HEADER VIRAL PROTEIN 12-NOV-18 6N1W TITLE CRYO-EM STRUCTURE AT 4.2 A RESOLUTION OF VACCINE-ELICITED ANTIBODY TITLE 2 DFPH-A.15 IN COMPLEX WITH HIV-1 ENV BG505 DS-SOSIP, AND ANTIBODIES TITLE 3 VRC03 AND PGT122 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP120; COMPND 3 CHAIN: 2, C, c; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: DFPH-A.15 HEAVY CHAIN; COMPND 7 CHAIN: 3, H, h; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: DFPH-A.15 LIGHT CHAIN; COMPND 11 CHAIN: 4, L, l; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: PGT122 HEAVY CHAIN; COMPND 15 CHAIN: 5, M, m; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: PGT122 LIGHT CHAIN; COMPND 19 CHAIN: 6, N, n; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 6; COMPND 22 MOLECULE: VRC03 LIGHT CHAIN; COMPND 23 CHAIN: 7, R, r; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 7; COMPND 26 MOLECULE: VRC03 HEAVY CHAIN; COMPND 27 CHAIN: 8, Q, q; COMPND 28 ENGINEERED: YES; COMPND 29 MOL_ID: 8; COMPND 30 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 31 CHAIN: A, D, d; COMPND 32 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 GENE: ENV; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 10 ORGANISM_TAXID: 9544; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 16 ORGANISM_TAXID: 9544; 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: HOMO SAPIENS; SOURCE 22 ORGANISM_COMMON: HUMAN; SOURCE 23 ORGANISM_TAXID: 9606; 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: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 50 ORGANISM_TAXID: 11676; SOURCE 51 GENE: ENV; SOURCE 52 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 53 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 54 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV-1 ENV COMPLEX, NEUTRALIZING ANTIBODY, FUSION PEPTIDE-DIRECTED, KEYWDS 2 VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR P.ACHARYA,P.D.KWONG REVDAT 1 24-JUL-19 6N1W 0 JRNL AUTH R.KONG,P.ACHARYA,K.XU,B.ZHANG,V.P.DANDEY,E.T.ENG,H.WEI, JRNL AUTH 2 B.CARRAGHER,C.S.POTTER,J.MASCOLA,P.D.KWONG JRNL TITL VACCINE-INDUCED DEVELOPMENTAL PATHWAYS FOR JRNL TITL 2 HIV-1-NEUTRALIZING FUSION PEPTIDE-DIRECTED ANTIBODIES IN JRNL TITL 3 RHESUS MACAQUES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 4.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : LEGINON, GCTF, COOT, PHENIX, CRYOSPARC, REMARK 3 CRYOSPARC, 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 : REAL REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT REMARK 3 REFINEMENT TARGET : CORRELATION COEFFICIENT 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) : 4.200 REMARK 3 NUMBER OF PARTICLES : 56291 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 6N1W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-NOV-18. REMARK 100 THE DEPOSITION ID IS D_1000238034. 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 : QUATERNARY COMPLEX OF HIV-1 ENV REMARK 245 BG505 DS-SOSIP WITH ANTIBODIES REMARK 245 DFPH-A.15, VRC03 AND PGT122.; REMARK 245 ENVELOPE GLYCOPROTEIN GP120; REMARK 245 DFPH-A.15; ENVELOPE REMARK 245 GLYCOPROTEIN GP41; PGT122; VRC03 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.50 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) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 69.98 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : 22500 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: 2, 3, 4, 5, 6, 7, 8, A, C, D, REMARK 350 AND CHAINS: H, L, M, N, Q, R, c, d, h, REMARK 350 AND CHAINS: l, m, n, q, r 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 GLU 2 185A REMARK 465 ASN 2 185B REMARK 465 GLN 2 185C REMARK 465 GLY 2 185D REMARK 465 ASN 2 185E REMARK 465 ARG 2 185F REMARK 465 SER 2 185G REMARK 465 ASN 2 185H REMARK 465 ASN 2 185I REMARK 465 THR 2 400 REMARK 465 SER 2 401 REMARK 465 VAL 2 402 REMARK 465 GLN 2 403 REMARK 465 GLY 2 404 REMARK 465 SER 2 405 REMARK 465 ASN 2 406 REMARK 465 SER 2 407 REMARK 465 THR 2 408 REMARK 465 GLY 2 409 REMARK 465 SER 2 410 REMARK 465 SER 3 113 REMARK 465 ALA 3 114 REMARK 465 SER 3 115 REMARK 465 THR 3 116 REMARK 465 LYS 3 117 REMARK 465 GLY 3 118 REMARK 465 PRO 3 119 REMARK 465 SER 3 120 REMARK 465 VAL 3 121 REMARK 465 PHE 3 122 REMARK 465 PRO 3 123 REMARK 465 LEU 3 124 REMARK 465 ALA 3 125 REMARK 465 PRO 3 126 REMARK 465 SER 3 127 REMARK 465 SER 3 128 REMARK 465 GLU 3 129 REMARK 465 SER 3 130 REMARK 465 THR 3 131 REMARK 465 ALA 3 132 REMARK 465 ALA 3 133 REMARK 465 LEU 3 134 REMARK 465 GLY 3 135 REMARK 465 CYS 3 136 REMARK 465 LEU 3 137 REMARK 465 VAL 3 138 REMARK 465 LYS 3 139 REMARK 465 ASP 3 140 REMARK 465 TYR 3 141 REMARK 465 PHE 3 142 REMARK 465 PRO 3 143 REMARK 465 GLU 3 144 REMARK 465 PRO 3 145 REMARK 465 VAL 3 146 REMARK 465 THR 3 147 REMARK 465 VAL 3 148 REMARK 465 SER 3 149 REMARK 465 TRP 3 150 REMARK 465 ASN 3 151 REMARK 465 SER 3 152 REMARK 465 GLY 3 153 REMARK 465 SER 3 154 REMARK 465 LEU 3 155 REMARK 465 THR 3 156 REMARK 465 SER 3 157 REMARK 465 GLY 3 158 REMARK 465 VAL 3 159 REMARK 465 HIS 3 160 REMARK 465 THR 3 161 REMARK 465 PHE 3 162 REMARK 465 PRO 3 163 REMARK 465 ALA 3 164 REMARK 465 VAL 3 165 REMARK 465 LEU 3 166 REMARK 465 GLN 3 167 REMARK 465 SER 3 168 REMARK 465 SER 3 169 REMARK 465 GLY 3 170 REMARK 465 LEU 3 171 REMARK 465 TYR 3 172 REMARK 465 SER 3 173 REMARK 465 LEU 3 174 REMARK 465 SER 3 175 REMARK 465 SER 3 176 REMARK 465 VAL 3 177 REMARK 465 VAL 3 178 REMARK 465 THR 3 179 REMARK 465 VAL 3 180 REMARK 465 PRO 3 181 REMARK 465 SER 3 182 REMARK 465 SER 3 183 REMARK 465 SER 3 184 REMARK 465 LEU 3 185 REMARK 465 GLY 3 186 REMARK 465 THR 3 187 REMARK 465 GLN 3 188 REMARK 465 THR 3 189 REMARK 465 TYR 3 190 REMARK 465 VAL 3 191 REMARK 465 CYS 3 192 REMARK 465 ASN 3 193 REMARK 465 VAL 3 194 REMARK 465 ASN 3 195 REMARK 465 HIS 3 196 REMARK 465 LYS 3 197 REMARK 465 PRO 3 198 REMARK 465 SER 3 199 REMARK 465 ASN 3 200 REMARK 465 THR 3 201 REMARK 465 LYS 3 202 REMARK 465 VAL 3 203 REMARK 465 ASP 3 204 REMARK 465 LYS 3 205 REMARK 465 ARG 3 206 REMARK 465 VAL 3 207 REMARK 465 GLU 3 208 REMARK 465 ILE 3 209 REMARK 465 PHE 4 106 REMARK 465 LYS 4 107 REMARK 465 ARG 4 108 REMARK 465 THR 4 109 REMARK 465 VAL 4 110 REMARK 465 ALA 4 111 REMARK 465 ALA 4 112 REMARK 465 PRO 4 113 REMARK 465 SER 4 114 REMARK 465 VAL 4 115 REMARK 465 PHE 4 116 REMARK 465 ILE 4 117 REMARK 465 PHE 4 118 REMARK 465 PRO 4 119 REMARK 465 PRO 4 120 REMARK 465 SER 4 121 REMARK 465 GLU 4 122 REMARK 465 ASP 4 123 REMARK 465 GLN 4 124 REMARK 465 VAL 4 125 REMARK 465 LYS 4 126 REMARK 465 SER 4 127 REMARK 465 GLY 4 128 REMARK 465 THR 4 129 REMARK 465 VAL 4 130 REMARK 465 SER 4 131 REMARK 465 VAL 4 132 REMARK 465 VAL 4 133 REMARK 465 CYS 4 134 REMARK 465 LEU 4 135 REMARK 465 LEU 4 136 REMARK 465 ASN 4 137 REMARK 465 ASN 4 138 REMARK 465 PHE 4 139 REMARK 465 TYR 4 140 REMARK 465 PRO 4 141 REMARK 465 ARG 4 142 REMARK 465 GLU 4 143 REMARK 465 ALA 4 144 REMARK 465 SER 4 145 REMARK 465 VAL 4 146 REMARK 465 LYS 4 147 REMARK 465 TRP 4 148 REMARK 465 LYS 4 149 REMARK 465 VAL 4 150 REMARK 465 ASP 4 151 REMARK 465 GLY 4 152 REMARK 465 VAL 4 153 REMARK 465 LEU 4 154 REMARK 465 LYS 4 155 REMARK 465 THR 4 156 REMARK 465 GLY 4 157 REMARK 465 ASN 4 158 REMARK 465 SER 4 159 REMARK 465 GLN 4 160 REMARK 465 GLU 4 161 REMARK 465 SER 4 162 REMARK 465 VAL 4 163 REMARK 465 THR 4 164 REMARK 465 GLU 4 165 REMARK 465 GLN 4 166 REMARK 465 ASP 4 167 REMARK 465 SER 4 168 REMARK 465 LYS 4 169 REMARK 465 ASP 4 170 REMARK 465 ASN 4 171 REMARK 465 THR 4 172 REMARK 465 TYR 4 173 REMARK 465 SER 4 174 REMARK 465 LEU 4 175 REMARK 465 SER 4 176 REMARK 465 SER 4 177 REMARK 465 THR 4 178 REMARK 465 LEU 4 179 REMARK 465 THR 4 180 REMARK 465 LEU 4 181 REMARK 465 SER 4 182 REMARK 465 ASN 4 183 REMARK 465 THR 4 184 REMARK 465 ASP 4 185 REMARK 465 TYR 4 186 REMARK 465 GLN 4 187 REMARK 465 SER 4 188 REMARK 465 HIS 4 189 REMARK 465 ASN 4 190 REMARK 465 VAL 4 191 REMARK 465 TYR 4 192 REMARK 465 ALA 4 193 REMARK 465 CYS 4 194 REMARK 465 GLU 4 195 REMARK 465 VAL 4 196 REMARK 465 THR 4 197 REMARK 465 HIS 4 198 REMARK 465 GLN 4 199 REMARK 465 GLY 4 200 REMARK 465 LEU 4 201 REMARK 465 SER 4 202 REMARK 465 SER 4 203 REMARK 465 PRO 4 204 REMARK 465 VAL 4 205 REMARK 465 THR 4 206 REMARK 465 LYS 4 207 REMARK 465 SER 4 208 REMARK 465 PHE 4 209 REMARK 465 ASN 4 210 REMARK 465 ARG 4 211 REMARK 465 GLY 4 212 REMARK 465 ILE A 548 REMARK 465 VAL A 549 REMARK 465 GLN A 550 REMARK 465 GLN A 551 REMARK 465 GLN A 552 REMARK 465 SER A 553 REMARK 465 ASN A 554 REMARK 465 LEU A 555 REMARK 465 LEU A 556 REMARK 465 ARG A 557 REMARK 465 ALA A 558 REMARK 465 ILE A 559 REMARK 465 GLU A 560 REMARK 465 ALA A 561 REMARK 465 GLN A 562 REMARK 465 GLN A 563 REMARK 465 HIS A 564 REMARK 465 LEU A 565 REMARK 465 LEU A 566 REMARK 465 LYS A 567 REMARK 465 LEU A 568 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 SER H 113 REMARK 465 ALA H 114 REMARK 465 SER H 115 REMARK 465 THR H 116 REMARK 465 LYS H 117 REMARK 465 GLY H 118 REMARK 465 PRO H 119 REMARK 465 SER H 120 REMARK 465 VAL H 121 REMARK 465 PHE H 122 REMARK 465 PRO H 123 REMARK 465 LEU H 124 REMARK 465 ALA H 125 REMARK 465 PRO H 126 REMARK 465 SER H 127 REMARK 465 SER H 128 REMARK 465 GLU H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 ALA H 132 REMARK 465 ALA H 133 REMARK 465 LEU H 134 REMARK 465 GLY H 135 REMARK 465 CYS H 136 REMARK 465 LEU H 137 REMARK 465 VAL H 138 REMARK 465 LYS H 139 REMARK 465 ASP H 140 REMARK 465 TYR H 141 REMARK 465 PHE H 142 REMARK 465 PRO H 143 REMARK 465 GLU H 144 REMARK 465 PRO H 145 REMARK 465 VAL H 146 REMARK 465 THR H 147 REMARK 465 VAL H 148 REMARK 465 SER H 149 REMARK 465 TRP H 150 REMARK 465 ASN H 151 REMARK 465 SER H 152 REMARK 465 GLY H 153 REMARK 465 SER H 154 REMARK 465 LEU H 155 REMARK 465 THR H 156 REMARK 465 SER H 157 REMARK 465 GLY H 158 REMARK 465 VAL H 159 REMARK 465 HIS H 160 REMARK 465 THR H 161 REMARK 465 PHE H 162 REMARK 465 PRO H 163 REMARK 465 ALA H 164 REMARK 465 VAL H 165 REMARK 465 LEU H 166 REMARK 465 GLN H 167 REMARK 465 SER H 168 REMARK 465 SER H 169 REMARK 465 GLY H 170 REMARK 465 LEU H 171 REMARK 465 TYR H 172 REMARK 465 SER H 173 REMARK 465 LEU H 174 REMARK 465 SER H 175 REMARK 465 SER H 176 REMARK 465 VAL H 177 REMARK 465 VAL H 178 REMARK 465 THR H 179 REMARK 465 VAL H 180 REMARK 465 PRO H 181 REMARK 465 SER H 182 REMARK 465 SER H 183 REMARK 465 SER H 184 REMARK 465 LEU H 185 REMARK 465 GLY H 186 REMARK 465 THR H 187 REMARK 465 GLN H 188 REMARK 465 THR H 189 REMARK 465 TYR H 190 REMARK 465 VAL H 191 REMARK 465 CYS H 192 REMARK 465 ASN H 193 REMARK 465 VAL H 194 REMARK 465 ASN H 195 REMARK 465 HIS H 196 REMARK 465 LYS H 197 REMARK 465 PRO H 198 REMARK 465 SER H 199 REMARK 465 ASN H 200 REMARK 465 THR H 201 REMARK 465 LYS H 202 REMARK 465 VAL H 203 REMARK 465 ASP H 204 REMARK 465 LYS H 205 REMARK 465 ARG H 206 REMARK 465 VAL H 207 REMARK 465 GLU H 208 REMARK 465 ILE H 209 REMARK 465 PHE L 106 REMARK 465 LYS L 107 REMARK 465 ARG L 108 REMARK 465 THR L 109 REMARK 465 VAL L 110 REMARK 465 ALA L 111 REMARK 465 ALA L 112 REMARK 465 PRO L 113 REMARK 465 SER L 114 REMARK 465 VAL L 115 REMARK 465 PHE L 116 REMARK 465 ILE L 117 REMARK 465 PHE L 118 REMARK 465 PRO L 119 REMARK 465 PRO L 120 REMARK 465 SER L 121 REMARK 465 GLU L 122 REMARK 465 ASP L 123 REMARK 465 GLN L 124 REMARK 465 VAL L 125 REMARK 465 LYS L 126 REMARK 465 SER L 127 REMARK 465 GLY L 128 REMARK 465 THR L 129 REMARK 465 VAL L 130 REMARK 465 SER L 131 REMARK 465 VAL L 132 REMARK 465 VAL L 133 REMARK 465 CYS L 134 REMARK 465 LEU L 135 REMARK 465 LEU L 136 REMARK 465 ASN L 137 REMARK 465 ASN L 138 REMARK 465 PHE L 139 REMARK 465 TYR L 140 REMARK 465 PRO L 141 REMARK 465 ARG L 142 REMARK 465 GLU L 143 REMARK 465 ALA L 144 REMARK 465 SER L 145 REMARK 465 VAL L 146 REMARK 465 LYS L 147 REMARK 465 TRP L 148 REMARK 465 LYS L 149 REMARK 465 VAL L 150 REMARK 465 ASP L 151 REMARK 465 GLY L 152 REMARK 465 VAL L 153 REMARK 465 LEU L 154 REMARK 465 LYS L 155 REMARK 465 THR L 156 REMARK 465 GLY L 157 REMARK 465 ASN L 158 REMARK 465 SER L 159 REMARK 465 GLN L 160 REMARK 465 GLU L 161 REMARK 465 SER L 162 REMARK 465 VAL L 163 REMARK 465 THR L 164 REMARK 465 GLU L 165 REMARK 465 GLN L 166 REMARK 465 ASP L 167 REMARK 465 SER L 168 REMARK 465 LYS L 169 REMARK 465 ASP L 170 REMARK 465 ASN L 171 REMARK 465 THR L 172 REMARK 465 TYR L 173 REMARK 465 SER L 174 REMARK 465 LEU L 175 REMARK 465 SER L 176 REMARK 465 SER L 177 REMARK 465 THR L 178 REMARK 465 LEU L 179 REMARK 465 THR L 180 REMARK 465 LEU L 181 REMARK 465 SER L 182 REMARK 465 ASN L 183 REMARK 465 THR L 184 REMARK 465 ASP L 185 REMARK 465 TYR L 186 REMARK 465 GLN L 187 REMARK 465 SER L 188 REMARK 465 HIS L 189 REMARK 465 ASN L 190 REMARK 465 VAL L 191 REMARK 465 TYR L 192 REMARK 465 ALA L 193 REMARK 465 CYS L 194 REMARK 465 GLU L 195 REMARK 465 VAL L 196 REMARK 465 THR L 197 REMARK 465 HIS L 198 REMARK 465 GLN L 199 REMARK 465 GLY L 200 REMARK 465 LEU L 201 REMARK 465 SER L 202 REMARK 465 SER L 203 REMARK 465 PRO L 204 REMARK 465 VAL L 205 REMARK 465 THR L 206 REMARK 465 LYS L 207 REMARK 465 SER L 208 REMARK 465 PHE L 209 REMARK 465 ASN L 210 REMARK 465 ARG L 211 REMARK 465 GLY L 212 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 SER h 113 REMARK 465 ALA h 114 REMARK 465 SER h 115 REMARK 465 THR h 116 REMARK 465 LYS h 117 REMARK 465 GLY h 118 REMARK 465 PRO h 119 REMARK 465 SER h 120 REMARK 465 VAL h 121 REMARK 465 PHE h 122 REMARK 465 PRO h 123 REMARK 465 LEU h 124 REMARK 465 ALA h 125 REMARK 465 PRO h 126 REMARK 465 SER h 127 REMARK 465 SER h 128 REMARK 465 GLU h 129 REMARK 465 SER h 130 REMARK 465 THR h 131 REMARK 465 ALA h 132 REMARK 465 ALA h 133 REMARK 465 LEU h 134 REMARK 465 GLY h 135 REMARK 465 CYS h 136 REMARK 465 LEU h 137 REMARK 465 VAL h 138 REMARK 465 LYS h 139 REMARK 465 ASP h 140 REMARK 465 TYR h 141 REMARK 465 PHE h 142 REMARK 465 PRO h 143 REMARK 465 GLU h 144 REMARK 465 PRO h 145 REMARK 465 VAL h 146 REMARK 465 THR h 147 REMARK 465 VAL h 148 REMARK 465 SER h 149 REMARK 465 TRP h 150 REMARK 465 ASN h 151 REMARK 465 SER h 152 REMARK 465 GLY h 153 REMARK 465 SER h 154 REMARK 465 LEU h 155 REMARK 465 THR h 156 REMARK 465 SER h 157 REMARK 465 GLY h 158 REMARK 465 VAL h 159 REMARK 465 HIS h 160 REMARK 465 THR h 161 REMARK 465 PHE h 162 REMARK 465 PRO h 163 REMARK 465 ALA h 164 REMARK 465 VAL h 165 REMARK 465 LEU h 166 REMARK 465 GLN h 167 REMARK 465 SER h 168 REMARK 465 SER h 169 REMARK 465 GLY h 170 REMARK 465 LEU h 171 REMARK 465 TYR h 172 REMARK 465 SER h 173 REMARK 465 LEU h 174 REMARK 465 SER h 175 REMARK 465 SER h 176 REMARK 465 VAL h 177 REMARK 465 VAL h 178 REMARK 465 THR h 179 REMARK 465 VAL h 180 REMARK 465 PRO h 181 REMARK 465 SER h 182 REMARK 465 SER h 183 REMARK 465 SER h 184 REMARK 465 LEU h 185 REMARK 465 GLY h 186 REMARK 465 THR h 187 REMARK 465 GLN h 188 REMARK 465 THR h 189 REMARK 465 TYR h 190 REMARK 465 VAL h 191 REMARK 465 CYS h 192 REMARK 465 ASN h 193 REMARK 465 VAL h 194 REMARK 465 ASN h 195 REMARK 465 HIS h 196 REMARK 465 LYS h 197 REMARK 465 PRO h 198 REMARK 465 SER h 199 REMARK 465 ASN h 200 REMARK 465 THR h 201 REMARK 465 LYS h 202 REMARK 465 VAL h 203 REMARK 465 ASP h 204 REMARK 465 LYS h 205 REMARK 465 ARG h 206 REMARK 465 VAL h 207 REMARK 465 GLU h 208 REMARK 465 ILE h 209 REMARK 465 PHE l 106 REMARK 465 LYS l 107 REMARK 465 ARG l 108 REMARK 465 THR l 109 REMARK 465 VAL l 110 REMARK 465 ALA l 111 REMARK 465 ALA l 112 REMARK 465 PRO l 113 REMARK 465 SER l 114 REMARK 465 VAL l 115 REMARK 465 PHE l 116 REMARK 465 ILE l 117 REMARK 465 PHE l 118 REMARK 465 PRO l 119 REMARK 465 PRO l 120 REMARK 465 SER l 121 REMARK 465 GLU l 122 REMARK 465 ASP l 123 REMARK 465 GLN l 124 REMARK 465 VAL l 125 REMARK 465 LYS l 126 REMARK 465 SER l 127 REMARK 465 GLY l 128 REMARK 465 THR l 129 REMARK 465 VAL l 130 REMARK 465 SER l 131 REMARK 465 VAL l 132 REMARK 465 VAL l 133 REMARK 465 CYS l 134 REMARK 465 LEU l 135 REMARK 465 LEU l 136 REMARK 465 ASN l 137 REMARK 465 ASN l 138 REMARK 465 PHE l 139 REMARK 465 TYR l 140 REMARK 465 PRO l 141 REMARK 465 ARG l 142 REMARK 465 GLU l 143 REMARK 465 ALA l 144 REMARK 465 SER l 145 REMARK 465 VAL l 146 REMARK 465 LYS l 147 REMARK 465 TRP l 148 REMARK 465 LYS l 149 REMARK 465 VAL l 150 REMARK 465 ASP l 151 REMARK 465 GLY l 152 REMARK 465 VAL l 153 REMARK 465 LEU l 154 REMARK 465 LYS l 155 REMARK 465 THR l 156 REMARK 465 GLY l 157 REMARK 465 ASN l 158 REMARK 465 SER l 159 REMARK 465 GLN l 160 REMARK 465 GLU l 161 REMARK 465 SER l 162 REMARK 465 VAL l 163 REMARK 465 THR l 164 REMARK 465 GLU l 165 REMARK 465 GLN l 166 REMARK 465 ASP l 167 REMARK 465 SER l 168 REMARK 465 LYS l 169 REMARK 465 ASP l 170 REMARK 465 ASN l 171 REMARK 465 THR l 172 REMARK 465 TYR l 173 REMARK 465 SER l 174 REMARK 465 LEU l 175 REMARK 465 SER l 176 REMARK 465 SER l 177 REMARK 465 THR l 178 REMARK 465 LEU l 179 REMARK 465 THR l 180 REMARK 465 LEU l 181 REMARK 465 SER l 182 REMARK 465 ASN l 183 REMARK 465 THR l 184 REMARK 465 ASP l 185 REMARK 465 TYR l 186 REMARK 465 GLN l 187 REMARK 465 SER l 188 REMARK 465 HIS l 189 REMARK 465 ASN l 190 REMARK 465 VAL l 191 REMARK 465 TYR l 192 REMARK 465 ALA l 193 REMARK 465 CYS l 194 REMARK 465 GLU l 195 REMARK 465 VAL l 196 REMARK 465 THR l 197 REMARK 465 HIS l 198 REMARK 465 GLN l 199 REMARK 465 GLY l 200 REMARK 465 LEU l 201 REMARK 465 SER l 202 REMARK 465 SER l 203 REMARK 465 PRO l 204 REMARK 465 VAL l 205 REMARK 465 THR l 206 REMARK 465 LYS l 207 REMARK 465 SER l 208 REMARK 465 PHE l 209 REMARK 465 ASN l 210 REMARK 465 ARG l 211 REMARK 465 GLY l 212 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 MET 2 100 -3.44 63.10 REMARK 500 LEU 2 122 53.07 -92.02 REMARK 500 LEU 2 259 71.84 60.04 REMARK 500 GLU 2 370 32.37 -96.22 REMARK 500 ASN 2 392 42.91 -145.11 REMARK 500 SER 2 397 32.44 -93.16 REMARK 500 PRO 2 493 -168.58 -74.46 REMARK 500 LEU 2 494 68.90 62.44 REMARK 500 TYR 3 100D -167.85 -101.51 REMARK 500 ASP 4 32 75.23 -100.26 REMARK 500 ALA 4 51 -6.99 66.11 REMARK 500 SER 4 52 -2.83 -140.67 REMARK 500 LYS 5 64 -15.00 69.20 REMARK 500 SER 5 65 -38.44 -133.36 REMARK 500 GLU 5 100I 57.63 -95.17 REMARK 500 ASN 6 50 -164.94 -126.12 REMARK 500 ASN 6 52 43.73 -142.45 REMARK 500 PHE 6 62 75.29 -100.35 REMARK 500 GLU 6 83 96.99 -66.62 REMARK 500 THR 7 50 -5.95 68.82 REMARK 500 SER 7 51 -3.94 -141.39 REMARK 500 PRO 8 100E 79.53 -68.52 REMARK 500 MET C 100 -3.03 63.00 REMARK 500 LEU C 122 54.44 -92.40 REMARK 500 LEU C 259 71.32 59.52 REMARK 500 GLU C 370 32.89 -95.24 REMARK 500 ASN C 392 42.52 -144.07 REMARK 500 SER C 397 33.07 -93.04 REMARK 500 PRO C 493 -168.55 -74.26 REMARK 500 LEU C 494 68.13 62.95 REMARK 500 ALA H 100B -9.59 -59.62 REMARK 500 TYR H 100D -168.15 -101.37 REMARK 500 ASP L 32 75.13 -100.56 REMARK 500 ALA L 51 -6.85 66.14 REMARK 500 SER L 52 -2.91 -141.00 REMARK 500 LYS M 64 -16.68 69.05 REMARK 500 SER M 65 -38.03 -133.76 REMARK 500 GLU M 100I 58.09 -94.49 REMARK 500 ASN N 50 -166.47 -126.47 REMARK 500 ASN N 52 43.92 -144.02 REMARK 500 PHE N 62 76.38 -101.55 REMARK 500 GLU N 83 97.52 -65.36 REMARK 500 PRO Q 100E 79.35 -67.75 REMARK 500 ASP R 49 19.25 58.23 REMARK 500 THR R 50 -5.34 68.58 REMARK 500 SER R 51 -4.03 -141.04 REMARK 500 MET c 100 -3.64 63.14 REMARK 500 LEU c 122 54.75 -93.18 REMARK 500 THR c 163 -168.91 -79.91 REMARK 500 LEU c 259 71.40 60.81 REMARK 500 REMARK 500 THIS ENTRY HAS 71 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 ILE 4 29 ASP 4 30 -144.87 REMARK 500 GLN 7 89 PHE 7 90 -133.96 REMARK 500 ILE L 29 ASP L 30 -143.78 REMARK 500 GLN R 89 PHE R 90 -135.68 REMARK 500 ILE l 29 ASP l 30 -144.43 REMARK 500 GLN r 89 PHE r 90 -134.52 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 2 641 REMARK 610 NAG C 641 REMARK 610 NAG c 641 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 601 through NAG 2 602 bound to ASN 2 133 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 603 through MAN 2 606 bound to ASN 2 137 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 607 through NAG 2 608 bound to ASN 2 156 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 609 through NAG 2 610 bound to ASN 2 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG 2 611 bound REMARK 800 to ASN 2 197 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 612 through NAG 2 613 bound to ASN 2 234 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 614 through MAN 2 618 bound to ASN 2 262 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 643 through MAN 2 646 bound to ASN 2 276 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 619 through NAG 2 620 bound to ASN 2 295 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 621 through NAG 2 622 bound to ASN 2 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 632 through MAN 2 640 bound to ASN 2 332 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG 2 623 bound REMARK 800 to ASN 2 355 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 624 through BMA 2 626 bound to ASN 2 363 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 627 through MAN 2 630 bound to ASN 2 386 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG 2 631 bound REMARK 800 to ASN 2 392 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 601 through NAG C 602 bound to ASN C 133 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 603 through MAN C 606 bound to ASN C 137 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 607 through NAG C 608 bound to ASN C 156 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 609 through NAG C 610 bound to ASN C 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 611 bound REMARK 800 to ASN C 197 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 612 through NAG C 613 bound to ASN C 234 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 614 through MAN C 618 bound to ASN C 262 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 643 through MAN C 646 bound to ASN C 276 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 619 through NAG C 620 bound to ASN C 295 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 621 through NAG C 622 bound to ASN C 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 632 through MAN C 640 bound to ASN C 332 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 623 bound REMARK 800 to ASN C 355 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 624 through BMA C 626 bound to ASN C 363 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 627 through MAN C 630 bound to ASN C 386 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 631 bound REMARK 800 to ASN C 392 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG c REMARK 800 601 through NAG c 602 bound to ASN c 133 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG c REMARK 800 603 through MAN c 606 bound to ASN c 137 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG c REMARK 800 607 through NAG c 608 bound to ASN c 156 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG c REMARK 800 609 through NAG c 610 bound to ASN c 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG c 611 bound REMARK 800 to ASN c 197 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG c REMARK 800 612 through NAG c 613 bound to ASN c 234 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG c REMARK 800 614 through MAN c 618 bound to ASN c 262 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG c REMARK 800 643 through MAN c 646 bound to ASN c 276 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG c REMARK 800 619 through NAG c 620 bound to ASN c 295 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG c REMARK 800 621 through NAG c 622 bound to ASN c 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG c REMARK 800 632 through MAN c 640 bound to ASN c 332 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG c 623 bound REMARK 800 to ASN c 355 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG c REMARK 800 624 through BMA c 626 bound to ASN c 363 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG c REMARK 800 627 through MAN c 630 bound to ASN c 386 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG c 631 bound REMARK 800 to ASN c 392 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 641 through NAG 2 642 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 641 through NAG C 642 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG c REMARK 800 641 through NAG c 642 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-9320 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE AT 4.2 A RESOLUTION OF VACCINE-ELICITED ANTIBODY REMARK 900 DFPH-A.15 IN COMPLEX WITH HIV-1 ENV BG505 DS-SOSIP, AND ANTIBODIES REMARK 900 VRC03 AND PGT122 DBREF 6N1W 2 31 505 UNP Q2N0S6 Q2N0S6_9HIV1 30 502 DBREF 6N1W 3 1 209 PDB 6N1W 6N1W 1 209 DBREF 6N1W 4 1 212 PDB 6N1W 6N1W 1 212 DBREF 6N1W 5 1 111 PDB 6N1W 6N1W 1 111 DBREF 6N1W 6 8 107 PDB 6N1W 6N1W 8 107 DBREF 6N1W 7 1 102 PDB 6N1W 6N1W 1 102 DBREF 6N1W 8 1 111 PDB 6N1W 6N1W 1 111 DBREF 6N1W A 512 664 UNP Q2N0S7 Q2N0S7_9HIV1 509 661 DBREF 6N1W C 31 505 UNP Q2N0S6 Q2N0S6_9HIV1 30 502 DBREF 6N1W D 512 664 UNP Q2N0S7 Q2N0S7_9HIV1 509 661 DBREF 6N1W H 1 209 PDB 6N1W 6N1W 1 209 DBREF 6N1W L 1 212 PDB 6N1W 6N1W 1 212 DBREF 6N1W M 1 111 PDB 6N1W 6N1W 1 111 DBREF 6N1W N 8 107 PDB 6N1W 6N1W 8 107 DBREF 6N1W Q 1 111 PDB 6N1W 6N1W 1 111 DBREF 6N1W R 1 102 PDB 6N1W 6N1W 1 102 DBREF 6N1W c 31 505 UNP Q2N0S6 Q2N0S6_9HIV1 30 502 DBREF 6N1W d 512 664 UNP Q2N0S7 Q2N0S7_9HIV1 509 661 DBREF 6N1W h 1 209 PDB 6N1W 6N1W 1 209 DBREF 6N1W l 1 212 PDB 6N1W 6N1W 1 212 DBREF 6N1W m 1 111 PDB 6N1W 6N1W 1 111 DBREF 6N1W n 8 107 PDB 6N1W 6N1W 8 107 DBREF 6N1W q 1 111 PDB 6N1W 6N1W 1 111 DBREF 6N1W r 1 102 PDB 6N1W 6N1W 1 102 SEQADV 6N1W CYS 2 201 UNP Q2N0S6 ILE 200 CONFLICT SEQADV 6N1W ASN 2 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 6N1W CYS 2 433 UNP Q2N0S6 ALA 430 CONFLICT SEQADV 6N1W CYS 2 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 6N1W CYS A 605 UNP Q2N0S7 THR 602 CONFLICT SEQADV 6N1W CYS C 201 UNP Q2N0S6 ILE 200 CONFLICT SEQADV 6N1W ASN C 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 6N1W CYS C 433 UNP Q2N0S6 ALA 430 CONFLICT SEQADV 6N1W CYS C 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 6N1W CYS D 605 UNP Q2N0S7 THR 602 CONFLICT SEQADV 6N1W CYS c 201 UNP Q2N0S6 ILE 200 CONFLICT SEQADV 6N1W ASN c 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 6N1W CYS c 433 UNP Q2N0S6 ALA 430 CONFLICT SEQADV 6N1W CYS c 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 6N1W CYS d 605 UNP Q2N0S7 THR 602 CONFLICT SEQRES 1 2 473 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 2 473 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 2 473 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 2 473 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 2 473 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 2 473 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 2 473 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 2 473 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 2 473 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 2 473 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 2 473 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 2 473 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 2 473 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 2 473 ALA CYS THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 2 473 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 2 473 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 2 473 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 2 473 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 2 473 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 2 473 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 2 473 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 2 473 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 2 473 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 2 473 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 2 473 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 2 473 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 2 473 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 2 473 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 2 473 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 2 473 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 2 473 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR SEQRES 32 2 473 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 2 473 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 2 473 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 2 473 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 2 473 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 2 473 CYS LYS ARG ARG VAL SEQRES 1 3 224 GLN VAL GLN LEU GLN VAL SER GLY PRO GLY VAL VAL ARG SEQRES 2 3 224 PRO SER GLU THR LEU SER LEU THR CYS GLU VAL SER SER SEQRES 3 3 224 GLY SER THR SER ARG ASP PHE PHE TYR TRP SER TRP VAL SEQRES 4 3 224 ARG GLN THR PRO GLY LYS GLY LEU GLU TRP ILE GLY GLY SEQRES 5 3 224 MET TYR SER ASN SER GLU GLU THR ASN HIS ASN PRO SER SEQRES 6 3 224 LEU LYS SER ARG VAL ILE ILE SER LYS ASP THR SER LYS SEQRES 7 3 224 ASN GLU PHE SER LEU ARG LEU THR SER VAL THR ALA ALA SEQRES 8 3 224 ASP THR ALA VAL TYR PHE CYS SER SER ARG ALA LYS ILE SEQRES 9 3 224 TYR TYR SER ALA SER TYR SER GLY GLY ARG ILE ASP VAL SEQRES 10 3 224 TRP GLY PRO GLY LEU LEU VAL THR VAL SER SER ALA SER SEQRES 11 3 224 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER SEQRES 12 3 224 GLU SER THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 3 224 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SER SEQRES 14 3 224 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 3 224 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 3 224 PRO SER SER SER LEU GLY THR GLN THR TYR VAL CYS ASN SEQRES 17 3 224 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG SEQRES 18 3 224 VAL GLU ILE SEQRES 1 4 212 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 4 212 SER ILE GLY ASP ARG VAL THR VAL THR CYS ARG ALA SER SEQRES 3 4 212 GLN GLY ILE ASP LYS ASP LEU SER TRP PHE GLN GLN LYS SEQRES 4 4 212 PRO GLY LYS ALA PRO THR LEU LEU ILE TYR THR ALA SER SEQRES 5 4 212 THR LEU GLN THR GLY VAL SER SER ARG PHE SER GLY SER SEQRES 6 4 212 GLY SER GLY THR ASP PHE SER LEU THR ILE ASN ASN LEU SEQRES 7 4 212 GLN PRO GLU ASP VAL ALA THR TYR PHE CYS GLN GLN ASP SEQRES 8 4 212 PHE SER PHE PRO LEU THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 4 212 ASP PHE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 4 212 PHE PRO PRO SER GLU ASP GLN VAL LYS SER GLY THR VAL SEQRES 11 4 212 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 4 212 ALA SER VAL LYS TRP LYS VAL ASP GLY VAL LEU LYS THR SEQRES 13 4 212 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 4 212 ASP ASN THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 4 212 ASN THR ASP TYR GLN SER HIS ASN VAL TYR ALA CYS GLU SEQRES 16 4 212 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 4 212 PHE ASN ARG GLY SEQRES 1 5 132 GLN VAL HIS LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 5 132 PRO SER GLU THR LEU SER LEU THR CYS ASN VAL SER GLY SEQRES 3 5 132 THR LEU VAL ARG ASP ASN TYR TRP SER TRP ILE ARG GLN SEQRES 4 5 132 PRO LEU GLY LYS GLN PRO GLU TRP ILE GLY TYR VAL HIS SEQRES 5 5 132 ASP SER GLY ASP THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 5 132 ARG VAL HIS LEU SER LEU ASP LYS SER LYS ASN LEU VAL SEQRES 7 5 132 SER LEU ARG LEU THR GLY VAL THR ALA ALA ASP SER ALA SEQRES 8 5 132 ILE TYR TYR CYS ALA THR THR LYS HIS GLY ARG ARG ILE SEQRES 9 5 132 TYR GLY VAL VAL ALA PHE LYS GLU TRP PHE THR TYR PHE SEQRES 10 5 132 TYR MET ASP VAL TRP GLY LYS GLY THR SER VAL THR VAL SEQRES 11 5 132 SER SER SEQRES 1 6 105 THR PHE VAL SER VAL ALA PRO GLY GLN THR ALA ARG ILE SEQRES 2 6 105 THR CYS GLY GLU GLU SER LEU GLY SER ARG SER VAL ILE SEQRES 3 6 105 TRP TYR GLN GLN ARG PRO GLY GLN ALA PRO SER LEU ILE SEQRES 4 6 105 ILE TYR ASN ASN ASN ASP ARG PRO SER GLY ILE PRO ASP SEQRES 5 6 105 ARG PHE SER GLY SER PRO GLY SER THR PHE GLY THR THR SEQRES 6 6 105 ALA THR LEU THR ILE THR SER VAL GLU ALA GLY ASP GLU SEQRES 7 6 105 ALA ASP TYR TYR CYS HIS ILE TRP ASP SER ARG ARG PRO SEQRES 8 6 105 THR ASN TRP VAL PHE GLY GLU GLY THR THR LEU ILE VAL SEQRES 9 6 105 LEU SEQRES 1 7 102 GLU ILE VAL LEU THR GLN SER PRO GLY ILE LEU SER LEU SEQRES 2 7 102 SER PRO GLY GLU THR ALA THR LEU PHE CYS LYS ALA SER SEQRES 3 7 102 GLN GLY GLY ASN ALA MET THR TRP TYR GLN LYS ARG ARG SEQRES 4 7 102 GLY GLN VAL PRO ARG LEU LEU ILE TYR ASP THR SER ARG SEQRES 5 7 102 ARG ALA SER GLY VAL PRO ASP ARG PHE VAL GLY SER GLY SEQRES 6 7 102 SER GLY THR ASP PHE PHE LEU THR ILE ASN LYS LEU ASP SEQRES 7 7 102 ARG GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN PHE GLU SEQRES 8 7 102 PHE PHE GLY LEU GLY SER GLU LEU GLU VAL HIS SEQRES 1 8 128 GLN VAL GLN LEU VAL GLN SER GLY ALA VAL ILE LYS THR SEQRES 2 8 128 PRO GLY SER SER VAL LYS ILE SER CYS ARG ALA SER GLY SEQRES 3 8 128 TYR ASN PHE ARG ASP TYR SER ILE HIS TRP VAL ARG LEU SEQRES 4 8 128 ILE PRO ASP LYS GLY PHE GLU TRP ILE GLY TRP ILE LYS SEQRES 5 8 128 PRO LEU TRP GLY ALA VAL SER TYR ALA ARG GLN LEU GLN SEQRES 6 8 128 GLY ARG VAL SER MET THR ARG GLN LEU SER GLN ASP PRO SEQRES 7 8 128 ASP ASP PRO ASP TRP GLY VAL ALA TYR MET GLU PHE SER SEQRES 8 8 128 GLY LEU THR PRO ALA ASP THR ALA GLU TYR PHE CYS VAL SEQRES 9 8 128 ARG ARG GLY SER CYS ASP TYR CYS GLY ASP PHE PRO TRP SEQRES 10 8 128 GLN TYR TRP GLY GLN GLY THR VAL VAL VAL VAL SEQRES 1 A 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 A 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 A 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 A 153 GLN GLN SER ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 A 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 A 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 A 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 A 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 A 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 A 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 A 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 A 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP 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 H 224 GLN VAL GLN LEU GLN VAL SER GLY PRO GLY VAL VAL ARG SEQRES 2 H 224 PRO SER GLU THR LEU SER LEU THR CYS GLU VAL SER SER SEQRES 3 H 224 GLY SER THR SER ARG ASP PHE PHE TYR TRP SER TRP VAL SEQRES 4 H 224 ARG GLN THR PRO GLY LYS GLY LEU GLU TRP ILE GLY GLY SEQRES 5 H 224 MET TYR SER ASN SER GLU GLU THR ASN HIS ASN PRO SER SEQRES 6 H 224 LEU LYS SER ARG VAL ILE ILE SER LYS ASP THR SER LYS SEQRES 7 H 224 ASN GLU PHE SER LEU ARG LEU THR SER VAL THR ALA ALA SEQRES 8 H 224 ASP THR ALA VAL TYR PHE CYS SER SER ARG ALA LYS ILE SEQRES 9 H 224 TYR TYR SER ALA SER TYR SER GLY GLY ARG ILE ASP VAL SEQRES 10 H 224 TRP GLY PRO GLY LEU LEU VAL THR VAL SER SER ALA SER SEQRES 11 H 224 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER SEQRES 12 H 224 GLU SER THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 H 224 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SER SEQRES 14 H 224 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 H 224 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 H 224 PRO SER SER SER LEU GLY THR GLN THR TYR VAL CYS ASN SEQRES 17 H 224 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG SEQRES 18 H 224 VAL GLU ILE SEQRES 1 L 212 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 212 SER ILE GLY ASP ARG VAL THR VAL THR CYS ARG ALA SER SEQRES 3 L 212 GLN GLY ILE ASP LYS ASP LEU SER TRP PHE GLN GLN LYS SEQRES 4 L 212 PRO GLY LYS ALA PRO THR LEU LEU ILE TYR THR ALA SER SEQRES 5 L 212 THR LEU GLN THR GLY VAL SER SER ARG PHE SER GLY SER SEQRES 6 L 212 GLY SER GLY THR ASP PHE SER LEU THR ILE ASN ASN LEU SEQRES 7 L 212 GLN PRO GLU ASP VAL ALA THR TYR PHE CYS GLN GLN ASP SEQRES 8 L 212 PHE SER PHE PRO LEU THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 L 212 ASP PHE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 212 PHE PRO PRO SER GLU ASP GLN VAL LYS SER GLY THR VAL SEQRES 11 L 212 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 212 ALA SER VAL LYS TRP LYS VAL ASP GLY VAL LEU LYS THR SEQRES 13 L 212 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 212 ASP ASN THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 212 ASN THR ASP TYR GLN SER HIS ASN VAL TYR ALA CYS GLU SEQRES 16 L 212 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 212 PHE ASN ARG GLY 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 105 THR PHE VAL SER VAL ALA PRO GLY GLN THR ALA ARG ILE SEQRES 2 N 105 THR CYS GLY GLU GLU SER LEU GLY SER ARG SER VAL ILE SEQRES 3 N 105 TRP TYR GLN GLN ARG PRO GLY GLN ALA PRO SER LEU ILE SEQRES 4 N 105 ILE TYR ASN ASN ASN ASP ARG PRO SER GLY ILE PRO ASP SEQRES 5 N 105 ARG PHE SER GLY SER PRO GLY SER THR PHE GLY THR THR SEQRES 6 N 105 ALA THR LEU THR ILE THR SER VAL GLU ALA GLY ASP GLU SEQRES 7 N 105 ALA ASP TYR TYR CYS HIS ILE TRP ASP SER ARG ARG PRO SEQRES 8 N 105 THR ASN TRP VAL PHE GLY GLU GLY THR THR LEU ILE VAL SEQRES 9 N 105 LEU SEQRES 1 Q 128 GLN VAL GLN LEU VAL GLN SER GLY ALA VAL ILE LYS THR SEQRES 2 Q 128 PRO GLY SER SER VAL LYS ILE SER CYS ARG ALA SER GLY SEQRES 3 Q 128 TYR ASN PHE ARG ASP TYR SER ILE HIS TRP VAL ARG LEU SEQRES 4 Q 128 ILE PRO ASP LYS GLY PHE GLU TRP ILE GLY TRP ILE LYS SEQRES 5 Q 128 PRO LEU TRP GLY ALA VAL SER TYR ALA ARG GLN LEU GLN SEQRES 6 Q 128 GLY ARG VAL SER MET THR ARG GLN LEU SER GLN ASP PRO SEQRES 7 Q 128 ASP ASP PRO ASP TRP GLY VAL ALA TYR MET GLU PHE SER SEQRES 8 Q 128 GLY LEU THR PRO ALA ASP THR ALA GLU TYR PHE CYS VAL SEQRES 9 Q 128 ARG ARG GLY SER CYS ASP TYR CYS GLY ASP PHE PRO TRP SEQRES 10 Q 128 GLN TYR TRP GLY GLN GLY THR VAL VAL VAL VAL 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 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 h 224 GLN VAL GLN LEU GLN VAL SER GLY PRO GLY VAL VAL ARG SEQRES 2 h 224 PRO SER GLU THR LEU SER LEU THR CYS GLU VAL SER SER SEQRES 3 h 224 GLY SER THR SER ARG ASP PHE PHE TYR TRP SER TRP VAL SEQRES 4 h 224 ARG GLN THR PRO GLY LYS GLY LEU GLU TRP ILE GLY GLY SEQRES 5 h 224 MET TYR SER ASN SER GLU GLU THR ASN HIS ASN PRO SER SEQRES 6 h 224 LEU LYS SER ARG VAL ILE ILE SER LYS ASP THR SER LYS SEQRES 7 h 224 ASN GLU PHE SER LEU ARG LEU THR SER VAL THR ALA ALA SEQRES 8 h 224 ASP THR ALA VAL TYR PHE CYS SER SER ARG ALA LYS ILE SEQRES 9 h 224 TYR TYR SER ALA SER TYR SER GLY GLY ARG ILE ASP VAL SEQRES 10 h 224 TRP GLY PRO GLY LEU LEU VAL THR VAL SER SER ALA SER SEQRES 11 h 224 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER SEQRES 12 h 224 GLU SER THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 h 224 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SER SEQRES 14 h 224 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 h 224 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 h 224 PRO SER SER SER LEU GLY THR GLN THR TYR VAL CYS ASN SEQRES 17 h 224 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG SEQRES 18 h 224 VAL GLU ILE SEQRES 1 l 212 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 l 212 SER ILE GLY ASP ARG VAL THR VAL THR CYS ARG ALA SER SEQRES 3 l 212 GLN GLY ILE ASP LYS ASP LEU SER TRP PHE GLN GLN LYS SEQRES 4 l 212 PRO GLY LYS ALA PRO THR LEU LEU ILE TYR THR ALA SER SEQRES 5 l 212 THR LEU GLN THR GLY VAL SER SER ARG PHE SER GLY SER SEQRES 6 l 212 GLY SER GLY THR ASP PHE SER LEU THR ILE ASN ASN LEU SEQRES 7 l 212 GLN PRO GLU ASP VAL ALA THR TYR PHE CYS GLN GLN ASP SEQRES 8 l 212 PHE SER PHE PRO LEU THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 l 212 ASP PHE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 l 212 PHE PRO PRO SER GLU ASP GLN VAL LYS SER GLY THR VAL SEQRES 11 l 212 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 l 212 ALA SER VAL LYS TRP LYS VAL ASP GLY VAL LEU LYS THR SEQRES 13 l 212 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 l 212 ASP ASN THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 l 212 ASN THR ASP TYR GLN SER HIS ASN VAL TYR ALA CYS GLU SEQRES 16 l 212 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 l 212 PHE ASN ARG GLY 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 105 THR PHE VAL SER VAL ALA PRO GLY GLN THR ALA ARG ILE SEQRES 2 n 105 THR CYS GLY GLU GLU SER LEU GLY SER ARG SER VAL ILE SEQRES 3 n 105 TRP TYR GLN GLN ARG PRO GLY GLN ALA PRO SER LEU ILE SEQRES 4 n 105 ILE TYR ASN ASN ASN ASP ARG PRO SER GLY ILE PRO ASP SEQRES 5 n 105 ARG PHE SER GLY SER PRO GLY SER THR PHE GLY THR THR SEQRES 6 n 105 ALA THR LEU THR ILE THR SER VAL GLU ALA GLY ASP GLU SEQRES 7 n 105 ALA ASP TYR TYR CYS HIS ILE TRP ASP SER ARG ARG PRO SEQRES 8 n 105 THR ASN TRP VAL PHE GLY GLU GLY THR THR LEU ILE VAL SEQRES 9 n 105 LEU SEQRES 1 q 128 GLN VAL GLN LEU VAL GLN SER GLY ALA VAL ILE LYS THR SEQRES 2 q 128 PRO GLY SER SER VAL LYS ILE SER CYS ARG ALA SER GLY SEQRES 3 q 128 TYR ASN PHE ARG ASP TYR SER ILE HIS TRP VAL ARG LEU SEQRES 4 q 128 ILE PRO ASP LYS GLY PHE GLU TRP ILE GLY TRP ILE LYS SEQRES 5 q 128 PRO LEU TRP GLY ALA VAL SER TYR ALA ARG GLN LEU GLN SEQRES 6 q 128 GLY ARG VAL SER MET THR ARG GLN LEU SER GLN ASP PRO SEQRES 7 q 128 ASP ASP PRO ASP TRP GLY VAL ALA TYR MET GLU PHE SER SEQRES 8 q 128 GLY LEU THR PRO ALA ASP THR ALA GLU TYR PHE CYS VAL SEQRES 9 q 128 ARG ARG GLY SER CYS ASP TYR CYS GLY ASP PHE PRO TRP SEQRES 10 q 128 GLN TYR TRP GLY GLN GLY THR VAL VAL VAL VAL 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 HET NAG 2 601 14 HET NAG 2 602 14 HET NAG 2 603 14 HET NAG 2 604 14 HET BMA 2 605 11 HET MAN 2 606 11 HET NAG 2 607 14 HET NAG 2 608 14 HET NAG 2 609 14 HET NAG 2 610 14 HET NAG 2 611 14 HET NAG 2 612 14 HET NAG 2 613 14 HET NAG 2 614 14 HET NAG 2 615 14 HET BMA 2 616 11 HET MAN 2 617 11 HET MAN 2 618 11 HET NAG 2 619 14 HET NAG 2 620 14 HET NAG 2 621 14 HET NAG 2 622 14 HET NAG 2 623 14 HET NAG 2 624 14 HET NAG 2 625 14 HET BMA 2 626 11 HET NAG 2 627 14 HET NAG 2 628 14 HET BMA 2 629 11 HET MAN 2 630 11 HET NAG 2 631 14 HET NAG 2 632 14 HET NAG 2 633 14 HET BMA 2 634 11 HET MAN 2 635 11 HET MAN 2 636 11 HET MAN 2 637 11 HET MAN 2 638 11 HET MAN 2 639 11 HET MAN 2 640 11 HET NAG 2 641 14 HET NAG 2 642 14 HET NAG 2 643 14 HET NAG 2 644 14 HET BMA 2 645 11 HET MAN 2 646 11 HET NAG C 601 14 HET NAG C 602 14 HET NAG C 603 14 HET NAG C 604 14 HET BMA C 605 11 HET MAN C 606 11 HET NAG C 607 14 HET NAG C 608 14 HET NAG C 609 14 HET NAG C 610 14 HET NAG C 611 14 HET NAG C 612 14 HET NAG C 613 14 HET NAG C 614 14 HET NAG C 615 14 HET BMA C 616 11 HET MAN C 617 11 HET MAN C 618 11 HET NAG C 619 14 HET NAG C 620 14 HET NAG C 621 14 HET NAG C 622 14 HET NAG C 623 14 HET NAG C 624 14 HET NAG C 625 14 HET BMA C 626 11 HET NAG C 627 14 HET NAG C 628 14 HET BMA C 629 11 HET MAN C 630 11 HET NAG C 631 14 HET NAG C 632 14 HET NAG C 633 14 HET BMA C 634 11 HET MAN C 635 11 HET MAN C 636 11 HET MAN C 637 11 HET MAN C 638 11 HET MAN C 639 11 HET MAN C 640 11 HET NAG C 641 14 HET NAG C 642 14 HET NAG C 643 14 HET NAG C 644 14 HET BMA C 645 11 HET MAN C 646 11 HET NAG c 601 14 HET NAG c 602 14 HET NAG c 603 14 HET NAG c 604 14 HET BMA c 605 11 HET MAN c 606 11 HET NAG c 607 14 HET NAG c 608 14 HET NAG c 609 14 HET NAG c 610 14 HET NAG c 611 14 HET NAG c 612 14 HET NAG c 613 14 HET NAG c 614 14 HET NAG c 615 14 HET BMA c 616 11 HET MAN c 617 11 HET MAN c 618 11 HET NAG c 619 14 HET NAG c 620 14 HET NAG c 621 14 HET NAG c 622 14 HET NAG c 623 14 HET NAG c 624 14 HET NAG c 625 14 HET BMA c 626 11 HET NAG c 627 14 HET NAG c 628 14 HET BMA c 629 11 HET MAN c 630 11 HET NAG c 631 14 HET NAG c 632 14 HET NAG c 633 14 HET BMA c 634 11 HET MAN c 635 11 HET MAN c 636 11 HET MAN c 637 11 HET MAN c 638 11 HET MAN c 639 11 HET MAN c 640 11 HET NAG c 641 14 HET NAG c 642 14 HET NAG c 643 14 HET NAG c 644 14 HET BMA c 645 11 HET MAN c 646 11 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 25 NAG 87(C8 H15 N O6) FORMUL 26 BMA 18(C6 H12 O6) FORMUL 26 MAN 33(C6 H12 O6) HELIX 1 AA1 ALA 2 58 THR 2 63 1 6 HELIX 2 AA2 MET 2 100 SER 2 115 1 16 HELIX 3 AA3 LEU 2 122 CYS 2 126 5 5 HELIX 4 AA4 ASN 2 195 THR 2 198 5 4 HELIX 5 AA5 LYS 2 335 ARG 2 350 1 16 HELIX 6 AA6 ASP 2 368 THR 2 373 1 6 HELIX 7 AA7 ASN 2 425 ARG 2 429 5 5 HELIX 8 AA8 MET 2 475 ARG 2 480 1 6 HELIX 9 AA9 PRO 3 61 LYS 3 64 5 4 HELIX 10 AB1 THR 3 83 THR 3 87 5 5 HELIX 11 AB2 GLN 4 79 VAL 4 83 5 5 HELIX 12 AB3 THR 5 83 SER 5 87 5 5 HELIX 13 AB4 ASP 7 78 PHE 7 82 5 5 HELIX 14 AB5 ARG 8 61 GLN 8 64 5 4 HELIX 15 AB6 THR 8 83 THR 8 87 5 5 HELIX 16 AB7 THR A 529 ASN A 543 1 15 HELIX 17 AB8 VAL A 570 ILE A 595 1 26 HELIX 18 AB9 ASN A 618 ASN A 625 1 8 HELIX 19 AC1 THR A 627 ILE A 635 1 9 HELIX 20 AC2 TYR A 638 LEU A 661 1 24 HELIX 21 AC3 ALA C 58 THR C 63 1 6 HELIX 22 AC4 MET C 100 SER C 115 1 16 HELIX 23 AC5 LEU C 122 CYS C 126 5 5 HELIX 24 AC6 ASN C 195 THR C 198 5 4 HELIX 25 AC7 LYS C 335 ARG C 350 1 16 HELIX 26 AC8 ASP C 368 THR C 373 1 6 HELIX 27 AC9 ASN C 425 ARG C 429 5 5 HELIX 28 AD1 MET C 475 SER C 481 1 7 HELIX 29 AD2 THR D 529 ASN D 543 1 15 HELIX 30 AD3 VAL D 570 ILE D 595 1 26 HELIX 31 AD4 ASN D 618 ASN D 625 1 8 HELIX 32 AD5 THR D 627 ILE D 635 1 9 HELIX 33 AD6 TYR D 638 LEU D 661 1 24 HELIX 34 AD7 PRO H 61 LYS H 64 5 4 HELIX 35 AD8 THR H 83 THR H 87 5 5 HELIX 36 AD9 GLN L 79 VAL L 83 5 5 HELIX 37 AE1 THR M 83 SER M 87 5 5 HELIX 38 AE2 ARG Q 61 GLN Q 64 5 4 HELIX 39 AE3 THR Q 83 THR Q 87 5 5 HELIX 40 AE4 ASP R 78 PHE R 82 5 5 HELIX 41 AE5 ALA c 58 THR c 63 1 6 HELIX 42 AE6 MET c 100 SER c 115 1 16 HELIX 43 AE7 LEU c 122 CYS c 126 5 5 HELIX 44 AE8 ASN c 195 THR c 198 5 4 HELIX 45 AE9 LYS c 335 ARG c 350 1 16 HELIX 46 AF1 ASP c 368 THR c 373 1 6 HELIX 47 AF2 ASN c 425 ARG c 429 5 5 HELIX 48 AF3 MET c 475 ARG c 480 1 6 HELIX 49 AF4 THR d 529 ASN d 543 1 15 HELIX 50 AF5 VAL d 570 ILE d 595 1 26 HELIX 51 AF6 ASN d 618 ASN d 625 1 8 HELIX 52 AF7 THR d 627 ILE d 635 1 9 HELIX 53 AF8 TYR d 638 LEU d 661 1 24 HELIX 54 AF9 PRO h 61 LYS h 64 5 4 HELIX 55 AG1 THR h 83 THR h 87 5 5 HELIX 56 AG2 GLN l 79 VAL l 83 5 5 HELIX 57 AG3 THR m 83 SER m 87 5 5 HELIX 58 AG4 ARG q 61 GLN q 64 5 4 HELIX 59 AG5 THR q 83 THR q 87 5 5 HELIX 60 AG6 ASP r 78 PHE r 82 5 5 SHEET 1 AA1 3 GLY 2 495 THR 2 499 0 SHEET 2 AA1 3 TRP 2 35 TYR 2 39 -1 N TRP 2 35 O THR 2 499 SHEET 3 AA1 3 ILE A 603 PRO A 609 -1 O VAL A 608 N VAL 2 36 SHEET 1 AA2 5 TRP 2 45 ASP 2 47 0 SHEET 2 AA2 5 TYR 2 486 ILE 2 491 -1 O LYS 2 490 N LYS 2 46 SHEET 3 AA2 5 PHE 2 223 CYS 2 228 -1 N ALA 2 224 O VAL 2 489 SHEET 4 AA2 5 VAL 2 242 VAL 2 245 -1 O SER 2 243 N LYS 2 227 SHEET 5 AA2 5 ILE 2 84 HIS 2 85 -1 N ILE 2 84 O THR 2 244 SHEET 1 AA3 2 PHE 2 53 SER 2 56 0 SHEET 2 AA3 2 ILE 2 215 CYS 2 218 -1 O CYS 2 218 N PHE 2 53 SHEET 1 AA4 2 GLU 2 91 ASN 2 94 0 SHEET 2 AA4 2 THR 2 236 CYS 2 239 -1 O CYS 2 239 N GLU 2 91 SHEET 1 AA5 5 LYS 2 169 TYR 2 177 0 SHEET 2 AA5 5 LEU 2 154 THR 2 162 -1 N MET 2 161 O GLN 2 170 SHEET 3 AA5 5 LEU 2 129 ASN 2 133 -1 N GLN 2 130 O SER 2 158 SHEET 4 AA5 5 GLU 2 190 LEU 2 193 -1 O TYR 2 191 N LEU 2 129 SHEET 5 AA5 5 VAL 2 181 GLN 2 183 -1 N VAL 2 182 O ARG 2 192 SHEET 1 AA6 3 THR 2 202 GLN 2 203 0 SHEET 2 AA6 3 MET 2 434 TYR 2 435 1 O TYR 2 435 N THR 2 202 SHEET 3 AA6 3 ILE 2 423 ILE 2 424 -1 N ILE 2 424 O MET 2 434 SHEET 1 AA7 6 MET 2 271 ARG 2 273 0 SHEET 2 AA7 6 ILE 2 284 ARG 2 298 -1 O GLN 2 287 N MET 2 271 SHEET 3 AA7 6 HIS 2 330 SER 2 334 -1 O HIS 2 330 N THR 2 297 SHEET 4 AA7 6 SER 2 413 LYS 2 421 -1 O LEU 2 416 N CYS 2 331 SHEET 5 AA7 6 PHE 2 382 CYS 2 385 -1 N TYR 2 384 O ARG 2 419 SHEET 6 AA7 6 HIS 2 374 ASN 2 377 -1 N HIS 2 374 O CYS 2 385 SHEET 1 AA8 6 MET 2 271 ARG 2 273 0 SHEET 2 AA8 6 ILE 2 284 ARG 2 298 -1 O GLN 2 287 N MET 2 271 SHEET 3 AA8 6 ILE 2 443 ARG 2 456 -1 O SER 2 447 N ILE 2 294 SHEET 4 AA8 6 THR 2 465 PRO 2 470 -1 O ARG 2 469 N THR 2 455 SHEET 5 AA8 6 ILE 2 358 PHE 2 361 1 N ILE 2 358 O GLU 2 466 SHEET 6 AA8 6 SER 2 393 TRP 2 395 -1 O SER 2 393 N PHE 2 361 SHEET 1 AA9 2 ARG 2 304 GLY 2 312 0 SHEET 2 AA9 2 GLN 2 315 THR 2 320 -1 O PHE 2 317 N ILE 2 307 SHEET 1 AB1 4 VAL 3 6 SER 3 7 0 SHEET 2 AB1 4 LEU 3 18 GLU 3 23 -1 O THR 3 21 N SER 3 7 SHEET 3 AB1 4 GLU 3 77 LEU 3 82 -1 O LEU 3 80 N LEU 3 20 SHEET 4 AB1 4 VAL 3 67 ASP 3 72 -1 N SER 3 70 O SER 3 79 SHEET 1 AB2 4 VAL 3 11 VAL 3 12 0 SHEET 2 AB2 4 LEU 3 107 VAL 3 111 1 O THR 3 110 N VAL 3 12 SHEET 3 AB2 4 ALA 3 88 TYR 3 99 -1 N ALA 3 88 O VAL 3 109 SHEET 4 AB2 4 ARG 3 100H ILE 3 100I-1 O ILE 3 100I N ALA 3 96 SHEET 1 AB3 5 THR 3 57 HIS 3 59 0 SHEET 2 AB3 5 LEU 3 45 TYR 3 52 -1 N GLY 3 50 O ASN 3 58 SHEET 3 AB3 5 TYR 3 33 GLN 3 39 -1 N ARG 3 38 O GLU 3 46 SHEET 4 AB3 5 ALA 3 88 TYR 3 99 -1 O PHE 3 91 N VAL 3 37 SHEET 5 AB3 5 VAL A 518 PHE A 519 1 O VAL A 518 N LYS 3 97 SHEET 1 AB4 4 MET 4 4 SER 4 7 0 SHEET 2 AB4 4 VAL 4 19 ALA 4 25 -1 O ARG 4 24 N THR 4 5 SHEET 3 AB4 4 ASP 4 70 ILE 4 75 -1 O PHE 4 71 N CYS 4 23 SHEET 4 AB4 4 PHE 4 62 SER 4 67 -1 N SER 4 63 O THR 4 74 SHEET 1 AB5 6 SER 4 10 SER 4 12 0 SHEET 2 AB5 6 THR 4 102 ASP 4 105 1 O LYS 4 103 N LEU 4 11 SHEET 3 AB5 6 THR 4 85 GLN 4 90 -1 N TYR 4 86 O THR 4 102 SHEET 4 AB5 6 LEU 4 33 GLN 4 38 -1 N GLN 4 38 O THR 4 85 SHEET 5 AB5 6 PRO 4 44 TYR 4 49 -1 O THR 4 45 N GLN 4 37 SHEET 6 AB5 6 THR 4 53 LEU 4 54 -1 O THR 4 53 N TYR 4 49 SHEET 1 AB6 4 GLN 5 5 SER 5 7 0 SHEET 2 AB6 4 SER 5 19 ASN 5 23 -1 O ASN 5 23 N GLN 5 5 SHEET 3 AB6 4 LEU 5 77 LEU 5 82 -1 O LEU 5 80 N LEU 5 20 SHEET 4 AB6 4 VAL 5 67 ASP 5 72 -1 N SER 5 70 O SER 5 79 SHEET 1 AB7 5 LEU 5 11 VAL 5 12 0 SHEET 2 AB7 5 THR 5 105 VAL 5 109 1 O THR 5 108 N VAL 5 12 SHEET 3 AB7 5 ALA 5 88 ALA 5 93 -1 N ALA 5 88 O VAL 5 107 SHEET 4 AB7 5 TRP 5 34 GLN 5 39 -1 N GLN 5 39 O ILE 5 89 SHEET 5 AB7 5 GLU 5 46 VAL 5 51 -1 O GLU 5 46 N ARG 5 38 SHEET 1 AB8 2 THR 5 95 LYS 5 96 0 SHEET 2 AB8 2 TYR 5 100O MET 5 100P-1 O TYR 5 100O N LYS 5 96 SHEET 1 AB9 2 ARG 5 99 ILE 5 100A 0 SHEET 2 AB9 2 TRP 5 100J THR 5 100L-1 O PHE 5 100K N ARG 5 100 SHEET 1 AC1 5 PHE 6 9 SER 6 12 0 SHEET 2 AC1 5 THR 6 102 ILE 6 105 1 O ILE 6 105 N VAL 6 11 SHEET 3 AC1 5 ASP 6 85 HIS 6 89 -1 N TYR 6 86 O THR 6 102 SHEET 4 AC1 5 ILE 6 34 GLN 6 38 -1 N GLN 6 38 O ASP 6 85 SHEET 5 AC1 5 PRO 6 44 ILE 6 48 -1 O SER 6 45 N GLN 6 37 SHEET 1 AC2 3 THR 6 18 CYS 6 23 0 SHEET 2 AC2 3 ALA 6 71 THR 6 76 -1 O ILE 6 75 N ALA 6 19 SHEET 3 AC2 3 PHE 6 62 GLY 6 64 -1 N SER 6 63 O THR 6 74 SHEET 1 AC3 4 LEU 7 4 GLN 7 6 0 SHEET 2 AC3 4 ALA 7 19 ALA 7 25 -1 O LYS 7 24 N THR 7 5 SHEET 3 AC3 4 ASP 7 69 ILE 7 74 -1 O LEU 7 72 N LEU 7 21 SHEET 4 AC3 4 PHE 7 61 SER 7 66 -1 N VAL 7 62 O THR 7 73 SHEET 1 AC4 6 ILE 7 10 LEU 7 13 0 SHEET 2 AC4 6 SER 7 97 VAL 7 101 1 O GLU 7 98 N LEU 7 11 SHEET 3 AC4 6 VAL 7 84 GLN 7 89 -1 N TYR 7 85 O SER 7 97 SHEET 4 AC4 6 THR 7 33 LYS 7 37 -1 N LYS 7 37 O VAL 7 84 SHEET 5 AC4 6 ARG 7 44 TYR 7 48 -1 O ARG 7 44 N GLN 7 36 SHEET 6 AC4 6 ARG 7 52 ARG 7 53 -1 O ARG 7 52 N TYR 7 48 SHEET 1 AC5 4 ILE 7 10 LEU 7 13 0 SHEET 2 AC5 4 SER 7 97 VAL 7 101 1 O GLU 7 98 N LEU 7 11 SHEET 3 AC5 4 VAL 7 84 GLN 7 89 -1 N TYR 7 85 O SER 7 97 SHEET 4 AC5 4 PHE 7 92 PHE 7 93 -1 O PHE 7 92 N GLN 7 89 SHEET 1 AC6 4 GLN 8 3 GLN 8 6 0 SHEET 2 AC6 4 VAL 8 18 SER 8 25 -1 O ARG 8 23 N VAL 8 5 SHEET 3 AC6 4 GLY 8 76G PHE 8 82 -1 O GLY 8 76G N ALA 8 24 SHEET 4 AC6 4 VAL 8 67 SER 8 68 -1 N SER 8 68 O GLU 8 81 SHEET 1 AC7 4 GLN 8 3 GLN 8 6 0 SHEET 2 AC7 4 VAL 8 18 SER 8 25 -1 O ARG 8 23 N VAL 8 5 SHEET 3 AC7 4 GLY 8 76G PHE 8 82 -1 O GLY 8 76G N ALA 8 24 SHEET 4 AC7 4 ARG 8 71 GLN 8 72 -1 N GLN 8 72 O VAL 8 77 SHEET 1 AC8 6 VAL 8 10 ILE 8 11 0 SHEET 2 AC8 6 THR 8 107 VAL 8 110 1 O VAL 8 108 N VAL 8 10 SHEET 3 AC8 6 ALA 8 88 ARG 8 95 -1 N ALA 8 88 O VAL 8 109 SHEET 4 AC8 6 ILE 8 34 ILE 8 40 -1 N VAL 8 37 O PHE 8 91 SHEET 5 AC8 6 GLY 8 44 ILE 8 51 -1 O GLY 8 49 N TRP 8 36 SHEET 6 AC8 6 VAL 8 57 TYR 8 59 -1 O SER 8 58 N TRP 8 50 SHEET 1 AC9 4 VAL 8 10 ILE 8 11 0 SHEET 2 AC9 4 THR 8 107 VAL 8 110 1 O VAL 8 108 N VAL 8 10 SHEET 3 AC9 4 ALA 8 88 ARG 8 95 -1 N ALA 8 88 O VAL 8 109 SHEET 4 AC9 4 TRP 8 100F TRP 8 103 -1 O TYR 8 102 N ARG 8 94 SHEET 1 AD1 3 GLY C 495 THR C 499 0 SHEET 2 AD1 3 TRP C 35 TYR C 39 -1 N TRP C 35 O THR C 499 SHEET 3 AD1 3 ILE D 603 PRO D 609 -1 O VAL D 608 N VAL C 36 SHEET 1 AD2 5 TRP C 45 ASP C 47 0 SHEET 2 AD2 5 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AD2 5 PHE C 223 CYS C 228 -1 N ALA C 224 O VAL C 489 SHEET 4 AD2 5 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 AD2 5 ILE C 84 HIS C 85 -1 N ILE C 84 O THR C 244 SHEET 1 AD3 2 PHE C 53 SER C 56 0 SHEET 2 AD3 2 ILE C 215 CYS C 218 -1 O CYS C 218 N PHE C 53 SHEET 1 AD4 2 GLU C 91 ASN C 94 0 SHEET 2 AD4 2 THR C 236 CYS C 239 -1 O GLY C 237 N PHE C 93 SHEET 1 AD5 5 LYS C 169 TYR C 177 0 SHEET 2 AD5 5 LEU C 154 THR C 162 -1 N MET C 161 O GLN C 170 SHEET 3 AD5 5 LEU C 129 ASN C 133 -1 N GLN C 130 O SER C 158 SHEET 4 AD5 5 GLU C 190 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AD5 5 VAL C 181 GLN C 183 -1 N VAL C 182 O ARG C 192 SHEET 1 AD6 3 THR C 202 GLN C 203 0 SHEET 2 AD6 3 MET C 434 TYR C 435 1 O TYR C 435 N THR C 202 SHEET 3 AD6 3 ILE C 423 ILE C 424 -1 N ILE C 424 O MET C 434 SHEET 1 AD7 6 MET C 271 ARG C 273 0 SHEET 2 AD7 6 ILE C 284 ARG C 298 -1 O GLN C 287 N MET C 271 SHEET 3 AD7 6 HIS C 330 SER C 334 -1 O ASN C 332 N ASN C 295 SHEET 4 AD7 6 SER C 413 ILE C 420 -1 O LEU C 416 N CYS C 331 SHEET 5 AD7 6 PHE C 382 CYS C 385 -1 N TYR C 384 O ARG C 419 SHEET 6 AD7 6 HIS C 374 ASN C 377 -1 N HIS C 374 O CYS C 385 SHEET 1 AD8 6 MET C 271 ARG C 273 0 SHEET 2 AD8 6 ILE C 284 ARG C 298 -1 O GLN C 287 N MET C 271 SHEET 3 AD8 6 ILE C 443 ARG C 456 -1 O LEU C 452 N VAL C 286 SHEET 4 AD8 6 THR C 465 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 5 AD8 6 ILE C 358 PHE C 361 1 N ILE C 358 O GLU C 466 SHEET 6 AD8 6 SER C 393 TRP C 395 -1 O SER C 393 N PHE C 361 SHEET 1 AD9 2 ARG C 304 GLY C 312 0 SHEET 2 AD9 2 GLN C 315 THR C 320 -1 O PHE C 317 N ILE C 307 SHEET 1 AE1 5 VAL D 518 PHE D 519 0 SHEET 2 AE1 5 ALA H 88 TYR H 99 1 O LYS H 97 N VAL D 518 SHEET 3 AE1 5 TYR H 33 GLN H 39 -1 N VAL H 37 O PHE H 91 SHEET 4 AE1 5 LEU H 45 TYR H 52 -1 O GLU H 46 N ARG H 38 SHEET 5 AE1 5 THR H 57 HIS H 59 -1 O ASN H 58 N GLY H 50 SHEET 1 AE2 4 VAL H 11 VAL H 12 0 SHEET 2 AE2 4 LEU H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AE2 4 ALA H 88 TYR H 99 -1 N ALA H 88 O VAL H 109 SHEET 4 AE2 4 ARG H 100H ILE H 100I-1 O ILE H 100I N ALA H 96 SHEET 1 AE3 4 VAL H 6 SER H 7 0 SHEET 2 AE3 4 LEU H 18 CYS H 22 -1 O THR H 21 N SER H 7 SHEET 3 AE3 4 GLU H 77 LEU H 82 -1 O LEU H 80 N LEU H 20 SHEET 4 AE3 4 VAL H 67 ASP H 72 -1 N SER H 70 O SER H 79 SHEET 1 AE4 4 MET L 4 SER L 7 0 SHEET 2 AE4 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AE4 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AE4 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AE5 6 SER L 10 SER L 12 0 SHEET 2 AE5 6 THR L 102 ASP L 105 1 O LYS L 103 N LEU L 11 SHEET 3 AE5 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AE5 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AE5 6 PRO L 44 TYR L 49 -1 O THR L 45 N GLN L 37 SHEET 6 AE5 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AE6 4 GLN M 5 SER M 7 0 SHEET 2 AE6 4 SER M 19 ASN M 23 -1 O ASN M 23 N GLN M 5 SHEET 3 AE6 4 LEU M 77 LEU M 82 -1 O LEU M 80 N LEU M 20 SHEET 4 AE6 4 VAL M 67 ASP M 72 -1 N SER M 70 O SER M 79 SHEET 1 AE7 5 LEU M 11 VAL M 12 0 SHEET 2 AE7 5 THR M 105 VAL M 109 1 O THR M 108 N VAL M 12 SHEET 3 AE7 5 ALA M 88 THR M 95 -1 N ALA M 88 O VAL M 107 SHEET 4 AE7 5 TYR M 33 GLN M 39 -1 N GLN M 39 O ILE M 89 SHEET 5 AE7 5 GLU M 46 VAL M 51 -1 O GLU M 46 N ARG M 38 SHEET 1 AE8 2 ARG M 99 ILE M 100A 0 SHEET 2 AE8 2 TRP M 100J THR M 100L-1 O PHE M 100K N ARG M 100 SHEET 1 AE9 5 PHE N 9 SER N 12 0 SHEET 2 AE9 5 THR N 102 ILE N 105 1 O ILE N 105 N VAL N 11 SHEET 3 AE9 5 ASP N 85 CYS N 88 -1 N TYR N 86 O THR N 102 SHEET 4 AE9 5 TRP N 35 GLN N 38 -1 N GLN N 38 O ASP N 85 SHEET 5 AE9 5 PRO N 44 ILE N 48 -1 O SER N 45 N GLN N 37 SHEET 1 AF1 3 ALA N 19 GLU N 26 0 SHEET 2 AF1 3 THR N 70 ILE N 75 -1 O ILE N 75 N ALA N 19 SHEET 3 AF1 3 PHE N 62 GLY N 64 -1 N SER N 63 O THR N 74 SHEET 1 AF2 4 GLN Q 3 GLN Q 6 0 SHEET 2 AF2 4 SER Q 17 SER Q 25 -1 O SER Q 25 N GLN Q 3 SHEET 3 AF2 4 GLY Q 76G SER Q 82A-1 O GLY Q 76G N ALA Q 24 SHEET 4 AF2 4 VAL Q 67 SER Q 68 -1 N SER Q 68 O GLU Q 81 SHEET 1 AF3 4 GLN Q 3 GLN Q 6 0 SHEET 2 AF3 4 SER Q 17 SER Q 25 -1 O SER Q 25 N GLN Q 3 SHEET 3 AF3 4 GLY Q 76G SER Q 82A-1 O GLY Q 76G N ALA Q 24 SHEET 4 AF3 4 ARG Q 71 GLN Q 72 -1 N GLN Q 72 O VAL Q 77 SHEET 1 AF4 6 VAL Q 10 ILE Q 11 0 SHEET 2 AF4 6 THR Q 107 VAL Q 110 1 O VAL Q 108 N VAL Q 10 SHEET 3 AF4 6 ALA Q 88 ARG Q 95 -1 N ALA Q 88 O VAL Q 109 SHEET 4 AF4 6 ILE Q 34 ILE Q 40 -1 N LEU Q 39 O GLU Q 89 SHEET 5 AF4 6 GLY Q 44 ILE Q 51 -1 O GLY Q 49 N TRP Q 36 SHEET 6 AF4 6 VAL Q 57 TYR Q 59 -1 O SER Q 58 N TRP Q 50 SHEET 1 AF5 4 VAL Q 10 ILE Q 11 0 SHEET 2 AF5 4 THR Q 107 VAL Q 110 1 O VAL Q 108 N VAL Q 10 SHEET 3 AF5 4 ALA Q 88 ARG Q 95 -1 N ALA Q 88 O VAL Q 109 SHEET 4 AF5 4 TRP Q 100F TRP Q 103 -1 O TYR Q 102 N ARG Q 94 SHEET 1 AF6 4 LEU R 4 GLN R 6 0 SHEET 2 AF6 4 ALA R 19 ALA R 25 -1 O LYS R 24 N THR R 5 SHEET 3 AF6 4 ASP R 69 ILE R 74 -1 O LEU R 72 N LEU R 21 SHEET 4 AF6 4 PHE R 61 SER R 66 -1 N VAL R 62 O THR R 73 SHEET 1 AF7 6 ILE R 10 LEU R 13 0 SHEET 2 AF7 6 SER R 97 VAL R 101 1 O GLU R 98 N LEU R 11 SHEET 3 AF7 6 VAL R 84 GLN R 89 -1 N TYR R 85 O SER R 97 SHEET 4 AF7 6 THR R 33 LYS R 37 -1 N LYS R 37 O VAL R 84 SHEET 5 AF7 6 ARG R 44 TYR R 48 -1 O ARG R 44 N GLN R 36 SHEET 6 AF7 6 ARG R 52 ARG R 53 -1 O ARG R 52 N TYR R 48 SHEET 1 AF8 4 ILE R 10 LEU R 13 0 SHEET 2 AF8 4 SER R 97 VAL R 101 1 O GLU R 98 N LEU R 11 SHEET 3 AF8 4 VAL R 84 GLN R 89 -1 N TYR R 85 O SER R 97 SHEET 4 AF8 4 PHE R 92 PHE R 93 -1 O PHE R 92 N GLN R 89 SHEET 1 AF9 3 GLY c 495 THR c 499 0 SHEET 2 AF9 3 TRP c 35 TYR c 39 -1 N TRP c 35 O THR c 499 SHEET 3 AF9 3 ILE d 603 PRO d 609 -1 O VAL d 608 N VAL c 36 SHEET 1 AG1 5 TRP c 45 ASP c 47 0 SHEET 2 AG1 5 TYR c 486 ILE c 491 -1 O LYS c 490 N LYS c 46 SHEET 3 AG1 5 PHE c 223 CYS c 228 -1 N ALA c 224 O VAL c 489 SHEET 4 AG1 5 VAL c 242 VAL c 245 -1 O SER c 243 N LYS c 227 SHEET 5 AG1 5 ILE c 84 HIS c 85 -1 N ILE c 84 O THR c 244 SHEET 1 AG2 2 PHE c 53 SER c 56 0 SHEET 2 AG2 2 ILE c 215 CYS c 218 -1 O CYS c 218 N PHE c 53 SHEET 1 AG3 2 GLU c 91 ASN c 94 0 SHEET 2 AG3 2 THR c 236 CYS c 239 -1 O GLY c 237 N PHE c 93 SHEET 1 AG4 5 LYS c 169 TYR c 177 0 SHEET 2 AG4 5 LEU c 154 THR c 162 -1 N MET c 161 O GLN c 170 SHEET 3 AG4 5 LEU c 129 ASN c 133 -1 N GLN c 130 O SER c 158 SHEET 4 AG4 5 GLU c 190 LEU c 193 -1 O TYR c 191 N LEU c 129 SHEET 5 AG4 5 VAL c 181 GLN c 183 -1 N VAL c 182 O ARG c 192 SHEET 1 AG5 3 THR c 202 GLN c 203 0 SHEET 2 AG5 3 MET c 434 TYR c 435 1 O TYR c 435 N THR c 202 SHEET 3 AG5 3 ILE c 423 ILE c 424 -1 N ILE c 424 O MET c 434 SHEET 1 AG6 6 MET c 271 ARG c 273 0 SHEET 2 AG6 6 ILE c 284 ARG c 298 -1 O GLN c 287 N MET c 271 SHEET 3 AG6 6 HIS c 330 SER c 334 -1 O HIS c 330 N THR c 297 SHEET 4 AG6 6 SER c 413 ILE c 420 -1 O LEU c 416 N CYS c 331 SHEET 5 AG6 6 PHE c 382 CYS c 385 -1 N TYR c 384 O ARG c 419 SHEET 6 AG6 6 HIS c 374 ASN c 377 -1 N HIS c 374 O CYS c 385 SHEET 1 AG7 6 MET c 271 ARG c 273 0 SHEET 2 AG7 6 ILE c 284 ARG c 298 -1 O GLN c 287 N MET c 271 SHEET 3 AG7 6 ILE c 443 ARG c 456 -1 O SER c 447 N ILE c 294 SHEET 4 AG7 6 THR c 465 PRO c 470 -1 O ARG c 469 N THR c 455 SHEET 5 AG7 6 ILE c 358 PHE c 361 1 N ILE c 358 O GLU c 466 SHEET 6 AG7 6 SER c 393 TRP c 395 -1 O SER c 393 N PHE c 361 SHEET 1 AG8 2 ARG c 304 GLY c 312 0 SHEET 2 AG8 2 GLN c 315 THR c 320 -1 O PHE c 317 N ILE c 307 SHEET 1 AG9 5 VAL d 518 PHE d 519 0 SHEET 2 AG9 5 ALA h 88 TYR h 99 1 O LYS h 97 N VAL d 518 SHEET 3 AG9 5 TYR h 33 GLN h 39 -1 N VAL h 37 O PHE h 91 SHEET 4 AG9 5 LEU h 45 TYR h 52 -1 O GLU h 46 N ARG h 38 SHEET 5 AG9 5 THR h 57 HIS h 59 -1 O ASN h 58 N GLY h 50 SHEET 1 AH1 4 VAL h 11 VAL h 12 0 SHEET 2 AH1 4 LEU h 107 VAL h 111 1 O THR h 110 N VAL h 12 SHEET 3 AH1 4 ALA h 88 TYR h 99 -1 N ALA h 88 O VAL h 109 SHEET 4 AH1 4 ARG h 100H ILE h 100I-1 O ILE h 100I N ALA h 96 SHEET 1 AH2 4 VAL h 6 SER h 7 0 SHEET 2 AH2 4 LEU h 18 GLU h 23 -1 O THR h 21 N SER h 7 SHEET 3 AH2 4 GLU h 77 LEU h 82 -1 O LEU h 80 N LEU h 20 SHEET 4 AH2 4 VAL h 67 ASP h 72 -1 N SER h 70 O SER h 79 SHEET 1 AH3 4 MET l 4 SER l 7 0 SHEET 2 AH3 4 VAL l 19 ALA l 25 -1 O ARG l 24 N THR l 5 SHEET 3 AH3 4 ASP l 70 ILE l 75 -1 O PHE l 71 N CYS l 23 SHEET 4 AH3 4 PHE l 62 SER l 67 -1 N SER l 63 O THR l 74 SHEET 1 AH4 6 SER l 10 SER l 12 0 SHEET 2 AH4 6 THR l 102 ASP l 105 1 O LYS l 103 N LEU l 11 SHEET 3 AH4 6 THR l 85 GLN l 90 -1 N TYR l 86 O THR l 102 SHEET 4 AH4 6 LEU l 33 GLN l 38 -1 N GLN l 38 O THR l 85 SHEET 5 AH4 6 PRO l 44 TYR l 49 -1 O THR l 45 N GLN l 37 SHEET 6 AH4 6 THR l 53 LEU l 54 -1 O THR l 53 N TYR l 49 SHEET 1 AH5 4 GLN m 5 SER m 7 0 SHEET 2 AH5 4 SER m 19 ASN m 23 -1 O ASN m 23 N GLN m 5 SHEET 3 AH5 4 LEU m 77 LEU m 82 -1 O LEU m 80 N LEU m 20 SHEET 4 AH5 4 VAL m 67 ASP m 72 -1 N SER m 70 O SER m 79 SHEET 1 AH6 5 LEU m 11 VAL m 12 0 SHEET 2 AH6 5 THR m 105 VAL m 109 1 O THR m 108 N VAL m 12 SHEET 3 AH6 5 ALA m 88 ALA m 93 -1 N ALA m 88 O VAL m 107 SHEET 4 AH6 5 TRP m 34 GLN m 39 -1 N GLN m 39 O ILE m 89 SHEET 5 AH6 5 GLU m 46 VAL m 51 -1 O GLU m 46 N ARG m 38 SHEET 1 AH7 2 ARG m 99 ILE m 100A 0 SHEET 2 AH7 2 TRP m 100J THR m 100L-1 O PHE m 100K N ARG m 100 SHEET 1 AH8 5 PHE n 9 SER n 12 0 SHEET 2 AH8 5 THR n 102 ILE n 105 1 O ILE n 105 N VAL n 11 SHEET 3 AH8 5 ASP n 85 HIS n 89 -1 N TYR n 86 O THR n 102 SHEET 4 AH8 5 ILE n 34 GLN n 38 -1 N GLN n 38 O ASP n 85 SHEET 5 AH8 5 PRO n 44 ILE n 48 -1 O SER n 45 N GLN n 37 SHEET 1 AH9 3 THR n 18 GLU n 26 0 SHEET 2 AH9 3 THR n 70 THR n 76 -1 O ILE n 75 N ALA n 19 SHEET 3 AH9 3 PHE n 62 GLY n 64 -1 N SER n 63 O THR n 74 SHEET 1 AI1 4 GLN q 3 GLN q 6 0 SHEET 2 AI1 4 VAL q 18 SER q 25 -1 O SER q 25 N GLN q 3 SHEET 3 AI1 4 GLY q 76G PHE q 82 -1 O PHE q 82 N VAL q 18 SHEET 4 AI1 4 VAL q 67 SER q 68 -1 N SER q 68 O GLU q 81 SHEET 1 AI2 4 GLN q 3 GLN q 6 0 SHEET 2 AI2 4 VAL q 18 SER q 25 -1 O SER q 25 N GLN q 3 SHEET 3 AI2 4 GLY q 76G PHE q 82 -1 O PHE q 82 N VAL q 18 SHEET 4 AI2 4 ARG q 71 GLN q 72 -1 N GLN q 72 O VAL q 77 SHEET 1 AI3 6 VAL q 10 ILE q 11 0 SHEET 2 AI3 6 THR q 107 VAL q 110 1 O VAL q 108 N VAL q 10 SHEET 3 AI3 6 ALA q 88 ARG q 95 -1 N ALA q 88 O VAL q 109 SHEET 4 AI3 6 ILE q 34 ILE q 40 -1 N VAL q 37 O PHE q 91 SHEET 5 AI3 6 GLY q 44 ILE q 51 -1 O GLY q 49 N TRP q 36 SHEET 6 AI3 6 VAL q 57 TYR q 59 -1 O SER q 58 N TRP q 50 SHEET 1 AI4 4 VAL q 10 ILE q 11 0 SHEET 2 AI4 4 THR q 107 VAL q 110 1 O VAL q 108 N VAL q 10 SHEET 3 AI4 4 ALA q 88 ARG q 95 -1 N ALA q 88 O VAL q 109 SHEET 4 AI4 4 TRP q 100F TRP q 103 -1 O TYR q 102 N ARG q 94 SHEET 1 AI5 4 LEU r 4 GLN r 6 0 SHEET 2 AI5 4 ALA r 19 ALA r 25 -1 O LYS r 24 N THR r 5 SHEET 3 AI5 4 ASP r 69 ILE r 74 -1 O LEU r 72 N LEU r 21 SHEET 4 AI5 4 PHE r 61 SER r 66 -1 N VAL r 62 O THR r 73 SHEET 1 AI6 6 ILE r 10 LEU r 13 0 SHEET 2 AI6 6 SER r 97 VAL r 101 1 O GLU r 98 N LEU r 11 SHEET 3 AI6 6 VAL r 84 GLN r 89 -1 N TYR r 85 O SER r 97 SHEET 4 AI6 6 THR r 33 LYS r 37 -1 N LYS r 37 O VAL r 84 SHEET 5 AI6 6 ARG r 44 TYR r 48 -1 O ARG r 44 N GLN r 36 SHEET 6 AI6 6 ARG r 52 ARG r 53 -1 O ARG r 52 N TYR r 48 SHEET 1 AI7 4 ILE r 10 LEU r 13 0 SHEET 2 AI7 4 SER r 97 VAL r 101 1 O GLU r 98 N LEU r 11 SHEET 3 AI7 4 VAL r 84 GLN r 89 -1 N TYR r 85 O SER r 97 SHEET 4 AI7 4 PHE r 92 PHE r 93 -1 O PHE r 92 N GLN r 89 SSBOND 1 CYS 2 119 CYS 2 205 1555 1555 2.03 SSBOND 2 CYS 2 131 CYS 2 157 1555 1555 2.03 SSBOND 3 CYS 2 201 CYS 2 433 1555 1555 2.03 SSBOND 4 CYS 2 218 CYS 2 247 1555 1555 2.03 SSBOND 5 CYS 2 228 CYS 2 239 1555 1555 2.03 SSBOND 6 CYS 2 296 CYS 2 331 1555 1555 2.03 SSBOND 7 CYS 2 378 CYS 2 445 1555 1555 2.03 SSBOND 8 CYS 2 385 CYS 2 418 1555 1555 2.03 SSBOND 9 CYS 3 22 CYS 3 92 1555 1555 2.03 SSBOND 10 CYS 4 23 CYS 4 88 1555 1555 2.03 SSBOND 11 CYS 5 22 CYS 5 92 1555 1555 2.03 SSBOND 12 CYS 6 23 CYS 6 88 1555 1555 2.03 SSBOND 13 CYS 8 22 CYS 8 92 1555 1555 2.03 SSBOND 14 CYS 8 98 CYS 8 100A 1555 1555 2.03 SSBOND 15 CYS A 598 CYS A 604 1555 1555 2.02 SSBOND 16 CYS C 119 CYS C 205 1555 1555 2.03 SSBOND 17 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 18 CYS C 201 CYS C 433 1555 1555 2.03 SSBOND 19 CYS C 218 CYS C 247 1555 1555 2.03 SSBOND 20 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 21 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 22 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 23 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 24 CYS D 598 CYS D 604 1555 1555 2.03 SSBOND 25 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 26 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 27 CYS M 22 CYS M 92 1555 1555 2.03 SSBOND 28 CYS N 23 CYS N 88 1555 1555 2.03 SSBOND 29 CYS Q 22 CYS Q 92 1555 1555 2.03 SSBOND 30 CYS Q 98 CYS Q 100A 1555 1555 2.03 SSBOND 31 CYS c 119 CYS c 205 1555 1555 2.03 SSBOND 32 CYS c 131 CYS c 157 1555 1555 2.03 SSBOND 33 CYS c 201 CYS c 433 1555 1555 2.03 SSBOND 34 CYS c 218 CYS c 247 1555 1555 2.03 SSBOND 35 CYS c 228 CYS c 239 1555 1555 2.03 SSBOND 36 CYS c 296 CYS c 331 1555 1555 2.03 SSBOND 37 CYS c 378 CYS c 445 1555 1555 2.03 SSBOND 38 CYS c 385 CYS c 418 1555 1555 2.03 SSBOND 39 CYS d 598 CYS d 604 1555 1555 2.02 SSBOND 40 CYS h 22 CYS h 92 1555 1555 2.03 SSBOND 41 CYS l 23 CYS l 88 1555 1555 2.03 SSBOND 42 CYS m 22 CYS m 92 1555 1555 2.03 SSBOND 43 CYS n 23 CYS n 88 1555 1555 2.03 SSBOND 44 CYS q 22 CYS q 92 1555 1555 2.03 SSBOND 45 CYS q 98 CYS q 100A 1555 1555 2.03 LINK ND2 ASN 2 133 C1 NAG 2 601 1555 1555 1.45 LINK ND2 ASN 2 137 C1 NAG 2 603 1555 1555 1.44 LINK ND2 ASN 2 156 C1 NAG 2 607 1555 1555 1.43 LINK ND2 ASN 2 160 C1 NAG 2 609 1555 1555 1.45 LINK ND2 ASN 2 197 C1 NAG 2 611 1555 1555 1.44 LINK ND2 ASN 2 234 C1 NAG 2 612 1555 1555 1.45 LINK ND2 ASN 2 262 C1 NAG 2 614 1555 1555 1.43 LINK ND2 ASN 2 276 C1 NAG 2 643 1555 1555 1.44 LINK ND2 ASN 2 295 C1 NAG 2 619 1555 1555 1.42 LINK ND2 ASN 2 301 C1 NAG 2 621 1555 1555 1.44 LINK ND2 ASN 2 332 C1 NAG 2 632 1555 1555 1.42 LINK ND2 ASN 2 355 C1 NAG 2 623 1555 1555 1.44 LINK ND2 ASN 2 363 C1 NAG 2 624 1555 1555 1.43 LINK ND2 ASN 2 386 C1 NAG 2 627 1555 1555 1.44 LINK ND2 ASN 2 392 C1 NAG 2 631 1555 1555 1.43 LINK ND2 ASN C 133 C1 NAG C 601 1555 1555 1.45 LINK ND2 ASN C 137 C1 NAG C 603 1555 1555 1.44 LINK ND2 ASN C 156 C1 NAG C 607 1555 1555 1.44 LINK ND2 ASN C 160 C1 NAG C 609 1555 1555 1.44 LINK ND2 ASN C 197 C1 NAG C 611 1555 1555 1.44 LINK ND2 ASN C 234 C1 NAG C 612 1555 1555 1.45 LINK ND2 ASN C 262 C1 NAG C 614 1555 1555 1.43 LINK ND2 ASN C 276 C1 NAG C 643 1555 1555 1.45 LINK ND2 ASN C 295 C1 NAG C 619 1555 1555 1.43 LINK ND2 ASN C 301 C1 NAG C 621 1555 1555 1.44 LINK ND2 ASN C 332 C1 NAG C 632 1555 1555 1.42 LINK ND2 ASN C 355 C1 NAG C 623 1555 1555 1.44 LINK ND2 ASN C 363 C1 NAG C 624 1555 1555 1.43 LINK ND2 ASN C 386 C1 NAG C 627 1555 1555 1.44 LINK ND2 ASN C 392 C1 NAG C 631 1555 1555 1.43 LINK ND2 ASN c 133 C1 NAG c 601 1555 1555 1.45 LINK ND2 ASN c 137 C1 NAG c 603 1555 1555 1.44 LINK ND2 ASN c 156 C1 NAG c 607 1555 1555 1.44 LINK ND2 ASN c 160 C1 NAG c 609 1555 1555 1.45 LINK ND2 ASN c 197 C1 NAG c 611 1555 1555 1.44 LINK ND2 ASN c 234 C1 NAG c 612 1555 1555 1.45 LINK ND2 ASN c 262 C1 NAG c 614 1555 1555 1.43 LINK ND2 ASN c 276 C1 NAG c 643 1555 1555 1.44 LINK ND2 ASN c 295 C1 NAG c 619 1555 1555 1.42 LINK ND2 ASN c 301 C1 NAG c 621 1555 1555 1.44 LINK ND2 ASN c 332 C1 NAG c 632 1555 1555 1.42 LINK ND2 ASN c 355 C1 NAG c 623 1555 1555 1.44 LINK ND2 ASN c 363 C1 NAG c 624 1555 1555 1.43 LINK ND2 ASN c 386 C1 NAG c 627 1555 1555 1.44 LINK ND2 ASN c 392 C1 NAG c 631 1555 1555 1.42 LINK O4 NAG 2 601 C1 NAG 2 602 1555 1555 1.45 LINK O4 NAG 2 603 C1 NAG 2 604 1555 1555 1.43 LINK O4 NAG 2 604 C1 BMA 2 605 1555 1555 1.45 LINK O3 BMA 2 605 C1 MAN 2 606 1555 1555 1.44 LINK O4 NAG 2 607 C1 NAG 2 608 1555 1555 1.45 LINK O4 NAG 2 609 C1 NAG 2 610 1555 1555 1.44 LINK O4 NAG 2 612 C1 NAG 2 613 1555 1555 1.44 LINK O4 NAG 2 614 C1 NAG 2 615 1555 1555 1.44 LINK O4 NAG 2 615 C1 BMA 2 616 1555 1555 1.44 LINK O3 BMA 2 616 C1 MAN 2 617 1555 1555 1.44 LINK O6 BMA 2 616 C1 MAN 2 618 1555 1555 1.44 LINK O4 NAG 2 619 C1 NAG 2 620 1555 1555 1.44 LINK O4 NAG 2 621 C1 NAG 2 622 1555 1555 1.45 LINK O4 NAG 2 624 C1 NAG 2 625 1555 1555 1.45 LINK O4 NAG 2 625 C1 BMA 2 626 1555 1555 1.45 LINK O4 NAG 2 627 C1 NAG 2 628 1555 1555 1.44 LINK O4 NAG 2 628 C1 BMA 2 629 1555 1555 1.44 LINK O3 BMA 2 629 C1 MAN 2 630 1555 1555 1.44 LINK O4 NAG 2 632 C1 NAG 2 633 1555 1555 1.44 LINK O4 NAG 2 633 C1 BMA 2 634 1555 1555 1.44 LINK O3 BMA 2 634 C1 MAN 2 635 1555 1555 1.45 LINK O6 BMA 2 634 C1 MAN 2 636 1555 1555 1.44 LINK O2 MAN 2 635 C1 MAN 2 637 1555 1555 1.45 LINK O3 MAN 2 636 C1 MAN 2 638 1555 1555 1.44 LINK O6 MAN 2 636 C1 MAN 2 639 1555 1555 1.44 LINK O2 MAN 2 637 C1 MAN 2 640 1555 1555 1.43 LINK O4 NAG 2 641 C1 NAG 2 642 1555 1555 1.44 LINK O4 NAG 2 643 C1 NAG 2 644 1555 1555 1.44 LINK O4 NAG 2 644 C1 BMA 2 645 1555 1555 1.44 LINK O3 BMA 2 645 C1 MAN 2 646 1555 1555 1.45 LINK O4 NAG C 601 C1 NAG C 602 1555 1555 1.45 LINK O4 NAG C 603 C1 NAG C 604 1555 1555 1.43 LINK O4 NAG C 604 C1 BMA C 605 1555 1555 1.44 LINK O3 BMA C 605 C1 MAN C 606 1555 1555 1.44 LINK O4 NAG C 607 C1 NAG C 608 1555 1555 1.45 LINK O4 NAG C 609 C1 NAG C 610 1555 1555 1.43 LINK O4 NAG C 612 C1 NAG C 613 1555 1555 1.44 LINK O4 NAG C 614 C1 NAG C 615 1555 1555 1.44 LINK O4 NAG C 615 C1 BMA C 616 1555 1555 1.44 LINK O3 BMA C 616 C1 MAN C 617 1555 1555 1.44 LINK O6 BMA C 616 C1 MAN C 618 1555 1555 1.44 LINK O4 NAG C 619 C1 NAG C 620 1555 1555 1.44 LINK O4 NAG C 621 C1 NAG C 622 1555 1555 1.45 LINK O4 NAG C 624 C1 NAG C 625 1555 1555 1.45 LINK O4 NAG C 625 C1 BMA C 626 1555 1555 1.46 LINK O4 NAG C 627 C1 NAG C 628 1555 1555 1.44 LINK O4 NAG C 628 C1 BMA C 629 1555 1555 1.44 LINK O3 BMA C 629 C1 MAN C 630 1555 1555 1.44 LINK O4 NAG C 632 C1 NAG C 633 1555 1555 1.44 LINK O4 NAG C 633 C1 BMA C 634 1555 1555 1.43 LINK O3 BMA C 634 C1 MAN C 635 1555 1555 1.45 LINK O6 BMA C 634 C1 MAN C 636 1555 1555 1.44 LINK O2 MAN C 635 C1 MAN C 637 1555 1555 1.44 LINK O3 MAN C 636 C1 MAN C 638 1555 1555 1.44 LINK O6 MAN C 636 C1 MAN C 639 1555 1555 1.44 LINK O2 MAN C 637 C1 MAN C 640 1555 1555 1.43 LINK O4 NAG C 641 C1 NAG C 642 1555 1555 1.44 LINK O4 NAG C 643 C1 NAG C 644 1555 1555 1.44 LINK O4 NAG C 644 C1 BMA C 645 1555 1555 1.44 LINK O3 BMA C 645 C1 MAN C 646 1555 1555 1.44 LINK O4 NAG c 601 C1 NAG c 602 1555 1555 1.45 LINK O4 NAG c 603 C1 NAG c 604 1555 1555 1.43 LINK O4 NAG c 604 C1 BMA c 605 1555 1555 1.45 LINK O3 BMA c 605 C1 MAN c 606 1555 1555 1.44 LINK O4 NAG c 607 C1 NAG c 608 1555 1555 1.45 LINK O4 NAG c 609 C1 NAG c 610 1555 1555 1.44 LINK O4 NAG c 612 C1 NAG c 613 1555 1555 1.44 LINK O4 NAG c 614 C1 NAG c 615 1555 1555 1.44 LINK O4 NAG c 615 C1 BMA c 616 1555 1555 1.44 LINK O3 BMA c 616 C1 MAN c 617 1555 1555 1.44 LINK O6 BMA c 616 C1 MAN c 618 1555 1555 1.44 LINK O4 NAG c 619 C1 NAG c 620 1555 1555 1.44 LINK O4 NAG c 621 C1 NAG c 622 1555 1555 1.45 LINK O4 NAG c 624 C1 NAG c 625 1555 1555 1.45 LINK O4 NAG c 625 C1 BMA c 626 1555 1555 1.45 LINK O4 NAG c 627 C1 NAG c 628 1555 1555 1.43 LINK O4 NAG c 628 C1 BMA c 629 1555 1555 1.44 LINK O3 BMA c 629 C1 MAN c 630 1555 1555 1.44 LINK O4 NAG c 632 C1 NAG c 633 1555 1555 1.44 LINK O4 NAG c 633 C1 BMA c 634 1555 1555 1.43 LINK O3 BMA c 634 C1 MAN c 635 1555 1555 1.45 LINK O6 BMA c 634 C1 MAN c 636 1555 1555 1.44 LINK O2 MAN c 635 C1 MAN c 637 1555 1555 1.45 LINK O3 MAN c 636 C1 MAN c 638 1555 1555 1.44 LINK O6 MAN c 636 C1 MAN c 639 1555 1555 1.44 LINK O2 MAN c 637 C1 MAN c 640 1555 1555 1.43 LINK O4 NAG c 641 C1 NAG c 642 1555 1555 1.44 LINK O4 NAG c 643 C1 NAG c 644 1555 1555 1.44 LINK O4 NAG c 644 C1 BMA c 645 1555 1555 1.44 LINK O3 BMA c 645 C1 MAN c 646 1555 1555 1.45 CISPEP 1 SER 4 7 PRO 4 8 0 -3.77 CISPEP 2 PHE 4 94 PRO 4 95 0 -1.44 CISPEP 3 SER L 7 PRO L 8 0 -3.70 CISPEP 4 PHE L 94 PRO L 95 0 -0.68 CISPEP 5 SER l 7 PRO l 8 0 -3.49 CISPEP 6 PHE l 94 PRO l 95 0 -1.66 SITE 1 AC1 4 ASN 2 133 ASP 2 140 MET 2 150 LYS 2 189 SITE 1 AC2 6 ASN 2 137 ILE 2 138 PHE m 100K THR m 100L SITE 2 AC2 6 ASP n 92 THR n 95B SITE 1 AC3 4 THR 2 135 ASN 2 156 SER 2 158 TYR 2 173 SITE 1 AC4 5 GLN 2 130 SER 2 158 ASN 2 160 LYS 2 169 SITE 2 AC4 5 LYS 2 171 SITE 1 AC5 2 ARG 2 192 ASN 2 197 SITE 1 AC6 3 ASN 2 234 SER 2 274 HIS 2 352 SITE 1 AC7 4 ASN 2 262 ASN 2 377 GLY 2 379 SER 2 447 SITE 1 AC8 8 LYS 2 97 GLU 2 275 ASN 2 276 ASN r 30 SITE 2 AC8 8 ALA r 31 ASP r 49 SER r 51 PHE r 90 SITE 1 AC9 4 GLN 2 293 ASN 2 295 VAL 2 446 NAG 2 632 SITE 1 AD1 2 ASN 2 301 ILE 2 323 SITE 1 AD2 14 HIS 2 330 ASN 2 332 SER 2 413 THR 2 415 SITE 2 AD2 14 NAG 2 619 ARG m 100 ILE m 100A GLY m 100C SITE 3 AD2 14 SER n 30 ASN n 50 ASN n 51 ASN n 52 SITE 4 AD2 14 PRO n 66 GLY n 67 SITE 1 AD3 1 ASN 2 355 SITE 1 AD4 5 ASN 2 363 SER 2 364 SER 2 388 NAG 2 627 SITE 2 AD4 5 NAG 2 628 SITE 1 AD5 5 ASN 2 386 SER 2 388 NAG 2 624 NAG 2 625 SITE 2 AD5 5 NAG 2 631 SITE 1 AD6 3 ASN 2 392 NAG 2 627 NAG 2 628 SITE 1 AD7 4 ASN C 133 ASP C 140 MET C 150 LYS C 189 SITE 1 AD8 6 PHE 5 100K THR 5 100L ASP 6 92 THR 6 95B SITE 2 AD8 6 ASN C 137 ILE C 138 SITE 1 AD9 4 THR C 135 ASN C 156 SER C 158 TYR C 173 SITE 1 AE1 6 GLN C 130 SER C 158 PHE C 159 ASN C 160 SITE 2 AE1 6 LYS C 169 LYS C 171 SITE 1 AE2 2 ARG C 192 ASN C 197 SITE 1 AE3 3 ASN C 234 SER C 274 HIS C 352 SITE 1 AE4 4 ASN C 262 ASN C 377 GLY C 379 SER C 447 SITE 1 AE5 8 ASN 7 30 ALA 7 31 ASP 7 49 SER 7 51 SITE 2 AE5 8 PHE 7 90 LYS C 97 GLU C 275 ASN C 276 SITE 1 AE6 4 GLN C 293 ASN C 295 VAL C 446 NAG C 632 SITE 1 AE7 2 ASN C 301 ILE C 323 SITE 1 AE8 14 ARG 5 100 ILE 5 100A GLY 5 100C SER 6 30 SITE 2 AE8 14 ASN 6 50 ASN 6 51 ASN 6 52 PRO 6 66 SITE 3 AE8 14 GLY 6 67 ARG C 327 HIS C 330 ASN C 332 SITE 4 AE8 14 SER C 413 NAG C 619 SITE 1 AE9 1 ASN C 355 SITE 1 AF1 5 ASN C 363 SER C 364 SER C 388 NAG C 627 SITE 2 AF1 5 NAG C 628 SITE 1 AF2 5 ASN C 386 SER C 388 NAG C 624 NAG C 625 SITE 2 AF2 5 NAG C 631 SITE 1 AF3 3 ASN C 392 NAG C 627 NAG C 628 SITE 1 AF4 4 ASN c 133 ASP c 140 MET c 150 LYS c 189 SITE 1 AF5 6 PHE M 100K THR M 100L ASP N 92 THR N 95B SITE 2 AF5 6 ASN c 137 ILE c 138 SITE 1 AF6 4 THR c 135 ASN c 156 SER c 158 TYR c 173 SITE 1 AF7 5 GLN c 130 SER c 158 ASN c 160 LYS c 169 SITE 2 AF7 5 LYS c 171 SITE 1 AF8 2 ARG c 192 ASN c 197 SITE 1 AF9 2 ASN c 234 HIS c 352 SITE 1 AG1 5 ASN c 262 ASN c 377 GLY c 379 VAL c 446 SITE 2 AG1 5 SER c 447 SITE 1 AG2 7 ASN R 30 ALA R 31 ASP R 49 SER R 51 SITE 2 AG2 7 PHE R 90 LYS c 97 ASN c 276 SITE 1 AG3 4 GLN c 293 ASN c 295 VAL c 446 NAG c 632 SITE 1 AG4 2 ASN c 301 ILE c 323 SITE 1 AG5 14 ARG M 100 ILE M 100A GLY M 100C SER N 30 SITE 2 AG5 14 ASN N 50 ASN N 51 ASN N 52 PRO N 66 SITE 3 AG5 14 GLY N 67 HIS c 330 ASN c 332 SER c 413 SITE 4 AG5 14 THR c 415 NAG c 619 SITE 1 AG6 1 ASN c 355 SITE 1 AG7 5 ASN c 363 SER c 364 SER c 388 NAG c 627 SITE 2 AG7 5 NAG c 628 SITE 1 AG8 5 ASN c 386 SER c 388 NAG c 624 NAG c 625 SITE 2 AG8 5 NAG c 631 SITE 1 AG9 3 ASN c 392 NAG c 627 NAG c 628 SITE 1 AH1 2 PRO 2 291 ASN 2 448 SITE 1 AH2 2 PRO C 291 ASN C 448 SITE 1 AH3 2 PRO c 291 ASN c 448 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