HEADER VIRAL PROTEIN 06-OCT-18 6MPH TITLE CRYO-EM STRUCTURE AT 3.8 A RESOLUTION OF HIV-1 FUSION PEPTIDE-DIRECTED TITLE 2 ANTIBODY, DF1W-A.01, ELICITED BY VACCINATION OF RHESUS MACAQUES, IN TITLE 3 COMPLEX WITH STABILIZED HIV-1 ENV BG505 DS-SOSIP, WHICH WAS ALSO TITLE 4 BOUND TO ANTIBODIES VRC03 AND PGT122 COMPND MOL_ID: 1; COMPND 2 MOLECULE: DF1W-A.01 HEAVY CHAIN; COMPND 3 CHAIN: 1, 3, H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: DF1W-A.01 LIGHT CHAIN; COMPND 7 CHAIN: 2, 4, L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 11 CHAIN: 6, D, E; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: ENVELOPE GLYCOPROTEIN GP120; COMPND 15 CHAIN: A, B, C; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: PGT122 HEAVY CHAIN; COMPND 19 CHAIN: M, X, Y; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 6; COMPND 22 MOLECULE: PGT122 LIGHT CHAIN; COMPND 23 CHAIN: N, Z, a; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 7; COMPND 26 MOLECULE: VRC03 HEAVY CHAIN; COMPND 27 CHAIN: Q, f, g; COMPND 28 ENGINEERED: YES; COMPND 29 MOL_ID: 8; COMPND 30 MOLECULE: VRC03 LIGHT CHAIN; COMPND 31 CHAIN: R, h, i; COMPND 32 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 3 ORGANISM_TAXID: 9544; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 9 ORGANISM_TAXID: 9544; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 15 ORGANISM_TAXID: 11676; SOURCE 16 GENE: ENV; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 22 ORGANISM_TAXID: 11676; SOURCE 23 GENE: ENV; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 27 MOL_ID: 5; SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 29 ORGANISM_COMMON: HUMAN; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 32 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 34 MOL_ID: 6; SOURCE 35 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 36 ORGANISM_COMMON: HUMAN; SOURCE 37 ORGANISM_TAXID: 9606; SOURCE 38 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 39 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 40 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 41 MOL_ID: 7; SOURCE 42 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 43 ORGANISM_COMMON: HUMAN; SOURCE 44 ORGANISM_TAXID: 9606; SOURCE 45 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 46 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 47 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 48 MOL_ID: 8; SOURCE 49 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 50 ORGANISM_COMMON: HUMAN; SOURCE 51 ORGANISM_TAXID: 9606; SOURCE 52 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 53 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 54 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS COMPLEX, FUSION PEPTIDE, NEUTRALIZING ANTIBODY, HIV-1 ENVELOPE, VIRAL KEYWDS 2 PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR P.ACHARYA,K.XU,P.D.KWONG REVDAT 1 24-JUL-19 6MPH 0 JRNL AUTH R.KONG,H.DUAN,Z.SHENG,K.XU,P.ACHARYA,P.D.KWONG,J.M.MASCOLA JRNL TITL VACCINE-INDUCED DEVELOPMENTAL PATHWAYS IN RHESUS MACAQUES JRNL TITL 2 FOR NEUTRALIZING ANTIBODIES TARGETING THE HIV-1 FUSION JRNL TITL 3 PEPTIDE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : LEGINON, GCTF, CRYOSPARC, CRYOSPARC, REMARK 3 CRYOSPARC, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL 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) : 3.800 REMARK 3 NUMBER OF PARTICLES : 120981 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 6MPH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-18. REMARK 100 THE DEPOSITION ID IS D_1000237354. 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 : DF1W-A.01 FAB BOUND TO HIV-1 REMARK 245 ENV BG505 DS-SOSIP-VRC03 FAB- REMARK 245 PGT122 FAB; DF1W-A.01; ENVELOPE REMARK 245 GLYCOPROTEIN GP120; ENVELOPE REMARK 245 GLYCOPROTEIN GP41; PGT122; VRC03 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.25 REMARK 245 SAMPLE SUPPORT DETAILS : UNSPECIFIED REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : NULL REMARK 245 MAXIMUM DEFOCUS (NM) : NULL 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) : 1.78 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: 24-MERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 1, 2, 3, 4, 6, A, B, C, D, E, REMARK 350 AND CHAINS: H, L, M, N, Q, R, X, Y, Z, REMARK 350 AND CHAINS: a, f, g, h, i 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 ILE 6 548 REMARK 465 VAL 6 549 REMARK 465 GLN 6 550 REMARK 465 GLN 6 551 REMARK 465 GLN 6 552 REMARK 465 SER 6 553 REMARK 465 ASN 6 554 REMARK 465 LEU 6 555 REMARK 465 LEU 6 556 REMARK 465 ARG 6 557 REMARK 465 ALA 6 558 REMARK 465 ILE 6 559 REMARK 465 GLU 6 560 REMARK 465 ALA 6 561 REMARK 465 GLN 6 562 REMARK 465 GLN 6 563 REMARK 465 HIS 6 564 REMARK 465 LEU 6 565 REMARK 465 LEU 6 566 REMARK 465 LYS 6 567 REMARK 465 LEU 6 568 REMARK 465 GLU A 185A REMARK 465 ASN A 185B REMARK 465 GLN A 185C REMARK 465 GLY A 185D REMARK 465 ASN A 185E REMARK 465 ARG A 185F REMARK 465 SER A 185G REMARK 465 ASN A 185H REMARK 465 ASN A 185I REMARK 465 THR A 400 REMARK 465 SER A 401 REMARK 465 VAL A 402 REMARK 465 GLN A 403 REMARK 465 GLY A 404 REMARK 465 SER A 405 REMARK 465 ASN A 406 REMARK 465 SER A 407 REMARK 465 THR A 408 REMARK 465 GLY A 409 REMARK 465 SER A 410 REMARK 465 GLU B 185A REMARK 465 ASN B 185B REMARK 465 GLN B 185C REMARK 465 GLY B 185D REMARK 465 ASN B 185E REMARK 465 ARG B 185F REMARK 465 SER B 185G REMARK 465 ASN B 185H REMARK 465 ASN B 185I REMARK 465 THR B 400 REMARK 465 SER B 401 REMARK 465 VAL B 402 REMARK 465 GLN B 403 REMARK 465 GLY B 404 REMARK 465 SER B 405 REMARK 465 ASN B 406 REMARK 465 SER B 407 REMARK 465 THR B 408 REMARK 465 GLY B 409 REMARK 465 SER B 410 REMARK 465 GLU C 185A REMARK 465 ASN C 185B REMARK 465 GLN C 185C REMARK 465 GLY C 185D REMARK 465 ASN C 185E REMARK 465 ARG C 185F REMARK 465 SER C 185G REMARK 465 ASN C 185H REMARK 465 ASN C 185I REMARK 465 THR C 400 REMARK 465 SER C 401 REMARK 465 VAL C 402 REMARK 465 GLN C 403 REMARK 465 GLY C 404 REMARK 465 SER C 405 REMARK 465 ASN C 406 REMARK 465 SER C 407 REMARK 465 THR C 408 REMARK 465 GLY C 409 REMARK 465 SER C 410 REMARK 465 ILE D 548 REMARK 465 VAL D 549 REMARK 465 GLN D 550 REMARK 465 GLN D 551 REMARK 465 GLN D 552 REMARK 465 SER D 553 REMARK 465 ASN D 554 REMARK 465 LEU D 555 REMARK 465 LEU D 556 REMARK 465 ARG D 557 REMARK 465 ALA D 558 REMARK 465 ILE D 559 REMARK 465 GLU D 560 REMARK 465 ALA D 561 REMARK 465 GLN D 562 REMARK 465 GLN D 563 REMARK 465 HIS D 564 REMARK 465 LEU D 565 REMARK 465 LEU D 566 REMARK 465 LYS D 567 REMARK 465 LEU D 568 REMARK 465 ILE E 548 REMARK 465 VAL E 549 REMARK 465 GLN E 550 REMARK 465 GLN E 551 REMARK 465 GLN E 552 REMARK 465 SER E 553 REMARK 465 ASN E 554 REMARK 465 LEU E 555 REMARK 465 LEU E 556 REMARK 465 ARG E 557 REMARK 465 ALA E 558 REMARK 465 ILE E 559 REMARK 465 GLU E 560 REMARK 465 ALA E 561 REMARK 465 GLN E 562 REMARK 465 GLN E 563 REMARK 465 HIS E 564 REMARK 465 LEU E 565 REMARK 465 LEU E 566 REMARK 465 LYS E 567 REMARK 465 LEU E 568 REMARK 465 ALA N 7 REMARK 465 PRO N 8 REMARK 465 THR N 9 REMARK 465 PHE N 10 REMARK 465 SER Q 130 REMARK 465 ALA Q 131 REMARK 465 SER Q 132 REMARK 465 THR Q 133 REMARK 465 LYS Q 134 REMARK 465 GLY Q 135 REMARK 465 PRO Q 136 REMARK 465 SER Q 137 REMARK 465 VAL Q 138 REMARK 465 PHE Q 139 REMARK 465 PRO Q 140 REMARK 465 LEU Q 141 REMARK 465 ALA Q 142 REMARK 465 PRO Q 143 REMARK 465 SER Q 144 REMARK 465 SER Q 145 REMARK 465 GLY Q 146 REMARK 465 GLY Q 147 REMARK 465 THR Q 148 REMARK 465 ALA Q 149 REMARK 465 ALA Q 150 REMARK 465 LEU Q 151 REMARK 465 GLY Q 152 REMARK 465 CYS Q 153 REMARK 465 LEU Q 154 REMARK 465 VAL Q 155 REMARK 465 LYS Q 156 REMARK 465 ASP Q 157 REMARK 465 TYR Q 158 REMARK 465 PHE Q 159 REMARK 465 PRO Q 160 REMARK 465 GLU Q 161 REMARK 465 PRO Q 162 REMARK 465 VAL Q 163 REMARK 465 THR Q 164 REMARK 465 VAL Q 165 REMARK 465 SER Q 166 REMARK 465 TRP Q 167 REMARK 465 ASN Q 168 REMARK 465 SER Q 169 REMARK 465 GLY Q 170 REMARK 465 ALA Q 171 REMARK 465 LEU Q 172 REMARK 465 THR Q 173 REMARK 465 SER Q 174 REMARK 465 GLY Q 175 REMARK 465 VAL Q 176 REMARK 465 HIS Q 177 REMARK 465 THR Q 178 REMARK 465 PHE Q 179 REMARK 465 PRO Q 180 REMARK 465 ALA Q 181 REMARK 465 VAL Q 182 REMARK 465 LEU Q 183 REMARK 465 GLN Q 184 REMARK 465 SER Q 185 REMARK 465 SER Q 186 REMARK 465 GLY Q 187 REMARK 465 LEU Q 188 REMARK 465 TYR Q 189 REMARK 465 SER Q 190 REMARK 465 LEU Q 191 REMARK 465 SER Q 192 REMARK 465 SER Q 193 REMARK 465 VAL Q 194 REMARK 465 VAL Q 195 REMARK 465 THR Q 196 REMARK 465 VAL Q 197 REMARK 465 PRO Q 198 REMARK 465 SER Q 199 REMARK 465 SER Q 200 REMARK 465 SER Q 201 REMARK 465 LEU Q 202 REMARK 465 GLY Q 203 REMARK 465 THR Q 204 REMARK 465 GLN Q 205 REMARK 465 THR Q 206 REMARK 465 TYR Q 207 REMARK 465 ILE Q 208 REMARK 465 CYS Q 209 REMARK 465 ASN Q 210 REMARK 465 VAL Q 211 REMARK 465 ASN Q 212 REMARK 465 HIS Q 213 REMARK 465 LYS Q 214 REMARK 465 PRO Q 215 REMARK 465 SER Q 216 REMARK 465 ASN Q 217 REMARK 465 THR Q 218 REMARK 465 LYS Q 219 REMARK 465 VAL Q 220 REMARK 465 ASP Q 221 REMARK 465 LYS Q 222 REMARK 465 LYS Q 223 REMARK 465 VAL Q 224 REMARK 465 GLU Q 225 REMARK 465 PRO Q 226 REMARK 465 LYS Q 227 REMARK 465 ALA Z 7 REMARK 465 PRO Z 8 REMARK 465 THR Z 9 REMARK 465 PHE Z 10 REMARK 465 ALA a 7 REMARK 465 PRO a 8 REMARK 465 THR a 9 REMARK 465 PHE a 10 REMARK 465 SER f 130 REMARK 465 ALA f 131 REMARK 465 SER f 132 REMARK 465 THR f 133 REMARK 465 LYS f 134 REMARK 465 GLY f 135 REMARK 465 PRO f 136 REMARK 465 SER f 137 REMARK 465 VAL f 138 REMARK 465 PHE f 139 REMARK 465 PRO f 140 REMARK 465 LEU f 141 REMARK 465 ALA f 142 REMARK 465 PRO f 143 REMARK 465 SER f 144 REMARK 465 SER f 145 REMARK 465 GLY f 146 REMARK 465 GLY f 147 REMARK 465 THR f 148 REMARK 465 ALA f 149 REMARK 465 ALA f 150 REMARK 465 LEU f 151 REMARK 465 GLY f 152 REMARK 465 CYS f 153 REMARK 465 LEU f 154 REMARK 465 VAL f 155 REMARK 465 LYS f 156 REMARK 465 ASP f 157 REMARK 465 TYR f 158 REMARK 465 PHE f 159 REMARK 465 PRO f 160 REMARK 465 GLU f 161 REMARK 465 PRO f 162 REMARK 465 VAL f 163 REMARK 465 THR f 164 REMARK 465 VAL f 165 REMARK 465 SER f 166 REMARK 465 TRP f 167 REMARK 465 ASN f 168 REMARK 465 SER f 169 REMARK 465 GLY f 170 REMARK 465 ALA f 171 REMARK 465 LEU f 172 REMARK 465 THR f 173 REMARK 465 SER f 174 REMARK 465 GLY f 175 REMARK 465 VAL f 176 REMARK 465 HIS f 177 REMARK 465 THR f 178 REMARK 465 PHE f 179 REMARK 465 PRO f 180 REMARK 465 ALA f 181 REMARK 465 VAL f 182 REMARK 465 LEU f 183 REMARK 465 GLN f 184 REMARK 465 SER f 185 REMARK 465 SER f 186 REMARK 465 GLY f 187 REMARK 465 LEU f 188 REMARK 465 TYR f 189 REMARK 465 SER f 190 REMARK 465 LEU f 191 REMARK 465 SER f 192 REMARK 465 SER f 193 REMARK 465 VAL f 194 REMARK 465 VAL f 195 REMARK 465 THR f 196 REMARK 465 VAL f 197 REMARK 465 PRO f 198 REMARK 465 SER f 199 REMARK 465 SER f 200 REMARK 465 SER f 201 REMARK 465 LEU f 202 REMARK 465 GLY f 203 REMARK 465 THR f 204 REMARK 465 GLN f 205 REMARK 465 THR f 206 REMARK 465 TYR f 207 REMARK 465 ILE f 208 REMARK 465 CYS f 209 REMARK 465 ASN f 210 REMARK 465 VAL f 211 REMARK 465 ASN f 212 REMARK 465 HIS f 213 REMARK 465 LYS f 214 REMARK 465 PRO f 215 REMARK 465 SER f 216 REMARK 465 ASN f 217 REMARK 465 THR f 218 REMARK 465 LYS f 219 REMARK 465 VAL f 220 REMARK 465 ASP f 221 REMARK 465 LYS f 222 REMARK 465 LYS f 223 REMARK 465 VAL f 224 REMARK 465 GLU f 225 REMARK 465 PRO f 226 REMARK 465 LYS f 227 REMARK 465 SER g 130 REMARK 465 ALA g 131 REMARK 465 SER g 132 REMARK 465 THR g 133 REMARK 465 LYS g 134 REMARK 465 GLY g 135 REMARK 465 PRO g 136 REMARK 465 SER g 137 REMARK 465 VAL g 138 REMARK 465 PHE g 139 REMARK 465 PRO g 140 REMARK 465 LEU g 141 REMARK 465 ALA g 142 REMARK 465 PRO g 143 REMARK 465 SER g 144 REMARK 465 SER g 145 REMARK 465 GLY g 146 REMARK 465 GLY g 147 REMARK 465 THR g 148 REMARK 465 ALA g 149 REMARK 465 ALA g 150 REMARK 465 LEU g 151 REMARK 465 GLY g 152 REMARK 465 CYS g 153 REMARK 465 LEU g 154 REMARK 465 VAL g 155 REMARK 465 LYS g 156 REMARK 465 ASP g 157 REMARK 465 TYR g 158 REMARK 465 PHE g 159 REMARK 465 PRO g 160 REMARK 465 GLU g 161 REMARK 465 PRO g 162 REMARK 465 VAL g 163 REMARK 465 THR g 164 REMARK 465 VAL g 165 REMARK 465 SER g 166 REMARK 465 TRP g 167 REMARK 465 ASN g 168 REMARK 465 SER g 169 REMARK 465 GLY g 170 REMARK 465 ALA g 171 REMARK 465 LEU g 172 REMARK 465 THR g 173 REMARK 465 SER g 174 REMARK 465 GLY g 175 REMARK 465 VAL g 176 REMARK 465 HIS g 177 REMARK 465 THR g 178 REMARK 465 PHE g 179 REMARK 465 PRO g 180 REMARK 465 ALA g 181 REMARK 465 VAL g 182 REMARK 465 LEU g 183 REMARK 465 GLN g 184 REMARK 465 SER g 185 REMARK 465 SER g 186 REMARK 465 GLY g 187 REMARK 465 LEU g 188 REMARK 465 TYR g 189 REMARK 465 SER g 190 REMARK 465 LEU g 191 REMARK 465 SER g 192 REMARK 465 SER g 193 REMARK 465 VAL g 194 REMARK 465 VAL g 195 REMARK 465 THR g 196 REMARK 465 VAL g 197 REMARK 465 PRO g 198 REMARK 465 SER g 199 REMARK 465 SER g 200 REMARK 465 SER g 201 REMARK 465 LEU g 202 REMARK 465 GLY g 203 REMARK 465 THR g 204 REMARK 465 GLN g 205 REMARK 465 THR g 206 REMARK 465 TYR g 207 REMARK 465 ILE g 208 REMARK 465 CYS g 209 REMARK 465 ASN g 210 REMARK 465 VAL g 211 REMARK 465 ASN g 212 REMARK 465 HIS g 213 REMARK 465 LYS g 214 REMARK 465 PRO g 215 REMARK 465 SER g 216 REMARK 465 ASN g 217 REMARK 465 THR g 218 REMARK 465 LYS g 219 REMARK 465 VAL g 220 REMARK 465 ASP g 221 REMARK 465 LYS g 222 REMARK 465 LYS g 223 REMARK 465 VAL g 224 REMARK 465 GLU g 225 REMARK 465 PRO g 226 REMARK 465 LYS g 227 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 LEU A 494 CA - CB - CG ANGL. DEV. = 16.0 DEGREES REMARK 500 LEU B 494 CA - CB - CG ANGL. DEV. = 16.0 DEGREES REMARK 500 LEU C 494 CA - CB - CG ANGL. DEV. = 16.2 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 LEU 2 47 -62.59 -91.26 REMARK 500 GLN 2 50 70.57 55.85 REMARK 500 LEU 4 47 -62.57 -91.18 REMARK 500 GLN 4 50 70.50 55.83 REMARK 500 LEU 6 523 17.44 58.13 REMARK 500 LEU 6 602 -13.34 72.04 REMARK 500 ASN 6 616 42.96 39.35 REMARK 500 GLN 6 640 -6.37 69.98 REMARK 500 LEU A 52 -168.49 -128.08 REMARK 500 HIS A 66 63.54 60.48 REMARK 500 ASN A 80 69.17 36.64 REMARK 500 MET A 100 -12.81 69.87 REMARK 500 THR A 257 -61.56 -99.86 REMARK 500 GLU A 268 -51.37 -120.84 REMARK 500 TRP A 427 -4.58 68.02 REMARK 500 SER A 460 -168.90 -128.80 REMARK 500 LEU B 52 -168.65 -127.57 REMARK 500 HIS B 66 63.47 60.49 REMARK 500 ASN B 80 69.02 36.45 REMARK 500 MET B 100 -12.67 69.85 REMARK 500 THR B 257 -62.67 -99.59 REMARK 500 GLU B 268 -51.46 -120.33 REMARK 500 TRP B 427 -3.80 68.22 REMARK 500 SER B 460 -168.53 -129.15 REMARK 500 LEU C 52 -169.40 -127.01 REMARK 500 HIS C 66 63.36 60.32 REMARK 500 ASN C 80 69.24 36.51 REMARK 500 MET C 100 -13.19 69.96 REMARK 500 THR C 198 -30.10 -133.05 REMARK 500 THR C 257 -62.50 -99.63 REMARK 500 GLU C 268 -51.52 -120.87 REMARK 500 TRP C 427 -3.86 68.05 REMARK 500 SER C 460 -168.58 -128.87 REMARK 500 LEU D 523 18.19 57.85 REMARK 500 LEU D 602 -12.72 72.13 REMARK 500 ASN D 616 42.89 39.43 REMARK 500 GLN D 640 -7.01 70.04 REMARK 500 LEU E 523 17.61 58.06 REMARK 500 LEU E 602 -12.89 71.90 REMARK 500 ASN E 616 43.01 39.18 REMARK 500 GLN E 640 -6.85 69.99 REMARK 500 LEU L 47 -62.50 -91.28 REMARK 500 GLN L 50 70.50 55.81 REMARK 500 LYS M 64 -10.15 65.27 REMARK 500 SER M 65 -35.97 -132.35 REMARK 500 ASN M 76 61.32 61.88 REMARK 500 ALA Q 99 -169.43 -161.33 REMARK 500 PRO Q 116 83.47 -67.49 REMARK 500 THR R 51 -8.82 69.59 REMARK 500 SER R 52 -5.18 -142.99 REMARK 500 REMARK 500 THIS ENTRY HAS 70 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 GLN 2 50 VAL 2 51 -137.76 REMARK 500 GLN 4 50 VAL 4 51 -137.41 REMARK 500 GLN L 50 VAL L 51 -137.35 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 A 606 REMARK 610 NAG A 608 REMARK 610 NAG A 612 REMARK 610 NAG A 620 REMARK 610 NAG A 622 REMARK 610 NAG A 625 REMARK 610 NAG A 633 REMARK 610 NAG B 605 REMARK 610 NAG B 607 REMARK 610 NAG B 611 REMARK 610 NAG B 619 REMARK 610 NAG B 621 REMARK 610 NAG B 624 REMARK 610 NAG B 632 REMARK 610 NAG C 606 REMARK 610 NAG C 608 REMARK 610 NAG C 612 REMARK 610 NAG C 620 REMARK 610 NAG C 622 REMARK 610 NAG C 625 REMARK 610 NAG C 633 REMARK 610 NAG R 201 REMARK 610 NAG h 201 REMARK 610 NAG i 201 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-9189 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE AT 3.8 A RESOLUTION OF HIV-1 FUSION PEPTIDE- REMARK 900 DIRECTED ANTIBODY, DF1W-A.01, ELICITED BY VACCINATION OF RHESUS REMARK 900 MACAQUES, IN COMPLEX WITH STABILIZED HIV-1 ENV BG505 DS-SOSIP, REMARK 900 WHICH WAS ALSO BOUND TO ANTIBODIES VRC03 AND PGT122 DBREF 6MPH 1 1 113 PDB 6MPH 6MPH 1 113 DBREF 6MPH 2 1 107 PDB 6MPH 6MPH 1 107 DBREF 6MPH 3 1 113 PDB 6MPH 6MPH 1 113 DBREF 6MPH 4 1 107 PDB 6MPH 6MPH 1 107 DBREF 6MPH 6 512 664 UNP Q2N0S7 Q2N0S7_9HIV1 509 661 DBREF 6MPH A 31 505 UNP Q2N0S6 Q2N0S6_9HIV1 30 502 DBREF 6MPH B 31 505 UNP Q2N0S6 Q2N0S6_9HIV1 30 502 DBREF 6MPH C 31 505 UNP Q2N0S6 Q2N0S6_9HIV1 30 502 DBREF 6MPH D 512 664 UNP Q2N0S7 Q2N0S7_9HIV1 509 661 DBREF 6MPH E 512 664 UNP Q2N0S7 Q2N0S7_9HIV1 509 661 DBREF 6MPH H 1 113 PDB 6MPH 6MPH 1 113 DBREF 6MPH L 1 107 PDB 6MPH 6MPH 1 107 DBREF 6MPH M 1 111 PDB 6MPH 6MPH 1 111 DBREF 6MPH N 7 107 PDB 6MPH 6MPH 7 107 DBREF 6MPH Q 1 227 PDB 6MPH 6MPH 1 227 DBREF 6MPH R 1 107 PDB 6MPH 6MPH 1 107 DBREF 6MPH X 1 111 PDB 6MPH 6MPH 1 111 DBREF 6MPH Y 1 111 PDB 6MPH 6MPH 1 111 DBREF 6MPH Z 7 107 PDB 6MPH 6MPH 7 107 DBREF 6MPH a 7 107 PDB 6MPH 6MPH 7 107 DBREF 6MPH f 1 227 PDB 6MPH 6MPH 1 227 DBREF 6MPH g 1 227 PDB 6MPH 6MPH 1 227 DBREF 6MPH h 1 107 PDB 6MPH 6MPH 1 107 DBREF 6MPH i 1 107 PDB 6MPH 6MPH 1 107 SEQADV 6MPH CYS 6 605 UNP Q2N0S7 THR 602 CONFLICT SEQADV 6MPH CYS A 201 UNP Q2N0S6 ILE 200 CONFLICT SEQADV 6MPH ASN A 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 6MPH CYS A 433 UNP Q2N0S6 ALA 430 CONFLICT SEQADV 6MPH CYS A 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 6MPH CYS B 201 UNP Q2N0S6 ILE 200 CONFLICT SEQADV 6MPH ASN B 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 6MPH CYS B 433 UNP Q2N0S6 ALA 430 CONFLICT SEQADV 6MPH CYS B 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 6MPH CYS C 201 UNP Q2N0S6 ILE 200 CONFLICT SEQADV 6MPH ASN C 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 6MPH CYS C 433 UNP Q2N0S6 ALA 430 CONFLICT SEQADV 6MPH CYS C 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 6MPH CYS D 605 UNP Q2N0S7 THR 602 CONFLICT SEQADV 6MPH CYS E 605 UNP Q2N0S7 THR 602 CONFLICT SEQRES 1 1 118 GLN VAL GLN LEU VAL GLU SER GLY PRO GLY LEU VAL ARG SEQRES 2 1 118 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 1 118 ALA SER ILE ARG THR LYS ALA TRP TRP SER TRP ILE ARG SEQRES 4 1 118 GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR VAL SEQRES 5 1 118 SER GLY GLY TRP ASP LEU PRO ASN TYR ASN PRO SER LEU SEQRES 6 1 118 LYS ASN ARG VAL ILE ILE LEU LYS ASP THR SER LEU ASN SEQRES 7 1 118 GLN PHE SER LEU ARG LEU THR SER VAL THR ALA ALA ASP SEQRES 8 1 118 THR ALA LEU TYR TYR CYS ALA ARG GLU GLY PRO GLU ASP SEQRES 9 1 118 PHE ASP VAL TRP GLY PRO GLY PHE LEU VAL THR VAL SER SEQRES 10 1 118 SER SEQRES 1 2 112 ASP VAL VAL MET THR GLN SER PRO LEU SER LEU SER ILE SEQRES 2 2 112 THR PRO GLY GLN PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 2 112 GLN SER LEU VAL HIS SER ASP GLY LYS THR TYR LEU SER SEQRES 4 2 112 TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO ARG LEU LEU SEQRES 5 2 112 ILE TYR GLN VAL SER ASN TRP TYR SER GLY VAL PRO ASP SEQRES 6 2 112 ARG PHE SER GLY SER GLY THR GLY THR ASN PHE THR LEU SEQRES 7 2 112 LYS ILE SER ARG VAL GLU ALA ALA ASP VAL GLY VAL TYR SEQRES 8 2 112 TYR CYS GLY GLN GLY VAL HIS LEU PRO ARG THR PHE GLY SEQRES 9 2 112 GLN GLY THR LYS VAL ASP ILE LYS SEQRES 1 3 118 GLN VAL GLN LEU VAL GLU SER GLY PRO GLY LEU VAL ARG SEQRES 2 3 118 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 3 118 ALA SER ILE ARG THR LYS ALA TRP TRP SER TRP ILE ARG SEQRES 4 3 118 GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR VAL SEQRES 5 3 118 SER GLY GLY TRP ASP LEU PRO ASN TYR ASN PRO SER LEU SEQRES 6 3 118 LYS ASN ARG VAL ILE ILE LEU LYS ASP THR SER LEU ASN SEQRES 7 3 118 GLN PHE SER LEU ARG LEU THR SER VAL THR ALA ALA ASP SEQRES 8 3 118 THR ALA LEU TYR TYR CYS ALA ARG GLU GLY PRO GLU ASP SEQRES 9 3 118 PHE ASP VAL TRP GLY PRO GLY PHE LEU VAL THR VAL SER SEQRES 10 3 118 SER SEQRES 1 4 112 ASP VAL VAL MET THR GLN SER PRO LEU SER LEU SER ILE SEQRES 2 4 112 THR PRO GLY GLN PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 4 112 GLN SER LEU VAL HIS SER ASP GLY LYS THR TYR LEU SER SEQRES 4 4 112 TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO ARG LEU LEU SEQRES 5 4 112 ILE TYR GLN VAL SER ASN TRP TYR SER GLY VAL PRO ASP SEQRES 6 4 112 ARG PHE SER GLY SER GLY THR GLY THR ASN PHE THR LEU SEQRES 7 4 112 LYS ILE SER ARG VAL GLU ALA ALA ASP VAL GLY VAL TYR SEQRES 8 4 112 TYR CYS GLY GLN GLY VAL HIS LEU PRO ARG THR PHE GLY SEQRES 9 4 112 GLN GLY THR LYS VAL ASP ILE LYS SEQRES 1 6 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 6 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 6 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 6 153 GLN GLN SER ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 6 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 6 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 6 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 6 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 6 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 6 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 6 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 6 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 A 473 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 A 473 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 A 473 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 A 473 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 A 473 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 A 473 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 A 473 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 A 473 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 A 473 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 A 473 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 A 473 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 A 473 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 A 473 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 A 473 ALA CYS THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 A 473 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 A 473 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 A 473 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 A 473 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 A 473 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 A 473 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 A 473 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 A 473 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 A 473 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 A 473 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 A 473 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 A 473 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 A 473 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 A 473 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 A 473 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 A 473 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 A 473 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR SEQRES 32 A 473 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 A 473 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 A 473 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 A 473 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 A 473 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 A 473 CYS LYS ARG ARG VAL SEQRES 1 B 473 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 B 473 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 B 473 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 B 473 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 B 473 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 B 473 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 B 473 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 B 473 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 B 473 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 B 473 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 B 473 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 B 473 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 B 473 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 B 473 ALA CYS THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 B 473 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 B 473 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 B 473 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 B 473 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 B 473 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 B 473 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 B 473 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 B 473 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 B 473 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 B 473 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 B 473 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 B 473 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 B 473 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 B 473 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 B 473 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 B 473 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 B 473 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR SEQRES 32 B 473 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 B 473 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 B 473 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 B 473 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 B 473 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 B 473 CYS LYS ARG ARG VAL SEQRES 1 C 473 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 C 473 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 C 473 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 C 473 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 C 473 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 C 473 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 C 473 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 C 473 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 C 473 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 C 473 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 C 473 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 C 473 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 C 473 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 C 473 ALA CYS THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 C 473 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 C 473 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 C 473 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 C 473 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 C 473 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 C 473 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 C 473 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 C 473 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 C 473 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 C 473 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 C 473 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 C 473 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 C 473 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 C 473 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 C 473 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 C 473 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 C 473 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR SEQRES 32 C 473 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 C 473 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 C 473 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 C 473 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 C 473 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 C 473 CYS LYS ARG ARG VAL SEQRES 1 D 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 D 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 D 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 D 153 GLN GLN SER ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 D 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 D 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 D 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 D 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 D 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 D 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 D 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 D 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 E 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 E 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 E 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 E 153 GLN GLN SER ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 E 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 E 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 E 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 E 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 E 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 E 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 E 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 E 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 H 118 GLN VAL GLN LEU VAL GLU SER GLY PRO GLY LEU VAL ARG SEQRES 2 H 118 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 H 118 ALA SER ILE ARG THR LYS ALA TRP TRP SER TRP ILE ARG SEQRES 4 H 118 GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR VAL SEQRES 5 H 118 SER GLY GLY TRP ASP LEU PRO ASN TYR ASN PRO SER LEU SEQRES 6 H 118 LYS ASN ARG VAL ILE ILE LEU LYS ASP THR SER LEU ASN SEQRES 7 H 118 GLN PHE SER LEU ARG LEU THR SER VAL THR ALA ALA ASP SEQRES 8 H 118 THR ALA LEU TYR TYR CYS ALA ARG GLU GLY PRO GLU ASP SEQRES 9 H 118 PHE ASP VAL TRP GLY PRO GLY PHE LEU VAL THR VAL SER SEQRES 10 H 118 SER SEQRES 1 L 112 ASP VAL VAL MET THR GLN SER PRO LEU SER LEU SER ILE SEQRES 2 L 112 THR PRO GLY GLN PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 L 112 GLN SER LEU VAL HIS SER ASP GLY LYS THR TYR LEU SER SEQRES 4 L 112 TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO ARG LEU LEU SEQRES 5 L 112 ILE TYR GLN VAL SER ASN TRP TYR SER GLY VAL PRO ASP SEQRES 6 L 112 ARG PHE SER GLY SER GLY THR GLY THR ASN PHE THR LEU SEQRES 7 L 112 LYS ILE SER ARG VAL GLU ALA ALA ASP VAL GLY VAL TYR SEQRES 8 L 112 TYR CYS GLY GLN GLY VAL HIS LEU PRO ARG THR PHE GLY SEQRES 9 L 112 GLN GLY THR LYS VAL ASP ILE LYS SEQRES 1 M 132 GLN VAL HIS LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 M 132 PRO SER GLU THR LEU SER LEU THR CYS ASN VAL SER GLY SEQRES 3 M 132 THR LEU VAL ARG ASP ASN TYR TRP SER TRP ILE ARG GLN SEQRES 4 M 132 PRO LEU GLY LYS GLN PRO GLU TRP ILE GLY TYR VAL HIS SEQRES 5 M 132 ASP SER GLY ASP THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 M 132 ARG VAL HIS LEU SER LEU ASP LYS SER LYS ASN LEU VAL SEQRES 7 M 132 SER LEU ARG LEU THR GLY VAL THR ALA ALA ASP SER ALA SEQRES 8 M 132 ILE TYR TYR CYS ALA THR THR LYS HIS GLY ARG ARG ILE SEQRES 9 M 132 TYR GLY VAL VAL ALA PHE LYS GLU TRP PHE THR TYR PHE SEQRES 10 M 132 TYR MET ASP VAL TRP GLY LYS GLY THR SER VAL THR VAL SEQRES 11 M 132 SER SER SEQRES 1 N 107 ALA PRO THR PHE VAL SER VAL ALA PRO GLY GLN THR ALA SEQRES 2 N 107 ARG ILE THR CYS GLY GLU GLU SER LEU GLY SER ARG SER SEQRES 3 N 107 VAL ILE TRP TYR GLN GLN ARG PRO GLY GLN ALA PRO SER SEQRES 4 N 107 LEU ILE ILE TYR ASN ASN ASN ASP ARG PRO SER GLY ILE SEQRES 5 N 107 PRO ASP ARG PHE SER GLY SER PRO GLY SER THR PHE GLY SEQRES 6 N 107 THR THR ALA THR LEU THR ILE THR SER VAL GLU ALA GLY SEQRES 7 N 107 ASP GLU ALA ASP TYR TYR CYS HIS ILE TRP ASP SER ARG SEQRES 8 N 107 ARG PRO THR ASN TRP VAL PHE GLY GLU GLY THR THR LEU SEQRES 9 N 107 ILE VAL LEU SEQRES 1 Q 227 GLN VAL GLN LEU VAL GLN SER GLY ALA VAL ILE LYS THR SEQRES 2 Q 227 PRO GLY SER SER VAL LYS ILE SER CYS ARG ALA SER GLY SEQRES 3 Q 227 TYR ASN PHE ARG ASP TYR SER ILE HIS TRP VAL ARG LEU SEQRES 4 Q 227 ILE PRO ASP LYS GLY PHE GLU TRP ILE GLY TRP ILE LYS SEQRES 5 Q 227 PRO LEU TRP GLY ALA VAL SER TYR ALA ARG GLN LEU GLN SEQRES 6 Q 227 GLY ARG VAL SER MET THR ARG GLN LEU SER GLN ASP PRO SEQRES 7 Q 227 ASP ASP PRO ASP TRP GLY VAL ALA TYR MET GLU PHE SER SEQRES 8 Q 227 GLY LEU THR PRO ALA ASP THR ALA GLU TYR PHE CYS VAL SEQRES 9 Q 227 ARG ARG GLY SER CYS ASP TYR CYS GLY ASP PHE PRO TRP SEQRES 10 Q 227 GLN TYR TRP GLY GLN GLY THR VAL VAL VAL VAL SER SER SEQRES 11 Q 227 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 12 Q 227 SER SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 Q 227 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 Q 227 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 Q 227 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 Q 227 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 Q 227 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 Q 227 LYS LYS VAL GLU PRO LYS SEQRES 1 R 102 GLU ILE VAL LEU THR GLN SER PRO GLY ILE LEU SER LEU SEQRES 2 R 102 SER PRO GLY GLU THR ALA THR LEU PHE CYS LYS ALA SER SEQRES 3 R 102 GLN GLY GLY ASN ALA MET THR TRP TYR GLN LYS ARG ARG SEQRES 4 R 102 GLY GLN VAL PRO ARG LEU LEU ILE TYR ASP THR SER ARG SEQRES 5 R 102 ARG ALA SER GLY VAL PRO ASP ARG PHE VAL GLY SER GLY SEQRES 6 R 102 SER GLY THR ASP PHE PHE LEU THR ILE ASN LYS LEU ASP SEQRES 7 R 102 ARG GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN PHE GLU SEQRES 8 R 102 PHE PHE GLY LEU GLY SER GLU LEU GLU VAL HIS SEQRES 1 X 132 GLN VAL HIS LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 X 132 PRO SER GLU THR LEU SER LEU THR CYS ASN VAL SER GLY SEQRES 3 X 132 THR LEU VAL ARG ASP ASN TYR TRP SER TRP ILE ARG GLN SEQRES 4 X 132 PRO LEU GLY LYS GLN PRO GLU TRP ILE GLY TYR VAL HIS SEQRES 5 X 132 ASP SER GLY ASP THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 X 132 ARG VAL HIS LEU SER LEU ASP LYS SER LYS ASN LEU VAL SEQRES 7 X 132 SER LEU ARG LEU THR GLY VAL THR ALA ALA ASP SER ALA SEQRES 8 X 132 ILE TYR TYR CYS ALA THR THR LYS HIS GLY ARG ARG ILE SEQRES 9 X 132 TYR GLY VAL VAL ALA PHE LYS GLU TRP PHE THR TYR PHE SEQRES 10 X 132 TYR MET ASP VAL TRP GLY LYS GLY THR SER VAL THR VAL SEQRES 11 X 132 SER SER SEQRES 1 Y 132 GLN VAL HIS LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 Y 132 PRO SER GLU THR LEU SER LEU THR CYS ASN VAL SER GLY SEQRES 3 Y 132 THR LEU VAL ARG ASP ASN TYR TRP SER TRP ILE ARG GLN SEQRES 4 Y 132 PRO LEU GLY LYS GLN PRO GLU TRP ILE GLY TYR VAL HIS SEQRES 5 Y 132 ASP SER GLY ASP THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 Y 132 ARG VAL HIS LEU SER LEU ASP LYS SER LYS ASN LEU VAL SEQRES 7 Y 132 SER LEU ARG LEU THR GLY VAL THR ALA ALA ASP SER ALA SEQRES 8 Y 132 ILE TYR TYR CYS ALA THR THR LYS HIS GLY ARG ARG ILE SEQRES 9 Y 132 TYR GLY VAL VAL ALA PHE LYS GLU TRP PHE THR TYR PHE SEQRES 10 Y 132 TYR MET ASP VAL TRP GLY LYS GLY THR SER VAL THR VAL SEQRES 11 Y 132 SER SER SEQRES 1 Z 107 ALA PRO THR PHE VAL SER VAL ALA PRO GLY GLN THR ALA SEQRES 2 Z 107 ARG ILE THR CYS GLY GLU GLU SER LEU GLY SER ARG SER SEQRES 3 Z 107 VAL ILE TRP TYR GLN GLN ARG PRO GLY GLN ALA PRO SER SEQRES 4 Z 107 LEU ILE ILE TYR ASN ASN ASN ASP ARG PRO SER GLY ILE SEQRES 5 Z 107 PRO ASP ARG PHE SER GLY SER PRO GLY SER THR PHE GLY SEQRES 6 Z 107 THR THR ALA THR LEU THR ILE THR SER VAL GLU ALA GLY SEQRES 7 Z 107 ASP GLU ALA ASP TYR TYR CYS HIS ILE TRP ASP SER ARG SEQRES 8 Z 107 ARG PRO THR ASN TRP VAL PHE GLY GLU GLY THR THR LEU SEQRES 9 Z 107 ILE VAL LEU SEQRES 1 a 107 ALA PRO THR PHE VAL SER VAL ALA PRO GLY GLN THR ALA SEQRES 2 a 107 ARG ILE THR CYS GLY GLU GLU SER LEU GLY SER ARG SER SEQRES 3 a 107 VAL ILE TRP TYR GLN GLN ARG PRO GLY GLN ALA PRO SER SEQRES 4 a 107 LEU ILE ILE TYR ASN ASN ASN ASP ARG PRO SER GLY ILE SEQRES 5 a 107 PRO ASP ARG PHE SER GLY SER PRO GLY SER THR PHE GLY SEQRES 6 a 107 THR THR ALA THR LEU THR ILE THR SER VAL GLU ALA GLY SEQRES 7 a 107 ASP GLU ALA ASP TYR TYR CYS HIS ILE TRP ASP SER ARG SEQRES 8 a 107 ARG PRO THR ASN TRP VAL PHE GLY GLU GLY THR THR LEU SEQRES 9 a 107 ILE VAL LEU SEQRES 1 f 227 GLN VAL GLN LEU VAL GLN SER GLY ALA VAL ILE LYS THR SEQRES 2 f 227 PRO GLY SER SER VAL LYS ILE SER CYS ARG ALA SER GLY SEQRES 3 f 227 TYR ASN PHE ARG ASP TYR SER ILE HIS TRP VAL ARG LEU SEQRES 4 f 227 ILE PRO ASP LYS GLY PHE GLU TRP ILE GLY TRP ILE LYS SEQRES 5 f 227 PRO LEU TRP GLY ALA VAL SER TYR ALA ARG GLN LEU GLN SEQRES 6 f 227 GLY ARG VAL SER MET THR ARG GLN LEU SER GLN ASP PRO SEQRES 7 f 227 ASP ASP PRO ASP TRP GLY VAL ALA TYR MET GLU PHE SER SEQRES 8 f 227 GLY LEU THR PRO ALA ASP THR ALA GLU TYR PHE CYS VAL SEQRES 9 f 227 ARG ARG GLY SER CYS ASP TYR CYS GLY ASP PHE PRO TRP SEQRES 10 f 227 GLN TYR TRP GLY GLN GLY THR VAL VAL VAL VAL SER SER SEQRES 11 f 227 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 12 f 227 SER SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 f 227 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 f 227 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 f 227 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 f 227 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 f 227 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 f 227 LYS LYS VAL GLU PRO LYS SEQRES 1 g 227 GLN VAL GLN LEU VAL GLN SER GLY ALA VAL ILE LYS THR SEQRES 2 g 227 PRO GLY SER SER VAL LYS ILE SER CYS ARG ALA SER GLY SEQRES 3 g 227 TYR ASN PHE ARG ASP TYR SER ILE HIS TRP VAL ARG LEU SEQRES 4 g 227 ILE PRO ASP LYS GLY PHE GLU TRP ILE GLY TRP ILE LYS SEQRES 5 g 227 PRO LEU TRP GLY ALA VAL SER TYR ALA ARG GLN LEU GLN SEQRES 6 g 227 GLY ARG VAL SER MET THR ARG GLN LEU SER GLN ASP PRO SEQRES 7 g 227 ASP ASP PRO ASP TRP GLY VAL ALA TYR MET GLU PHE SER SEQRES 8 g 227 GLY LEU THR PRO ALA ASP THR ALA GLU TYR PHE CYS VAL SEQRES 9 g 227 ARG ARG GLY SER CYS ASP TYR CYS GLY ASP PHE PRO TRP SEQRES 10 g 227 GLN TYR TRP GLY GLN GLY THR VAL VAL VAL VAL SER SER SEQRES 11 g 227 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 12 g 227 SER SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 g 227 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 g 227 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 g 227 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 g 227 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 g 227 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 g 227 LYS LYS VAL GLU PRO LYS SEQRES 1 h 102 GLU ILE VAL LEU THR GLN SER PRO GLY ILE LEU SER LEU SEQRES 2 h 102 SER PRO GLY GLU THR ALA THR LEU PHE CYS LYS ALA SER SEQRES 3 h 102 GLN GLY GLY ASN ALA MET THR TRP TYR GLN LYS ARG ARG SEQRES 4 h 102 GLY GLN VAL PRO ARG LEU LEU ILE TYR ASP THR SER ARG SEQRES 5 h 102 ARG ALA SER GLY VAL PRO ASP ARG PHE VAL GLY SER GLY SEQRES 6 h 102 SER GLY THR ASP PHE PHE LEU THR ILE ASN LYS LEU ASP SEQRES 7 h 102 ARG GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN PHE GLU SEQRES 8 h 102 PHE PHE GLY LEU GLY SER GLU LEU GLU VAL HIS SEQRES 1 i 102 GLU ILE VAL LEU THR GLN SER PRO GLY ILE LEU SER LEU SEQRES 2 i 102 SER PRO GLY GLU THR ALA THR LEU PHE CYS LYS ALA SER SEQRES 3 i 102 GLN GLY GLY ASN ALA MET THR TRP TYR GLN LYS ARG ARG SEQRES 4 i 102 GLY GLN VAL PRO ARG LEU LEU ILE TYR ASP THR SER ARG SEQRES 5 i 102 ARG ALA SER GLY VAL PRO ASP ARG PHE VAL GLY SER GLY SEQRES 6 i 102 SER GLY THR ASP PHE PHE LEU THR ILE ASN LYS LEU ASP SEQRES 7 i 102 ARG GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN PHE GLU SEQRES 8 i 102 PHE PHE GLY LEU GLY SER GLU LEU GLU VAL HIS HET NAG 6 701 14 HET NAG A 601 14 HET NAG A 602 14 HET BMA A 603 11 HET MAN A 604 11 HET MAN A 605 11 HET NAG A 606 14 HET NAG A 607 14 HET NAG A 608 14 HET NAG A 609 14 HET BMA A 610 11 HET MAN A 611 11 HET NAG A 612 14 HET NAG A 613 14 HET BMA A 614 11 HET MAN A 615 11 HET MAN A 616 11 HET NAG A 617 14 HET NAG A 618 14 HET BMA A 619 11 HET NAG A 620 14 HET NAG A 621 14 HET NAG A 622 14 HET NAG A 623 14 HET BMA A 624 11 HET NAG A 625 14 HET NAG A 626 14 HET BMA A 627 11 HET MAN A 628 11 HET MAN A 629 11 HET MAN A 630 11 HET NAG A 631 14 HET NAG A 632 14 HET NAG A 633 14 HET NAG A 634 14 HET NAG A 635 14 HET NAG A 636 14 HET NAG A 637 14 HET BMA A 638 11 HET NAG A 639 14 HET NAG A 640 14 HET BMA A 641 11 HET MAN A 642 11 HET MAN A 643 11 HET NAG A 644 14 HET NAG A 645 14 HET BMA A 646 11 HET NAG A 647 14 HET NAG B 601 14 HET NAG B 602 14 HET BMA B 603 11 HET MAN B 604 11 HET NAG B 605 14 HET NAG B 606 14 HET NAG B 607 14 HET NAG B 608 14 HET BMA B 609 11 HET MAN B 610 11 HET NAG B 611 14 HET NAG B 612 14 HET BMA B 613 11 HET MAN B 614 11 HET MAN B 615 11 HET NAG B 616 14 HET NAG B 617 14 HET BMA B 618 11 HET NAG B 619 14 HET NAG B 620 14 HET NAG B 621 14 HET NAG B 622 14 HET BMA B 623 11 HET NAG B 624 14 HET NAG B 625 14 HET BMA B 626 11 HET MAN B 627 11 HET MAN B 628 11 HET MAN B 629 11 HET NAG B 630 14 HET NAG B 631 14 HET NAG B 632 14 HET NAG B 633 14 HET NAG B 634 14 HET NAG B 635 14 HET NAG B 636 14 HET BMA B 637 11 HET NAG B 638 14 HET NAG B 639 14 HET BMA B 640 11 HET MAN B 641 11 HET MAN B 642 11 HET NAG B 643 14 HET NAG B 644 14 HET BMA B 645 11 HET NAG B 646 14 HET NAG C 601 14 HET NAG C 602 14 HET BMA C 603 11 HET MAN C 604 11 HET MAN C 605 11 HET NAG C 606 14 HET NAG C 607 14 HET NAG C 608 14 HET NAG C 609 14 HET BMA C 610 11 HET MAN C 611 11 HET NAG C 612 14 HET NAG C 613 14 HET BMA C 614 11 HET MAN C 615 11 HET MAN C 616 11 HET NAG C 617 14 HET NAG C 618 14 HET BMA C 619 11 HET NAG C 620 14 HET NAG C 621 14 HET NAG C 622 14 HET NAG C 623 14 HET BMA C 624 11 HET NAG C 625 14 HET NAG C 626 14 HET BMA C 627 11 HET MAN C 628 11 HET MAN C 629 11 HET MAN C 630 11 HET NAG C 631 14 HET NAG C 632 14 HET NAG C 633 14 HET NAG C 634 14 HET NAG C 635 14 HET NAG C 636 14 HET NAG C 637 14 HET BMA C 638 11 HET NAG C 639 14 HET NAG C 640 14 HET BMA C 641 11 HET MAN C 642 11 HET MAN C 643 11 HET NAG C 644 14 HET NAG C 645 14 HET BMA C 646 11 HET NAG C 647 14 HET NAG D 701 14 HET NAG E 701 14 HET NAG R 201 14 HET NAG R 202 14 HET BMA R 203 11 HET MAN R 204 11 HET NAG h 201 14 HET NAG h 202 14 HET BMA h 203 11 HET MAN h 204 11 HET NAG i 201 14 HET NAG i 202 14 HET BMA i 203 11 HET MAN i 204 11 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 25 NAG 93(C8 H15 N O6) FORMUL 26 BMA 30(C6 H12 O6) FORMUL 26 MAN 32(C6 H12 O6) HELIX 1 AA1 ASN 1 60 LYS 1 64 5 5 HELIX 2 AA2 THR 1 83 THR 1 87 5 5 HELIX 3 AA3 GLU 2 79 VAL 2 83 5 5 HELIX 4 AA4 ASN 3 60 LYS 3 64 5 5 HELIX 5 AA5 THR 3 83 THR 3 87 5 5 HELIX 6 AA6 GLU 4 79 VAL 4 83 5 5 HELIX 7 AA7 THR 6 529 SER 6 534 1 6 HELIX 8 AA8 LEU 6 537 ASN 6 543 1 7 HELIX 9 AA9 VAL 6 570 ILE 6 595 1 26 HELIX 10 AB1 ASN 6 611 ASN 6 616 1 6 HELIX 11 AB2 ASN 6 618 MET 6 626 1 9 HELIX 12 AB3 THR 6 627 ILE 6 635 1 9 HELIX 13 AB4 ILE 6 641 ASP 6 664 1 24 HELIX 14 AB5 ASP A 57 GLU A 62 1 6 HELIX 15 AB6 MET A 100 SER A 115 1 16 HELIX 16 AB7 LEU A 122 CYS A 126 5 5 HELIX 17 AB8 ASN A 195 THR A 198 5 4 HELIX 18 AB9 SER A 334 ARG A 350 1 17 HELIX 19 AC1 ASP A 368 THR A 373 1 6 HELIX 20 AC2 MET A 475 ARG A 480 1 6 HELIX 21 AC3 ASP B 57 GLU B 62 1 6 HELIX 22 AC4 THR B 63 ASN B 67 5 5 HELIX 23 AC5 MET B 100 SER B 115 1 16 HELIX 24 AC6 LEU B 122 CYS B 126 5 5 HELIX 25 AC7 ASN B 195 THR B 198 5 4 HELIX 26 AC8 LYS B 335 ARG B 350 1 16 HELIX 27 AC9 ASP B 368 THR B 373 1 6 HELIX 28 AD1 MET B 475 ARG B 480 1 6 HELIX 29 AD2 ASP C 57 GLU C 62 1 6 HELIX 30 AD3 THR C 63 ASN C 67 5 5 HELIX 31 AD4 MET C 100 SER C 115 1 16 HELIX 32 AD5 LEU C 122 CYS C 126 5 5 HELIX 33 AD6 ASN C 195 THR C 198 5 4 HELIX 34 AD7 LYS C 335 ARG C 350 1 16 HELIX 35 AD8 ASP C 368 THR C 373 1 6 HELIX 36 AD9 MET C 475 ARG C 480 1 6 HELIX 37 AE1 THR D 529 SER D 534 1 6 HELIX 38 AE2 LEU D 537 ASN D 543 1 7 HELIX 39 AE3 VAL D 570 ILE D 595 1 26 HELIX 40 AE4 ASN D 611 ASN D 616 1 6 HELIX 41 AE5 ASN D 618 MET D 626 1 9 HELIX 42 AE6 THR D 627 ILE D 635 1 9 HELIX 43 AE7 ILE D 641 ASP D 664 1 24 HELIX 44 AE8 LEU E 523 GLY E 527 5 5 HELIX 45 AE9 THR E 529 SER E 534 1 6 HELIX 46 AF1 LEU E 537 ASN E 543 1 7 HELIX 47 AF2 VAL E 570 ILE E 595 1 26 HELIX 48 AF3 ASN E 611 ASN E 616 1 6 HELIX 49 AF4 ASN E 618 MET E 626 1 9 HELIX 50 AF5 THR E 627 ILE E 635 1 9 HELIX 51 AF6 ILE E 641 ASP E 664 1 24 HELIX 52 AF7 ASN H 60 LYS H 64 5 5 HELIX 53 AF8 THR H 83 THR H 87 5 5 HELIX 54 AF9 GLU L 79 VAL L 83 5 5 HELIX 55 AG1 THR M 83 SER M 87 5 5 HELIX 56 AG2 GLU N 79 GLU N 83 5 5 HELIX 57 AG3 ARG Q 62 GLN Q 65 5 4 HELIX 58 AG4 THR Q 94 THR Q 98 5 5 HELIX 59 AG5 THR X 83 SER X 87 5 5 HELIX 60 AG6 THR Y 83 SER Y 87 5 5 HELIX 61 AG7 GLU Z 79 GLU Z 83 5 5 HELIX 62 AG8 GLU a 79 GLU a 83 5 5 HELIX 63 AG9 ARG f 62 GLN f 65 5 4 HELIX 64 AH1 THR f 94 THR f 98 5 5 HELIX 65 AH2 ARG g 62 GLN g 65 5 4 HELIX 66 AH3 THR g 94 THR g 98 5 5 SHEET 1 AA1 4 GLN 1 3 SER 1 7 0 SHEET 2 AA1 4 THR 1 21 SER 1 25 -1 O ALA 1 23 N VAL 1 5 SHEET 3 AA1 4 GLN 1 77 SER 1 79 -1 O PHE 1 78 N CYS 1 22 SHEET 4 AA1 4 LEU 1 70 ASP 1 72 -1 N ASP 1 72 O GLN 1 77 SHEET 1 AA2 5 LEU 1 11 VAL 1 12 0 SHEET 2 AA2 5 PHE 1 107 VAL 1 111 1 O THR 1 110 N VAL 1 12 SHEET 3 AA2 5 ALA 1 88 GLU 1 95 -1 N ALA 1 88 O VAL 1 109 SHEET 4 AA2 5 TRP 1 33 GLN 1 39 -1 N GLN 1 39 O LEU 1 89 SHEET 5 AA2 5 GLU 1 46 SER 1 52 -1 O GLU 1 46 N ARG 1 38 SHEET 1 AA3 2 LEU 1 18 SER 1 19 0 SHEET 2 AA3 2 ARG 1 81 LEU 1 82 -1 O LEU 1 82 N LEU 1 18 SHEET 1 AA4 4 MET 2 4 SER 2 7 0 SHEET 2 AA4 4 ALA 2 19 SER 2 25 -1 O SER 2 22 N SER 2 7 SHEET 3 AA4 4 ASN 2 70 ILE 2 75 -1 O LEU 2 73 N ILE 2 21 SHEET 4 AA4 4 PHE 2 62 THR 2 67 -1 N SER 2 65 O THR 2 72 SHEET 1 AA5 4 ARG 2 45 TYR 2 49 0 SHEET 2 AA5 4 LEU 2 33 GLN 2 38 -1 N GLN 2 37 O ARG 2 45 SHEET 3 AA5 4 GLY 2 84 GLN 2 90 -1 O VAL 2 85 N GLN 2 38 SHEET 4 AA5 4 LYS 2 103 VAL 2 104 -1 O VAL 2 104 N GLY 2 84 SHEET 1 AA6 4 GLN 3 3 SER 3 7 0 SHEET 2 AA6 4 THR 3 21 SER 3 25 -1 O ALA 3 23 N VAL 3 5 SHEET 3 AA6 4 GLN 3 77 SER 3 79 -1 O PHE 3 78 N CYS 3 22 SHEET 4 AA6 4 LEU 3 70 ASP 3 72 -1 N ASP 3 72 O GLN 3 77 SHEET 1 AA7 5 LEU 3 11 VAL 3 12 0 SHEET 2 AA7 5 PHE 3 107 VAL 3 111 1 O THR 3 110 N VAL 3 12 SHEET 3 AA7 5 ALA 3 88 GLU 3 95 -1 N ALA 3 88 O VAL 3 109 SHEET 4 AA7 5 TRP 3 33 GLN 3 39 -1 N GLN 3 39 O LEU 3 89 SHEET 5 AA7 5 GLU 3 46 SER 3 52 -1 O GLU 3 46 N ARG 3 38 SHEET 1 AA8 2 LEU 3 18 SER 3 19 0 SHEET 2 AA8 2 ARG 3 81 LEU 3 82 -1 O LEU 3 82 N LEU 3 18 SHEET 1 AA9 4 MET 4 4 SER 4 7 0 SHEET 2 AA9 4 ALA 4 19 SER 4 25 -1 O SER 4 22 N SER 4 7 SHEET 3 AA9 4 ASN 4 70 ILE 4 75 -1 O LEU 4 73 N ILE 4 21 SHEET 4 AA9 4 PHE 4 62 THR 4 67 -1 N SER 4 63 O LYS 4 74 SHEET 1 AB1 4 ARG 4 45 TYR 4 49 0 SHEET 2 AB1 4 LEU 4 33 GLN 4 38 -1 N GLN 4 37 O ARG 4 45 SHEET 3 AB1 4 GLY 4 84 GLN 4 90 -1 O GLY 4 89 N SER 4 34 SHEET 4 AB1 4 LYS 4 103 VAL 4 104 -1 O VAL 4 104 N GLY 4 84 SHEET 1 AB2 3 ILE 6 603 PRO 6 609 0 SHEET 2 AB2 3 TRP A 35 TYR A 39 -1 O VAL A 38 N CYS 6 604 SHEET 3 AB2 3 GLY A 495 THR A 499 -1 O GLY A 495 N TYR A 39 SHEET 1 AB3 4 TRP A 45 ASP A 47 0 SHEET 2 AB3 4 TYR A 486 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AB3 4 PHE A 223 CYS A 228 -1 N ALA A 224 O VAL A 489 SHEET 4 AB3 4 VAL A 242 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 1 AB4 3 VAL A 75 PRO A 76 0 SHEET 2 AB4 3 PHE A 53 SER A 56 1 N SER A 56 O VAL A 75 SHEET 3 AB4 3 ILE A 215 CYS A 218 -1 O HIS A 216 N ALA A 55 SHEET 1 AB5 2 GLU A 91 ASN A 94 0 SHEET 2 AB5 2 THR A 236 CYS A 239 -1 O CYS A 239 N GLU A 91 SHEET 1 AB6 5 LYS A 169 TYR A 177 0 SHEET 2 AB6 5 LEU A 154 THR A 162 -1 N MET A 161 O GLN A 170 SHEET 3 AB6 5 LEU A 129 ASN A 133 -1 N GLN A 130 O SER A 158 SHEET 4 AB6 5 GLU A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 5 AB6 5 VAL A 181 GLN A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AB7 3 CYS A 201 GLN A 203 0 SHEET 2 AB7 3 CYS A 433 TYR A 435 1 O CYS A 433 N THR A 202 SHEET 3 AB7 3 ILE A 423 ILE A 424 -1 N ILE A 424 O MET A 434 SHEET 1 AB8 7 LEU A 260 LEU A 261 0 SHEET 2 AB8 7 ILE A 443 ARG A 456 -1 O THR A 450 N LEU A 260 SHEET 3 AB8 7 ILE A 284 ARG A 298 -1 N VAL A 292 O ILE A 449 SHEET 4 AB8 7 HIS A 330 VAL A 333 -1 O ASN A 332 N ASN A 295 SHEET 5 AB8 7 LEU A 416 ARG A 419 -1 O LEU A 416 N CYS A 331 SHEET 6 AB8 7 GLU A 381 CYS A 385 -1 N TYR A 384 O ARG A 419 SHEET 7 AB8 7 HIS A 374 CYS A 378 -1 N HIS A 374 O CYS A 385 SHEET 1 AB9 6 MET A 271 SER A 274 0 SHEET 2 AB9 6 ILE A 284 ARG A 298 -1 O GLN A 287 N MET A 271 SHEET 3 AB9 6 ILE A 443 ARG A 456 -1 O ILE A 449 N VAL A 292 SHEET 4 AB9 6 GLU A 466 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 5 AB9 6 ILE A 359 PHE A 361 1 N ARG A 360 O PHE A 468 SHEET 6 AB9 6 SER A 393 TRP A 395 -1 O SER A 393 N PHE A 361 SHEET 1 AC1 2 ASN A 302 GLY A 312 0 SHEET 2 AC1 2 GLN A 315 ILE A 322 -1 O GLY A 321 N THR A 303 SHEET 1 AC2 3 GLY B 495 THR B 499 0 SHEET 2 AC2 3 TRP B 35 TYR B 39 -1 N TYR B 39 O GLY B 495 SHEET 3 AC2 3 ILE E 603 PRO E 609 -1 O CYS E 604 N VAL B 38 SHEET 1 AC3 4 TRP B 45 ASP B 47 0 SHEET 2 AC3 4 TYR B 486 ILE B 491 -1 O LYS B 490 N LYS B 46 SHEET 3 AC3 4 PHE B 223 CYS B 228 -1 N ALA B 224 O VAL B 489 SHEET 4 AC3 4 VAL B 242 VAL B 245 -1 O SER B 243 N LYS B 227 SHEET 1 AC4 3 VAL B 75 PRO B 76 0 SHEET 2 AC4 3 PHE B 53 SER B 56 1 N SER B 56 O VAL B 75 SHEET 3 AC4 3 ILE B 215 CYS B 218 -1 O HIS B 216 N ALA B 55 SHEET 1 AC5 2 GLU B 91 ASN B 94 0 SHEET 2 AC5 2 THR B 236 CYS B 239 -1 O CYS B 239 N GLU B 91 SHEET 1 AC6 5 LYS B 169 TYR B 177 0 SHEET 2 AC6 5 LEU B 154 THR B 162 -1 N MET B 161 O GLN B 170 SHEET 3 AC6 5 LEU B 129 ASN B 133 -1 N GLN B 130 O SER B 158 SHEET 4 AC6 5 GLU B 190 LEU B 193 -1 O TYR B 191 N LEU B 129 SHEET 5 AC6 5 VAL B 181 GLN B 183 -1 N VAL B 182 O ARG B 192 SHEET 1 AC7 3 CYS B 201 GLN B 203 0 SHEET 2 AC7 3 CYS B 433 TYR B 435 1 O CYS B 433 N THR B 202 SHEET 3 AC7 3 ILE B 423 ILE B 424 -1 N ILE B 424 O MET B 434 SHEET 1 AC8 7 LEU B 260 LEU B 261 0 SHEET 2 AC8 7 ILE B 443 ARG B 456 -1 O THR B 450 N LEU B 260 SHEET 3 AC8 7 ILE B 284 ARG B 298 -1 N VAL B 292 O ILE B 449 SHEET 4 AC8 7 HIS B 330 SER B 334 -1 O ASN B 332 N ASN B 295 SHEET 5 AC8 7 SER B 413 ARG B 419 -1 O LEU B 416 N CYS B 331 SHEET 6 AC8 7 GLU B 381 CYS B 385 -1 N TYR B 384 O ARG B 419 SHEET 7 AC8 7 HIS B 374 CYS B 378 -1 N HIS B 374 O CYS B 385 SHEET 1 AC9 6 MET B 271 SER B 274 0 SHEET 2 AC9 6 ILE B 284 ARG B 298 -1 O GLN B 287 N MET B 271 SHEET 3 AC9 6 ILE B 443 ARG B 456 -1 O ILE B 449 N VAL B 292 SHEET 4 AC9 6 GLU B 466 PRO B 470 -1 O ARG B 469 N THR B 455 SHEET 5 AC9 6 ILE B 359 PHE B 361 1 N ARG B 360 O PHE B 468 SHEET 6 AC9 6 SER B 393 TRP B 395 -1 O SER B 393 N PHE B 361 SHEET 1 AD1 2 ASN B 302 GLY B 312 0 SHEET 2 AD1 2 GLN B 315 ILE B 322 -1 O GLY B 321 N THR B 303 SHEET 1 AD2 3 GLY C 495 THR C 499 0 SHEET 2 AD2 3 TRP C 35 TYR C 39 -1 N TYR C 39 O GLY C 495 SHEET 3 AD2 3 ILE D 603 PRO D 609 -1 O CYS D 604 N VAL C 38 SHEET 1 AD3 4 TRP C 45 ASP C 47 0 SHEET 2 AD3 4 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AD3 4 PHE C 223 CYS C 228 -1 N ALA C 224 O VAL C 489 SHEET 4 AD3 4 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 1 AD4 3 VAL C 75 PRO C 76 0 SHEET 2 AD4 3 PHE C 53 SER C 56 1 N SER C 56 O VAL C 75 SHEET 3 AD4 3 ILE C 215 CYS C 218 -1 O HIS C 216 N ALA C 55 SHEET 1 AD5 2 GLU C 91 ASN C 94 0 SHEET 2 AD5 2 THR C 236 CYS C 239 -1 O CYS C 239 N GLU C 91 SHEET 1 AD6 5 LYS C 169 TYR C 177 0 SHEET 2 AD6 5 LEU C 154 THR C 162 -1 N MET C 161 O GLN C 170 SHEET 3 AD6 5 LEU C 129 ASN C 133 -1 N GLN C 130 O SER C 158 SHEET 4 AD6 5 GLU C 190 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AD6 5 VAL C 181 GLN C 183 -1 N VAL C 182 O ARG C 192 SHEET 1 AD7 3 CYS C 201 GLN C 203 0 SHEET 2 AD7 3 CYS C 433 TYR C 435 1 O CYS C 433 N THR C 202 SHEET 3 AD7 3 ILE C 423 ILE C 424 -1 N ILE C 424 O MET C 434 SHEET 1 AD8 7 LEU C 260 LEU C 261 0 SHEET 2 AD8 7 ILE C 443 ARG C 456 -1 O THR C 450 N LEU C 260 SHEET 3 AD8 7 ILE C 284 ARG C 298 -1 N VAL C 292 O ILE C 449 SHEET 4 AD8 7 HIS C 330 SER C 334 -1 O ASN C 332 N ASN C 295 SHEET 5 AD8 7 SER C 413 ARG C 419 -1 O LEU C 416 N CYS C 331 SHEET 6 AD8 7 GLU C 381 CYS C 385 -1 N TYR C 384 O ARG C 419 SHEET 7 AD8 7 HIS C 374 CYS C 378 -1 N HIS C 374 O CYS C 385 SHEET 1 AD9 6 MET C 271 ARG C 273 0 SHEET 2 AD9 6 ILE C 284 ARG C 298 -1 O GLN C 287 N MET C 271 SHEET 3 AD9 6 ILE C 443 ARG C 456 -1 O ILE C 449 N VAL C 292 SHEET 4 AD9 6 GLU C 466 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 5 AD9 6 ILE C 359 PHE C 361 1 N ARG C 360 O PHE C 468 SHEET 6 AD9 6 SER C 393 TRP C 395 -1 O SER C 393 N PHE C 361 SHEET 1 AE1 2 ASN C 302 GLY C 312 0 SHEET 2 AE1 2 GLN C 315 ILE C 322 -1 O GLY C 321 N THR C 303 SHEET 1 AE2 4 GLN H 3 SER H 7 0 SHEET 2 AE2 4 THR H 21 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AE2 4 GLN H 77 SER H 79 -1 O PHE H 78 N CYS H 22 SHEET 4 AE2 4 LEU H 70 ASP H 72 -1 N ASP H 72 O GLN H 77 SHEET 1 AE3 2 LEU H 18 SER H 19 0 SHEET 2 AE3 2 ARG H 81 LEU H 82 -1 O LEU H 82 N LEU H 18 SHEET 1 AE4 4 GLU H 46 SER H 52 0 SHEET 2 AE4 4 TRP H 33 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 3 AE4 4 ALA H 88 GLU H 95 -1 O LEU H 89 N GLN H 39 SHEET 4 AE4 4 PHE H 107 VAL H 109 -1 O VAL H 109 N ALA H 88 SHEET 1 AE5 4 MET L 4 SER L 7 0 SHEET 2 AE5 4 ALA L 19 SER L 25 -1 O SER L 22 N SER L 7 SHEET 3 AE5 4 ASN L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AE5 4 PHE L 62 THR L 67 -1 N SER L 63 O LYS L 74 SHEET 1 AE6 4 ARG L 45 TYR L 49 0 SHEET 2 AE6 4 LEU L 33 GLN L 38 -1 N GLN L 37 O ARG L 45 SHEET 3 AE6 4 GLY L 84 GLN L 90 -1 O VAL L 85 N GLN L 38 SHEET 4 AE6 4 LYS L 103 VAL L 104 -1 O VAL L 104 N GLY L 84 SHEET 1 AE7 4 GLN M 5 SER M 7 0 SHEET 2 AE7 4 LEU M 18 ASN M 23 -1 O THR M 21 N SER M 7 SHEET 3 AE7 4 LEU M 77 LEU M 82 -1 O LEU M 82 N LEU M 18 SHEET 4 AE7 4 VAL M 67 ASP M 72 -1 N HIS M 68 O ARG M 81 SHEET 1 AE8 5 LEU M 11 VAL M 12 0 SHEET 2 AE8 5 THR M 105 VAL M 109 1 O THR M 108 N VAL M 12 SHEET 3 AE8 5 ALA M 88 ILE M 100A-1 N TYR M 90 O THR M 105 SHEET 4 AE8 5 TYR M 33 GLN M 39 -1 N ILE M 37 O TYR M 91 SHEET 5 AE8 5 GLU M 46 VAL M 51 -1 O GLU M 46 N ARG M 38 SHEET 1 AE9 4 LEU M 11 VAL M 12 0 SHEET 2 AE9 4 THR M 105 VAL M 109 1 O THR M 108 N VAL M 12 SHEET 3 AE9 4 ALA M 88 ILE M 100A-1 N TYR M 90 O THR M 105 SHEET 4 AE9 4 TRP M 100J MET M 100P-1 O PHE M 100K N ARG M 100 SHEET 1 AF1 2 SER N 12 VAL N 13 0 SHEET 2 AF1 2 ILE N 105 VAL N 106 1 O ILE N 105 N VAL N 13 SHEET 1 AF2 3 ALA N 19 GLU N 26 0 SHEET 2 AF2 3 THR N 70 ILE N 75 -1 O LEU N 73 N ILE N 21 SHEET 3 AF2 3 PHE N 62 GLY N 64 -1 N SER N 63 O THR N 74 SHEET 1 AF3 4 PRO N 44 ILE N 48 0 SHEET 2 AF3 4 ARG N 31 GLN N 38 -1 N GLN N 37 O SER N 45 SHEET 3 AF3 4 ASP N 85 ASP N 92 -1 O TYR N 87 N TYR N 36 SHEET 4 AF3 4 THR N 102 THR N 103 -1 O THR N 102 N TYR N 86 SHEET 1 AF4 4 GLN Q 3 VAL Q 5 0 SHEET 2 AF4 4 VAL Q 18 SER Q 25 -1 O ARG Q 23 N VAL Q 5 SHEET 3 AF4 4 GLY Q 84 PHE Q 90 -1 O ALA Q 86 N CYS Q 22 SHEET 4 AF4 4 VAL Q 68 GLN Q 73 -1 N SER Q 69 O GLU Q 89 SHEET 1 AF5 6 VAL Q 10 LYS Q 12 0 SHEET 2 AF5 6 THR Q 124 VAL Q 128 1 O VAL Q 125 N VAL Q 10 SHEET 3 AF5 6 ALA Q 99 ARG Q 106 -1 N ALA Q 99 O VAL Q 126 SHEET 4 AF5 6 ILE Q 34 ILE Q 40 -1 N VAL Q 37 O PHE Q 102 SHEET 5 AF5 6 GLY Q 44 LYS Q 52 -1 O ILE Q 48 N TRP Q 36 SHEET 6 AF5 6 ALA Q 57 TYR Q 60 -1 O ALA Q 57 N LYS Q 52 SHEET 1 AF6 4 VAL Q 10 LYS Q 12 0 SHEET 2 AF6 4 THR Q 124 VAL Q 128 1 O VAL Q 125 N VAL Q 10 SHEET 3 AF6 4 ALA Q 99 ARG Q 106 -1 N ALA Q 99 O VAL Q 126 SHEET 4 AF6 4 TRP Q 117 TRP Q 120 -1 O TYR Q 119 N ARG Q 105 SHEET 1 AF7 4 THR R 5 GLN R 6 0 SHEET 2 AF7 4 ALA R 19 LYS R 24 -1 O LYS R 24 N THR R 5 SHEET 3 AF7 4 ASP R 70 ILE R 75 -1 O PHE R 71 N CYS R 23 SHEET 4 AF7 4 PHE R 62 SER R 67 -1 N VAL R 63 O THR R 74 SHEET 1 AF8 6 ILE R 10 LEU R 13 0 SHEET 2 AF8 6 SER R 102 VAL R 106 1 O GLU R 105 N LEU R 11 SHEET 3 AF8 6 VAL R 85 GLN R 90 -1 N TYR R 86 O SER R 102 SHEET 4 AF8 6 THR R 33 LYS R 38 -1 N LYS R 38 O VAL R 85 SHEET 5 AF8 6 ARG R 45 TYR R 49 -1 O ARG R 45 N GLN R 37 SHEET 6 AF8 6 ARG R 53 ARG R 54 -1 O ARG R 53 N TYR R 49 SHEET 1 AF9 4 ILE R 10 LEU R 13 0 SHEET 2 AF9 4 SER R 102 VAL R 106 1 O GLU R 105 N LEU R 11 SHEET 3 AF9 4 VAL R 85 GLN R 90 -1 N TYR R 86 O SER R 102 SHEET 4 AF9 4 PHE R 97 PHE R 98 -1 O PHE R 97 N GLN R 90 SHEET 1 AG1 4 GLN X 5 SER X 7 0 SHEET 2 AG1 4 LEU X 18 ASN X 23 -1 O THR X 21 N SER X 7 SHEET 3 AG1 4 LEU X 77 LEU X 82 -1 O LEU X 82 N LEU X 18 SHEET 4 AG1 4 VAL X 67 ASP X 72 -1 N HIS X 68 O ARG X 81 SHEET 1 AG2 5 LEU X 11 VAL X 12 0 SHEET 2 AG2 5 THR X 105 VAL X 109 1 O THR X 108 N VAL X 12 SHEET 3 AG2 5 ALA X 88 ILE X 100A-1 N TYR X 90 O THR X 105 SHEET 4 AG2 5 TYR X 33 GLN X 39 -1 N ILE X 37 O TYR X 91 SHEET 5 AG2 5 GLU X 46 VAL X 51 -1 O GLU X 46 N ARG X 38 SHEET 1 AG3 4 LEU X 11 VAL X 12 0 SHEET 2 AG3 4 THR X 105 VAL X 109 1 O THR X 108 N VAL X 12 SHEET 3 AG3 4 ALA X 88 ILE X 100A-1 N TYR X 90 O THR X 105 SHEET 4 AG3 4 TRP X 100J MET X 100P-1 O PHE X 100K N ARG X 100 SHEET 1 AG4 4 GLN Y 5 SER Y 7 0 SHEET 2 AG4 4 LEU Y 18 ASN Y 23 -1 O THR Y 21 N SER Y 7 SHEET 3 AG4 4 LEU Y 77 LEU Y 82 -1 O LEU Y 82 N LEU Y 18 SHEET 4 AG4 4 VAL Y 67 ASP Y 72 -1 N HIS Y 68 O ARG Y 81 SHEET 1 AG5 5 LEU Y 11 VAL Y 12 0 SHEET 2 AG5 5 THR Y 105 VAL Y 109 1 O THR Y 108 N VAL Y 12 SHEET 3 AG5 5 ALA Y 88 ILE Y 100A-1 N TYR Y 90 O THR Y 105 SHEET 4 AG5 5 TYR Y 33 GLN Y 39 -1 N ILE Y 37 O TYR Y 91 SHEET 5 AG5 5 GLU Y 46 VAL Y 51 -1 O GLU Y 46 N ARG Y 38 SHEET 1 AG6 4 LEU Y 11 VAL Y 12 0 SHEET 2 AG6 4 THR Y 105 VAL Y 109 1 O THR Y 108 N VAL Y 12 SHEET 3 AG6 4 ALA Y 88 ILE Y 100A-1 N TYR Y 90 O THR Y 105 SHEET 4 AG6 4 TRP Y 100J MET Y 100P-1 O PHE Y 100K N ARG Y 100 SHEET 1 AG7 2 SER Z 12 VAL Z 13 0 SHEET 2 AG7 2 ILE Z 105 VAL Z 106 1 O ILE Z 105 N VAL Z 13 SHEET 1 AG8 3 ALA Z 19 GLU Z 26 0 SHEET 2 AG8 3 THR Z 70 ILE Z 75 -1 O ILE Z 75 N ALA Z 19 SHEET 3 AG8 3 PHE Z 62 GLY Z 64 -1 N SER Z 63 O THR Z 74 SHEET 1 AG9 4 PRO Z 44 ILE Z 48 0 SHEET 2 AG9 4 ARG Z 31 GLN Z 38 -1 N GLN Z 37 O SER Z 45 SHEET 3 AG9 4 ASP Z 85 ASP Z 92 -1 O TYR Z 87 N TYR Z 36 SHEET 4 AG9 4 THR Z 102 THR Z 103 -1 O THR Z 102 N TYR Z 86 SHEET 1 AH1 2 SER a 12 VAL a 13 0 SHEET 2 AH1 2 ILE a 105 VAL a 106 1 O ILE a 105 N VAL a 13 SHEET 1 AH2 3 ALA a 19 GLU a 26 0 SHEET 2 AH2 3 THR a 70 ILE a 75 -1 O ILE a 75 N ALA a 19 SHEET 3 AH2 3 PHE a 62 GLY a 64 -1 N SER a 63 O THR a 74 SHEET 1 AH3 4 PRO a 44 ILE a 48 0 SHEET 2 AH3 4 ARG a 31 GLN a 38 -1 N GLN a 37 O SER a 45 SHEET 3 AH3 4 ASP a 85 ASP a 92 -1 O TYR a 87 N TYR a 36 SHEET 4 AH3 4 THR a 102 THR a 103 -1 O THR a 102 N TYR a 86 SHEET 1 AH4 4 GLN f 3 VAL f 5 0 SHEET 2 AH4 4 VAL f 18 SER f 25 -1 O ARG f 23 N VAL f 5 SHEET 3 AH4 4 GLY f 84 PHE f 90 -1 O ALA f 86 N CYS f 22 SHEET 4 AH4 4 VAL f 68 GLN f 73 -1 N SER f 69 O GLU f 89 SHEET 1 AH5 6 VAL f 10 LYS f 12 0 SHEET 2 AH5 6 THR f 124 VAL f 128 1 O VAL f 125 N VAL f 10 SHEET 3 AH5 6 ALA f 99 ARG f 106 -1 N ALA f 99 O VAL f 126 SHEET 4 AH5 6 ILE f 34 ILE f 40 -1 N VAL f 37 O PHE f 102 SHEET 5 AH5 6 GLY f 44 LYS f 52 -1 O ILE f 48 N TRP f 36 SHEET 6 AH5 6 ALA f 57 TYR f 60 -1 O ALA f 57 N LYS f 52 SHEET 1 AH6 4 VAL f 10 LYS f 12 0 SHEET 2 AH6 4 THR f 124 VAL f 128 1 O VAL f 125 N VAL f 10 SHEET 3 AH6 4 ALA f 99 ARG f 106 -1 N ALA f 99 O VAL f 126 SHEET 4 AH6 4 TRP f 117 TRP f 120 -1 O TYR f 119 N ARG f 105 SHEET 1 AH7 4 GLN g 3 VAL g 5 0 SHEET 2 AH7 4 VAL g 18 SER g 25 -1 O ARG g 23 N VAL g 5 SHEET 3 AH7 4 GLY g 84 PHE g 90 -1 O ALA g 86 N CYS g 22 SHEET 4 AH7 4 VAL g 68 GLN g 73 -1 N SER g 69 O GLU g 89 SHEET 1 AH8 6 VAL g 10 LYS g 12 0 SHEET 2 AH8 6 THR g 124 VAL g 128 1 O VAL g 125 N VAL g 10 SHEET 3 AH8 6 ALA g 99 ARG g 106 -1 N TYR g 101 O THR g 124 SHEET 4 AH8 6 ILE g 34 ILE g 40 -1 N VAL g 37 O PHE g 102 SHEET 5 AH8 6 GLY g 44 LYS g 52 -1 O ILE g 48 N TRP g 36 SHEET 6 AH8 6 ALA g 57 TYR g 60 -1 O ALA g 57 N LYS g 52 SHEET 1 AH9 4 VAL g 10 LYS g 12 0 SHEET 2 AH9 4 THR g 124 VAL g 128 1 O VAL g 125 N VAL g 10 SHEET 3 AH9 4 ALA g 99 ARG g 106 -1 N TYR g 101 O THR g 124 SHEET 4 AH9 4 TRP g 117 TRP g 120 -1 O TYR g 119 N ARG g 105 SHEET 1 AI1 4 THR h 5 GLN h 6 0 SHEET 2 AI1 4 ALA h 19 LYS h 24 -1 O LYS h 24 N THR h 5 SHEET 3 AI1 4 ASP h 70 ILE h 75 -1 O PHE h 71 N CYS h 23 SHEET 4 AI1 4 PHE h 62 SER h 67 -1 N VAL h 63 O THR h 74 SHEET 1 AI2 6 ILE h 10 LEU h 13 0 SHEET 2 AI2 6 SER h 102 VAL h 106 1 O GLU h 105 N LEU h 11 SHEET 3 AI2 6 VAL h 85 GLN h 90 -1 N TYR h 86 O SER h 102 SHEET 4 AI2 6 THR h 33 LYS h 38 -1 N LYS h 38 O VAL h 85 SHEET 5 AI2 6 ARG h 45 TYR h 49 -1 O ARG h 45 N GLN h 37 SHEET 6 AI2 6 ARG h 53 ARG h 54 -1 O ARG h 53 N TYR h 49 SHEET 1 AI3 4 ILE h 10 LEU h 13 0 SHEET 2 AI3 4 SER h 102 VAL h 106 1 O GLU h 105 N LEU h 11 SHEET 3 AI3 4 VAL h 85 GLN h 90 -1 N TYR h 86 O SER h 102 SHEET 4 AI3 4 PHE h 97 PHE h 98 -1 O PHE h 97 N GLN h 90 SHEET 1 AI4 4 THR i 5 GLN i 6 0 SHEET 2 AI4 4 ALA i 19 LYS i 24 -1 O LYS i 24 N THR i 5 SHEET 3 AI4 4 ASP i 70 ILE i 75 -1 O PHE i 71 N CYS i 23 SHEET 4 AI4 4 PHE i 62 SER i 67 -1 N VAL i 63 O THR i 74 SHEET 1 AI5 6 ILE i 10 LEU i 13 0 SHEET 2 AI5 6 SER i 102 VAL i 106 1 O GLU i 105 N LEU i 11 SHEET 3 AI5 6 VAL i 85 GLN i 90 -1 N TYR i 86 O SER i 102 SHEET 4 AI5 6 THR i 33 LYS i 38 -1 N LYS i 38 O VAL i 85 SHEET 5 AI5 6 ARG i 45 TYR i 49 -1 O ARG i 45 N GLN i 37 SHEET 6 AI5 6 ARG i 53 ARG i 54 -1 O ARG i 53 N TYR i 49 SHEET 1 AI6 4 ILE i 10 LEU i 13 0 SHEET 2 AI6 4 SER i 102 VAL i 106 1 O GLU i 105 N LEU i 11 SHEET 3 AI6 4 VAL i 85 GLN i 90 -1 N TYR i 86 O SER i 102 SHEET 4 AI6 4 PHE i 97 PHE i 98 -1 O PHE i 97 N GLN i 90 SSBOND 1 CYS 1 22 CYS 1 92 1555 1555 2.03 SSBOND 2 CYS 2 23 CYS 2 88 1555 1555 2.03 SSBOND 3 CYS 3 22 CYS 3 92 1555 1555 2.03 SSBOND 4 CYS 4 23 CYS 4 88 1555 1555 2.03 SSBOND 5 CYS 6 598 CYS 6 604 1555 1555 2.02 SSBOND 6 CYS 6 605 CYS A 501 1555 1555 2.03 SSBOND 7 CYS A 54 CYS A 74 1555 1555 2.03 SSBOND 8 CYS A 119 CYS A 205 1555 1555 2.03 SSBOND 9 CYS A 126 CYS A 196 1555 1555 2.03 SSBOND 10 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 11 CYS A 201 CYS A 433 1555 1555 2.03 SSBOND 12 CYS A 218 CYS A 247 1555 1555 2.03 SSBOND 13 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 14 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 15 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 16 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 17 CYS B 54 CYS B 74 1555 1555 2.03 SSBOND 18 CYS B 119 CYS B 205 1555 1555 2.03 SSBOND 19 CYS B 126 CYS B 196 1555 1555 2.03 SSBOND 20 CYS B 131 CYS B 157 1555 1555 2.03 SSBOND 21 CYS B 201 CYS B 433 1555 1555 2.03 SSBOND 22 CYS B 218 CYS B 247 1555 1555 2.03 SSBOND 23 CYS B 228 CYS B 239 1555 1555 2.03 SSBOND 24 CYS B 296 CYS B 331 1555 1555 2.03 SSBOND 25 CYS B 378 CYS B 445 1555 1555 2.03 SSBOND 26 CYS B 385 CYS B 418 1555 1555 2.03 SSBOND 27 CYS B 501 CYS E 605 1555 1555 2.04 SSBOND 28 CYS C 54 CYS C 74 1555 1555 2.03 SSBOND 29 CYS C 119 CYS C 205 1555 1555 2.03 SSBOND 30 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 31 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 32 CYS C 201 CYS C 433 1555 1555 2.03 SSBOND 33 CYS C 218 CYS C 247 1555 1555 2.03 SSBOND 34 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 35 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 36 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 37 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 38 CYS C 501 CYS D 605 1555 1555 2.03 SSBOND 39 CYS D 598 CYS D 604 1555 1555 2.02 SSBOND 40 CYS E 598 CYS E 604 1555 1555 2.02 SSBOND 41 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 42 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 43 CYS M 22 CYS M 92 1555 1555 2.03 SSBOND 44 CYS N 23 CYS N 88 1555 1555 2.03 SSBOND 45 CYS Q 22 CYS Q 103 1555 1555 2.03 SSBOND 46 CYS Q 109 CYS Q 112 1555 1555 2.03 SSBOND 47 CYS X 22 CYS X 92 1555 1555 2.03 SSBOND 48 CYS Y 22 CYS Y 92 1555 1555 2.03 SSBOND 49 CYS Z 23 CYS Z 88 1555 1555 2.03 SSBOND 50 CYS a 23 CYS a 88 1555 1555 2.03 SSBOND 51 CYS f 22 CYS f 103 1555 1555 2.03 SSBOND 52 CYS f 109 CYS f 112 1555 1555 2.03 SSBOND 53 CYS g 22 CYS g 103 1555 1555 2.03 SSBOND 54 CYS g 109 CYS g 112 1555 1555 2.03 LINK ND2 ASN 6 637 C1 NAG 6 701 1555 1555 1.43 LINK ND2 ASN A 88 C1 NAG A 647 1555 1555 1.44 LINK ND2 ASN A 160 C1 NAG A 617 1555 1555 1.45 LINK ND2 ASN A 295 C1 NAG A 631 1555 1555 1.43 LINK ND2 ASN A 332 C1 NAG A 601 1555 1555 1.42 LINK ND2 ASN A 339 C1 NAG A 635 1555 1555 1.44 LINK ND2 ASN A 363 C1 NAG A 636 1555 1555 1.43 LINK ND2 ASN A 386 C1 NAG A 639 1555 1555 1.43 LINK ND2 ASN A 392 C1 NAG A 644 1555 1555 1.45 LINK ND2 ASN B 88 C1 NAG B 646 1555 1555 1.45 LINK ND2 ASN B 160 C1 NAG B 616 1555 1555 1.45 LINK ND2 ASN B 295 C1 NAG B 630 1555 1555 1.43 LINK ND2 ASN B 332 C1 NAG B 601 1555 1555 1.42 LINK ND2 ASN B 339 C1 NAG B 634 1555 1555 1.44 LINK ND2 ASN B 363 C1 NAG B 635 1555 1555 1.43 LINK ND2 ASN B 386 C1 NAG B 638 1555 1555 1.43 LINK ND2 ASN B 392 C1 NAG B 643 1555 1555 1.45 LINK ND2 ASN C 88 C1 NAG C 647 1555 1555 1.44 LINK ND2 ASN C 160 C1 NAG C 617 1555 1555 1.45 LINK ND2 ASN C 295 C1 NAG C 631 1555 1555 1.43 LINK ND2 ASN C 332 C1 NAG C 601 1555 1555 1.42 LINK ND2 ASN C 339 C1 NAG C 635 1555 1555 1.44 LINK ND2 ASN C 363 C1 NAG C 636 1555 1555 1.43 LINK ND2 ASN C 386 C1 NAG C 639 1555 1555 1.43 LINK ND2 ASN C 392 C1 NAG C 644 1555 1555 1.45 LINK ND2 ASN D 637 C1 NAG D 701 1555 1555 1.44 LINK ND2 ASN E 637 C1 NAG E 701 1555 1555 1.43 LINK O4 NAG A 601 C1 NAG A 602 1555 1555 1.42 LINK O4 NAG A 602 C1 BMA A 603 1555 1555 1.44 LINK O3 BMA A 603 C1 MAN A 604 1555 1555 1.44 LINK O6 BMA A 603 C1 MAN A 605 1555 1555 1.44 LINK O4 NAG A 606 C1 NAG A 607 1555 1555 1.45 LINK O4 NAG A 608 C1 NAG A 609 1555 1555 1.44 LINK O4 NAG A 609 C1 BMA A 610 1555 1555 1.45 LINK O3 BMA A 610 C1 MAN A 611 1555 1555 1.45 LINK O4 NAG A 612 C1 NAG A 613 1555 1555 1.45 LINK O4 NAG A 613 C1 BMA A 614 1555 1555 1.45 LINK O3 BMA A 614 C1 MAN A 615 1555 1555 1.44 LINK O6 BMA A 614 C1 MAN A 616 1555 1555 1.44 LINK O4 NAG A 617 C1 NAG A 618 1555 1555 1.43 LINK O4 NAG A 618 C1 BMA A 619 1555 1555 1.45 LINK O4 NAG A 620 C1 NAG A 621 1555 1555 1.44 LINK O4 NAG A 622 C1 NAG A 623 1555 1555 1.45 LINK O4 NAG A 623 C1 BMA A 624 1555 1555 1.44 LINK O4 NAG A 625 C1 NAG A 626 1555 1555 1.44 LINK O4 NAG A 626 C1 BMA A 627 1555 1555 1.44 LINK O3 BMA A 627 C1 MAN A 628 1555 1555 1.44 LINK O6 BMA A 627 C1 MAN A 629 1555 1555 1.44 LINK O2 MAN A 628 C1 MAN A 630 1555 1555 1.44 LINK O4 NAG A 631 C1 NAG A 632 1555 1555 1.44 LINK O4 NAG A 633 C1 NAG A 634 1555 1555 1.45 LINK O4 NAG A 636 C1 NAG A 637 1555 1555 1.44 LINK O4 NAG A 637 C1 BMA A 638 1555 1555 1.45 LINK O4 NAG A 639 C1 NAG A 640 1555 1555 1.42 LINK O4 NAG A 640 C1 BMA A 641 1555 1555 1.45 LINK O3 BMA A 641 C1 MAN A 642 1555 1555 1.44 LINK O6 BMA A 641 C1 MAN A 643 1555 1555 1.44 LINK O4 NAG A 644 C1 NAG A 645 1555 1555 1.45 LINK O4 NAG A 645 C1 BMA A 646 1555 1555 1.45 LINK O4 NAG B 601 C1 NAG B 602 1555 1555 1.43 LINK O4 NAG B 602 C1 BMA B 603 1555 1555 1.44 LINK O3 BMA B 603 C1 MAN B 604 1555 1555 1.44 LINK O4 NAG B 605 C1 NAG B 606 1555 1555 1.45 LINK O4 NAG B 607 C1 NAG B 608 1555 1555 1.44 LINK O4 NAG B 608 C1 BMA B 609 1555 1555 1.45 LINK O3 BMA B 609 C1 MAN B 610 1555 1555 1.45 LINK O4 NAG B 611 C1 NAG B 612 1555 1555 1.45 LINK O4 NAG B 612 C1 BMA B 613 1555 1555 1.45 LINK O3 BMA B 613 C1 MAN B 614 1555 1555 1.44 LINK O6 BMA B 613 C1 MAN B 615 1555 1555 1.44 LINK O4 NAG B 616 C1 NAG B 617 1555 1555 1.44 LINK O4 NAG B 617 C1 BMA B 618 1555 1555 1.45 LINK O4 NAG B 619 C1 NAG B 620 1555 1555 1.44 LINK O4 NAG B 621 C1 NAG B 622 1555 1555 1.45 LINK O4 NAG B 622 C1 BMA B 623 1555 1555 1.44 LINK O4 NAG B 624 C1 NAG B 625 1555 1555 1.44 LINK O4 NAG B 625 C1 BMA B 626 1555 1555 1.44 LINK O3 BMA B 626 C1 MAN B 627 1555 1555 1.44 LINK O6 BMA B 626 C1 MAN B 628 1555 1555 1.44 LINK O2 MAN B 627 C1 MAN B 629 1555 1555 1.44 LINK O4 NAG B 630 C1 NAG B 631 1555 1555 1.45 LINK O4 NAG B 632 C1 NAG B 633 1555 1555 1.45 LINK O4 NAG B 635 C1 NAG B 636 1555 1555 1.44 LINK O4 NAG B 636 C1 BMA B 637 1555 1555 1.45 LINK O4 NAG B 638 C1 NAG B 639 1555 1555 1.43 LINK O4 NAG B 639 C1 BMA B 640 1555 1555 1.45 LINK O3 BMA B 640 C1 MAN B 641 1555 1555 1.44 LINK O6 BMA B 640 C1 MAN B 642 1555 1555 1.44 LINK O4 NAG B 643 C1 NAG B 644 1555 1555 1.44 LINK O4 NAG B 644 C1 BMA B 645 1555 1555 1.45 LINK O4 NAG C 601 C1 NAG C 602 1555 1555 1.42 LINK O4 NAG C 602 C1 BMA C 603 1555 1555 1.43 LINK O3 BMA C 603 C1 MAN C 604 1555 1555 1.44 LINK O6 BMA C 603 C1 MAN C 605 1555 1555 1.44 LINK O4 NAG C 606 C1 NAG C 607 1555 1555 1.44 LINK O4 NAG C 608 C1 NAG C 609 1555 1555 1.44 LINK O4 NAG C 609 C1 BMA C 610 1555 1555 1.45 LINK O3 BMA C 610 C1 MAN C 611 1555 1555 1.45 LINK O4 NAG C 612 C1 NAG C 613 1555 1555 1.45 LINK O4 NAG C 613 C1 BMA C 614 1555 1555 1.45 LINK O3 BMA C 614 C1 MAN C 615 1555 1555 1.44 LINK O6 BMA C 614 C1 MAN C 616 1555 1555 1.44 LINK O4 NAG C 617 C1 NAG C 618 1555 1555 1.43 LINK O4 NAG C 618 C1 BMA C 619 1555 1555 1.45 LINK O4 NAG C 620 C1 NAG C 621 1555 1555 1.44 LINK O4 NAG C 622 C1 NAG C 623 1555 1555 1.45 LINK O4 NAG C 623 C1 BMA C 624 1555 1555 1.44 LINK O4 NAG C 625 C1 NAG C 626 1555 1555 1.44 LINK O4 NAG C 626 C1 BMA C 627 1555 1555 1.44 LINK O3 BMA C 627 C1 MAN C 628 1555 1555 1.44 LINK O6 BMA C 627 C1 MAN C 629 1555 1555 1.44 LINK O2 MAN C 628 C1 MAN C 630 1555 1555 1.44 LINK O4 NAG C 631 C1 NAG C 632 1555 1555 1.44 LINK O4 NAG C 633 C1 NAG C 634 1555 1555 1.45 LINK O4 NAG C 636 C1 NAG C 637 1555 1555 1.44 LINK O4 NAG C 637 C1 BMA C 638 1555 1555 1.45 LINK O4 NAG C 639 C1 NAG C 640 1555 1555 1.42 LINK O4 NAG C 640 C1 BMA C 641 1555 1555 1.45 LINK O3 BMA C 641 C1 MAN C 642 1555 1555 1.44 LINK O6 BMA C 641 C1 MAN C 643 1555 1555 1.44 LINK O4 NAG C 644 C1 NAG C 645 1555 1555 1.44 LINK O4 NAG C 645 C1 BMA C 646 1555 1555 1.45 LINK O4 NAG R 201 C1 NAG R 202 1555 1555 1.43 LINK O4 NAG R 202 C1 BMA R 203 1555 1555 1.45 LINK O3 BMA R 203 C1 MAN R 204 1555 1555 1.45 LINK O4 NAG h 201 C1 NAG h 202 1555 1555 1.43 LINK O4 NAG h 202 C1 BMA h 203 1555 1555 1.45 LINK O3 BMA h 203 C1 MAN h 204 1555 1555 1.45 LINK O4 NAG i 201 C1 NAG i 202 1555 1555 1.44 LINK O4 NAG i 202 C1 BMA i 203 1555 1555 1.45 LINK O3 BMA i 203 C1 MAN i 204 1555 1555 1.45 CISPEP 1 SER 2 7 PRO 2 8 0 -0.04 CISPEP 2 LEU 2 94 PRO 2 95 0 -0.42 CISPEP 3 SER 4 7 PRO 4 8 0 0.03 CISPEP 4 LEU 4 94 PRO 4 95 0 -0.55 CISPEP 5 SER L 7 PRO L 8 0 -0.07 CISPEP 6 LEU L 94 PRO L 95 0 -0.43 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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