HEADER VIRAL PROTEIN 06-OCT-18 6MPG TITLE CRYO-EM STRUCTURE AT 3.2 A RESOLUTION OF HIV-1 FUSION PEPTIDE-DIRECTED TITLE 2 ANTIBODY, A12V163-B.01, ELICITED BY VACCINATION OF RHESUS MACAQUES, TITLE 3 IN COMPLEX WITH STABILIZED HIV-1 ENV BG505 DS-SOSIP, WHICH WAS ALSO TITLE 4 BOUND TO ANTIBODIES VRC03 AND PGT122 COMPND MOL_ID: 1; COMPND 2 MOLECULE: A12V163-B.01 LIGHT CHAIN; COMPND 3 CHAIN: B, 4, Y; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 7 CHAIN: U, A, D; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ENVELOPE GLYCOPROTEIN GP120; COMPND 11 CHAIN: V, 2, C; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: A12V163-B.01 HEAVY CHAIN; COMPND 15 CHAIN: W, 3, X; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: PGT122 HEAVY CHAIN; COMPND 19 CHAIN: m, 5, M; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 6; COMPND 22 MOLECULE: PGT122 LIGHT CHAIN; COMPND 23 CHAIN: n, 6, N; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 7; COMPND 26 MOLECULE: VRC03 HEAVY CHAIN; COMPND 27 CHAIN: q, 8, Q; COMPND 28 ENGINEERED: YES; COMPND 29 MOL_ID: 8; COMPND 30 MOLECULE: VRC03 LIGHT CHAIN; COMPND 31 CHAIN: r, 7, R; COMPND 32 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 3 ORGANISM_TAXID: 9544; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 9 ORGANISM_TAXID: 11676; SOURCE 10 GENE: ENV; 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: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 16 ORGANISM_TAXID: 11676; SOURCE 17 GENE: ENV; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 21 MOL_ID: 4; SOURCE 22 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 23 ORGANISM_TAXID: 9544; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 27 MOL_ID: 5; SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 29 ORGANISM_COMMON: HUMAN; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 32 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 34 MOL_ID: 6; SOURCE 35 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 36 ORGANISM_COMMON: HUMAN; SOURCE 37 ORGANISM_TAXID: 9606; SOURCE 38 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 39 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 40 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 41 MOL_ID: 7; SOURCE 42 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 43 ORGANISM_COMMON: HUMAN; SOURCE 44 ORGANISM_TAXID: 9606; SOURCE 45 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 46 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 47 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 48 MOL_ID: 8; SOURCE 49 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 50 ORGANISM_COMMON: HUMAN; SOURCE 51 ORGANISM_TAXID: 9606; SOURCE 52 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 53 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 54 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS COMPLEX, FUSION PEPTIDE, NEUTRALIZING ANTIBODY, HIV-1 ENVELOPE, VIRAL KEYWDS 2 PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR P.ACHARYA,P.D.KWONG REVDAT 1 24-JUL-19 6MPG 0 JRNL AUTH R.KONG,H.DUAN,Z.SHENG,K.XU,P.ACHARYA,P.D.KWONG,J.M.MASCOLA JRNL TITL VACCINE-INDUCED DEVELOPMENTAL PATHWAYS IN RHESUS MACAQUES JRNL TITL 2 FOR NEUTRALIZING ANTIBODIES TARGETING THE HIV-1 FUSION JRNL TITL 3 PEPTIDE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : DOG PICKER, LEGINON, GCTF, 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 : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.200 REMARK 3 NUMBER OF PARTICLES : 138170 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 6MPG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-18. REMARK 100 THE DEPOSITION ID IS D_1000237353. 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 : A12V163-B.01 FAB BOUND TO HIV-1 REMARK 245 ENV BG505 DS-SOSIP-VRC03 FAB- REMARK 245 PGT122 FAB; A12V163-B.01; REMARK 245 ENVELOPE GLYCOPROTEIN GP41; REMARK 245 ENVELOPE GLYCOPROTEIN GP120; REMARK 245 PGT122; VRC03 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.25 REMARK 245 SAMPLE SUPPORT DETAILS : UNSPECIFIED REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : NULL REMARK 245 MAXIMUM DEFOCUS (NM) : NULL REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 1.75 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 24-MERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, U, V, W, m, n, q, r, 2, 3, REMARK 350 AND CHAINS: 4, 5, 6, 7, 8, A, C, D, M, REMARK 350 AND CHAINS: N, Q, R, X, Y REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ILE U 548 REMARK 465 VAL U 549 REMARK 465 GLN U 550 REMARK 465 GLN U 551 REMARK 465 GLN U 552 REMARK 465 SER U 553 REMARK 465 ASN U 554 REMARK 465 LEU U 555 REMARK 465 LEU U 556 REMARK 465 ARG U 557 REMARK 465 ALA U 558 REMARK 465 ILE U 559 REMARK 465 GLU U 560 REMARK 465 ALA U 561 REMARK 465 GLN U 562 REMARK 465 GLN U 563 REMARK 465 HIS U 564 REMARK 465 LEU U 565 REMARK 465 LEU U 566 REMARK 465 LYS U 567 REMARK 465 LEU U 568 REMARK 465 GLU V 185A REMARK 465 ASN V 185B REMARK 465 GLN V 185C REMARK 465 GLY V 185D REMARK 465 ASN V 185E REMARK 465 ARG V 185F REMARK 465 SER V 185G REMARK 465 ASN V 185H REMARK 465 ASN V 185I REMARK 465 THR V 400 REMARK 465 SER V 401 REMARK 465 VAL V 402 REMARK 465 GLN V 403 REMARK 465 GLY V 404 REMARK 465 SER V 405 REMARK 465 ASN V 406 REMARK 465 SER V 407 REMARK 465 THR V 408 REMARK 465 GLY V 409 REMARK 465 SER V 410 REMARK 465 ALA n 6 REMARK 465 PRO n 7 REMARK 465 SER q 112 REMARK 465 SER q 113 REMARK 465 ALA q 114 REMARK 465 SER q 115 REMARK 465 THR q 116 REMARK 465 LYS q 117 REMARK 465 GLY q 118 REMARK 465 PRO q 119 REMARK 465 SER q 120 REMARK 465 VAL q 121 REMARK 465 PHE q 122 REMARK 465 PRO q 123 REMARK 465 LEU q 124 REMARK 465 ALA q 125 REMARK 465 PRO q 126 REMARK 465 SER q 127 REMARK 465 SER q 128 REMARK 465 GLY q 129 REMARK 465 GLY q 130 REMARK 465 THR q 131 REMARK 465 ALA q 132 REMARK 465 ALA q 133 REMARK 465 LEU q 134 REMARK 465 GLY q 135 REMARK 465 CYS q 136 REMARK 465 LEU q 137 REMARK 465 VAL q 138 REMARK 465 LYS q 139 REMARK 465 ASP q 140 REMARK 465 TYR q 141 REMARK 465 PHE q 142 REMARK 465 PRO q 143 REMARK 465 GLU q 144 REMARK 465 PRO q 145 REMARK 465 VAL q 146 REMARK 465 THR q 147 REMARK 465 VAL q 148 REMARK 465 SER q 149 REMARK 465 TRP q 150 REMARK 465 ASN q 151 REMARK 465 SER q 152 REMARK 465 GLY q 153 REMARK 465 ALA q 154 REMARK 465 LEU q 155 REMARK 465 THR q 156 REMARK 465 SER q 157 REMARK 465 GLY q 158 REMARK 465 VAL q 159 REMARK 465 HIS q 160 REMARK 465 THR q 161 REMARK 465 PHE q 162 REMARK 465 PRO q 163 REMARK 465 ALA q 164 REMARK 465 VAL q 165 REMARK 465 LEU q 166 REMARK 465 GLN q 167 REMARK 465 SER q 168 REMARK 465 SER q 169 REMARK 465 GLY q 170 REMARK 465 LEU q 171 REMARK 465 TYR q 172 REMARK 465 SER q 173 REMARK 465 LEU q 174 REMARK 465 SER q 175 REMARK 465 SER q 176 REMARK 465 VAL q 177 REMARK 465 VAL q 178 REMARK 465 THR q 179 REMARK 465 VAL q 180 REMARK 465 PRO q 181 REMARK 465 SER q 182 REMARK 465 SER q 183 REMARK 465 SER q 184 REMARK 465 LEU q 185 REMARK 465 GLY q 186 REMARK 465 THR q 187 REMARK 465 GLN q 188 REMARK 465 THR q 189 REMARK 465 TYR q 190 REMARK 465 ILE q 191 REMARK 465 CYS q 192 REMARK 465 ASN q 193 REMARK 465 VAL q 194 REMARK 465 ASN q 195 REMARK 465 HIS q 196 REMARK 465 LYS q 197 REMARK 465 PRO q 198 REMARK 465 SER q 199 REMARK 465 ASN q 200 REMARK 465 THR q 201 REMARK 465 LYS q 202 REMARK 465 VAL q 203 REMARK 465 ASP q 204 REMARK 465 LYS q 205 REMARK 465 LYS q 206 REMARK 465 VAL q 207 REMARK 465 GLU q 208 REMARK 465 PRO q 209 REMARK 465 LYS q 210 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 ALA 6 6 REMARK 465 PRO 6 7 REMARK 465 SER 8 112 REMARK 465 SER 8 113 REMARK 465 ALA 8 114 REMARK 465 SER 8 115 REMARK 465 THR 8 116 REMARK 465 LYS 8 117 REMARK 465 GLY 8 118 REMARK 465 PRO 8 119 REMARK 465 SER 8 120 REMARK 465 VAL 8 121 REMARK 465 PHE 8 122 REMARK 465 PRO 8 123 REMARK 465 LEU 8 124 REMARK 465 ALA 8 125 REMARK 465 PRO 8 126 REMARK 465 SER 8 127 REMARK 465 SER 8 128 REMARK 465 GLY 8 129 REMARK 465 GLY 8 130 REMARK 465 THR 8 131 REMARK 465 ALA 8 132 REMARK 465 ALA 8 133 REMARK 465 LEU 8 134 REMARK 465 GLY 8 135 REMARK 465 CYS 8 136 REMARK 465 LEU 8 137 REMARK 465 VAL 8 138 REMARK 465 LYS 8 139 REMARK 465 ASP 8 140 REMARK 465 TYR 8 141 REMARK 465 PHE 8 142 REMARK 465 PRO 8 143 REMARK 465 GLU 8 144 REMARK 465 PRO 8 145 REMARK 465 VAL 8 146 REMARK 465 THR 8 147 REMARK 465 VAL 8 148 REMARK 465 SER 8 149 REMARK 465 TRP 8 150 REMARK 465 ASN 8 151 REMARK 465 SER 8 152 REMARK 465 GLY 8 153 REMARK 465 ALA 8 154 REMARK 465 LEU 8 155 REMARK 465 THR 8 156 REMARK 465 SER 8 157 REMARK 465 GLY 8 158 REMARK 465 VAL 8 159 REMARK 465 HIS 8 160 REMARK 465 THR 8 161 REMARK 465 PHE 8 162 REMARK 465 PRO 8 163 REMARK 465 ALA 8 164 REMARK 465 VAL 8 165 REMARK 465 LEU 8 166 REMARK 465 GLN 8 167 REMARK 465 SER 8 168 REMARK 465 SER 8 169 REMARK 465 GLY 8 170 REMARK 465 LEU 8 171 REMARK 465 TYR 8 172 REMARK 465 SER 8 173 REMARK 465 LEU 8 174 REMARK 465 SER 8 175 REMARK 465 SER 8 176 REMARK 465 VAL 8 177 REMARK 465 VAL 8 178 REMARK 465 THR 8 179 REMARK 465 VAL 8 180 REMARK 465 PRO 8 181 REMARK 465 SER 8 182 REMARK 465 SER 8 183 REMARK 465 SER 8 184 REMARK 465 LEU 8 185 REMARK 465 GLY 8 186 REMARK 465 THR 8 187 REMARK 465 GLN 8 188 REMARK 465 THR 8 189 REMARK 465 TYR 8 190 REMARK 465 ILE 8 191 REMARK 465 CYS 8 192 REMARK 465 ASN 8 193 REMARK 465 VAL 8 194 REMARK 465 ASN 8 195 REMARK 465 HIS 8 196 REMARK 465 LYS 8 197 REMARK 465 PRO 8 198 REMARK 465 SER 8 199 REMARK 465 ASN 8 200 REMARK 465 THR 8 201 REMARK 465 LYS 8 202 REMARK 465 VAL 8 203 REMARK 465 ASP 8 204 REMARK 465 LYS 8 205 REMARK 465 LYS 8 206 REMARK 465 VAL 8 207 REMARK 465 GLU 8 208 REMARK 465 PRO 8 209 REMARK 465 LYS 8 210 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 ALA N 6 REMARK 465 PRO N 7 REMARK 465 SER Q 112 REMARK 465 SER Q 113 REMARK 465 ALA Q 114 REMARK 465 SER Q 115 REMARK 465 THR Q 116 REMARK 465 LYS Q 117 REMARK 465 GLY Q 118 REMARK 465 PRO Q 119 REMARK 465 SER Q 120 REMARK 465 VAL Q 121 REMARK 465 PHE Q 122 REMARK 465 PRO Q 123 REMARK 465 LEU Q 124 REMARK 465 ALA Q 125 REMARK 465 PRO Q 126 REMARK 465 SER Q 127 REMARK 465 SER Q 128 REMARK 465 GLY Q 129 REMARK 465 GLY Q 130 REMARK 465 THR Q 131 REMARK 465 ALA Q 132 REMARK 465 ALA Q 133 REMARK 465 LEU Q 134 REMARK 465 GLY Q 135 REMARK 465 CYS Q 136 REMARK 465 LEU Q 137 REMARK 465 VAL Q 138 REMARK 465 LYS Q 139 REMARK 465 ASP Q 140 REMARK 465 TYR Q 141 REMARK 465 PHE Q 142 REMARK 465 PRO Q 143 REMARK 465 GLU Q 144 REMARK 465 PRO Q 145 REMARK 465 VAL Q 146 REMARK 465 THR Q 147 REMARK 465 VAL Q 148 REMARK 465 SER Q 149 REMARK 465 TRP Q 150 REMARK 465 ASN Q 151 REMARK 465 SER Q 152 REMARK 465 GLY Q 153 REMARK 465 ALA Q 154 REMARK 465 LEU Q 155 REMARK 465 THR Q 156 REMARK 465 SER Q 157 REMARK 465 GLY Q 158 REMARK 465 VAL Q 159 REMARK 465 HIS Q 160 REMARK 465 THR Q 161 REMARK 465 PHE Q 162 REMARK 465 PRO Q 163 REMARK 465 ALA Q 164 REMARK 465 VAL Q 165 REMARK 465 LEU Q 166 REMARK 465 GLN Q 167 REMARK 465 SER Q 168 REMARK 465 SER Q 169 REMARK 465 GLY Q 170 REMARK 465 LEU Q 171 REMARK 465 TYR Q 172 REMARK 465 SER Q 173 REMARK 465 LEU Q 174 REMARK 465 SER Q 175 REMARK 465 SER Q 176 REMARK 465 VAL Q 177 REMARK 465 VAL Q 178 REMARK 465 THR Q 179 REMARK 465 VAL Q 180 REMARK 465 PRO Q 181 REMARK 465 SER Q 182 REMARK 465 SER Q 183 REMARK 465 SER Q 184 REMARK 465 LEU Q 185 REMARK 465 GLY Q 186 REMARK 465 THR Q 187 REMARK 465 GLN Q 188 REMARK 465 THR Q 189 REMARK 465 TYR Q 190 REMARK 465 ILE Q 191 REMARK 465 CYS Q 192 REMARK 465 ASN Q 193 REMARK 465 VAL Q 194 REMARK 465 ASN Q 195 REMARK 465 HIS Q 196 REMARK 465 LYS Q 197 REMARK 465 PRO Q 198 REMARK 465 SER Q 199 REMARK 465 ASN Q 200 REMARK 465 THR Q 201 REMARK 465 LYS Q 202 REMARK 465 VAL Q 203 REMARK 465 ASP Q 204 REMARK 465 LYS Q 205 REMARK 465 LYS Q 206 REMARK 465 VAL Q 207 REMARK 465 GLU Q 208 REMARK 465 PRO Q 209 REMARK 465 LYS Q 210 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OD2 ASP C 113 NH2 ARG C 429 2.19 REMARK 500 OD2 ASP V 113 NH2 ARG V 429 2.19 REMARK 500 OD2 ASP 2 113 NH2 ARG 2 429 2.19 REMARK 500 NH2 ARG 8 66 OD2 ASP 8 86 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ALA B 57 -3.67 62.16 REMARK 500 TRP U 596 -167.50 -101.06 REMARK 500 LEU U 602 -13.52 72.41 REMARK 500 GLN U 640 -9.67 76.25 REMARK 500 ASN V 80 76.48 52.40 REMARK 500 MET V 100 0.73 59.59 REMARK 500 LEU V 122 53.61 -93.00 REMARK 500 THR V 198 -31.17 -131.55 REMARK 500 GLU V 370 36.42 -94.55 REMARK 500 PHE V 391 79.24 -100.02 REMARK 500 ASN V 392 41.80 -142.18 REMARK 500 SER V 397 34.13 -92.20 REMARK 500 PRO V 493 -167.84 -74.25 REMARK 500 LEU V 494 64.25 63.14 REMARK 500 ALA W 91 -168.89 -161.66 REMARK 500 SER m 54 62.75 62.28 REMARK 500 LEU m 63 -69.02 -98.02 REMARK 500 LYS m 64 -8.94 62.78 REMARK 500 SER m 65 -14.56 -141.55 REMARK 500 ASN n 50 -165.94 -125.95 REMARK 500 ASN n 52 44.98 -140.20 REMARK 500 PRO q 100E 87.23 -68.69 REMARK 500 LEU r 46 -60.40 -93.76 REMARK 500 THR r 50 -15.61 71.91 REMARK 500 PHE r 90 -63.84 -28.38 REMARK 500 ASN 2 80 76.53 52.39 REMARK 500 MET 2 100 0.69 59.61 REMARK 500 LEU 2 122 53.60 -93.06 REMARK 500 THR 2 198 -31.20 -131.54 REMARK 500 GLU 2 370 36.36 -94.55 REMARK 500 PHE 2 391 79.36 -100.07 REMARK 500 ASN 2 392 41.85 -142.28 REMARK 500 SER 2 397 34.06 -92.23 REMARK 500 PRO 2 493 -167.79 -74.28 REMARK 500 LEU 2 494 64.26 63.14 REMARK 500 ALA 3 91 -168.83 -161.60 REMARK 500 ALA 4 57 -3.61 62.10 REMARK 500 SER 5 54 62.66 62.34 REMARK 500 LEU 5 63 -69.02 -97.96 REMARK 500 LYS 5 64 -9.08 62.93 REMARK 500 SER 5 65 -14.55 -141.53 REMARK 500 ASN 6 50 -165.95 -125.96 REMARK 500 ASN 6 52 44.93 -140.16 REMARK 500 LEU 7 46 -60.45 -93.71 REMARK 500 THR 7 50 -15.60 71.92 REMARK 500 PHE 7 90 -63.83 -28.33 REMARK 500 SER 8 97 32.40 -99.99 REMARK 500 PRO 8 100E 87.18 -68.63 REMARK 500 TRP A 596 -167.52 -101.05 REMARK 500 LEU A 602 -13.54 72.47 REMARK 500 REMARK 500 THIS ENTRY HAS 76 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 GLN r 89 PHE r 90 -128.61 REMARK 500 GLN 7 89 PHE 7 90 -128.64 REMARK 500 GLN R 89 PHE R 90 -128.64 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 W 601 REMARK 610 NAG 3 601 REMARK 610 NAG X 601 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 2 REMARK 800 641 through NAG 2 642 bound to ASN 2 448 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 701 bound REMARK 800 to ASN A 637 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 800 601 through NAG C 602 bound to ASN C 133 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 800 603 through MAN C 606 bound to ASN C 137 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 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: AE3 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: AE4 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: AE5 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: AE6 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: AE7 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: AE8 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: AE9 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: AF1 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: AF2 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: AF3 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: AF4 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: AF5 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: AF6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 641 through NAG C 642 bound to ASN C 448 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 701 bound REMARK 800 to ASN D 637 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG U 701 bound REMARK 800 to ASN U 637 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG V REMARK 800 601 through NAG V 602 bound to ASN V 133 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG V REMARK 800 603 through MAN V 606 bound to ASN V 137 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG V REMARK 800 607 through NAG V 608 bound to ASN V 156 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG V REMARK 800 609 through NAG V 610 bound to ASN V 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG V 611 bound REMARK 800 to ASN V 197 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG V REMARK 800 612 through NAG V 613 bound to ASN V 234 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG V REMARK 800 614 through MAN V 618 bound to ASN V 262 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG V REMARK 800 643 through MAN V 646 bound to ASN V 276 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG V REMARK 800 619 through NAG V 620 bound to ASN V 295 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG V REMARK 800 621 through NAG V 622 bound to ASN V 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG V REMARK 800 632 through MAN V 640 bound to ASN V 332 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG V 623 bound REMARK 800 to ASN V 355 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG V REMARK 800 624 through BMA V 626 bound to ASN V 363 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG V REMARK 800 627 through MAN V 630 bound to ASN V 386 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG V 631 bound REMARK 800 to ASN V 392 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG V REMARK 800 641 through NAG V 642 bound to ASN V 448 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 3 REMARK 800 601 through BMA 3 603 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG W REMARK 800 601 through BMA W 603 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG X REMARK 800 601 through BMA X 603 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-8977 RELATED DB: EMDB DBREF 6MPG B 1 113 PDB 6MPG 6MPG 1 113 DBREF 6MPG U 512 664 UNP Q2N0S7 Q2N0S7_9HIV1 509 661 DBREF 6MPG V 31 505 UNP Q2N0S6 Q2N0S6_9HIV1 30 502 DBREF 6MPG W 1 117 PDB 6MPG 6MPG 1 117 DBREF 6MPG m 1 111 PDB 6MPG 6MPG 1 111 DBREF 6MPG n 6 107 PDB 6MPG 6MPG 6 107 DBREF 6MPG q 1 210 PDB 6MPG 6MPG 1 210 DBREF 6MPG r 1 102 PDB 6MPG 6MPG 1 102 DBREF 6MPG 2 31 505 UNP Q2N0S6 Q2N0S6_9HIV1 30 502 DBREF 6MPG 3 1 117 PDB 6MPG 6MPG 1 117 DBREF 6MPG 4 1 113 PDB 6MPG 6MPG 1 113 DBREF 6MPG 5 1 111 PDB 6MPG 6MPG 1 111 DBREF 6MPG 6 6 107 PDB 6MPG 6MPG 6 107 DBREF 6MPG 7 1 102 PDB 6MPG 6MPG 1 102 DBREF 6MPG 8 1 210 PDB 6MPG 6MPG 1 210 DBREF 6MPG A 512 664 UNP Q2N0S7 Q2N0S7_9HIV1 509 661 DBREF 6MPG C 31 505 UNP Q2N0S6 Q2N0S6_9HIV1 30 502 DBREF 6MPG D 512 664 UNP Q2N0S7 Q2N0S7_9HIV1 509 661 DBREF 6MPG M 1 111 PDB 6MPG 6MPG 1 111 DBREF 6MPG N 6 107 PDB 6MPG 6MPG 6 107 DBREF 6MPG Q 1 210 PDB 6MPG 6MPG 1 210 DBREF 6MPG R 1 102 PDB 6MPG 6MPG 1 102 DBREF 6MPG X 1 117 PDB 6MPG 6MPG 1 117 DBREF 6MPG Y 1 113 PDB 6MPG 6MPG 1 113 SEQADV 6MPG CYS U 605 UNP Q2N0S7 THR 602 CONFLICT SEQADV 6MPG CYS V 201 UNP Q2N0S6 ILE 200 CONFLICT SEQADV 6MPG ASN V 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 6MPG CYS V 433 UNP Q2N0S6 ALA 430 CONFLICT SEQADV 6MPG CYS V 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 6MPG CYS 2 201 UNP Q2N0S6 ILE 200 CONFLICT SEQADV 6MPG ASN 2 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 6MPG CYS 2 433 UNP Q2N0S6 ALA 430 CONFLICT SEQADV 6MPG CYS 2 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 6MPG CYS A 605 UNP Q2N0S7 THR 602 CONFLICT SEQADV 6MPG CYS C 201 UNP Q2N0S6 ILE 200 CONFLICT SEQADV 6MPG ASN C 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 6MPG CYS C 433 UNP Q2N0S6 ALA 430 CONFLICT SEQADV 6MPG CYS C 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 6MPG CYS D 605 UNP Q2N0S7 THR 602 CONFLICT SEQRES 1 B 113 ASP ILE VAL MET THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2 B 113 SER LEU GLY GLU ARG VAL THR LEU ASN CYS LYS SER SER SEQRES 3 B 113 GLN SER LEU LEU ALA SER SER ASN ASN LYS ASN TYR LEU SEQRES 4 B 113 ALA TRP TYR TYR GLN LYS PRO GLY GLN ALA PRO LYS LEU SEQRES 5 B 113 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 B 113 ASN ARG PHE SER GLY SER GLY SER GLY SER ASP PHE THR SEQRES 7 B 113 LEU THR ILE SER GLY LEU GLN ALA GLU ASP VAL ALA VAL SEQRES 8 B 113 TYR TYR CYS GLN GLN TYR TYR THR THR PRO LEU THR PHE SEQRES 9 B 113 GLY GLY GLY THR LYS VAL GLU ILE LYS SEQRES 1 U 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 U 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 U 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 U 153 GLN GLN SER ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 U 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 U 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 U 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 U 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 U 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 U 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 U 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 U 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 V 473 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 V 473 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 V 473 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 V 473 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 V 473 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 V 473 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 V 473 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 V 473 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 V 473 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 V 473 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 V 473 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 V 473 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 V 473 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 V 473 ALA CYS THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 V 473 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 V 473 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 V 473 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 V 473 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 V 473 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 V 473 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 V 473 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 V 473 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 V 473 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 V 473 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 V 473 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 V 473 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 V 473 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 V 473 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 V 473 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 V 473 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 V 473 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR SEQRES 32 V 473 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 V 473 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 V 473 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 V 473 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 V 473 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 V 473 CYS LYS ARG ARG VAL SEQRES 1 W 117 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU ALA LYS SEQRES 2 W 117 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 W 117 PHE THR PHE SER ASP TYR TYR MET ASP TRP VAL ARG GLN SEQRES 4 W 117 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ARG ILE SER SEQRES 5 W 117 ASN SER GLY ILE THR TRP TYR THR ASP SER VAL ARG GLY SEQRES 6 W 117 ARG PHE THR ILE PHE ARG ASP ASN ALA LYS ASN THR LEU SEQRES 7 W 117 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 W 117 VAL TYR TYR CYS THR LYS GLU SER ALA ALA ALA ILE GLY SEQRES 9 W 117 HIS TYR TRP GLY GLN GLY VAL LEU VAL THR VAL SER SER SEQRES 1 m 132 GLN VAL HIS LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 m 132 PRO SER GLU THR LEU SER LEU THR CYS ASN VAL SER GLY SEQRES 3 m 132 THR LEU VAL ARG ASP ASN TYR TRP SER TRP ILE ARG GLN SEQRES 4 m 132 PRO LEU GLY LYS GLN PRO GLU TRP ILE GLY TYR VAL HIS SEQRES 5 m 132 ASP SER GLY ASP THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 m 132 ARG VAL HIS LEU SER LEU ASP LYS SER LYS ASN LEU VAL SEQRES 7 m 132 SER LEU ARG LEU THR GLY VAL THR ALA ALA ASP SER ALA SEQRES 8 m 132 ILE TYR TYR CYS ALA THR THR LYS HIS GLY ARG ARG ILE SEQRES 9 m 132 TYR GLY VAL VAL ALA PHE LYS GLU TRP PHE THR TYR PHE SEQRES 10 m 132 TYR MET ASP VAL TRP GLY LYS GLY THR SER VAL THR VAL SEQRES 11 m 132 SER SER SEQRES 1 n 107 ALA PRO THR PHE VAL SER VAL ALA PRO GLY GLN THR ALA SEQRES 2 n 107 ARG ILE THR CYS GLY GLU GLU SER LEU GLY SER ARG SER SEQRES 3 n 107 VAL ILE TRP TYR GLN GLN ARG PRO GLY GLN ALA PRO SER SEQRES 4 n 107 LEU ILE ILE TYR ASN ASN ASN ASP ARG PRO SER GLY ILE SEQRES 5 n 107 PRO ASP ARG PHE SER GLY SER PRO GLY SER THR PHE GLY SEQRES 6 n 107 THR THR ALA THR LEU THR ILE THR SER VAL GLU ALA GLY SEQRES 7 n 107 ASP GLU ALA ASP TYR TYR CYS HIS ILE TRP ASP SER ARG SEQRES 8 n 107 ARG PRO THR ASN TRP VAL PHE GLY GLU GLY THR THR LEU SEQRES 9 n 107 ILE VAL LEU SEQRES 1 q 227 GLN VAL GLN LEU VAL GLN SER GLY ALA VAL ILE LYS THR SEQRES 2 q 227 PRO GLY SER SER VAL LYS ILE SER CYS ARG ALA SER GLY SEQRES 3 q 227 TYR ASN PHE ARG ASP TYR SER ILE HIS TRP VAL ARG LEU SEQRES 4 q 227 ILE PRO ASP LYS GLY PHE GLU TRP ILE GLY TRP ILE LYS SEQRES 5 q 227 PRO LEU TRP GLY ALA VAL SER TYR ALA ARG GLN LEU GLN SEQRES 6 q 227 GLY ARG VAL SER MET THR ARG GLN LEU SER GLN ASP PRO SEQRES 7 q 227 ASP ASP PRO ASP TRP GLY VAL ALA TYR MET GLU PHE SER SEQRES 8 q 227 GLY LEU THR PRO ALA ASP THR ALA GLU TYR PHE CYS VAL SEQRES 9 q 227 ARG ARG GLY SER CYS ASP TYR CYS GLY ASP PHE PRO TRP SEQRES 10 q 227 GLN TYR TRP GLY GLN GLY THR VAL VAL VAL VAL SER SER SEQRES 11 q 227 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 12 q 227 SER SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 q 227 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 q 227 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 q 227 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 q 227 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 q 227 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 q 227 LYS LYS VAL GLU PRO LYS SEQRES 1 r 102 GLU ILE VAL LEU THR GLN SER PRO GLY ILE LEU SER LEU SEQRES 2 r 102 SER PRO GLY GLU THR ALA THR LEU PHE CYS LYS ALA SER SEQRES 3 r 102 GLN GLY GLY ASN ALA MET THR TRP TYR GLN LYS ARG ARG SEQRES 4 r 102 GLY GLN VAL PRO ARG LEU LEU ILE TYR ASP THR SER ARG SEQRES 5 r 102 ARG ALA SER GLY VAL PRO ASP ARG PHE VAL GLY SER GLY SEQRES 6 r 102 SER GLY THR ASP PHE PHE LEU THR ILE ASN LYS LEU ASP SEQRES 7 r 102 ARG GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN PHE GLU SEQRES 8 r 102 PHE PHE GLY LEU GLY SER GLU LEU GLU VAL HIS SEQRES 1 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 3 117 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU ALA LYS SEQRES 2 3 117 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 3 117 PHE THR PHE SER ASP TYR TYR MET ASP TRP VAL ARG GLN SEQRES 4 3 117 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ARG ILE SER SEQRES 5 3 117 ASN SER GLY ILE THR TRP TYR THR ASP SER VAL ARG GLY SEQRES 6 3 117 ARG PHE THR ILE PHE ARG ASP ASN ALA LYS ASN THR LEU SEQRES 7 3 117 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 3 117 VAL TYR TYR CYS THR LYS GLU SER ALA ALA ALA ILE GLY SEQRES 9 3 117 HIS TYR TRP GLY GLN GLY VAL LEU VAL THR VAL SER SER SEQRES 1 4 113 ASP ILE VAL MET THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2 4 113 SER LEU GLY GLU ARG VAL THR LEU ASN CYS LYS SER SER SEQRES 3 4 113 GLN SER LEU LEU ALA SER SER ASN ASN LYS ASN TYR LEU SEQRES 4 4 113 ALA TRP TYR TYR GLN LYS PRO GLY GLN ALA PRO LYS LEU SEQRES 5 4 113 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 4 113 ASN ARG PHE SER GLY SER GLY SER GLY SER ASP PHE THR SEQRES 7 4 113 LEU THR ILE SER GLY LEU GLN ALA GLU ASP VAL ALA VAL SEQRES 8 4 113 TYR TYR CYS GLN GLN TYR TYR THR THR PRO LEU THR PHE SEQRES 9 4 113 GLY GLY GLY THR LYS VAL GLU ILE LYS 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 6 107 ALA PRO THR PHE VAL SER VAL ALA PRO GLY GLN THR ALA SEQRES 2 6 107 ARG ILE THR CYS GLY GLU GLU SER LEU GLY SER ARG SER SEQRES 3 6 107 VAL ILE TRP TYR GLN GLN ARG PRO GLY GLN ALA PRO SER SEQRES 4 6 107 LEU ILE ILE TYR ASN ASN ASN ASP ARG PRO SER GLY ILE SEQRES 5 6 107 PRO ASP ARG PHE SER GLY SER PRO GLY SER THR PHE GLY SEQRES 6 6 107 THR THR ALA THR LEU THR ILE THR SER VAL GLU ALA GLY SEQRES 7 6 107 ASP GLU ALA ASP TYR TYR CYS HIS ILE TRP ASP SER ARG SEQRES 8 6 107 ARG PRO THR ASN TRP VAL PHE GLY GLU GLY THR THR LEU SEQRES 9 6 107 ILE VAL 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 8 227 GLN VAL GLN LEU VAL GLN SER GLY ALA VAL ILE LYS THR SEQRES 2 8 227 PRO GLY SER SER VAL LYS ILE SER CYS ARG ALA SER GLY SEQRES 3 8 227 TYR ASN PHE ARG ASP TYR SER ILE HIS TRP VAL ARG LEU SEQRES 4 8 227 ILE PRO ASP LYS GLY PHE GLU TRP ILE GLY TRP ILE LYS SEQRES 5 8 227 PRO LEU TRP GLY ALA VAL SER TYR ALA ARG GLN LEU GLN SEQRES 6 8 227 GLY ARG VAL SER MET THR ARG GLN LEU SER GLN ASP PRO SEQRES 7 8 227 ASP ASP PRO ASP TRP GLY VAL ALA TYR MET GLU PHE SER SEQRES 8 8 227 GLY LEU THR PRO ALA ASP THR ALA GLU TYR PHE CYS VAL SEQRES 9 8 227 ARG ARG GLY SER CYS ASP TYR CYS GLY ASP PHE PRO TRP SEQRES 10 8 227 GLN TYR TRP GLY GLN GLY THR VAL VAL VAL VAL SER SER SEQRES 11 8 227 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 12 8 227 SER SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 8 227 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 8 227 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 8 227 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 8 227 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 8 227 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 8 227 LYS LYS VAL GLU PRO LYS 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 M 132 GLN VAL HIS LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 M 132 PRO SER GLU THR LEU SER LEU THR CYS ASN VAL SER GLY SEQRES 3 M 132 THR LEU VAL ARG ASP ASN TYR TRP SER TRP ILE ARG GLN SEQRES 4 M 132 PRO LEU GLY LYS GLN PRO GLU TRP ILE GLY TYR VAL HIS SEQRES 5 M 132 ASP SER GLY ASP THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 M 132 ARG VAL HIS LEU SER LEU ASP LYS SER LYS ASN LEU VAL SEQRES 7 M 132 SER LEU ARG LEU THR GLY VAL THR ALA ALA ASP SER ALA SEQRES 8 M 132 ILE TYR TYR CYS ALA THR THR LYS HIS GLY ARG ARG ILE SEQRES 9 M 132 TYR GLY VAL VAL ALA PHE LYS GLU TRP PHE THR TYR PHE SEQRES 10 M 132 TYR MET ASP VAL TRP GLY LYS GLY THR SER VAL THR VAL SEQRES 11 M 132 SER SER SEQRES 1 N 107 ALA PRO THR PHE VAL SER VAL ALA PRO GLY GLN THR ALA SEQRES 2 N 107 ARG ILE THR CYS GLY GLU GLU SER LEU GLY SER ARG SER SEQRES 3 N 107 VAL ILE TRP TYR GLN GLN ARG PRO GLY GLN ALA PRO SER SEQRES 4 N 107 LEU ILE ILE TYR ASN ASN ASN ASP ARG PRO SER GLY ILE SEQRES 5 N 107 PRO ASP ARG PHE SER GLY SER PRO GLY SER THR PHE GLY SEQRES 6 N 107 THR THR ALA THR LEU THR ILE THR SER VAL GLU ALA GLY SEQRES 7 N 107 ASP GLU ALA ASP TYR TYR CYS HIS ILE TRP ASP SER ARG SEQRES 8 N 107 ARG PRO THR ASN TRP VAL PHE GLY GLU GLY THR THR LEU SEQRES 9 N 107 ILE VAL LEU SEQRES 1 Q 227 GLN VAL GLN LEU VAL GLN SER GLY ALA VAL ILE LYS THR SEQRES 2 Q 227 PRO GLY SER SER VAL LYS ILE SER CYS ARG ALA SER GLY SEQRES 3 Q 227 TYR ASN PHE ARG ASP TYR SER ILE HIS TRP VAL ARG LEU SEQRES 4 Q 227 ILE PRO ASP LYS GLY PHE GLU TRP ILE GLY TRP ILE LYS SEQRES 5 Q 227 PRO LEU TRP GLY ALA VAL SER TYR ALA ARG GLN LEU GLN SEQRES 6 Q 227 GLY ARG VAL SER MET THR ARG GLN LEU SER GLN ASP PRO SEQRES 7 Q 227 ASP ASP PRO ASP TRP GLY VAL ALA TYR MET GLU PHE SER SEQRES 8 Q 227 GLY LEU THR PRO ALA ASP THR ALA GLU TYR PHE CYS VAL SEQRES 9 Q 227 ARG ARG GLY SER CYS ASP TYR CYS GLY ASP PHE PRO TRP SEQRES 10 Q 227 GLN TYR TRP GLY GLN GLY THR VAL VAL VAL VAL SER SER SEQRES 11 Q 227 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 12 Q 227 SER SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 Q 227 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 Q 227 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 Q 227 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 Q 227 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 Q 227 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 Q 227 LYS LYS VAL GLU PRO LYS SEQRES 1 R 102 GLU ILE VAL LEU THR GLN SER PRO GLY ILE LEU SER LEU SEQRES 2 R 102 SER PRO GLY GLU THR ALA THR LEU PHE CYS LYS ALA SER SEQRES 3 R 102 GLN GLY GLY ASN ALA MET THR TRP TYR GLN LYS ARG ARG SEQRES 4 R 102 GLY GLN VAL PRO ARG LEU LEU ILE TYR ASP THR SER ARG SEQRES 5 R 102 ARG ALA SER GLY VAL PRO ASP ARG PHE VAL GLY SER GLY SEQRES 6 R 102 SER GLY THR ASP PHE PHE LEU THR ILE ASN LYS LEU ASP SEQRES 7 R 102 ARG GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN PHE GLU SEQRES 8 R 102 PHE PHE GLY LEU GLY SER GLU LEU GLU VAL HIS SEQRES 1 X 117 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU ALA LYS SEQRES 2 X 117 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 X 117 PHE THR PHE SER ASP TYR TYR MET ASP TRP VAL ARG GLN SEQRES 4 X 117 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ARG ILE SER SEQRES 5 X 117 ASN SER GLY ILE THR TRP TYR THR ASP SER VAL ARG GLY SEQRES 6 X 117 ARG PHE THR ILE PHE ARG ASP ASN ALA LYS ASN THR LEU SEQRES 7 X 117 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 X 117 VAL TYR TYR CYS THR LYS GLU SER ALA ALA ALA ILE GLY SEQRES 9 X 117 HIS TYR TRP GLY GLN GLY VAL LEU VAL THR VAL SER SER SEQRES 1 Y 113 ASP ILE VAL MET THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2 Y 113 SER LEU GLY GLU ARG VAL THR LEU ASN CYS LYS SER SER SEQRES 3 Y 113 GLN SER LEU LEU ALA SER SER ASN ASN LYS ASN TYR LEU SEQRES 4 Y 113 ALA TRP TYR TYR GLN LYS PRO GLY GLN ALA PRO LYS LEU SEQRES 5 Y 113 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 Y 113 ASN ARG PHE SER GLY SER GLY SER GLY SER ASP PHE THR SEQRES 7 Y 113 LEU THR ILE SER GLY LEU GLN ALA GLU ASP VAL ALA VAL SEQRES 8 Y 113 TYR TYR CYS GLN GLN TYR TYR THR THR PRO LEU THR PHE SEQRES 9 Y 113 GLY GLY GLY THR LYS VAL GLU ILE LYS HET NAG U 701 14 HET NAG V 601 14 HET NAG V 602 14 HET NAG V 603 14 HET NAG V 604 14 HET BMA V 605 11 HET MAN V 606 11 HET NAG V 607 14 HET NAG V 608 14 HET NAG V 609 14 HET NAG V 610 14 HET NAG V 611 14 HET NAG V 612 14 HET NAG V 613 14 HET NAG V 614 14 HET NAG V 615 14 HET BMA V 616 11 HET MAN V 617 11 HET MAN V 618 11 HET NAG V 619 14 HET NAG V 620 14 HET NAG V 621 14 HET NAG V 622 14 HET NAG V 623 14 HET NAG V 624 14 HET NAG V 625 14 HET BMA V 626 11 HET NAG V 627 14 HET NAG V 628 14 HET BMA V 629 11 HET MAN V 630 11 HET NAG V 631 14 HET NAG V 632 14 HET NAG V 633 14 HET BMA V 634 11 HET MAN V 635 11 HET MAN V 636 11 HET MAN V 637 11 HET MAN V 638 11 HET MAN V 639 11 HET MAN V 640 11 HET NAG V 641 14 HET NAG V 642 14 HET NAG V 643 14 HET NAG V 644 14 HET BMA V 645 11 HET MAN V 646 11 HET NAG W 601 14 HET NAG W 602 14 HET BMA W 603 11 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 3 601 14 HET NAG 3 602 14 HET BMA 3 603 11 HET NAG A 701 14 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 D 701 14 HET NAG X 601 14 HET NAG X 602 14 HET BMA X 603 11 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 25 NAG 96(C8 H15 N O6) FORMUL 27 BMA 21(C6 H12 O6) FORMUL 27 MAN 33(C6 H12 O6) HELIX 1 AA1 LEU U 537 ASN U 543 1 7 HELIX 2 AA2 VAL U 570 ILE U 595 1 26 HELIX 3 AA3 LEU U 619 ASP U 624 1 6 HELIX 4 AA4 THR U 627 ILE U 635 1 9 HELIX 5 AA5 ILE U 641 ASP U 664 1 24 HELIX 6 AA6 ALA V 58 THR V 63 1 6 HELIX 7 AA7 MET V 100 SER V 115 1 16 HELIX 8 AA8 ASN V 195 THR V 198 5 4 HELIX 9 AA9 LYS V 335 ARG V 350 1 16 HELIX 10 AB1 ASP V 368 THR V 372 5 5 HELIX 11 AB2 ASN V 425 ARG V 429 5 5 HELIX 12 AB3 MET V 475 SER V 481 1 7 HELIX 13 AB4 ARG W 86 THR W 90 5 5 HELIX 14 AB5 THR m 83 SER m 87 5 5 HELIX 15 AB6 VAL m 100D LYS m 100H 5 5 HELIX 16 AB7 GLU n 79 GLU n 83 5 5 HELIX 17 AB8 ARG q 61 GLN q 64 5 4 HELIX 18 AB9 THR q 83 THR q 87 5 5 HELIX 19 AC1 ASP r 78 PHE r 82 5 5 HELIX 20 AC2 ALA 2 58 THR 2 63 1 6 HELIX 21 AC3 MET 2 100 SER 2 115 1 16 HELIX 22 AC4 ASN 2 195 THR 2 198 5 4 HELIX 23 AC5 LYS 2 335 ARG 2 350 1 16 HELIX 24 AC6 ASP 2 368 THR 2 372 5 5 HELIX 25 AC7 ASN 2 425 ARG 2 429 5 5 HELIX 26 AC8 MET 2 475 SER 2 481 1 7 HELIX 27 AC9 ARG 3 86 THR 3 90 5 5 HELIX 28 AD1 THR 5 83 SER 5 87 5 5 HELIX 29 AD2 VAL 5 100D LYS 5 100H 5 5 HELIX 30 AD3 GLU 6 79 GLU 6 83 5 5 HELIX 31 AD4 ASP 7 78 PHE 7 82 5 5 HELIX 32 AD5 ARG 8 61 GLN 8 64 5 4 HELIX 33 AD6 THR 8 83 THR 8 87 5 5 HELIX 34 AD7 LEU A 537 ASN A 543 1 7 HELIX 35 AD8 VAL A 570 ILE A 595 1 26 HELIX 36 AD9 LEU A 619 ASP A 624 1 6 HELIX 37 AE1 THR A 627 ILE A 635 1 9 HELIX 38 AE2 ILE A 641 ASP A 664 1 24 HELIX 39 AE3 ALA C 58 THR C 63 1 6 HELIX 40 AE4 MET C 100 SER C 115 1 16 HELIX 41 AE5 ASN C 195 THR C 198 5 4 HELIX 42 AE6 LYS C 335 ARG C 350 1 16 HELIX 43 AE7 ASP C 368 THR C 372 5 5 HELIX 44 AE8 ASN C 425 ARG C 429 5 5 HELIX 45 AE9 MET C 475 SER C 481 1 7 HELIX 46 AF1 LEU D 537 ASN D 543 1 7 HELIX 47 AF2 VAL D 570 ILE D 595 1 26 HELIX 48 AF3 LEU D 619 ASP D 624 1 6 HELIX 49 AF4 THR D 627 ILE D 635 1 9 HELIX 50 AF5 ILE D 641 ASP D 664 1 24 HELIX 51 AF6 THR M 83 SER M 87 5 5 HELIX 52 AF7 VAL M 100D LYS M 100H 5 5 HELIX 53 AF8 GLU N 79 GLU N 83 5 5 HELIX 54 AF9 ARG Q 61 GLN Q 64 5 4 HELIX 55 AG1 THR Q 83 THR Q 87 5 5 HELIX 56 AG2 ASP R 78 PHE R 82 5 5 HELIX 57 AG3 ARG X 86 THR X 90 5 5 SHEET 1 AA1 4 MET B 4 GLN B 6 0 SHEET 2 AA1 4 THR B 20 SER B 25 -1 O LYS B 24 N THR B 5 SHEET 3 AA1 4 ASP B 76 ILE B 81 -1 O PHE B 77 N CYS B 23 SHEET 4 AA1 4 PHE B 68 SER B 71 -1 N SER B 69 O THR B 80 SHEET 1 AA2 6 SER B 10 VAL B 13 0 SHEET 2 AA2 6 THR B 108 ILE B 112 1 O GLU B 111 N VAL B 13 SHEET 3 AA2 6 VAL B 91 GLN B 96 -1 N TYR B 92 O THR B 108 SHEET 4 AA2 6 LEU B 39 GLN B 44 -1 N GLN B 44 O VAL B 91 SHEET 5 AA2 6 LYS B 51 TYR B 55 -1 O LEU B 53 N TRP B 41 SHEET 6 AA2 6 THR B 59 ARG B 60 -1 O THR B 59 N TYR B 55 SHEET 1 AA3 2 LEU B 30 ALA B 31 0 SHEET 2 AA3 2 LYS B 36 ASN B 37 -1 O LYS B 36 N ALA B 31 SHEET 1 AA4 3 ILE U 603 PRO U 609 0 SHEET 2 AA4 3 TRP V 35 TYR V 39 -1 O VAL V 36 N VAL U 608 SHEET 3 AA4 3 GLY V 495 THR V 499 -1 O THR V 499 N TRP V 35 SHEET 1 AA5 5 TRP V 45 ASP V 47 0 SHEET 2 AA5 5 LYS V 487 ILE V 491 -1 O LYS V 490 N LYS V 46 SHEET 3 AA5 5 PHE V 223 CYS V 228 -1 N ALA V 224 O VAL V 489 SHEET 4 AA5 5 VAL V 242 VAL V 245 -1 O SER V 243 N LYS V 227 SHEET 5 AA5 5 GLU V 83 HIS V 85 -1 N ILE V 84 O THR V 244 SHEET 1 AA6 2 ALA V 55 ASP V 57 0 SHEET 2 AA6 2 VAL V 75 THR V 77 1 O VAL V 75 N SER V 56 SHEET 1 AA7 2 GLU V 91 ASN V 94 0 SHEET 2 AA7 2 THR V 236 CYS V 239 -1 O CYS V 239 N GLU V 91 SHEET 1 AA8 5 LYS V 169 TYR V 177 0 SHEET 2 AA8 5 LEU V 154 THR V 162 -1 N MET V 161 O GLN V 170 SHEET 3 AA8 5 LEU V 129 ASN V 133 -1 N THR V 132 O ASN V 156 SHEET 4 AA8 5 GLU V 190 LEU V 193 -1 O TYR V 191 N LEU V 129 SHEET 5 AA8 5 VAL V 181 GLN V 183 -1 N VAL V 182 O ARG V 192 SHEET 1 AA9 3 THR V 202 GLN V 203 0 SHEET 2 AA9 3 MET V 434 TYR V 435 1 O TYR V 435 N THR V 202 SHEET 3 AA9 3 ILE V 423 ILE V 424 -1 N ILE V 424 O MET V 434 SHEET 1 AB1 6 MET V 271 ARG V 273 0 SHEET 2 AB1 6 ILE V 284 ARG V 298 -1 O GLN V 287 N MET V 271 SHEET 3 AB1 6 HIS V 330 SER V 334 -1 O ASN V 332 N ASN V 295 SHEET 4 AB1 6 SER V 413 LYS V 421 -1 O LEU V 416 N CYS V 331 SHEET 5 AB1 6 PHE V 382 CYS V 385 -1 N TYR V 384 O ARG V 419 SHEET 6 AB1 6 HIS V 374 ASN V 377 -1 N HIS V 374 O CYS V 385 SHEET 1 AB2 6 MET V 271 ARG V 273 0 SHEET 2 AB2 6 ILE V 284 ARG V 298 -1 O GLN V 287 N MET V 271 SHEET 3 AB2 6 ILE V 443 ARG V 456 -1 O ILE V 449 N VAL V 292 SHEET 4 AB2 6 THR V 465 PRO V 470 -1 O ARG V 469 N THR V 455 SHEET 5 AB2 6 ILE V 358 PHE V 361 1 N ILE V 358 O GLU V 466 SHEET 6 AB2 6 SER V 393 TRP V 395 -1 O SER V 393 N PHE V 361 SHEET 1 AB3 2 ASN V 301 GLY V 312 0 SHEET 2 AB3 2 GLN V 315 ILE V 323 -1 O GLY V 321 N THR V 303 SHEET 1 AB4 4 GLN W 3 SER W 7 0 SHEET 2 AB4 4 SER W 17 SER W 25 -1 O ALA W 23 N VAL W 5 SHEET 3 AB4 4 THR W 77 ASN W 83 -1 O MET W 82 N LEU W 18 SHEET 4 AB4 4 PHE W 67 ASP W 72 -1 N THR W 68 O GLN W 81 SHEET 1 AB5 6 LEU W 11 ALA W 12 0 SHEET 2 AB5 6 VAL W 111 VAL W 115 1 O THR W 114 N ALA W 12 SHEET 3 AB5 6 ALA W 91 LYS W 97 -1 N TYR W 93 O VAL W 111 SHEET 4 AB5 6 MET W 34 GLN W 39 -1 N VAL W 37 O TYR W 94 SHEET 5 AB5 6 LEU W 45 ILE W 51 -1 O GLU W 46 N ARG W 38 SHEET 6 AB5 6 THR W 57 TYR W 59 -1 O TRP W 58 N ARG W 50 SHEET 1 AB6 4 LEU W 11 ALA W 12 0 SHEET 2 AB6 4 VAL W 111 VAL W 115 1 O THR W 114 N ALA W 12 SHEET 3 AB6 4 ALA W 91 LYS W 97 -1 N TYR W 93 O VAL W 111 SHEET 4 AB6 4 TYR W 106 TRP W 107 -1 O TYR W 106 N LYS W 97 SHEET 1 AB7 4 GLN m 5 SER m 7 0 SHEET 2 AB7 4 LEU m 18 ASN m 23 -1 O ASN m 23 N GLN m 5 SHEET 3 AB7 4 LEU m 77 LEU m 82 -1 O LEU m 80 N LEU m 20 SHEET 4 AB7 4 VAL m 67 ASP m 72 -1 N SER m 70 O SER m 79 SHEET 1 AB8 6 LEU m 11 VAL m 12 0 SHEET 2 AB8 6 THR m 105 VAL m 109 1 O THR m 108 N VAL m 12 SHEET 3 AB8 6 ALA m 88 ALA m 93 -1 N ALA m 88 O VAL m 107 SHEET 4 AB8 6 TRP m 34 GLN m 39 -1 N GLN m 39 O ILE m 89 SHEET 5 AB8 6 GLU m 46 VAL m 51 -1 O GLU m 46 N ARG m 38 SHEET 6 AB8 6 THR m 57 TYR m 59 -1 O ASN m 58 N TYR m 50 SHEET 1 AB9 2 THR m 95 HIS m 97 0 SHEET 2 AB9 2 PHE m 100N MET m 100P-1 O TYR m 100O N LYS m 96 SHEET 1 AC1 2 ARG m 100 ILE m 100A 0 SHEET 2 AC1 2 TRP m 100J PHE m 100K-1 O PHE m 100K N ARG m 100 SHEET 1 AC2 4 SER n 45 ILE n 48 0 SHEET 2 AC2 4 TRP n 35 GLN n 38 -1 N TRP n 35 O ILE n 48 SHEET 3 AC2 4 ASP n 85 TYR n 87 -1 O TYR n 87 N TYR n 36 SHEET 4 AC2 4 THR n 102 THR n 103 -1 O THR n 102 N TYR n 86 SHEET 1 AC3 2 SER n 63 GLY n 64 0 SHEET 2 AC3 2 LEU n 73 THR n 74 -1 O THR n 74 N SER n 63 SHEET 1 AC4 4 GLN q 3 GLN q 6 0 SHEET 2 AC4 4 SER q 17 SER q 25 -1 O SER q 25 N GLN q 3 SHEET 3 AC4 4 TRP q 76F SER q 82A-1 O ALA q 78 N CYS q 22 SHEET 4 AC4 4 VAL q 67 GLN q 72 -1 N SER q 68 O GLU q 81 SHEET 1 AC5 6 VAL q 10 ILE q 11 0 SHEET 2 AC5 6 THR q 107 VAL q 110 1 O VAL q 108 N VAL q 10 SHEET 3 AC5 6 ALA q 88 ARG q 95 -1 N ALA q 88 O VAL q 109 SHEET 4 AC5 6 ILE q 34 ILE q 40 -1 N HIS q 35 O VAL q 93 SHEET 5 AC5 6 GLY q 44 LYS q 52 -1 O GLU q 46 N ARG q 38 SHEET 6 AC5 6 ALA q 56 TYR q 59 -1 O SER q 58 N TRP q 50 SHEET 1 AC6 4 VAL q 10 ILE q 11 0 SHEET 2 AC6 4 THR q 107 VAL q 110 1 O VAL q 108 N VAL q 10 SHEET 3 AC6 4 ALA q 88 ARG q 95 -1 N ALA q 88 O VAL q 109 SHEET 4 AC6 4 TRP q 100F TRP q 103 -1 O TYR q 102 N ARG q 94 SHEET 1 AC7 4 LEU r 4 GLN r 6 0 SHEET 2 AC7 4 ALA r 19 ALA r 25 -1 O LYS r 24 N THR r 5 SHEET 3 AC7 4 ASP r 69 ILE r 74 -1 O LEU r 72 N LEU r 21 SHEET 4 AC7 4 PHE r 61 SER r 66 -1 N VAL r 62 O THR r 73 SHEET 1 AC8 6 LEU r 11 LEU r 13 0 SHEET 2 AC8 6 SER r 97 VAL r 101 1 O GLU r 100 N LEU r 13 SHEET 3 AC8 6 VAL r 84 GLN r 89 -1 N TYR r 85 O SER r 97 SHEET 4 AC8 6 THR r 33 LYS r 37 -1 N LYS r 37 O VAL r 84 SHEET 5 AC8 6 ARG r 44 TYR r 48 -1 O ILE r 47 N TRP r 34 SHEET 6 AC8 6 ARG r 52 ARG r 53 -1 O ARG r 52 N TYR r 48 SHEET 1 AC9 4 LEU r 11 LEU r 13 0 SHEET 2 AC9 4 SER r 97 VAL r 101 1 O GLU r 100 N LEU r 13 SHEET 3 AC9 4 VAL r 84 GLN r 89 -1 N TYR r 85 O SER r 97 SHEET 4 AC9 4 PHE r 92 PHE r 93 -1 O PHE r 92 N GLN r 89 SHEET 1 AD1 3 GLY 2 495 THR 2 499 0 SHEET 2 AD1 3 TRP 2 35 TYR 2 39 -1 N TRP 2 35 O THR 2 499 SHEET 3 AD1 3 ILE A 603 PRO A 609 -1 O VAL A 608 N VAL 2 36 SHEET 1 AD2 5 TRP 2 45 ASP 2 47 0 SHEET 2 AD2 5 LYS 2 487 ILE 2 491 -1 O LYS 2 490 N LYS 2 46 SHEET 3 AD2 5 PHE 2 223 CYS 2 228 -1 N ALA 2 224 O VAL 2 489 SHEET 4 AD2 5 VAL 2 242 VAL 2 245 -1 O SER 2 243 N LYS 2 227 SHEET 5 AD2 5 GLU 2 83 HIS 2 85 -1 N ILE 2 84 O THR 2 244 SHEET 1 AD3 2 ALA 2 55 ASP 2 57 0 SHEET 2 AD3 2 VAL 2 75 THR 2 77 1 O VAL 2 75 N SER 2 56 SHEET 1 AD4 2 GLU 2 91 ASN 2 94 0 SHEET 2 AD4 2 THR 2 236 CYS 2 239 -1 O CYS 2 239 N GLU 2 91 SHEET 1 AD5 5 LYS 2 169 TYR 2 177 0 SHEET 2 AD5 5 LEU 2 154 THR 2 162 -1 N MET 2 161 O GLN 2 170 SHEET 3 AD5 5 LEU 2 129 ASN 2 133 -1 N THR 2 132 O ASN 2 156 SHEET 4 AD5 5 GLU 2 190 LEU 2 193 -1 O TYR 2 191 N LEU 2 129 SHEET 5 AD5 5 VAL 2 181 GLN 2 183 -1 N VAL 2 182 O ARG 2 192 SHEET 1 AD6 3 THR 2 202 GLN 2 203 0 SHEET 2 AD6 3 MET 2 434 TYR 2 435 1 O TYR 2 435 N THR 2 202 SHEET 3 AD6 3 ILE 2 423 ILE 2 424 -1 N ILE 2 424 O MET 2 434 SHEET 1 AD7 6 MET 2 271 ARG 2 273 0 SHEET 2 AD7 6 ILE 2 284 ARG 2 298 -1 O GLN 2 287 N MET 2 271 SHEET 3 AD7 6 HIS 2 330 SER 2 334 -1 O ASN 2 332 N ASN 2 295 SHEET 4 AD7 6 SER 2 413 LYS 2 421 -1 O LEU 2 416 N CYS 2 331 SHEET 5 AD7 6 PHE 2 382 CYS 2 385 -1 N TYR 2 384 O ARG 2 419 SHEET 6 AD7 6 HIS 2 374 ASN 2 377 -1 N HIS 2 374 O CYS 2 385 SHEET 1 AD8 6 MET 2 271 ARG 2 273 0 SHEET 2 AD8 6 ILE 2 284 ARG 2 298 -1 O GLN 2 287 N MET 2 271 SHEET 3 AD8 6 ILE 2 443 ARG 2 456 -1 O ILE 2 449 N VAL 2 292 SHEET 4 AD8 6 THR 2 465 PRO 2 470 -1 O ARG 2 469 N THR 2 455 SHEET 5 AD8 6 ILE 2 358 PHE 2 361 1 N ILE 2 358 O GLU 2 466 SHEET 6 AD8 6 SER 2 393 TRP 2 395 -1 O SER 2 393 N PHE 2 361 SHEET 1 AD9 2 ASN 2 301 GLY 2 312 0 SHEET 2 AD9 2 GLN 2 315 ILE 2 323 -1 O GLY 2 321 N THR 2 303 SHEET 1 AE1 4 GLN 3 3 SER 3 7 0 SHEET 2 AE1 4 SER 3 17 SER 3 25 -1 O ALA 3 23 N VAL 3 5 SHEET 3 AE1 4 THR 3 77 ASN 3 83 -1 O MET 3 82 N LEU 3 18 SHEET 4 AE1 4 PHE 3 67 ASP 3 72 -1 N THR 3 68 O GLN 3 81 SHEET 1 AE2 6 LEU 3 11 ALA 3 12 0 SHEET 2 AE2 6 VAL 3 111 VAL 3 115 1 O THR 3 114 N ALA 3 12 SHEET 3 AE2 6 ALA 3 91 LYS 3 97 -1 N TYR 3 93 O VAL 3 111 SHEET 4 AE2 6 MET 3 34 GLN 3 39 -1 N VAL 3 37 O TYR 3 94 SHEET 5 AE2 6 LEU 3 45 ILE 3 51 -1 O GLU 3 46 N ARG 3 38 SHEET 6 AE2 6 THR 3 57 TYR 3 59 -1 O TRP 3 58 N ARG 3 50 SHEET 1 AE3 4 LEU 3 11 ALA 3 12 0 SHEET 2 AE3 4 VAL 3 111 VAL 3 115 1 O THR 3 114 N ALA 3 12 SHEET 3 AE3 4 ALA 3 91 LYS 3 97 -1 N TYR 3 93 O VAL 3 111 SHEET 4 AE3 4 TYR 3 106 TRP 3 107 -1 O TYR 3 106 N LYS 3 97 SHEET 1 AE4 4 MET 4 4 GLN 4 6 0 SHEET 2 AE4 4 THR 4 20 SER 4 25 -1 O LYS 4 24 N THR 4 5 SHEET 3 AE4 4 ASP 4 76 ILE 4 81 -1 O PHE 4 77 N CYS 4 23 SHEET 4 AE4 4 PHE 4 68 SER 4 71 -1 N SER 4 69 O THR 4 80 SHEET 1 AE5 6 SER 4 10 VAL 4 13 0 SHEET 2 AE5 6 THR 4 108 ILE 4 112 1 O GLU 4 111 N VAL 4 13 SHEET 3 AE5 6 VAL 4 91 GLN 4 96 -1 N TYR 4 92 O THR 4 108 SHEET 4 AE5 6 LEU 4 39 GLN 4 44 -1 N GLN 4 44 O VAL 4 91 SHEET 5 AE5 6 LYS 4 51 TYR 4 55 -1 O LEU 4 53 N TRP 4 41 SHEET 6 AE5 6 THR 4 59 ARG 4 60 -1 O THR 4 59 N TYR 4 55 SHEET 1 AE6 2 LEU 4 30 ALA 4 31 0 SHEET 2 AE6 2 LYS 4 36 ASN 4 37 -1 O LYS 4 36 N ALA 4 31 SHEET 1 AE7 4 GLN 5 5 SER 5 7 0 SHEET 2 AE7 4 LEU 5 18 ASN 5 23 -1 O ASN 5 23 N GLN 5 5 SHEET 3 AE7 4 LEU 5 77 LEU 5 82 -1 O LEU 5 80 N LEU 5 20 SHEET 4 AE7 4 VAL 5 67 ASP 5 72 -1 N SER 5 70 O SER 5 79 SHEET 1 AE8 6 LEU 5 11 VAL 5 12 0 SHEET 2 AE8 6 THR 5 105 VAL 5 109 1 O THR 5 108 N VAL 5 12 SHEET 3 AE8 6 ALA 5 88 ALA 5 93 -1 N ALA 5 88 O VAL 5 107 SHEET 4 AE8 6 TRP 5 34 GLN 5 39 -1 N GLN 5 39 O ILE 5 89 SHEET 5 AE8 6 GLU 5 46 VAL 5 51 -1 O GLU 5 46 N ARG 5 38 SHEET 6 AE8 6 THR 5 57 TYR 5 59 -1 O ASN 5 58 N TYR 5 50 SHEET 1 AE9 2 THR 5 95 HIS 5 97 0 SHEET 2 AE9 2 PHE 5 100N MET 5 100P-1 O TYR 5 100O N LYS 5 96 SHEET 1 AF1 2 ARG 5 100 ILE 5 100A 0 SHEET 2 AF1 2 TRP 5 100J PHE 5 100K-1 O PHE 5 100K N ARG 5 100 SHEET 1 AF2 4 SER 6 45 ILE 6 48 0 SHEET 2 AF2 4 TRP 6 35 GLN 6 38 -1 N TRP 6 35 O ILE 6 48 SHEET 3 AF2 4 ASP 6 85 TYR 6 87 -1 O TYR 6 87 N TYR 6 36 SHEET 4 AF2 4 THR 6 102 THR 6 103 -1 O THR 6 102 N TYR 6 86 SHEET 1 AF3 2 SER 6 63 GLY 6 64 0 SHEET 2 AF3 2 LEU 6 73 THR 6 74 -1 O THR 6 74 N SER 6 63 SHEET 1 AF4 4 LEU 7 4 GLN 7 6 0 SHEET 2 AF4 4 ALA 7 19 ALA 7 25 -1 O LYS 7 24 N THR 7 5 SHEET 3 AF4 4 ASP 7 69 ILE 7 74 -1 O LEU 7 72 N LEU 7 21 SHEET 4 AF4 4 PHE 7 61 SER 7 66 -1 N VAL 7 62 O THR 7 73 SHEET 1 AF5 6 LEU 7 11 LEU 7 13 0 SHEET 2 AF5 6 SER 7 97 VAL 7 101 1 O GLU 7 100 N LEU 7 13 SHEET 3 AF5 6 VAL 7 84 GLN 7 89 -1 N TYR 7 85 O SER 7 97 SHEET 4 AF5 6 THR 7 33 LYS 7 37 -1 N LYS 7 37 O VAL 7 84 SHEET 5 AF5 6 ARG 7 44 TYR 7 48 -1 O ILE 7 47 N TRP 7 34 SHEET 6 AF5 6 ARG 7 52 ARG 7 53 -1 O ARG 7 52 N TYR 7 48 SHEET 1 AF6 4 LEU 7 11 LEU 7 13 0 SHEET 2 AF6 4 SER 7 97 VAL 7 101 1 O GLU 7 100 N LEU 7 13 SHEET 3 AF6 4 VAL 7 84 GLN 7 89 -1 N TYR 7 85 O SER 7 97 SHEET 4 AF6 4 PHE 7 92 PHE 7 93 -1 O PHE 7 92 N GLN 7 89 SHEET 1 AF7 4 GLN 8 3 GLN 8 6 0 SHEET 2 AF7 4 SER 8 17 SER 8 25 -1 O SER 8 25 N GLN 8 3 SHEET 3 AF7 4 TRP 8 76F SER 8 82A-1 O ALA 8 78 N CYS 8 22 SHEET 4 AF7 4 VAL 8 67 GLN 8 72 -1 N SER 8 68 O GLU 8 81 SHEET 1 AF8 6 VAL 8 10 ILE 8 11 0 SHEET 2 AF8 6 THR 8 107 VAL 8 110 1 O VAL 8 108 N VAL 8 10 SHEET 3 AF8 6 ALA 8 88 ARG 8 95 -1 N ALA 8 88 O VAL 8 109 SHEET 4 AF8 6 ILE 8 34 ILE 8 40 -1 N HIS 8 35 O VAL 8 93 SHEET 5 AF8 6 GLY 8 44 LYS 8 52 -1 O GLU 8 46 N ARG 8 38 SHEET 6 AF8 6 ALA 8 56 TYR 8 59 -1 O SER 8 58 N TRP 8 50 SHEET 1 AF9 4 VAL 8 10 ILE 8 11 0 SHEET 2 AF9 4 THR 8 107 VAL 8 110 1 O VAL 8 108 N VAL 8 10 SHEET 3 AF9 4 ALA 8 88 ARG 8 95 -1 N ALA 8 88 O VAL 8 109 SHEET 4 AF9 4 TRP 8 100F TRP 8 103 -1 O TYR 8 102 N ARG 8 94 SHEET 1 AG1 3 GLY C 495 THR C 499 0 SHEET 2 AG1 3 TRP C 35 TYR C 39 -1 N TRP C 35 O THR C 499 SHEET 3 AG1 3 ILE D 603 PRO D 609 -1 O VAL D 608 N VAL C 36 SHEET 1 AG2 5 TRP C 45 ASP C 47 0 SHEET 2 AG2 5 LYS C 487 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AG2 5 PHE C 223 CYS C 228 -1 N ALA C 224 O VAL C 489 SHEET 4 AG2 5 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 AG2 5 GLU C 83 HIS C 85 -1 N ILE C 84 O THR C 244 SHEET 1 AG3 2 ALA C 55 ASP C 57 0 SHEET 2 AG3 2 VAL C 75 THR C 77 1 O VAL C 75 N SER C 56 SHEET 1 AG4 2 GLU C 91 ASN C 94 0 SHEET 2 AG4 2 THR C 236 CYS C 239 -1 O CYS C 239 N GLU C 91 SHEET 1 AG5 5 LYS C 169 TYR C 177 0 SHEET 2 AG5 5 LEU C 154 THR C 162 -1 N MET C 161 O GLN C 170 SHEET 3 AG5 5 LEU C 129 ASN C 133 -1 N THR C 132 O ASN C 156 SHEET 4 AG5 5 GLU C 190 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AG5 5 VAL C 181 GLN C 183 -1 N VAL C 182 O ARG C 192 SHEET 1 AG6 3 THR C 202 GLN C 203 0 SHEET 2 AG6 3 MET C 434 TYR C 435 1 O TYR C 435 N THR C 202 SHEET 3 AG6 3 ILE C 423 ILE C 424 -1 N ILE C 424 O MET C 434 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 HIS C 330 SER C 334 -1 O ASN C 332 N ASN C 295 SHEET 4 AG7 6 SER C 413 LYS C 421 -1 O LEU C 416 N CYS C 331 SHEET 5 AG7 6 PHE C 382 CYS C 385 -1 N TYR C 384 O ARG C 419 SHEET 6 AG7 6 HIS C 374 ASN C 377 -1 N HIS C 374 O CYS C 385 SHEET 1 AG8 6 MET C 271 ARG C 273 0 SHEET 2 AG8 6 ILE C 284 ARG C 298 -1 O GLN C 287 N MET C 271 SHEET 3 AG8 6 ILE C 443 ARG C 456 -1 O ILE C 449 N VAL C 292 SHEET 4 AG8 6 THR C 465 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 5 AG8 6 ILE C 358 PHE C 361 1 N ILE C 358 O GLU C 466 SHEET 6 AG8 6 SER C 393 TRP C 395 -1 O SER C 393 N PHE C 361 SHEET 1 AG9 2 ASN C 301 GLY C 312 0 SHEET 2 AG9 2 GLN C 315 ILE C 323 -1 O GLY C 321 N THR C 303 SHEET 1 AH1 4 GLN M 5 SER M 7 0 SHEET 2 AH1 4 LEU M 18 ASN M 23 -1 O ASN M 23 N GLN M 5 SHEET 3 AH1 4 LEU M 77 LEU M 82 -1 O LEU M 80 N LEU M 20 SHEET 4 AH1 4 VAL M 67 ASP M 72 -1 N SER M 70 O SER M 79 SHEET 1 AH2 6 LEU M 11 VAL M 12 0 SHEET 2 AH2 6 THR M 105 VAL M 109 1 O THR M 108 N VAL M 12 SHEET 3 AH2 6 ALA M 88 ALA M 93 -1 N ALA M 88 O VAL M 107 SHEET 4 AH2 6 TRP M 34 GLN M 39 -1 N GLN M 39 O ILE M 89 SHEET 5 AH2 6 GLU M 46 VAL M 51 -1 O GLU M 46 N ARG M 38 SHEET 6 AH2 6 THR M 57 TYR M 59 -1 O ASN M 58 N TYR M 50 SHEET 1 AH3 2 THR M 95 HIS M 97 0 SHEET 2 AH3 2 PHE M 100N MET M 100P-1 O TYR M 100O N LYS M 96 SHEET 1 AH4 2 ARG M 100 ILE M 100A 0 SHEET 2 AH4 2 TRP M 100J PHE M 100K-1 O PHE M 100K N ARG M 100 SHEET 1 AH5 4 SER N 45 ILE N 48 0 SHEET 2 AH5 4 TRP N 35 GLN N 38 -1 N TRP N 35 O ILE N 48 SHEET 3 AH5 4 ASP N 85 TYR N 87 -1 O TYR N 87 N TYR N 36 SHEET 4 AH5 4 THR N 102 THR N 103 -1 O THR N 102 N TYR N 86 SHEET 1 AH6 2 SER N 63 GLY N 64 0 SHEET 2 AH6 2 LEU N 73 THR N 74 -1 O THR N 74 N SER N 63 SHEET 1 AH7 4 GLN Q 3 GLN Q 6 0 SHEET 2 AH7 4 SER Q 17 SER Q 25 -1 O SER Q 25 N GLN Q 3 SHEET 3 AH7 4 TRP Q 76F SER Q 82A-1 O ALA Q 78 N CYS Q 22 SHEET 4 AH7 4 VAL Q 67 GLN Q 72 -1 N SER Q 68 O GLU Q 81 SHEET 1 AH8 6 VAL Q 10 ILE Q 11 0 SHEET 2 AH8 6 THR Q 107 VAL Q 110 1 O VAL Q 108 N VAL Q 10 SHEET 3 AH8 6 ALA Q 88 ARG Q 95 -1 N ALA Q 88 O VAL Q 109 SHEET 4 AH8 6 ILE Q 34 ILE Q 40 -1 N HIS Q 35 O VAL Q 93 SHEET 5 AH8 6 GLY Q 44 LYS Q 52 -1 O GLU Q 46 N ARG Q 38 SHEET 6 AH8 6 ALA Q 56 TYR Q 59 -1 O SER Q 58 N TRP Q 50 SHEET 1 AH9 4 VAL Q 10 ILE Q 11 0 SHEET 2 AH9 4 THR Q 107 VAL Q 110 1 O VAL Q 108 N VAL Q 10 SHEET 3 AH9 4 ALA Q 88 ARG Q 95 -1 N ALA Q 88 O VAL Q 109 SHEET 4 AH9 4 TRP Q 100F TRP Q 103 -1 O TYR Q 102 N ARG Q 94 SHEET 1 AI1 4 LEU R 4 GLN R 6 0 SHEET 2 AI1 4 ALA R 19 ALA R 25 -1 O LYS R 24 N THR R 5 SHEET 3 AI1 4 ASP R 69 ILE R 74 -1 O LEU R 72 N LEU R 21 SHEET 4 AI1 4 PHE R 61 SER R 66 -1 N VAL R 62 O THR R 73 SHEET 1 AI2 6 LEU R 11 LEU R 13 0 SHEET 2 AI2 6 SER R 97 VAL R 101 1 O GLU R 100 N LEU R 13 SHEET 3 AI2 6 VAL R 84 GLN R 89 -1 N TYR R 85 O SER R 97 SHEET 4 AI2 6 THR R 33 LYS R 37 -1 N LYS R 37 O VAL R 84 SHEET 5 AI2 6 ARG R 44 TYR R 48 -1 O ILE R 47 N TRP R 34 SHEET 6 AI2 6 ARG R 52 ARG R 53 -1 O ARG R 52 N TYR R 48 SHEET 1 AI3 4 LEU R 11 LEU R 13 0 SHEET 2 AI3 4 SER R 97 VAL R 101 1 O GLU R 100 N LEU R 13 SHEET 3 AI3 4 VAL R 84 GLN R 89 -1 N TYR R 85 O SER R 97 SHEET 4 AI3 4 PHE R 92 PHE R 93 -1 O PHE R 92 N GLN R 89 SHEET 1 AI4 4 GLN X 3 SER X 7 0 SHEET 2 AI4 4 SER X 17 SER X 25 -1 O ALA X 23 N VAL X 5 SHEET 3 AI4 4 THR X 77 ASN X 83 -1 O MET X 82 N LEU X 18 SHEET 4 AI4 4 PHE X 67 ASP X 72 -1 N THR X 68 O GLN X 81 SHEET 1 AI5 6 LEU X 11 ALA X 12 0 SHEET 2 AI5 6 VAL X 111 VAL X 115 1 O THR X 114 N ALA X 12 SHEET 3 AI5 6 ALA X 91 LYS X 97 -1 N TYR X 93 O VAL X 111 SHEET 4 AI5 6 MET X 34 GLN X 39 -1 N VAL X 37 O TYR X 94 SHEET 5 AI5 6 LEU X 45 ILE X 51 -1 O GLU X 46 N ARG X 38 SHEET 6 AI5 6 THR X 57 TYR X 59 -1 O TRP X 58 N ARG X 50 SHEET 1 AI6 4 LEU X 11 ALA X 12 0 SHEET 2 AI6 4 VAL X 111 VAL X 115 1 O THR X 114 N ALA X 12 SHEET 3 AI6 4 ALA X 91 LYS X 97 -1 N TYR X 93 O VAL X 111 SHEET 4 AI6 4 TYR X 106 TRP X 107 -1 O TYR X 106 N LYS X 97 SHEET 1 AI7 4 MET Y 4 GLN Y 6 0 SHEET 2 AI7 4 THR Y 20 SER Y 25 -1 O LYS Y 24 N THR Y 5 SHEET 3 AI7 4 ASP Y 76 ILE Y 81 -1 O PHE Y 77 N CYS Y 23 SHEET 4 AI7 4 PHE Y 68 SER Y 71 -1 N SER Y 69 O THR Y 80 SHEET 1 AI8 6 SER Y 10 VAL Y 13 0 SHEET 2 AI8 6 THR Y 108 ILE Y 112 1 O GLU Y 111 N VAL Y 13 SHEET 3 AI8 6 VAL Y 91 GLN Y 96 -1 N TYR Y 92 O THR Y 108 SHEET 4 AI8 6 LEU Y 39 GLN Y 44 -1 N GLN Y 44 O VAL Y 91 SHEET 5 AI8 6 LYS Y 51 TYR Y 55 -1 O LEU Y 53 N TRP Y 41 SHEET 6 AI8 6 THR Y 59 ARG Y 60 -1 O THR Y 59 N TYR Y 55 SHEET 1 AI9 2 LEU Y 30 ALA Y 31 0 SHEET 2 AI9 2 LYS Y 36 ASN Y 37 -1 O LYS Y 36 N ALA Y 31 SSBOND 1 CYS B 23 CYS B 94 1555 1555 2.04 SSBOND 2 CYS U 598 CYS U 604 1555 1555 2.02 SSBOND 3 CYS V 54 CYS V 74 1555 1555 2.04 SSBOND 4 CYS V 119 CYS V 205 1555 1555 2.03 SSBOND 5 CYS V 131 CYS V 157 1555 1555 2.03 SSBOND 6 CYS V 201 CYS V 433 1555 1555 2.01 SSBOND 7 CYS V 218 CYS V 247 1555 1555 2.04 SSBOND 8 CYS V 228 CYS V 239 1555 1555 2.03 SSBOND 9 CYS V 296 CYS V 331 1555 1555 2.03 SSBOND 10 CYS V 378 CYS V 445 1555 1555 2.03 SSBOND 11 CYS V 385 CYS V 418 1555 1555 2.03 SSBOND 12 CYS W 22 CYS W 95 1555 1555 2.03 SSBOND 13 CYS m 22 CYS m 92 1555 1555 2.04 SSBOND 14 CYS n 23 CYS n 88 1555 1555 2.03 SSBOND 15 CYS q 22 CYS q 92 1555 1555 2.03 SSBOND 16 CYS q 98 CYS q 100A 1555 1555 2.04 SSBOND 17 CYS r 23 CYS r 87 1555 1555 2.04 SSBOND 18 CYS 2 54 CYS 2 74 1555 1555 2.04 SSBOND 19 CYS 2 119 CYS 2 205 1555 1555 2.03 SSBOND 20 CYS 2 131 CYS 2 157 1555 1555 2.03 SSBOND 21 CYS 2 201 CYS 2 433 1555 1555 2.02 SSBOND 22 CYS 2 218 CYS 2 247 1555 1555 2.04 SSBOND 23 CYS 2 228 CYS 2 239 1555 1555 2.03 SSBOND 24 CYS 2 296 CYS 2 331 1555 1555 2.03 SSBOND 25 CYS 2 378 CYS 2 445 1555 1555 2.03 SSBOND 26 CYS 2 385 CYS 2 418 1555 1555 2.03 SSBOND 27 CYS 3 22 CYS 3 95 1555 1555 2.03 SSBOND 28 CYS 4 23 CYS 4 94 1555 1555 2.04 SSBOND 29 CYS 5 22 CYS 5 92 1555 1555 2.04 SSBOND 30 CYS 6 23 CYS 6 88 1555 1555 2.03 SSBOND 31 CYS 7 23 CYS 7 87 1555 1555 2.04 SSBOND 32 CYS 8 22 CYS 8 92 1555 1555 2.03 SSBOND 33 CYS 8 98 CYS 8 100A 1555 1555 2.04 SSBOND 34 CYS A 598 CYS A 604 1555 1555 2.02 SSBOND 35 CYS C 54 CYS C 74 1555 1555 2.04 SSBOND 36 CYS C 119 CYS C 205 1555 1555 2.03 SSBOND 37 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 38 CYS C 201 CYS C 433 1555 1555 2.01 SSBOND 39 CYS C 218 CYS C 247 1555 1555 2.04 SSBOND 40 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 41 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 42 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 43 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 44 CYS D 598 CYS D 604 1555 1555 2.02 SSBOND 45 CYS M 22 CYS M 92 1555 1555 2.04 SSBOND 46 CYS N 23 CYS N 88 1555 1555 2.03 SSBOND 47 CYS Q 22 CYS Q 92 1555 1555 2.03 SSBOND 48 CYS Q 98 CYS Q 100A 1555 1555 2.04 SSBOND 49 CYS R 23 CYS R 87 1555 1555 2.04 SSBOND 50 CYS X 22 CYS X 95 1555 1555 2.03 SSBOND 51 CYS Y 23 CYS Y 94 1555 1555 2.04 LINK ND2 ASN U 637 C1 NAG U 701 1555 1555 1.45 LINK ND2 ASN V 133 C1 NAG V 601 1555 1555 1.44 LINK ND2 ASN V 137 C1 NAG V 603 1555 1555 1.44 LINK ND2 ASN V 156 C1 NAG V 607 1555 1555 1.43 LINK ND2 ASN V 160 C1 NAG V 609 1555 1555 1.46 LINK ND2 ASN V 197 C1 NAG V 611 1555 1555 1.44 LINK ND2 ASN V 234 C1 NAG V 612 1555 1555 1.44 LINK ND2 ASN V 262 C1 NAG V 614 1555 1555 1.43 LINK ND2 ASN V 276 C1 NAG V 643 1555 1555 1.45 LINK ND2 ASN V 295 C1 NAG V 619 1555 1555 1.43 LINK ND2 ASN V 301 C1 NAG V 621 1555 1555 1.44 LINK ND2 ASN V 332 C1 NAG V 632 1555 1555 1.43 LINK ND2 ASN V 355 C1 NAG V 623 1555 1555 1.44 LINK ND2 ASN V 363 C1 NAG V 624 1555 1555 1.44 LINK ND2 ASN V 386 C1 NAG V 627 1555 1555 1.43 LINK ND2 ASN V 392 C1 NAG V 631 1555 1555 1.43 LINK ND2 ASN V 448 C1 NAG V 641 1555 1555 1.43 LINK ND2 ASN 2 133 C1 NAG 2 601 1555 1555 1.44 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 1.46 LINK ND2 ASN 2 197 C1 NAG 2 611 1555 1555 1.44 LINK ND2 ASN 2 234 C1 NAG 2 612 1555 1555 1.44 LINK ND2 ASN 2 262 C1 NAG 2 614 1555 1555 1.43 LINK ND2 ASN 2 276 C1 NAG 2 643 1555 1555 1.45 LINK ND2 ASN 2 295 C1 NAG 2 619 1555 1555 1.43 LINK ND2 ASN 2 301 C1 NAG 2 621 1555 1555 1.44 LINK ND2 ASN 2 332 C1 NAG 2 632 1555 1555 1.43 LINK ND2 ASN 2 355 C1 NAG 2 623 1555 1555 1.44 LINK ND2 ASN 2 363 C1 NAG 2 624 1555 1555 1.44 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 2 448 C1 NAG 2 641 1555 1555 1.43 LINK ND2 ASN A 637 C1 NAG A 701 1555 1555 1.45 LINK ND2 ASN C 133 C1 NAG C 601 1555 1555 1.44 LINK ND2 ASN C 137 C1 NAG C 603 1555 1555 1.44 LINK ND2 ASN C 156 C1 NAG C 607 1555 1555 1.43 LINK ND2 ASN C 160 C1 NAG C 609 1555 1555 1.46 LINK ND2 ASN C 197 C1 NAG C 611 1555 1555 1.44 LINK ND2 ASN C 234 C1 NAG C 612 1555 1555 1.44 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 1.43 LINK ND2 ASN C 355 C1 NAG C 623 1555 1555 1.44 LINK ND2 ASN C 363 C1 NAG C 624 1555 1555 1.44 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 448 C1 NAG C 641 1555 1555 1.43 LINK ND2 ASN D 637 C1 NAG D 701 1555 1555 1.45 LINK O4 NAG V 601 C1 NAG V 602 1555 1555 1.45 LINK O4 NAG V 603 C1 NAG V 604 1555 1555 1.43 LINK O4 NAG V 604 C1 BMA V 605 1555 1555 1.44 LINK O3 BMA V 605 C1 MAN V 606 1555 1555 1.44 LINK O4 NAG V 607 C1 NAG V 608 1555 1555 1.45 LINK O4 NAG V 609 C1 NAG V 610 1555 1555 1.44 LINK O4 NAG V 612 C1 NAG V 613 1555 1555 1.44 LINK O4 NAG V 614 C1 NAG V 615 1555 1555 1.44 LINK O4 NAG V 615 C1 BMA V 616 1555 1555 1.45 LINK O3 BMA V 616 C1 MAN V 617 1555 1555 1.44 LINK O6 BMA V 616 C1 MAN V 618 1555 1555 1.44 LINK O4 NAG V 619 C1 NAG V 620 1555 1555 1.44 LINK O4 NAG V 621 C1 NAG V 622 1555 1555 1.45 LINK O4 NAG V 624 C1 NAG V 625 1555 1555 1.44 LINK O4 NAG V 625 C1 BMA V 626 1555 1555 1.45 LINK O4 NAG V 627 C1 NAG V 628 1555 1555 1.43 LINK O4 NAG V 628 C1 BMA V 629 1555 1555 1.44 LINK O3 BMA V 629 C1 MAN V 630 1555 1555 1.44 LINK O4 NAG V 632 C1 NAG V 633 1555 1555 1.44 LINK O4 NAG V 633 C1 BMA V 634 1555 1555 1.43 LINK O3 BMA V 634 C1 MAN V 635 1555 1555 1.45 LINK O6 BMA V 634 C1 MAN V 636 1555 1555 1.44 LINK O2 MAN V 635 C1 MAN V 637 1555 1555 1.44 LINK O3 MAN V 636 C1 MAN V 638 1555 1555 1.44 LINK O6 MAN V 636 C1 MAN V 639 1555 1555 1.44 LINK O2 MAN V 637 C1 MAN V 640 1555 1555 1.44 LINK O4 NAG V 641 C1 NAG V 642 1555 1555 1.44 LINK O4 NAG V 643 C1 NAG V 644 1555 1555 1.43 LINK O4 NAG V 644 C1 BMA V 645 1555 1555 1.45 LINK O3 BMA V 645 C1 MAN V 646 1555 1555 1.44 LINK O4 NAG W 601 C1 NAG W 602 1555 1555 1.44 LINK O4 NAG W 602 C1 BMA W 603 1555 1555 1.44 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 1.44 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 1.45 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 1.45 LINK O4 NAG 2 621 C1 NAG 2 622 1555 1555 1.45 LINK O4 NAG 2 624 C1 NAG 2 625 1555 1555 1.44 LINK O4 NAG 2 625 C1 BMA 2 626 1555 1555 1.45 LINK O4 NAG 2 627 C1 NAG 2 628 1555 1555 1.43 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 1.43 LINK O4 NAG 2 633 C1 BMA 2 634 1555 1555 1.43 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 1.44 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 1.44 LINK O4 NAG 2 641 C1 NAG 2 642 1555 1555 1.44 LINK O4 NAG 2 643 C1 NAG 2 644 1555 1555 1.43 LINK O4 NAG 2 644 C1 BMA 2 645 1555 1555 1.45 LINK O3 BMA 2 645 C1 MAN 2 646 1555 1555 1.44 LINK O4 NAG 3 601 C1 NAG 3 602 1555 1555 1.44 LINK O4 NAG 3 602 C1 BMA 3 603 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 1.44 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 1.44 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 1.45 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 1.45 LINK O4 NAG C 621 C1 NAG C 622 1555 1555 1.45 LINK O4 NAG C 624 C1 NAG C 625 1555 1555 1.44 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 1.44 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 1.44 LINK O4 NAG C 641 C1 NAG C 642 1555 1555 1.44 LINK O4 NAG C 643 C1 NAG C 644 1555 1555 1.43 LINK O4 NAG C 644 C1 BMA C 645 1555 1555 1.45 LINK O3 BMA C 645 C1 MAN C 646 1555 1555 1.44 LINK O4 NAG X 601 C1 NAG X 602 1555 1555 1.44 LINK O4 NAG X 602 C1 BMA X 603 1555 1555 1.44 CISPEP 1 THR B 100 PRO B 101 0 -0.53 CISPEP 2 THR 4 100 PRO 4 101 0 -0.55 CISPEP 3 THR Y 100 PRO Y 101 0 -0.61 SITE 1 AC1 4 ASN 2 133 ASP 2 140 MET 2 150 LYS 2 189 SITE 1 AC2 6 ASN 2 137 PHE 5 100K THR 5 100L PHE 5 100N SITE 2 AC2 6 ASP 6 92 THR 6 95B SITE 1 AC3 4 THR 2 135 ASN 2 156 SER 2 158 TYR 2 173 SITE 1 AC4 5 SER 2 158 PHE 2 159 ASN 2 160 LYS 2 169 SITE 2 AC4 5 LYS 2 171 SITE 1 AC5 3 ARG 2 192 ASN 2 197 ARG C 308 SITE 1 AC6 5 ASN 2 234 THR 2 236 SER 2 274 ILE 2 277 SITE 2 AC6 5 HIS 2 352 SITE 1 AC7 3 ASN 2 262 VAL 2 446 SER 2 447 SITE 1 AC8 7 ASN 2 94 LYS 2 97 ASN 2 276 ALA 7 31 SITE 2 AC8 7 ASP 7 49 SER 7 51 PHE 7 90 SITE 1 AC9 3 GLN 2 293 ASN 2 295 VAL 2 446 SITE 1 AD1 2 ASN 2 301 ILE 2 323 SITE 1 AD2 15 ARG 2 327 HIS 2 330 ASN 2 332 SER 2 413 SITE 2 AD2 15 THR 2 415 ARG 5 100 ILE 5 100A GLY 5 100C SITE 3 AD2 15 VAL 5 100D SER 6 30 ASN 6 50 ASN 6 51 SITE 4 AD2 15 ASN 6 52 GLY 6 67 SER 6 67A SITE 1 AD3 1 ASN 2 355 SITE 1 AD4 5 ASN 2 363 SER 2 388 NAG 2 627 NAG 2 628 SITE 2 AD4 5 NAG 2 631 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 4 ASN 2 392 NAG 2 624 NAG 2 627 NAG 2 628 SITE 1 AD7 3 PRO 2 291 VAL 2 446 ASN 2 448 SITE 1 AD8 3 GLU A 634 ASN A 637 TYR A 638 SITE 1 AD9 4 ASN C 133 ASP C 140 MET C 150 LYS C 189 SITE 1 AE1 6 ASN C 137 PHE M 100K THR M 100L PHE M 100N SITE 2 AE1 6 ASP N 92 THR N 95B SITE 1 AE2 4 THR C 135 ASN C 156 SER C 158 TYR C 173 SITE 1 AE3 5 SER C 158 PHE C 159 ASN C 160 LYS C 169 SITE 2 AE3 5 LYS C 171 SITE 1 AE4 3 ARG C 192 ASN C 197 ARG V 308 SITE 1 AE5 5 ASN C 234 THR C 236 SER C 274 ILE C 277 SITE 2 AE5 5 HIS C 352 SITE 1 AE6 3 ASN C 262 VAL C 446 SER C 447 SITE 1 AE7 7 ASN C 94 LYS C 97 ASN C 276 ALA R 31 SITE 2 AE7 7 ASP R 49 SER R 51 PHE R 90 SITE 1 AE8 3 GLN C 293 ASN C 295 VAL C 446 SITE 1 AE9 2 ASN C 301 ILE C 323 SITE 1 AF1 15 ARG C 327 HIS C 330 ASN C 332 SER C 413 SITE 2 AF1 15 THR C 415 ARG M 100 ILE M 100A GLY M 100C SITE 3 AF1 15 VAL M 100D SER N 30 ASN N 50 ASN N 51 SITE 4 AF1 15 ASN N 52 GLY N 67 SER N 67A SITE 1 AF2 1 ASN C 355 SITE 1 AF3 5 ASN C 363 SER C 388 NAG C 627 NAG C 628 SITE 2 AF3 5 NAG C 631 SITE 1 AF4 5 ASN C 386 SER C 388 NAG C 624 NAG C 625 SITE 2 AF4 5 NAG C 631 SITE 1 AF5 4 ASN C 392 NAG C 624 NAG C 627 NAG C 628 SITE 1 AF6 3 PRO C 291 VAL C 446 ASN C 448 SITE 1 AF7 3 GLU D 634 ASN D 637 TYR D 638 SITE 1 AF8 3 GLU U 634 ASN U 637 TYR U 638 SITE 1 AF9 4 ASN V 133 ASP V 140 MET V 150 LYS V 189 SITE 1 AG1 6 ASN V 137 PHE m 100K THR m 100L PHE m 100N SITE 2 AG1 6 ASP n 92 THR n 95B SITE 1 AG2 4 THR V 135 ASN V 156 SER V 158 TYR V 173 SITE 1 AG3 5 SER V 158 PHE V 159 ASN V 160 LYS V 169 SITE 2 AG3 5 LYS V 171 SITE 1 AG4 3 ARG 2 308 ARG V 192 ASN V 197 SITE 1 AG5 5 ASN V 234 THR V 236 SER V 274 ILE V 277 SITE 2 AG5 5 HIS V 352 SITE 1 AG6 3 ASN V 262 VAL V 446 SER V 447 SITE 1 AG7 7 ASN V 94 LYS V 97 ASN V 276 ALA r 31 SITE 2 AG7 7 ASP r 49 SER r 51 PHE r 90 SITE 1 AG8 3 GLN V 293 ASN V 295 VAL V 446 SITE 1 AG9 2 ASN V 301 ILE V 323 SITE 1 AH1 15 ARG V 327 HIS V 330 ASN V 332 SER V 413 SITE 2 AH1 15 THR V 415 ARG m 100 ILE m 100A GLY m 100C SITE 3 AH1 15 VAL m 100D SER n 30 ASN n 50 ASN n 51 SITE 4 AH1 15 ASN n 52 GLY n 67 SER n 67A SITE 1 AH2 1 ASN V 355 SITE 1 AH3 5 ASN V 363 SER V 388 NAG V 627 NAG V 628 SITE 2 AH3 5 NAG V 631 SITE 1 AH4 5 ASN V 386 SER V 388 NAG V 624 NAG V 625 SITE 2 AH4 5 NAG V 631 SITE 1 AH5 4 ASN V 392 NAG V 624 NAG V 627 NAG V 628 SITE 1 AH6 3 PRO V 291 VAL V 446 ASN V 448 SITE 1 AH7 4 ASN 2 88 GLY 3 55 THR 3 57 PHE 3 70 SITE 1 AH8 8 ASN 2 88 GLY 3 55 THR 3 57 PHE 3 70 SITE 2 AH8 8 ASN V 88 GLY W 55 THR W 57 PHE W 70 SITE 1 AH9 8 ASN C 88 ASN V 88 GLY W 55 THR W 57 SITE 2 AH9 8 PHE W 70 GLY X 55 THR X 57 PHE X 70 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