARK 465 THR E 189 REMARK 465 VAL E 190 REMARK 465 PRO E 191 REMARK 465 SER E 192 REMARK 465 SER E 193 REMARK 465 SER E 194 REMARK 465 LEU E 195 REMARK 465 GLY E 196 REMARK 465 THR E 197 REMARK 465 GLN E 198 REMARK 465 THR E 199 REMARK 465 TYR E 200 REMARK 465 ILE E 201 REMARK 465 CYS E 202 REMARK 465 ASN E 203 REMARK 465 VAL E 204 REMARK 465 ASN E 205 REMARK 465 HIS E 206 REMARK 465 LYS E 207 REMARK 465 PRO E 208 REMARK 465 SER E 209 REMARK 465 ASN E 210 REMARK 465 THR E 211 REMARK 465 LYS E 212 REMARK 465 VAL E 213 REMARK 465 ASP E 214 REMARK 465 LYS E 215 REMARK 465 LYS E 216 REMARK 465 VAL E 217 REMARK 465 GLU E 218 REMARK 465 PRO E 219 REMARK 465 LYS E 220 REMARK 465 SER E 221 REMARK 465 CYS E 222 REMARK 465 ALA E 223 REMARK 465 SER E 224 REMARK 465 LEU E 225 REMARK 465 VAL E 226 REMARK 465 PRO E 227 REMARK 465 ARG E 228 REMARK 465 PRO F 14 REMARK 465 GLY F 15 REMARK 465 GLU F 16 REMARK 465 ASP F 43 REMARK 465 ALA F 62 REMARK 465 GLY F 79 REMARK 465 ALA F 80 REMARK 465 GLN F 81 REMARK 465 THR F 107 REMARK 465 VAL F 108 REMARK 465 LEU F 109 REMARK 465 GLY F 110 REMARK 465 ARG F 111 REMARK 465 THR F 112 REMARK 465 VAL F 113 REMARK 465 ALA F 114 REMARK 465 ALA F 115 REMARK 465 PRO F 116 REMARK 465 SER F 117 REMARK 465 VAL F 118 REMARK 465 PHE F 119 REMARK 465 ILE F 120 REMARK 465 PHE F 121 REMARK 465 PRO F 122 REMARK 465 PRO F 123 REMARK 465 SER F 124 REMARK 465 ASP F 125 REMARK 465 GLU F 126 REMARK 465 GLN F 127 REMARK 465 LEU F 128 REMARK 465 LYS F 129 REMARK 465 SER F 130 REMARK 465 GLY F 131 REMARK 465 THR F 132 REMARK 465 ALA F 133 REMARK 465 SER F 134 REMARK 465 VAL F 135 REMARK 465 VAL F 136 REMARK 465 CYS F 137 REMARK 465 LEU F 138 REMARK 465 LEU F 139 REMARK 465 ASN F 140 REMARK 465 ASN F 141 REMARK 465 PHE F 142 REMARK 465 TYR F 143 REMARK 465 PRO F 144 REMARK 465 ARG F 145 REMARK 465 GLU F 146 REMARK 465 ALA F 147 REMARK 465 LYS F 148 REMARK 465 VAL F 149 REMARK 465 GLN F 150 REMARK 465 TRP F 151 REMARK 465 LYS F 152 REMARK 465 VAL F 153 REMARK 465 ASP F 154 REMARK 465 ASN F 155 REMARK 465 ALA F 156 REMARK 465 LEU F 157 REMARK 465 GLN F 158 REMARK 465 SER F 159 REMARK 465 GLY F 160 REMARK 465 ASN F 161 REMARK 465 SER F 162 REMARK 465 GLN F 163 REMARK 465 GLU F 164 REMARK 465 SER F 165 REMARK 465 VAL F 166 REMARK 465 THR F 167 REMARK 465 GLU F 168 REMARK 465 GLN F 169 REMARK 465 ASP F 170 REMARK 465 SER F 171 REMARK 465 LYS F 172 REMARK 465 ASP F 173 REMARK 465 SER F 174 REMARK 465 THR F 175 REMARK 465 TYR F 176 REMARK 465 SER F 177 REMARK 465 LEU F 178 REMARK 465 SER F 179 REMARK 465 SER F 180 REMARK 465 THR F 181 REMARK 465 LEU F 182 REMARK 465 THR F 183 REMARK 465 LEU F 184 REMARK 465 SER F 185 REMARK 465 LYS F 186 REMARK 465 ALA F 187 REMARK 465 ASP F 188 REMARK 465 TYR F 189 REMARK 465 GLU F 190 REMARK 465 LYS F 191 REMARK 465 HIS F 192 REMARK 465 LYS F 193 REMARK 465 VAL F 194 REMARK 465 TYR F 195 REMARK 465 ALA F 196 REMARK 465 CYS F 197 REMARK 465 GLU F 198 REMARK 465 VAL F 199 REMARK 465 THR F 200 REMARK 465 HIS F 201 REMARK 465 GLN F 202 REMARK 465 GLY F 203 REMARK 465 LEU F 204 REMARK 465 SER F 205 REMARK 465 SER F 206 REMARK 465 PRO F 207 REMARK 465 VAL F 208 REMARK 465 THR F 209 REMARK 465 LYS F 210 REMARK 465 SER F 211 REMARK 465 PHE F 212 REMARK 465 ASN F 213 REMARK 465 ARG F 214 REMARK 465 GLY F 215 REMARK 465 GLU F 216 REMARK 465 CYS F 217 REMARK 465 ALA G 120 REMARK 465 SER G 121 REMARK 465 THR G 122 REMARK 465 LYS G 123 REMARK 465 GLY G 124 REMARK 465 PRO G 125 REMARK 465 SER G 126 REMARK 465 VAL G 127 REMARK 465 PHE G 128 REMARK 465 PRO G 129 REMARK 465 LEU G 130 REMARK 465 ALA G 131 REMARK 465 PRO G 132 REMARK 465 SER G 133 REMARK 465 SER G 134 REMARK 465 LYS G 135 REMARK 465 SER G 136 REMARK 465 THR G 137 REMARK 465 SER G 138 REMARK 465 GLY G 139 REMARK 465 GLY G 140 REMARK 465 THR G 141 REMARK 465 ALA G 142 REMARK 465 ALA G 143 REMARK 465 LEU G 144 REMARK 465 GLY G 145 REMARK 465 CYS G 146 REMARK 465 LEU G 147 REMARK 465 VAL G 148 REMARK 465 LYS G 149 REMARK 465 ASP G 150 REMARK 465 TYR G 151 REMARK 465 PHE G 152 REMARK 465 PRO G 153 REMARK 465 GLU G 154 REMARK 465 PRO G 155 REMARK 465 VAL G 156 REMARK 465 THR G 157 REMARK 465 VAL G 158 REMARK 465 SER G 159 REMARK 465 TRP G 160 REMARK 465 ASN G 161 REMARK 465 SER G 162 REMARK 465 GLY G 163 REMARK 465 ALA G 164 REMARK 465 LEU G 165 REMARK 465 THR G 166 REMARK 465 SER G 167 REMARK 465 GLY G 168 REMARK 465 VAL G 169 REMARK 465 HIS G 170 REMARK 465 THR G 171 REMARK 465 PHE G 172 REMARK 465 PRO G 173 REMARK 465 ALA G 174 REMARK 465 VAL G 175 REMARK 465 LEU G 176 REMARK 465 GLN G 177 REMARK 465 SER G 178 REMARK 465 SER G 179 REMARK 465 GLY G 180 REMARK 465 LEU G 181 REMARK 465 TYR G 182 REMARK 465 SER G 183 REMARK 465 LEU G 184 REMARK 465 SER G 185 REMARK 465 SER G 186 REMARK 465 VAL G 187 REMARK 465 VAL G 188 REMARK 465 THR G 189 REMARK 465 VAL G 190 REMARK 465 PRO G 191 REMARK 465 SER G 192 REMARK 465 SER G 193 REMARK 465 SER G 194 REMARK 465 LEU G 195 REMARK 465 GLY G 196 REMARK 465 THR G 197 REMARK 465 GLN G 198 REMARK 465 THR G 199 REMARK 465 TYR G 200 REMARK 465 ILE G 201 REMARK 465 CYS G 202 REMARK 465 ASN G 203 REMARK 465 VAL G 204 REMARK 465 ASN G 205 REMARK 465 HIS G 206 REMARK 465 LYS G 207 REMARK 465 PRO G 208 REMARK 465 SER G 209 REMARK 465 ASN G 210 REMARK 465 THR G 211 REMARK 465 LYS G 212 REMARK 465 VAL G 213 REMARK 465 ASP G 214 REMARK 465 LYS G 215 REMARK 465 LYS G 216 REMARK 465 VAL G 217 REMARK 465 GLU G 218 REMARK 465 PRO G 219 REMARK 465 LYS G 220 REMARK 465 SER G 221 REMARK 465 CYS G 222 REMARK 465 ALA G 223 REMARK 465 SER G 224 REMARK 465 LEU G 225 REMARK 465 VAL G 226 REMARK 465 PRO G 227 REMARK 465 ARG G 228 REMARK 465 GLN H 1 REMARK 465 GLY H 15 REMARK 465 GLU H 16 REMARK 465 THR H 82 REMARK 465 ASP H 83 REMARK 465 LEU H 109 REMARK 465 GLY H 110 REMARK 465 ARG H 111 REMARK 465 THR H 112 REMARK 465 VAL H 113 REMARK 465 ALA H 114 REMARK 465 ALA H 115 REMARK 465 PRO H 116 REMARK 465 SER H 117 REMARK 465 VAL H 118 REMARK 465 PHE H 119 REMARK 465 ILE H 120 REMARK 465 PHE H 121 REMARK 465 PRO H 122 REMARK 465 PRO H 123 REMARK 465 SER H 124 REMARK 465 ASP H 125 REMARK 465 GLU H 126 REMARK 465 GLN H 127 REMARK 465 LEU H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 GLY H 131 REMARK 465 THR H 132 REMARK 465 ALA H 133 REMARK 465 SER H 134 REMARK 465 VAL H 135 REMARK 465 VAL H 136 REMARK 465 CYS H 137 REMARK 465 LEU H 138 REMARK 465 LEU H 139 REMARK 465 ASN H 140 REMARK 465 ASN H 141 REMARK 465 PHE H 142 REMARK 465 TYR H 143 REMARK 465 PRO H 144 REMARK 465 ARG H 145 REMARK 465 GLU H 146 REMARK 465 ALA H 147 REMARK 465 LYS H 148 REMARK 465 VAL H 149 REMARK 465 GLN H 150 REMARK 465 TRP H 151 REMARK 465 LYS H 152 REMARK 465 VAL H 153 REMARK 465 ASP H 154 REMARK 465 ASN H 155 REMARK 465 ALA H 156 REMARK 465 LEU H 157 REMARK 465 GLN H 158 REMARK 465 SER H 159 REMARK 465 GLY H 160 REMARK 465 ASN H 161 REMARK 465 SER H 162 REMARK 465 GLN H 163 REMARK 465 GLU H 164 REMARK 465 SER H 165 REMARK 465 VAL H 166 REMARK 465 THR H 167 REMARK 465 GLU H 168 REMARK 465 GLN H 169 REMARK 465 ASP H 170 REMARK 465 SER H 171 REMARK 465 LYS H 172 REMARK 465 ASP H 173 REMARK 465 SER H 174 REMARK 465 THR H 175 REMARK 465 TYR H 176 REMARK 465 SER H 177 REMARK 465 LEU H 178 REMARK 465 SER H 179 REMARK 465 SER H 180 REMARK 465 THR H 181 REMARK 465 LEU H 182 REMARK 465 THR H 183 REMARK 465 LEU H 184 REMARK 465 SER H 185 REMARK 465 LYS H 186 REMARK 465 ALA H 187 REMARK 465 ASP H 188 REMARK 465 TYR H 189 REMARK 465 GLU H 190 REMARK 465 LYS H 191 REMARK 465 HIS H 192 REMARK 465 LYS H 193 REMARK 465 VAL H 194 REMARK 465 TYR H 195 REMARK 465 ALA H 196 REMARK 465 CYS H 197 REMARK 465 GLU H 198 REMARK 465 VAL H 199 REMARK 465 THR H 200 REMARK 465 HIS H 201 REMARK 465 GLN H 202 REMARK 465 GLY H 203 REMARK 465 LEU H 204 REMARK 465 SER H 205 REMARK 465 SER H 206 REMARK 465 PRO H 207 REMARK 465 VAL H 208 REMARK 465 THR H 209 REMARK 465 LYS H 210 REMARK 465 SER H 211 REMARK 465 PHE H 212 REMARK 465 ASN H 213 REMARK 465 ARG H 214 REMARK 465 GLY H 215 REMARK 465 GLU H 216 REMARK 465 CYS H 217 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 VAL A 2 CG1 CG2 REMARK 470 HIS A 5 CG ND1 CD2 CE1 NE2 REMARK 470 GLN A 6 CG CD OE1 NE2 REMARK 470 SER A 25 OG REMARK 470 ARG A 40 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 46 CG CD OE1 OE2 REMARK 470 ASN A 52 CG OD1 ND2 REMARK 470 SER A 55 OG REMARK 470 ARG A 57 CG CD NE CZ NH1 NH2 REMARK 470 ASN A 66 CG OD1 ND2 REMARK 470 THR A 71 OG1 CG2 REMARK 470 LYS A 74 CG CD CE NZ REMARK 470 SER A 75 OG REMARK 470 SER A 85 OG REMARK 470 LEU A 86 CG CD1 CD2 REMARK 470 THR A 87 OG1 CG2 REMARK 470 SER A 91 OG REMARK 470 ASP A 104 CG OD1 OD2 REMARK 470 GLN A 108 CG CD OE1 NE2 REMARK 470 VAL B 3 CG1 CG2 REMARK 470 THR B 5 OG1 CG2 REMARK 470 SER B 7 OG REMARK 470 VAL B 19 CG1 CG2 REMARK 470 SER B 20 OG REMARK 470 SER B 22 OG REMARK 470 ARG B 24 CG CD NE CZ NH1 NH2 REMARK 470 SER B 26 OG REMARK 470 SER B 28 OG REMARK 470 GLN B 37 CG CD OE1 NE2 REMARK 470 GLU B 42 CG CD OE1 OE2 REMARK 470 ARG B 45 CG CD NE CZ NH1 NH2 REMARK 470 SER B 52 OG REMARK 470 SER B 54 OG REMARK 470 ASP B 70 CG OD1 OD2 REMARK 470 SER B 74 OG REMARK 470 GLN B 89 CG CD OE1 NE2 REMARK 470 THR B 97 OG1 CG2 REMARK 470 THR B 100 OG1 CG2 REMARK 470 SER C 440 OG REMARK 470 ASP C 458 CG OD1 OD2 REMARK 470 SER C 461 OG REMARK 470 HIS C 463 CG ND1 CD2 CE1 NE2 REMARK 470 ASN C 465 CG OD1 ND2 REMARK 470 ASP C 471 CG OD1 OD2 REMARK 470 VAL C 472 CG1 CG2 REMARK 470 ASP C 473 CG OD1 OD2 REMARK 470 GLN C 495 CG CD OE1 NE2 REMARK 470 GLU C 498 CG CD OE1 OE2 REMARK 470 ASP C 517 CG OD1 OD2 REMARK 470 ASN C 530 CG OD1 ND2 REMARK 470 ASN C 531 CG OD1 ND2 REMARK 470 GLN C 548 CG CD OE1 NE2 REMARK 470 ASP C 564 CG OD1 OD2 REMARK 470 ASP C 597 CG OD1 OD2 REMARK 470 GLU C 632 CG CD OE1 OE2 REMARK 470 SER D 443 OG REMARK 470 SER D 461 OG REMARK 470 ASP D 473 CG OD1 OD2 REMARK 470 SER D 486 OG REMARK 470 GLN D 495 CG CD OE1 NE2 REMARK 470 ILE D 512 CG1 CG2 CD1 REMARK 470 ASN D 530 CG OD1 ND2 REMARK 470 ASN D 531 CG OD1 ND2 REMARK 470 ASP D 564 CG OD1 OD2 REMARK 470 ASP D 574 CG OD1 OD2 REMARK 470 SER D 581 OG REMARK 470 GLN E 1 CG CD OE1 NE2 REMARK 470 GLN E 3 CG CD OE1 NE2 REMARK 470 SER E 7 OG REMARK 470 LEU E 11 CG CD1 CD2 REMARK 470 SER E 15 OG REMARK 470 SER E 25 OG REMARK 470 SER E 61 OG REMARK 470 ASP E 72 CG OD1 OD2 REMARK 470 ARG E 75 CG CD NE CZ NH1 NH2 REMARK 470 GLN E 86 CG CD OE1 NE2 REMARK 470 GLU F 7 CG CD OE1 OE2 REMARK 470 SER F 8 OG REMARK 470 THR F 11 OG1 CG2 REMARK 470 ARG F 23 CG CD NE CZ NH1 NH2 REMARK 470 GLU F 40 CG CD OE1 OE2 REMARK 470 LEU F 45 CG CD1 CD2 REMARK 470 SER F 65 OG REMARK 470 ASP F 71 CG OD1 OD2 REMARK 470 THR F 82 OG1 CG2 REMARK 470 ASP F 83 CG OD1 OD2 REMARK 470 ASP F 84 CG OD1 OD2 REMARK 470 GLU F 85 CG CD OE1 OE2 REMARK 470 LYS F 105 CG CD CE NZ REMARK 470 GLN G 1 CG CD OE1 NE2 REMARK 470 GLN G 3 CG CD OE1 NE2 REMARK 470 LYS G 5 CG CD CE NZ REMARK 470 LEU G 11 CG CD1 CD2 REMARK 470 SER G 15 OG REMARK 470 GLN G 16 CG CD OE1 NE2 REMARK 470 SER G 17 OG REMARK 470 SER G 28 OG REMARK 470 GLU G 46 CG CD OE1 OE2 REMARK 470 THR G 62 OG1 CG2 REMARK 470 LYS G 64 CG CD CE NZ REMARK 470 SER G 65 OG REMARK 470 ASP G 72 CG OD1 OD2 REMARK 470 ARG G 75 CG CD NE CZ NH1 NH2 REMARK 470 ASN G 83 CG OD1 ND2 REMARK 470 SER G 84 OG REMARK 470 GLN G 86 CG CD OE1 NE2 REMARK 470 GLN G 111 CG CD OE1 NE2 REMARK 470 GLN H 6 CG CD OE1 NE2 REMARK 470 GLU H 7 CG CD OE1 OE2 REMARK 470 THR H 21 OG1 CG2 REMARK 470 ARG H 23 CG CD NE CZ NH1 NH2 REMARK 470 ASP H 43 CG OD1 OD2 REMARK 470 ASN H 54 CG OD1 ND2 REMARK 470 ARG H 63 CG CD NE CZ NH1 NH2 REMARK 470 SER H 65 OG REMARK 470 SER H 67 OG REMARK 470 LEU H 68 CG CD1 CD2 REMARK 470 ILE H 69 CG1 CG2 CD1 REMARK 470 ASP H 71 CG OD1 OD2 REMARK 470 LYS H 72 CG CD CE NZ REMARK 470 THR H 78 OG1 CG2 REMARK 470 GLN H 81 CG CD OE1 NE2 REMARK 470 ASP H 84 CG OD1 OD2 REMARK 470 GLU H 85 CG CD OE1 OE2 REMARK 470 SER H 95 OG REMARK 470 THR H 104 OG1 CG2 REMARK 470 LYS H 105 CG CD CE NZ REMARK 470 THR H 107 OG1 CG2 REMARK 470 VAL H 108 CG1 CG2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 HD22 ASN D 445 HE1 PHE D 481 1.19 REMARK 500 HE1 TRP D 604 CD1 TRP D 606 1.28 REMARK 500 HE1 TRP D 604 NE1 TRP D 606 1.30 REMARK 500 HD22 ASN D 445 CE1 PHE D 481 1.50 REMARK 500 SG CYS B 23 SG CYS B 88 1.79 REMARK 500 OH TYR A 60 N LEU A 70 1.88 REMARK 500 NE1 TRP D 604 NE1 TRP D 606 1.99 REMARK 500 O SER F 65 OG1 THR F 76 2.04 REMARK 500 NE1 TRP D 604 CD1 TRP D 606 2.06 REMARK 500 CD PRO E 40 OE1 GLU E 46 2.07 REMARK 500 OG1 THR H 17 O ILE H 77 2.10 REMARK 500 O LEU G 29 NZ LYS G 71 2.11 REMARK 500 CA THR B 91 CD2 LEU B 96 2.13 REMARK 500 NE2 HIS G 35 OE2 GLU G 98 2.14 REMARK 500 O GLY F 51 ND2 ASN F 55 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 GLY E 10 C LEU E 11 N 0.239 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 TYR A 94 N - CA - CB ANGL. DEV. = -19.2 DEGREES REMARK 500 TYR A 94 N - CA - C ANGL. DEV. = 49.9 DEGREES REMARK 500 TYR A 95 CB - CA - C ANGL. DEV. = -14.0 DEGREES REMARK 500 TYR A 95 N - CA - CB ANGL. DEV. = -19.1 DEGREES REMARK 500 MET A 103 CB - CA - C ANGL. DEV. = -15.8 DEGREES REMARK 500 MET A 103 N - CA - CB ANGL. DEV. = 13.5 DEGREES REMARK 500 MET A 103 N - CA - C ANGL. DEV. = 27.3 DEGREES REMARK 500 ASP A 104 CB - CA - C ANGL. DEV. = 15.1 DEGREES REMARK 500 ASP A 104 N - CA - CB ANGL. DEV. = -12.5 DEGREES REMARK 500 TYR A 105 N - CA - CB ANGL. DEV. = -22.9 DEGREES REMARK 500 TYR A 105 N - CA - C ANGL. DEV. = 18.5 DEGREES REMARK 500 VAL C 510 N - CA - C ANGL. DEV. = -17.9 DEGREES REMARK 500 ALA E 54 CB - CA - C ANGL. DEV. = -15.4 DEGREES REMARK 500 PHE F 94 CB - CA - C ANGL. DEV. = 33.7 DEGREES REMARK 500 PHE F 94 N - CA - C ANGL. DEV. = -28.8 DEGREES REMARK 500 SER F 95 CB - CA - C ANGL. DEV. = 24.8 DEGREES REMARK 500 SER F 95 N - CA - CB ANGL. DEV. = -29.1 DEGREES REMARK 500 ASN F 96 N - CA - CB ANGL. DEV. = -20.1 DEGREES REMARK 500 TYR G 59 CB - CA - C ANGL. DEV. = 12.8 DEGREES REMARK 500 ASN G 60 CB - CA - C ANGL. DEV. = -31.6 DEGREES REMARK 500 ASN G 60 N - CA - C ANGL. DEV. = -26.1 DEGREES REMARK 500 SER G 61 N - CA - CB ANGL. DEV. = -17.5 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 TYR A 32 25.10 -140.86 REMARK 500 SER A 55 -14.12 75.04 REMARK 500 ASN A 66 -5.28 73.84 REMARK 500 ALA A 102 155.38 177.30 REMARK 500 MET A 103 24.67 45.44 REMARK 500 SER B 30 -126.35 56.47 REMARK 500 ALA B 51 -5.81 74.85 REMARK 500 THR B 69 -15.90 -141.36 REMARK 500 MET B 85 -121.50 41.81 REMARK 500 ASN C 511 -145.51 57.46 REMARK 500 ALA C 559 -169.95 -78.48 REMARK 500 TRP C 606 35.11 -99.84 REMARK 500 ASN C 614 30.02 70.60 REMARK 500 MET C 628 135.30 -170.80 REMARK 500 SER C 633 9.83 80.05 REMARK 500 ASN D 448 31.50 -98.51 REMARK 500 TYR D 475 142.09 -170.41 REMARK 500 THR D 491 -177.54 -68.47 REMARK 500 ASN D 511 -123.04 62.68 REMARK 500 ALA E 91 -178.73 -178.04 REMARK 500 TYR E 100 24.07 47.16 REMARK 500 ALA F 2 -169.09 -118.93 REMARK 500 THR F 53 -10.63 82.54 REMARK 500 PRO G 40 173.02 -58.55 REMARK 500 PHE G 104 -1.87 73.80 REMARK 500 THR H 53 -8.58 75.90 REMARK 500 ASN H 54 -32.00 -131.80 REMARK 500 SER H 67 -175.25 -171.01 REMARK 500 SER H 95 -12.56 72.55 REMARK 500 LYS H 105 60.31 65.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG I 1 REMARK 610 NAG J 2 REMARK 610 BMA J 3 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-45427 RELATED DB: EMDB REMARK 900 HASTV1 SPIKE IN COMPLEX WITH NEUTRALIZING FABS 3H4 AND 3B4 DBREF 9CBN A 1 225 PDB 9CBN 9CBN 1 225 DBREF 9CBN B 1 214 PDB 9CBN 9CBN 1 214 DBREF 9CBN C 429 645 UNP Q82452 Q82452_HASV1 429 645 DBREF 9CBN D 429 645 UNP Q82452 Q82452_HASV1 429 645 DBREF 9CBN E 1 228 PDB 9CBN 9CBN 1 228 DBREF 9CBN F 1 217 PDB 9CBN 9CBN 1 217 DBREF 9CBN G 1 228 PDB 9CBN 9CBN 1 228 DBREF 9CBN H 1 217 PDB 9CBN 9CBN 1 217 SEQADV 9CBN MET C 428 UNP Q82452 INITIATING METHIONINE SEQADV 9CBN ALA C 646 UNP Q82452 EXPRESSION TAG SEQADV 9CBN ALA C 647 UNP Q82452 EXPRESSION TAG SEQADV 9CBN ALA C 648 UNP Q82452 EXPRESSION TAG SEQADV 9CBN GLU C 649 UNP Q82452 EXPRESSION TAG SEQADV 9CBN LEU C 650 UNP Q82452 EXPRESSION TAG SEQADV 9CBN ALA C 651 UNP Q82452 EXPRESSION TAG SEQADV 9CBN LEU C 652 UNP Q82452 EXPRESSION TAG SEQADV 9CBN VAL C 653 UNP Q82452 EXPRESSION TAG SEQADV 9CBN PRO C 654 UNP Q82452 EXPRESSION TAG SEQADV 9CBN ARG C 655 UNP Q82452 EXPRESSION TAG SEQADV 9CBN MET D 428 UNP Q82452 INITIATING METHIONINE SEQADV 9CBN ALA D 646 UNP Q82452 EXPRESSION TAG SEQADV 9CBN ALA D 647 UNP Q82452 EXPRESSION TAG SEQADV 9CBN ALA D 648 UNP Q82452 EXPRESSION TAG SEQADV 9CBN GLU D 649 UNP Q82452 EXPRESSION TAG SEQADV 9CBN LEU D 650 UNP Q82452 EXPRESSION TAG SEQADV 9CBN ALA D 651 UNP Q82452 EXPRESSION TAG SEQADV 9CBN LEU D 652 UNP Q82452 EXPRESSION TAG SEQADV 9CBN VAL D 653 UNP Q82452 EXPRESSION TAG SEQADV 9CBN PRO D 654 UNP Q82452 EXPRESSION TAG SEQADV 9CBN ARG D 655 UNP Q82452 EXPRESSION TAG SEQRES 1 A 225 GLN VAL GLN LEU HIS GLN PRO GLY ALA GLU LEU VAL LYS SEQRES 2 A 225 PRO GLY ALA SER VAL ASN LEU SER CYS LYS ALA SER GLY SEQRES 3 A 225 TYR THR PHE THR SER TYR TRP MET HIS TRP VAL LYS GLN SEQRES 4 A 225 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY GLU ILE ASN SEQRES 5 A 225 PRO SER SER GLY ARG ALA ASN TYR ASN GLU LYS PHE LYS SEQRES 6 A 225 ASN LYS ALA THR LEU THR VAL ASP LYS SER SER ILE THR SEQRES 7 A 225 ALA TYR MET HIS LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 A 225 ALA VAL TYR TYR CYS HIS TRP ASP TYR TYR ALA MET ASP SEQRES 9 A 225 TYR TRP GLY GLN GLY THR SER VAL THR VAL SER SER ALA SEQRES 10 A 225 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 11 A 225 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 12 A 225 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 13 A 225 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 14 A 225 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 15 A 225 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 16 A 225 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 17 A 225 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ALA SER SEQRES 18 A 225 LEU VAL PRO ARG SEQRES 1 B 214 ASP ILE VAL LEU THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 B 214 THR PRO GLY ASP SER VAL SER LEU SER CYS ARG ALA SER SEQRES 3 B 214 GLN SER ILE SER ASN ASN LEU HIS TRP TYR GLN GLN LYS SEQRES 4 B 214 SER HIS GLU SER PRO ARG LEU LEU PHE LYS SER ALA SER SEQRES 5 B 214 GLN SER ILE SER GLY ILE PRO SER ARG PHE SER GLY SER SEQRES 6 B 214 GLY SER GLY THR ASP PHE THR LEU SER ILE ASN SER VAL SEQRES 7 B 214 GLU THR GLU ASP PHE GLY MET TYR PHE CYS GLN GLN THR SEQRES 8 B 214 ASN SER TRP PRO LEU THR PHE GLY THR GLY THR LYS LEU SEQRES 9 B 214 ASP LEU LYS ARG ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 B 214 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 B 214 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 B 214 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 B 214 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 B 214 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 B 214 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 B 214 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 B 214 SER PHE ASN ARG GLY GLU SEQRES 1 C 228 MET GLY GLU GLU TYR LYS VAL VAL LEU THR PHE GLY SER SEQRES 2 C 228 PRO MET SER PRO ASN ALA ASN ASN LYS GLN THR TRP VAL SEQRES 3 C 228 ASN LYS PRO LEU ASP ALA PRO SER GLY HIS TYR ASN VAL SEQRES 4 C 228 LYS ILE ALA LYS ASP VAL ASP HIS TYR LEU THR MET GLN SEQRES 5 C 228 GLY PHE THR SER ILE ALA SER VAL ASP TRP TYR THR ILE SEQRES 6 C 228 ASP PHE GLN PRO SER GLU ALA PRO ALA PRO ILE LYS GLY SEQRES 7 C 228 LEU GLN VAL LEU VAL ASN ILE SER LYS LYS ALA ASP VAL SEQRES 8 C 228 TYR ALA VAL LYS GLN PHE VAL THR ALA GLN THR ASN ASN SEQRES 9 C 228 LYS HIS GLN VAL THR SER LEU PHE LEU VAL LYS VAL THR SEQRES 10 C 228 THR GLY PHE GLN VAL ASN ASN TYR LEU SER TYR PHE TYR SEQRES 11 C 228 ARG ALA SER ALA THR GLY ASP ALA THR THR ASN LEU LEU SEQRES 12 C 228 VAL ARG GLY ASP THR TYR THR ALA GLY ILE SER PHE THR SEQRES 13 C 228 GLN GLY GLY TRP TYR LEU LEU THR ASN THR SER ILE VAL SEQRES 14 C 228 ASP GLY ALA MET PRO PRO GLY TRP VAL TRP ASN ASN VAL SEQRES 15 C 228 GLU LEU LYS THR ASN THR ALA TYR HIS MET ASP LYS GLY SEQRES 16 C 228 LEU VAL HIS LEU ILE MET PRO LEU PRO GLU SER THR GLN SEQRES 17 C 228 MET CYS TYR GLU MET LEU THR SER ILE PRO ALA ALA ALA SEQRES 18 C 228 GLU LEU ALA LEU VAL PRO ARG SEQRES 1 D 228 MET GLY GLU GLU TYR LYS VAL VAL LEU THR PHE GLY SER SEQRES 2 D 228 PRO MET SER PRO ASN ALA ASN ASN LYS GLN THR TRP VAL SEQRES 3 D 228 ASN LYS PRO LEU ASP ALA PRO SER GLY HIS TYR ASN VAL SEQRES 4 D 228 LYS ILE ALA LYS ASP VAL ASP HIS TYR LEU THR MET GLN SEQRES 5 D 228 GLY PHE THR SER ILE ALA SER VAL ASP TRP TYR THR ILE SEQRES 6 D 228 ASP PHE GLN PRO SER GLU ALA PRO ALA PRO ILE LYS GLY SEQRES 7 D 228 LEU GLN VAL LEU VAL ASN ILE SER LYS LYS ALA ASP VAL SEQRES 8 D 228 TYR ALA VAL LYS GLN PHE VAL THR ALA GLN THR ASN ASN SEQRES 9 D 228 LYS HIS GLN VAL THR SER LEU PHE LEU VAL LYS VAL THR SEQRES 10 D 228 THR GLY PHE GLN VAL ASN ASN TYR LEU SER TYR PHE TYR SEQRES 11 D 228 ARG ALA SER ALA THR GLY ASP ALA THR THR ASN LEU LEU SEQRES 12 D 228 VAL ARG GLY ASP THR TYR THR ALA GLY ILE SER PHE THR SEQRES 13 D 228 GLN GLY GLY TRP TYR LEU LEU THR ASN THR SER ILE VAL SEQRES 14 D 228 ASP GLY ALA MET PRO PRO GLY TRP VAL TRP ASN ASN VAL SEQRES 15 D 228 GLU LEU LYS THR ASN THR ALA TYR HIS MET ASP LYS GLY SEQRES 16 D 228 LEU VAL HIS LEU ILE MET PRO LEU PRO GLU SER THR GLN SEQRES 17 D 228 MET CYS TYR GLU MET LEU THR SER ILE PRO ALA ALA ALA SEQRES 18 D 228 GLU LEU ALA LEU VAL PRO ARG SEQRES 1 E 228 GLN VAL GLN LEU LYS GLU SER GLY PRO GLY LEU VAL ALA SEQRES 2 E 228 PRO SER GLN SER LEU SER ILE SER CYS THR VAL SER GLY SEQRES 3 E 228 PHE SER LEU THR THR PHE GLY ILE HIS TRP ILE ARG GLN SEQRES 4 E 228 PRO PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL ILE TRP SEQRES 5 E 228 ALA ALA GLY THR THR ASN TYR ASN SER THR LEU LYS SER SEQRES 6 E 228 ARG LEU THR ILE THR LYS ASP ASN SER ARG SER GLN VAL SEQRES 7 E 228 PHE LEU LYS MET ASN SER LEU GLN THR TYR ASP THR ALA SEQRES 8 E 228 ILE TYR TYR CYS VAL ARG GLU ASP TYR ASP TYR PHE PHE SEQRES 9 E 228 GLY LEU ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SEQRES 10 E 228 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11 E 228 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12 E 228 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 E 228 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14 E 228 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 E 228 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 E 228 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17 E 228 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 18 E 228 CYS ALA SER LEU VAL PRO ARG SEQRES 1 F 217 GLN ALA VAL VAL THR GLN GLU SER ALA LEU THR THR SER SEQRES 2 F 217 PRO GLY GLU THR VAL THR LEU THR CYS ARG SER SER THR SEQRES 3 F 217 GLY ALA VAL THR THR SER ASN TYR ALA SER TRP VAL GLN SEQRES 4 F 217 GLU LYS PRO ASP HIS LEU PHE ILE GLY LEU ILE GLY GLY SEQRES 5 F 217 THR ASN ASN ARG ALA PRO GLY VAL PRO ALA ARG PHE SER SEQRES 6 F 217 GLY SER LEU ILE GLY ASP LYS ALA ALA LEU THR ILE THR SEQRES 7 F 217 GLY ALA GLN THR ASP ASP GLU ALA ILE TYR PHE CYS ALA SEQRES 8 F 217 LEU TRP PHE SER ASN HIS TRP VAL PHE GLY GLY GLY THR SEQRES 9 F 217 LYS LEU THR VAL LEU GLY ARG THR VAL ALA ALA PRO SER SEQRES 10 F 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER SEQRES 11 F 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR SEQRES 12 F 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA SEQRES 13 F 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN SEQRES 14 F 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU SEQRES 15 F 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR SEQRES 16 F 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL SEQRES 17 F 217 THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 G 228 GLN VAL GLN LEU LYS GLU SER GLY PRO GLY LEU VAL ALA SEQRES 2 G 228 PRO SER GLN SER LEU SER ILE SER CYS THR VAL SER GLY SEQRES 3 G 228 PHE SER LEU THR THR PHE GLY ILE HIS TRP ILE ARG GLN SEQRES 4 G 228 PRO PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL ILE TRP SEQRES 5 G 228 ALA ALA GLY THR THR ASN TYR ASN SER THR LEU LYS SER SEQRES 6 G 228 ARG LEU THR ILE THR LYS ASP ASN SER ARG SER GLN VAL SEQRES 7 G 228 PHE LEU LYS MET ASN SER LEU GLN THR TYR ASP THR ALA SEQRES 8 G 228 ILE TYR TYR CYS VAL ARG GLU ASP TYR ASP TYR PHE PHE SEQRES 9 G 228 GLY LEU ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SEQRES 10 G 228 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11 G 228 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12 G 228 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 G 228 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14 G 228 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 G 228 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 G 228 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17 G 228 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 18 G 228 CYS ALA SER LEU VAL PRO ARG SEQRES 1 H 217 GLN ALA VAL VAL THR GLN GLU SER ALA LEU THR THR SER SEQRES 2 H 217 PRO GLY GLU THR VAL THR LEU THR CYS ARG SER SER THR SEQRES 3 H 217 GLY ALA VAL THR THR SER ASN TYR ALA SER TRP VAL GLN SEQRES 4 H 217 GLU LYS PRO ASP HIS LEU PHE ILE GLY LEU ILE GLY GLY SEQRES 5 H 217 THR ASN ASN ARG ALA PRO GLY VAL PRO ALA ARG PHE SER SEQRES 6 H 217 GLY SER LEU ILE GLY ASP LYS ALA ALA LEU THR ILE THR SEQRES 7 H 217 GLY ALA GLN THR ASP ASP GLU ALA ILE TYR PHE CYS ALA SEQRES 8 H 217 LEU TRP PHE SER ASN HIS TRP VAL PHE GLY GLY GLY THR SEQRES 9 H 217 LYS LEU THR VAL LEU GLY ARG THR VAL ALA ALA PRO SER SEQRES 10 H 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER SEQRES 11 H 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR SEQRES 12 H 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA SEQRES 13 H 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN SEQRES 14 H 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU SEQRES 15 H 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR SEQRES 16 H 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL SEQRES 17 H 217 THR LYS SER PHE ASN ARG GLY GLU CYS HET NAG I 1 14 HET NAG I 2 14 HET BMA I 3 11 HET NAG J 1 14 HET NAG J 2 13 HET BMA J 3 6 HET NAG A 301 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 9 NAG 5(C8 H15 N O6) FORMUL 9 BMA 2(C6 H12 O6) HELIX 1 AA1 ASN A 61 LYS A 65 5 5 HELIX 2 AA2 LEU C 623 ILE C 627 5 5 HELIX 3 AA3 ASP D 620 VAL D 624 5 5 HELIX 4 AA4 SER E 61 LYS E 64 5 4 HELIX 5 AA5 THR F 30 TYR F 34 5 5 HELIX 6 AA6 GLN G 86 THR G 90 5 5 HELIX 7 AA7 THR H 30 TYR H 34 5 5 SHEET 1 AA1 3 GLN A 3 HIS A 5 0 SHEET 2 AA1 3 VAL A 18 SER A 25 -1 O LYS A 23 N HIS A 5 SHEET 3 AA1 3 ALA A 79 LEU A 83 -1 O ALA A 79 N CYS A 22 SHEET 1 AA2 2 VAL A 37 LYS A 38 0 SHEET 2 AA2 2 GLU A 46 TRP A 47 -1 O GLU A 46 N LYS A 38 SHEET 1 AA3 4 THR B 5 SER B 7 0 SHEET 2 AA3 4 SER B 20 ARG B 24 -1 O ARG B 24 N THR B 5 SHEET 3 AA3 4 ASP B 70 ILE B 75 -1 O LEU B 73 N LEU B 21 SHEET 4 AA3 4 PHE B 62 SER B 65 -1 N SER B 63 O SER B 74 SHEET 1 AA4 4 GLN B 53 SER B 54 0 SHEET 2 AA4 4 ARG B 45 LYS B 49 -1 N LYS B 49 O GLN B 53 SHEET 3 AA4 4 LEU B 33 GLN B 37 -1 N GLN B 37 O ARG B 45 SHEET 4 AA4 4 PHE B 87 GLN B 90 -1 O PHE B 87 N TYR B 36 SHEET 1 AA5 7 GLN C 507 LEU C 509 0 SHEET 2 AA5 7 LYS C 514 THR C 529 -1 O ALA C 516 N VAL C 508 SHEET 3 AA5 7 LYS C 532 VAL C 543 -1 O GLN C 534 N THR C 526 SHEET 4 AA5 7 TRP C 587 ASP C 597 -1 O SER C 594 N VAL C 535 SHEET 5 AA5 7 SER C 483 TYR C 490 -1 N ILE C 484 O TRP C 587 SHEET 6 AA5 7 TYR C 432 PHE C 438 -1 N VAL C 435 O ASP C 488 SHEET 7 AA5 7 GLN C 635 MET C 640 -1 O TYR C 638 N VAL C 434 SHEET 1 AA6 3 VAL C 453 ASN C 454 0 SHEET 2 AA6 3 PHE C 547 SER C 554 -1 O SER C 554 N VAL C 453 SHEET 3 AA6 3 TYR C 576 PHE C 582 -1 O ILE C 580 N VAL C 549 SHEET 1 AA7 2 LYS C 467 ASP C 471 0 SHEET 2 AA7 2 HIS C 474 THR C 477 -1 O HIS C 474 N LYS C 470 SHEET 1 AA8 2 PHE C 556 TYR C 557 0 SHEET 2 AA8 2 LEU C 570 VAL C 571 -1 O LEU C 570 N TYR C 557 SHEET 1 AA9 6 TYR D 475 THR D 477 0 SHEET 2 AA9 6 VAL D 466 ALA D 469 -1 N ILE D 468 O LEU D 476 SHEET 3 AA9 6 GLN D 507 VAL D 510 -1 O LEU D 509 N LYS D 467 SHEET 4 AA9 6 SER D 513 ALA D 527 -1 O SER D 513 N VAL D 510 SHEET 5 AA9 6 LYS D 532 VAL D 543 -1 O GLN D 534 N THR D 526 SHEET 6 AA9 6 ASN D 592 ASP D 597 -1 O ASN D 592 N SER D 537 SHEET 1 AB1 9 TYR D 475 THR D 477 0 SHEET 2 AB1 9 VAL D 466 ALA D 469 -1 N ILE D 468 O LEU D 476 SHEET 3 AB1 9 GLN D 507 VAL D 510 -1 O LEU D 509 N LYS D 467 SHEET 4 AB1 9 SER D 513 ALA D 527 -1 O SER D 513 N VAL D 510 SHEET 5 AB1 9 LYS D 532 VAL D 543 -1 O GLN D 534 N THR D 526 SHEET 6 AB1 9 TRP D 587 LEU D 589 -1 O TYR D 588 N VAL D 541 SHEET 7 AB1 9 THR D 482 TYR D 490 -1 N ILE D 484 O TRP D 587 SHEET 8 AB1 9 LYS D 433 PHE D 438 -1 N THR D 437 O ALA D 485 SHEET 9 AB1 9 THR D 634 CYS D 637 -1 O THR D 634 N PHE D 438 SHEET 1 AB2 3 VAL D 453 ASN D 454 0 SHEET 2 AB2 3 GLN D 548 SER D 554 -1 O SER D 554 N VAL D 453 SHEET 3 AB2 3 TYR D 576 SER D 581 -1 O ILE D 580 N VAL D 549 SHEET 1 AB3 2 PHE D 556 TYR D 557 0 SHEET 2 AB3 2 LEU D 570 VAL D 571 -1 O LEU D 570 N TYR D 557 SHEET 1 AB4 4 GLN E 3 SER E 7 0 SHEET 2 AB4 4 LEU E 18 SER E 25 -1 O THR E 23 N LYS E 5 SHEET 3 AB4 4 GLN E 77 MET E 82 -1 O VAL E 78 N CYS E 22 SHEET 4 AB4 4 LEU E 67 ASP E 72 -1 N THR E 70 O PHE E 79 SHEET 1 AB5 5 THR E 57 TYR E 59 0 SHEET 2 AB5 5 GLU E 46 ILE E 51 -1 N VAL E 50 O ASN E 58 SHEET 3 AB5 5 GLY E 33 GLN E 39 -1 N TRP E 36 O GLY E 49 SHEET 4 AB5 5 ALA E 91 GLU E 98 -1 O TYR E 94 N ILE E 37 SHEET 5 AB5 5 LEU E 106 TRP E 109 -1 O TYR E 108 N ARG E 97 SHEET 1 AB6 5 THR E 57 TYR E 59 0 SHEET 2 AB6 5 GLU E 46 ILE E 51 -1 N VAL E 50 O ASN E 58 SHEET 3 AB6 5 GLY E 33 GLN E 39 -1 N TRP E 36 O GLY E 49 SHEET 4 AB6 5 ALA E 91 GLU E 98 -1 O TYR E 94 N ILE E 37 SHEET 5 AB6 5 THR E 113 VAL E 115 -1 O VAL E 115 N ALA E 91 SHEET 1 AB7 4 VAL F 4 GLN F 6 0 SHEET 2 AB7 4 VAL F 18 SER F 24 -1 O ARG F 23 N THR F 5 SHEET 3 AB7 4 LYS F 72 ILE F 77 -1 O ALA F 73 N CYS F 22 SHEET 4 AB7 4 SER F 67 ILE F 69 -1 N SER F 67 O ALA F 74 SHEET 1 AB8 2 GLN F 39 LYS F 41 0 SHEET 2 AB8 2 LEU F 45 ILE F 47 -1 O ILE F 47 N GLN F 39 SHEET 1 AB9 2 ILE F 87 TYR F 88 0 SHEET 2 AB9 2 THR F 104 LYS F 105 -1 O THR F 104 N TYR F 88 SHEET 1 AC1 3 LEU G 18 CYS G 22 0 SHEET 2 AC1 3 GLN G 77 MET G 82 -1 O MET G 82 N LEU G 18 SHEET 3 AC1 3 THR G 68 ASP G 72 -1 N THR G 70 O PHE G 79 SHEET 1 AC2 5 THR G 57 TYR G 59 0 SHEET 2 AC2 5 GLU G 46 ILE G 51 -1 N VAL G 50 O ASN G 58 SHEET 3 AC2 5 GLY G 33 GLN G 39 -1 N TRP G 36 O LEU G 48 SHEET 4 AC2 5 ALA G 91 GLU G 98 -1 O VAL G 96 N HIS G 35 SHEET 5 AC2 5 LEU G 106 TRP G 109 -1 O TYR G 108 N ARG G 97 SHEET 1 AC3 5 THR G 57 TYR G 59 0 SHEET 2 AC3 5 GLU G 46 ILE G 51 -1 N VAL G 50 O ASN G 58 SHEET 3 AC3 5 GLY G 33 GLN G 39 -1 N TRP G 36 O LEU G 48 SHEET 4 AC3 5 ALA G 91 GLU G 98 -1 O VAL G 96 N HIS G 35 SHEET 5 AC3 5 THR G 113 VAL G 115 -1 O THR G 113 N TYR G 93 SHEET 1 AC4 4 VAL H 4 GLN H 6 0 SHEET 2 AC4 4 VAL H 18 SER H 24 -1 O ARG H 23 N THR H 5 SHEET 3 AC4 4 LYS H 72 ILE H 77 -1 O ALA H 73 N CYS H 22 SHEET 4 AC4 4 PHE H 64 ILE H 69 -1 N SER H 65 O THR H 76 SHEET 1 AC5 4 LEU H 45 GLY H 51 0 SHEET 2 AC5 4 SER H 36 LYS H 41 -1 N TRP H 37 O LEU H 49 SHEET 3 AC5 4 ILE H 87 TRP H 93 -1 O ILE H 87 N GLU H 40 SHEET 4 AC5 4 TRP H 98 PHE H 100 -1 O VAL H 99 N LEU H 92 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.05 SSBOND 2 CYS C 637 CYS D 637 1555 1555 2.30 SSBOND 3 CYS E 22 CYS E 95 1555 1555 2.03 SSBOND 4 CYS F 22 CYS F 90 1555 1555 2.04 SSBOND 5 CYS G 22 CYS G 95 1555 1555 2.03 SSBOND 6 CYS H 22 CYS H 90 1555 1555 2.03 LINK ND2 ASN A 19 C1 NAG A 301 1555 1555 1.44 LINK ND2 ASN G 60 C1 NAG J 1 1555 1555 1.45 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.39 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.39 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.39 CISPEP 1 TRP B 94 PRO B 95 0 -12.96 CISPEP 2 SER C 443 PRO C 444 0 1.73 CISPEP 3 SER D 443 PRO D 444 0 -22.31 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000