HEADER VIRAL PROTEIN 17-AUG-15 5ACO TITLE CRYO-EM STRUCTURE OF PGT128 FAB IN COMPLEX WITH BG505 SOSIP. TITLE 2 664 ENV TRIMER COMPND MOL_ID: 1; COMPND 2 MOLECULE: HIV-1 ENVELOPE GLYCOPROTEIN; COMPND 3 CHAIN: A, C, D; COMPND 4 FRAGMENT: GP120, RESIDUES 30-505; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 OTHER_DETAILS: THE ENV SEQUENCE IS FROM THE CLADE A VIRUS BG505, COMPND 8 TRUNCATED AT RESIDUE 664 OF GP41, MUTATED TO HAVE THE N332 COMPND 9 GLYCOSYLATION SITE, AND CONTAINS STABILIZING SOSIP MUTATIONS.; COMPND 10 MOL_ID: 2; COMPND 11 MOLECULE: HIV-1 ENVELOPE GLYCOPROTEIN; COMPND 12 CHAIN: B, E, F; COMPND 13 FRAGMENT: GP41, RESIDUES 509-661; COMPND 14 ENGINEERED: YES; COMPND 15 MUTATION: YES; COMPND 16 OTHER_DETAILS: THE ENV SEQUENCE IS FROM THE CLADE A VIRUS BG505, COMPND 17 TRUNCATED AT RESIDUE 664 OF GP41, MUTATED TO HAVE THE N332 COMPND 18 GLYCOSYLATION SITE, AND CONTAINS STABILIZING SOSIP MUTATIONS.; COMPND 19 MOL_ID: 3; COMPND 20 MOLECULE: PGT128 FAB; COMPND 21 CHAIN: G, H, I; COMPND 22 FRAGMENT: HEAVY CHAIN OF FAB VARIABLE REGION; COMPND 23 ENGINEERED: YES; COMPND 24 OTHER_DETAILS: THE FRAGMENT ANTIGEN BINDING (FAB) OF BNAB PGT128.; COMPND 25 MOL_ID: 4; COMPND 26 MOLECULE: PGT128 FAB; COMPND 27 CHAIN: J, K, L; COMPND 28 FRAGMENT: LIGHT CHAIN OF FAB VARIABLE REGION; COMPND 29 ENGINEERED: YES; COMPND 30 OTHER_DETAILS: THE FRAGMENT ANTIGEN BINDING (FAB) OF BNAB PGT128. SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 VARIANT: BG505 SOSIP.664; SOURCE 5 GENE: ENV; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 12 ORGANISM_TAXID: 11676; SOURCE 13 VARIANT: BG505 SOSIP.664; SOURCE 14 GENE: ENV; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 19 MOL_ID: 3; SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 21 ORGANISM_COMMON: HUMAN; SOURCE 22 ORGANISM_TAXID: 9606; SOURCE 23 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 24 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 27 MOL_ID: 4; 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 EXPRESSION_SYSTEM_CELL_LINE: HEK293 KEYWDS VIRAL PROTEIN, IMMUNE SYSTEM, HIV-1, ENV, BNAB, ANTIBODY, PGT128 EXPDTA ELECTRON MICROSCOPY AUTHOR J.H.LEE,A.B.WARD REVDAT 2 21-OCT-15 5ACO 1 JRNL REVDAT 1 30-SEP-15 5ACO 0 JRNL AUTH J.H.LEE,N.DE VAL,D.LYUMKIS,A.B.WARD JRNL TITL MODEL BUILDING AND REFINEMENT OF A NATIVELY GLYCOSYLATED JRNL TITL 2 HIV-1 ENV PROTEIN BY HIGH-RESOLUTION CRYOELECTRON JRNL TITL 3 MICROSCOPY. JRNL REF STRUCTURE V. 23 1943 2015 JRNL REFN ISSN 0969-2126 JRNL PMID 26388028 JRNL DOI 10.1016/J.STR.2015.07.020 REMARK 2 REMARK 2 RESOLUTION. 4.36 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : RELION REMARK 3 RECONSTRUCTION SCHEMA : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : CRYOEM REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : GLOBAL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : 1.31 REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : 1.31 REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 4.36 REMARK 3 NUMBER OF PARTICLES : 92095 REMARK 3 CTF CORRECTION METHOD : WHOLE MICROGRAPH REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: REMARK 3 SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD-3121. REMARK 3 (DEPOSITION ID: 13671). REMARK 4 REMARK 4 5ACO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-AUG-15. REMARK 100 THE PDBE ID CODE IS EBI-64671. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : VITREOUS ICE REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : NULL REMARK 245 NAME OF SAMPLE : PGT128 FAB BOUND TO BG505 REMARK 245 SOSIP.664 ENV TRIMER REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.5 REMARK 245 SAMPLE SUPPORT DETAILS : HOLEY CARBON REMARK 245 SAMPLE VITRIFICATION DETAILS : FROZEN IN LIQUID ETHANE REMARK 245 AT 4 DEGREES C. REMARK 245 SAMPLE BUFFER : 50 MM TRIS, 150 MM NACL, REMARK 245 0.675 MM DDM REMARK 245 PH : 7.4 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : 07-OCT-14 REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 2000 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : OTHER REMARK 245 DETECTOR TYPE : DIRECT ELECTRON REMARK 245 DETECTOR REMARK 245 MINIMUM DEFOCUS (NM) : 1000 REMARK 245 MAXIMUM DEFOCUS (NM) : 3500 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : 0 REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.7 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : NULL REMARK 245 ILLUMINATION MODE : NULL REMARK 245 NOMINAL MAGNIFICATION : 22500 REMARK 245 CALIBRATED MAGNIFICATION : 22500 REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : IMAGED ON FEI TITAN REMARK 245 KRIOS 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 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I REMARK 350 AND CHAINS: J, K, L 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 ALA A 31 REMARK 465 GLU A 32 REMARK 465 LYS A 59 REMARK 465 ALA A 60 REMARK 465 TYR A 61 REMARK 465 GLU A 62 REMARK 465 THR A 63 REMARK 465 GLU A 64 REMARK 465 LYS A 65 REMARK 465 HIS A 66 REMARK 465 ASN A 67 REMARK 465 GLU A 185A REMARK 465 ASN A 185B REMARK 465 GLN A 185C REMARK 465 GLY A 185D REMARK 465 ASN A 185E REMARK 465 ARG A 185F REMARK 465 SER A 185G REMARK 465 ASN A 185H REMARK 465 ASN A 186 REMARK 465 SER A 187 REMARK 465 THR A 399 REMARK 465 SER A 400 REMARK 465 VAL A 401 REMARK 465 GLN A 402 REMARK 465 GLY A 403 REMARK 465 SER A 404 REMARK 465 ASN A 405 REMARK 465 SER A 406 REMARK 465 THR A 407 REMARK 465 GLY A 408 REMARK 465 SER A 409 REMARK 465 GLY A 458 REMARK 465 GLY A 459 REMARK 465 SER A 460 REMARK 465 VAL A 506 REMARK 465 GLY A 507 REMARK 465 ARG A 508 REMARK 465 ALA B 512 REMARK 465 VAL B 513 REMARK 465 GLY B 514 REMARK 465 ILE B 515 REMARK 465 GLY B 516 REMARK 465 ALA B 517 REMARK 465 GLN B 551 REMARK 465 GLN B 552 REMARK 465 SER B 553 REMARK 465 ASN B 554 REMARK 465 LEU B 555 REMARK 465 LEU B 556 REMARK 465 ARG B 557 REMARK 465 ALA B 558 REMARK 465 PRO B 559 REMARK 465 GLU B 560 REMARK 465 ALA B 561 REMARK 465 GLN B 562 REMARK 465 GLN B 563 REMARK 465 HIS B 564 REMARK 465 LEU B 565 REMARK 465 ALA C 31 REMARK 465 GLU C 32 REMARK 465 LYS C 59 REMARK 465 ALA C 60 REMARK 465 TYR C 61 REMARK 465 GLU C 62 REMARK 465 THR C 63 REMARK 465 GLU C 64 REMARK 465 LYS C 65 REMARK 465 HIS C 66 REMARK 465 ASN C 67 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 186 REMARK 465 SER C 187 REMARK 465 THR C 399 REMARK 465 SER C 400 REMARK 465 VAL C 401 REMARK 465 GLN C 402 REMARK 465 GLY C 403 REMARK 465 SER C 404 REMARK 465 ASN C 405 REMARK 465 SER C 406 REMARK 465 THR C 407 REMARK 465 GLY C 408 REMARK 465 SER C 409 REMARK 465 GLY C 458 REMARK 465 GLY C 459 REMARK 465 SER C 460 REMARK 465 VAL C 506 REMARK 465 GLY C 507 REMARK 465 ARG C 508 REMARK 465 ALA D 31 REMARK 465 GLU D 32 REMARK 465 LYS D 59 REMARK 465 ALA D 60 REMARK 465 TYR D 61 REMARK 465 GLU D 62 REMARK 465 THR D 63 REMARK 465 GLU D 64 REMARK 465 LYS D 65 REMARK 465 HIS D 66 REMARK 465 ASN D 67 REMARK 465 GLU D 185A REMARK 465 ASN D 185B REMARK 465 GLN D 185C REMARK 465 GLY D 185D REMARK 465 ASN D 185E REMARK 465 ARG D 185F REMARK 465 SER D 185G REMARK 465 ASN D 185H REMARK 465 ASN D 186 REMARK 465 SER D 187 REMARK 465 THR D 399 REMARK 465 SER D 400 REMARK 465 VAL D 401 REMARK 465 GLN D 402 REMARK 465 GLY D 403 REMARK 465 SER D 404 REMARK 465 ASN D 405 REMARK 465 SER D 406 REMARK 465 THR D 407 REMARK 465 GLY D 408 REMARK 465 SER D 409 REMARK 465 GLY D 458 REMARK 465 GLY D 459 REMARK 465 SER D 460 REMARK 465 VAL D 506 REMARK 465 GLY D 507 REMARK 465 ARG D 508 REMARK 465 ALA E 512 REMARK 465 VAL E 513 REMARK 465 GLY E 514 REMARK 465 ILE E 515 REMARK 465 GLY E 516 REMARK 465 ALA E 517 REMARK 465 GLN E 551 REMARK 465 GLN E 552 REMARK 465 SER E 553 REMARK 465 ASN E 554 REMARK 465 LEU E 555 REMARK 465 LEU E 556 REMARK 465 ARG E 557 REMARK 465 ALA E 558 REMARK 465 PRO E 559 REMARK 465 GLU E 560 REMARK 465 ALA E 561 REMARK 465 GLN E 562 REMARK 465 GLN E 563 REMARK 465 HIS E 564 REMARK 465 LEU E 565 REMARK 465 ALA F 512 REMARK 465 VAL F 513 REMARK 465 GLY F 514 REMARK 465 ILE F 515 REMARK 465 GLY F 516 REMARK 465 ALA F 517 REMARK 465 GLN F 551 REMARK 465 GLN F 552 REMARK 465 SER F 553 REMARK 465 ASN F 554 REMARK 465 LEU F 555 REMARK 465 LEU F 556 REMARK 465 ARG F 557 REMARK 465 ALA F 558 REMARK 465 PRO F 559 REMARK 465 GLU F 560 REMARK 465 ALA F 561 REMARK 465 GLN F 562 REMARK 465 GLN F 563 REMARK 465 HIS F 564 REMARK 465 LEU F 565 REMARK 465 GLU G 1 REMARK 465 SER G 112 REMARK 465 SER G 113 REMARK 465 ALA G 114 REMARK 465 SER G 115 REMARK 465 THR G 116 REMARK 465 LYS G 117 REMARK 465 GLY G 118 REMARK 465 PRO G 119 REMARK 465 SER G 120 REMARK 465 VAL G 121 REMARK 465 PHE G 122 REMARK 465 PRO G 123 REMARK 465 LEU G 124 REMARK 465 ALA G 125 REMARK 465 PRO G 126 REMARK 465 SER G 127 REMARK 465 SER G 128 REMARK 465 LYS G 129 REMARK 465 SER G 130 REMARK 465 THR G 131 REMARK 465 SER G 132 REMARK 465 GLY G 133 REMARK 465 GLY G 134 REMARK 465 THR G 135 REMARK 465 ALA G 136 REMARK 465 ALA G 137 REMARK 465 LEU G 138 REMARK 465 GLY G 139 REMARK 465 CYS G 140 REMARK 465 LEU G 141 REMARK 465 VAL G 142 REMARK 465 LYS G 143 REMARK 465 ASP G 144 REMARK 465 TYR G 145 REMARK 465 PHE G 146 REMARK 465 PRO G 147 REMARK 465 GLU G 148 REMARK 465 PRO G 149 REMARK 465 VAL G 150 REMARK 465 THR G 151 REMARK 465 VAL G 152 REMARK 465 SER G 153 REMARK 465 TRP G 154 REMARK 465 ASN G 155 REMARK 465 SER G 156 REMARK 465 GLY G 157 REMARK 465 ALA G 158 REMARK 465 LEU G 159 REMARK 465 THR G 160 REMARK 465 SER G 161 REMARK 465 GLY G 162 REMARK 465 VAL G 163 REMARK 465 HIS G 164 REMARK 465 THR G 165 REMARK 465 PHE G 166 REMARK 465 PRO G 167 REMARK 465 ALA G 168 REMARK 465 VAL G 169 REMARK 465 LEU G 170 REMARK 465 GLN G 171 REMARK 465 SER G 172 REMARK 465 SER G 173 REMARK 465 GLY G 174 REMARK 465 LEU G 175 REMARK 465 TYR G 176 REMARK 465 SER G 177 REMARK 465 LEU G 178 REMARK 465 SER G 179 REMARK 465 SER G 180 REMARK 465 VAL G 181 REMARK 465 VAL G 182 REMARK 465 THR G 183 REMARK 465 VAL G 184 REMARK 465 PRO G 185 REMARK 465 SER G 186 REMARK 465 SER G 187 REMARK 465 SER G 188 REMARK 465 LEU G 189 REMARK 465 GLY G 190 REMARK 465 THR G 191 REMARK 465 GLN G 192 REMARK 465 THR G 193 REMARK 465 TYR G 194 REMARK 465 ILE G 195 REMARK 465 CYS G 196 REMARK 465 ASN G 197 REMARK 465 VAL G 198 REMARK 465 ASN G 199 REMARK 465 HIS G 200 REMARK 465 LYS G 201 REMARK 465 PRO G 202 REMARK 465 SER G 203 REMARK 465 ASN G 204 REMARK 465 THR G 205 REMARK 465 LYS G 206 REMARK 465 VAL G 207 REMARK 465 ASP G 208 REMARK 465 LYS G 209 REMARK 465 ARG G 210 REMARK 465 VAL G 211 REMARK 465 GLU G 212 REMARK 465 PRO G 213 REMARK 465 LYS G 214 REMARK 465 SER G 215 REMARK 465 CYS G 216 REMARK 465 ASP G 217 REMARK 465 GLU H 1 REMARK 465 SER H 112 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 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 GLY H 134 REMARK 465 THR H 135 REMARK 465 ALA H 136 REMARK 465 ALA H 137 REMARK 465 LEU H 138 REMARK 465 GLY H 139 REMARK 465 CYS H 140 REMARK 465 LEU H 141 REMARK 465 VAL H 142 REMARK 465 LYS H 143 REMARK 465 ASP H 144 REMARK 465 TYR H 145 REMARK 465 PHE H 146 REMARK 465 PRO H 147 REMARK 465 GLU H 148 REMARK 465 PRO H 149 REMARK 465 VAL H 150 REMARK 465 THR H 151 REMARK 465 VAL H 152 REMARK 465 SER H 153 REMARK 465 TRP H 154 REMARK 465 ASN H 155 REMARK 465 SER H 156 REMARK 465 GLY H 157 REMARK 465 ALA H 158 REMARK 465 LEU H 159 REMARK 465 THR H 160 REMARK 465 SER H 161 REMARK 465 GLY H 162 REMARK 465 VAL H 163 REMARK 465 HIS H 164 REMARK 465 THR H 165 REMARK 465 PHE H 166 REMARK 465 PRO H 167 REMARK 465 ALA H 168 REMARK 465 VAL H 169 REMARK 465 LEU H 170 REMARK 465 GLN H 171 REMARK 465 SER H 172 REMARK 465 SER H 173 REMARK 465 GLY H 174 REMARK 465 LEU H 175 REMARK 465 TYR H 176 REMARK 465 SER H 177 REMARK 465 LEU H 178 REMARK 465 SER H 179 REMARK 465 SER H 180 REMARK 465 VAL H 181 REMARK 465 VAL H 182 REMARK 465 THR H 183 REMARK 465 VAL H 184 REMARK 465 PRO H 185 REMARK 465 SER H 186 REMARK 465 SER H 187 REMARK 465 SER H 188 REMARK 465 LEU H 189 REMARK 465 GLY H 190 REMARK 465 THR H 191 REMARK 465 GLN H 192 REMARK 465 THR H 193 REMARK 465 TYR H 194 REMARK 465 ILE H 195 REMARK 465 CYS H 196 REMARK 465 ASN H 197 REMARK 465 VAL H 198 REMARK 465 ASN H 199 REMARK 465 HIS H 200 REMARK 465 LYS H 201 REMARK 465 PRO H 202 REMARK 465 SER H 203 REMARK 465 ASN H 204 REMARK 465 THR H 205 REMARK 465 LYS H 206 REMARK 465 VAL H 207 REMARK 465 ASP H 208 REMARK 465 LYS H 209 REMARK 465 ARG H 210 REMARK 465 VAL H 211 REMARK 465 GLU H 212 REMARK 465 PRO H 213 REMARK 465 LYS H 214 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 GLU I 1 REMARK 465 SER I 112 REMARK 465 SER I 113 REMARK 465 ALA I 114 REMARK 465 SER I 115 REMARK 465 THR I 116 REMARK 465 LYS I 117 REMARK 465 GLY I 118 REMARK 465 PRO I 119 REMARK 465 SER I 120 REMARK 465 VAL I 121 REMARK 465 PHE I 122 REMARK 465 PRO I 123 REMARK 465 LEU I 124 REMARK 465 ALA I 125 REMARK 465 PRO I 126 REMARK 465 SER I 127 REMARK 465 SER I 128 REMARK 465 LYS I 129 REMARK 465 SER I 130 REMARK 465 THR I 131 REMARK 465 SER I 132 REMARK 465 GLY I 133 REMARK 465 GLY I 134 REMARK 465 THR I 135 REMARK 465 ALA I 136 REMARK 465 ALA I 137 REMARK 465 LEU I 138 REMARK 465 GLY I 139 REMARK 465 CYS I 140 REMARK 465 LEU I 141 REMARK 465 VAL I 142 REMARK 465 LYS I 143 REMARK 465 ASP I 144 REMARK 465 TYR I 145 REMARK 465 PHE I 146 REMARK 465 PRO I 147 REMARK 465 GLU I 148 REMARK 465 PRO I 149 REMARK 465 VAL I 150 REMARK 465 THR I 151 REMARK 465 VAL I 152 REMARK 465 SER I 153 REMARK 465 TRP I 154 REMARK 465 ASN I 155 REMARK 465 SER I 156 REMARK 465 GLY I 157 REMARK 465 ALA I 158 REMARK 465 LEU I 159 REMARK 465 THR I 160 REMARK 465 SER I 161 REMARK 465 GLY I 162 REMARK 465 VAL I 163 REMARK 465 HIS I 164 REMARK 465 THR I 165 REMARK 465 PHE I 166 REMARK 465 PRO I 167 REMARK 465 ALA I 168 REMARK 465 VAL I 169 REMARK 465 LEU I 170 REMARK 465 GLN I 171 REMARK 465 SER I 172 REMARK 465 SER I 173 REMARK 465 GLY I 174 REMARK 465 LEU I 175 REMARK 465 TYR I 176 REMARK 465 SER I 177 REMARK 465 LEU I 178 REMARK 465 SER I 179 REMARK 465 SER I 180 REMARK 465 VAL I 181 REMARK 465 VAL I 182 REMARK 465 THR I 183 REMARK 465 VAL I 184 REMARK 465 PRO I 185 REMARK 465 SER I 186 REMARK 465 SER I 187 REMARK 465 SER I 188 REMARK 465 LEU I 189 REMARK 465 GLY I 190 REMARK 465 THR I 191 REMARK 465 GLN I 192 REMARK 465 THR I 193 REMARK 465 TYR I 194 REMARK 465 ILE I 195 REMARK 465 CYS I 196 REMARK 465 ASN I 197 REMARK 465 VAL I 198 REMARK 465 ASN I 199 REMARK 465 HIS I 200 REMARK 465 LYS I 201 REMARK 465 PRO I 202 REMARK 465 SER I 203 REMARK 465 ASN I 204 REMARK 465 THR I 205 REMARK 465 LYS I 206 REMARK 465 VAL I 207 REMARK 465 ASP I 208 REMARK 465 LYS I 209 REMARK 465 ARG I 210 REMARK 465 VAL I 211 REMARK 465 GLU I 212 REMARK 465 PRO I 213 REMARK 465 LYS I 214 REMARK 465 SER I 215 REMARK 465 CYS I 216 REMARK 465 ASP I 217 REMARK 465 GLU J 1 REMARK 465 LEU J 107 REMARK 465 GLY J 108 REMARK 465 GLN J 109 REMARK 465 PRO J 110 REMARK 465 LYS J 111 REMARK 465 ALA J 112 REMARK 465 ALA J 113 REMARK 465 PRO J 114 REMARK 465 SER J 115 REMARK 465 VAL J 116 REMARK 465 THR J 117 REMARK 465 LEU J 118 REMARK 465 PHE J 119 REMARK 465 PRO J 120 REMARK 465 PRO J 121 REMARK 465 SER J 122 REMARK 465 SER J 123 REMARK 465 GLU J 124 REMARK 465 GLU J 125 REMARK 465 LEU J 126 REMARK 465 GLN J 127 REMARK 465 ALA J 128 REMARK 465 ASN J 129 REMARK 465 LYS J 130 REMARK 465 ALA J 131 REMARK 465 THR J 132 REMARK 465 LEU J 133 REMARK 465 VAL J 134 REMARK 465 CYS J 135 REMARK 465 LEU J 136 REMARK 465 ILE J 137 REMARK 465 SER J 138 REMARK 465 ASP J 139 REMARK 465 PHE J 140 REMARK 465 TYR J 141 REMARK 465 PRO J 142 REMARK 465 GLY J 143 REMARK 465 ALA J 144 REMARK 465 VAL J 145 REMARK 465 THR J 146 REMARK 465 VAL J 147 REMARK 465 ALA J 148 REMARK 465 TRP J 149 REMARK 465 LYS J 150 REMARK 465 ALA J 151 REMARK 465 ASP J 152 REMARK 465 SER J 153 REMARK 465 SER J 154 REMARK 465 PRO J 155 REMARK 465 VAL J 156 REMARK 465 LYS J 157 REMARK 465 ALA J 158 REMARK 465 GLY J 159 REMARK 465 VAL J 160 REMARK 465 GLU J 161 REMARK 465 THR J 162 REMARK 465 THR J 163 REMARK 465 THR J 164 REMARK 465 PRO J 165 REMARK 465 SER J 166 REMARK 465 LYS J 167 REMARK 465 GLN J 168 REMARK 465 SER J 169 REMARK 465 ASN J 170 REMARK 465 ASN J 171 REMARK 465 LYS J 172 REMARK 465 TYR J 173 REMARK 465 ALA J 174 REMARK 465 ALA J 175 REMARK 465 SER J 176 REMARK 465 SER J 177 REMARK 465 TYR J 178 REMARK 465 LEU J 179 REMARK 465 SER J 180 REMARK 465 LEU J 181 REMARK 465 THR J 182 REMARK 465 PRO J 183 REMARK 465 GLU J 184 REMARK 465 GLN J 185 REMARK 465 TRP J 186 REMARK 465 LYS J 187 REMARK 465 SER J 188 REMARK 465 HIS J 189 REMARK 465 ARG J 190 REMARK 465 SER J 191 REMARK 465 TYR J 192 REMARK 465 SER J 193 REMARK 465 CYS J 194 REMARK 465 GLN J 195 REMARK 465 VAL J 196 REMARK 465 THR J 197 REMARK 465 HIS J 198 REMARK 465 GLU J 199 REMARK 465 GLY J 200 REMARK 465 SER J 201 REMARK 465 THR J 202 REMARK 465 VAL J 203 REMARK 465 GLU J 204 REMARK 465 LYS J 205 REMARK 465 THR J 206 REMARK 465 VAL J 207 REMARK 465 ALA J 208 REMARK 465 PRO J 209 REMARK 465 THR J 210 REMARK 465 GLU J 211 REMARK 465 CYS J 212 REMARK 465 SER J 213 REMARK 465 GLU K 1 REMARK 465 LEU K 107 REMARK 465 GLY K 108 REMARK 465 GLN K 109 REMARK 465 PRO K 110 REMARK 465 LYS K 111 REMARK 465 ALA K 112 REMARK 465 ALA K 113 REMARK 465 PRO K 114 REMARK 465 SER K 115 REMARK 465 VAL K 116 REMARK 465 THR K 117 REMARK 465 LEU K 118 REMARK 465 PHE K 119 REMARK 465 PRO K 120 REMARK 465 PRO K 121 REMARK 465 SER K 122 REMARK 465 SER K 123 REMARK 465 GLU K 124 REMARK 465 GLU K 125 REMARK 465 LEU K 126 REMARK 465 GLN K 127 REMARK 465 ALA K 128 REMARK 465 ASN K 129 REMARK 465 LYS K 130 REMARK 465 ALA K 131 REMARK 465 THR K 132 REMARK 465 LEU K 133 REMARK 465 VAL K 134 REMARK 465 CYS K 135 REMARK 465 LEU K 136 REMARK 465 ILE K 137 REMARK 465 SER K 138 REMARK 465 ASP K 139 REMARK 465 PHE K 140 REMARK 465 TYR K 141 REMARK 465 PRO K 142 REMARK 465 GLY K 143 REMARK 465 ALA K 144 REMARK 465 VAL K 145 REMARK 465 THR K 146 REMARK 465 VAL K 147 REMARK 465 ALA K 148 REMARK 465 TRP K 149 REMARK 465 LYS K 150 REMARK 465 ALA K 151 REMARK 465 ASP K 152 REMARK 465 SER K 153 REMARK 465 SER K 154 REMARK 465 PRO K 155 REMARK 465 VAL K 156 REMARK 465 LYS K 157 REMARK 465 ALA K 158 REMARK 465 GLY K 159 REMARK 465 VAL K 160 REMARK 465 GLU K 161 REMARK 465 THR K 162 REMARK 465 THR K 163 REMARK 465 THR K 164 REMARK 465 PRO K 165 REMARK 465 SER K 166 REMARK 465 LYS K 167 REMARK 465 GLN K 168 REMARK 465 SER K 169 REMARK 465 ASN K 170 REMARK 465 ASN K 171 REMARK 465 LYS K 172 REMARK 465 TYR K 173 REMARK 465 ALA K 174 REMARK 465 ALA K 175 REMARK 465 SER K 176 REMARK 465 SER K 177 REMARK 465 TYR K 178 REMARK 465 LEU K 179 REMARK 465 SER K 180 REMARK 465 LEU K 181 REMARK 465 THR K 182 REMARK 465 PRO K 183 REMARK 465 GLU K 184 REMARK 465 GLN K 185 REMARK 465 TRP K 186 REMARK 465 LYS K 187 REMARK 465 SER K 188 REMARK 465 HIS K 189 REMARK 465 ARG K 190 REMARK 465 SER K 191 REMARK 465 TYR K 192 REMARK 465 SER K 193 REMARK 465 CYS K 194 REMARK 465 GLN K 195 REMARK 465 VAL K 196 REMARK 465 THR K 197 REMARK 465 HIS K 198 REMARK 465 GLU K 199 REMARK 465 GLY K 200 REMARK 465 SER K 201 REMARK 465 THR K 202 REMARK 465 VAL K 203 REMARK 465 GLU K 204 REMARK 465 LYS K 205 REMARK 465 THR K 206 REMARK 465 VAL K 207 REMARK 465 ALA K 208 REMARK 465 PRO K 209 REMARK 465 THR K 210 REMARK 465 GLU K 211 REMARK 465 CYS K 212 REMARK 465 SER K 213 REMARK 465 GLU L 1 REMARK 465 LEU L 107 REMARK 465 GLY L 108 REMARK 465 GLN L 109 REMARK 465 PRO L 110 REMARK 465 LYS L 111 REMARK 465 ALA L 112 REMARK 465 ALA L 113 REMARK 465 PRO L 114 REMARK 465 SER L 115 REMARK 465 VAL L 116 REMARK 465 THR L 117 REMARK 465 LEU L 118 REMARK 465 PHE L 119 REMARK 465 PRO L 120 REMARK 465 PRO L 121 REMARK 465 SER L 122 REMARK 465 SER L 123 REMARK 465 GLU L 124 REMARK 465 GLU L 125 REMARK 465 LEU L 126 REMARK 465 GLN L 127 REMARK 465 ALA L 128 REMARK 465 ASN L 129 REMARK 465 LYS L 130 REMARK 465 ALA L 131 REMARK 465 THR L 132 REMARK 465 LEU L 133 REMARK 465 VAL L 134 REMARK 465 CYS L 135 REMARK 465 LEU L 136 REMARK 465 ILE L 137 REMARK 465 SER L 138 REMARK 465 ASP L 139 REMARK 465 PHE L 140 REMARK 465 TYR L 141 REMARK 465 PRO L 142 REMARK 465 GLY L 143 REMARK 465 ALA L 144 REMARK 465 VAL L 145 REMARK 465 THR L 146 REMARK 465 VAL L 147 REMARK 465 ALA L 148 REMARK 465 TRP L 149 REMARK 465 LYS L 150 REMARK 465 ALA L 151 REMARK 465 ASP L 152 REMARK 465 SER L 153 REMARK 465 SER L 154 REMARK 465 PRO L 155 REMARK 465 VAL L 156 REMARK 465 LYS L 157 REMARK 465 ALA L 158 REMARK 465 GLY L 159 REMARK 465 VAL L 160 REMARK 465 GLU L 161 REMARK 465 THR L 162 REMARK 465 THR L 163 REMARK 465 THR L 164 REMARK 465 PRO L 165 REMARK 465 SER L 166 REMARK 465 LYS L 167 REMARK 465 GLN L 168 REMARK 465 SER L 169 REMARK 465 ASN L 170 REMARK 465 ASN L 171 REMARK 465 LYS L 172 REMARK 465 TYR L 173 REMARK 465 ALA L 174 REMARK 465 ALA L 175 REMARK 465 SER L 176 REMARK 465 SER L 177 REMARK 465 TYR L 178 REMARK 465 LEU L 179 REMARK 465 SER L 180 REMARK 465 LEU L 181 REMARK 465 THR L 182 REMARK 465 PRO L 183 REMARK 465 GLU L 184 REMARK 465 GLN L 185 REMARK 465 TRP L 186 REMARK 465 LYS L 187 REMARK 465 SER L 188 REMARK 465 HIS L 189 REMARK 465 ARG L 190 REMARK 465 SER L 191 REMARK 465 TYR L 192 REMARK 465 SER L 193 REMARK 465 CYS L 194 REMARK 465 GLN L 195 REMARK 465 VAL L 196 REMARK 465 THR L 197 REMARK 465 HIS L 198 REMARK 465 GLU L 199 REMARK 465 GLY L 200 REMARK 465 SER L 201 REMARK 465 THR L 202 REMARK 465 VAL L 203 REMARK 465 GLU L 204 REMARK 465 LYS L 205 REMARK 465 THR L 206 REMARK 465 VAL L 207 REMARK 465 ALA L 208 REMARK 465 PRO L 209 REMARK 465 THR L 210 REMARK 465 GLU L 211 REMARK 465 CYS L 212 REMARK 465 SER L 213 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS 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 CG ASN A 160 C1 NAG A 1160 2.08 REMARK 500 CD1 ILE A 194 O6 NAG A 1197 2.19 REMARK 500 CG ASN A 197 C1 NAG A 1197 2.09 REMARK 500 ND2 ASN A 197 O5 NAG A 1197 1.95 REMARK 500 ND2 ASN A 197 C2 NAG A 1197 2.20 REMARK 500 OD1 ASN A 234 O THR A 236 2.12 REMARK 500 ND2 ASN A 234 C2 NAG A 1234 2.09 REMARK 500 ND2 ASN A 234 O5 NAG A 1234 1.99 REMARK 500 ND2 ASN A 279 O6 NAG A 1276 1.99 REMARK 500 ND2 ASN A 295 O5 NAG A 1295 1.93 REMARK 500 CG ASN A 301 C1 NAG A 1301 2.16 REMARK 500 ND2 ASN A 301 O5 NAG A 1301 2.18 REMARK 500 ND2 ASN A 301 C2 NAG A 1301 2.16 REMARK 500 CG ASN A 332 C1 NAG A 1332 2.17 REMARK 500 ND2 ASN A 332 C2 NAG A 1332 2.08 REMARK 500 ND2 ASN A 332 O5 NAG A 1332 2.00 REMARK 500 O GLY B 527 C7 NAG A 1088 2.13 REMARK 500 CG ASN B 618 C1 NAG B 1618 2.17 REMARK 500 ND2 ASN B 618 O5 NAG B 1618 2.01 REMARK 500 CG ASN C 160 C1 NAG C 1160 2.08 REMARK 500 CD1 ILE C 194 O6 NAG C 1197 2.19 REMARK 500 CG ASN C 197 C1 NAG C 1197 2.09 REMARK 500 ND2 ASN C 197 C2 NAG C 1197 2.20 REMARK 500 ND2 ASN C 197 O5 NAG C 1197 1.95 REMARK 500 OD1 ASN C 234 O THR C 236 2.12 REMARK 500 ND2 ASN C 234 C2 NAG C 1234 2.09 REMARK 500 ND2 ASN C 234 O5 NAG C 1234 1.99 REMARK 500 ND2 ASN C 279 O6 NAG C 1276 1.99 REMARK 500 ND2 ASN C 295 O5 NAG C 1295 1.93 REMARK 500 CG ASN C 301 C1 NAG C 1301 2.16 REMARK 500 ND2 ASN C 301 O5 NAG C 1301 2.18 REMARK 500 ND2 ASN C 301 C2 NAG C 1301 2.16 REMARK 500 CG ASN C 332 C1 NAG C 1332 2.17 REMARK 500 ND2 ASN C 332 C2 NAG C 1332 2.08 REMARK 500 ND2 ASN C 332 O5 NAG C 1332 2.00 REMARK 500 CG ASN D 160 C1 NAG D 1160 2.08 REMARK 500 CD1 ILE D 194 O6 NAG D 1197 2.19 REMARK 500 CG ASN D 197 C1 NAG D 1197 2.09 REMARK 500 ND2 ASN D 197 C2 NAG D 1197 2.20 REMARK 500 ND2 ASN D 197 O5 NAG D 1197 1.95 REMARK 500 OD1 ASN D 234 O THR D 236 2.12 REMARK 500 ND2 ASN D 234 C2 NAG D 1234 2.09 REMARK 500 ND2 ASN D 234 O5 NAG D 1234 1.99 REMARK 500 ND2 ASN D 279 O6 NAG D 1276 1.99 REMARK 500 ND2 ASN D 295 O5 NAG D 1295 1.93 REMARK 500 CG ASN D 301 C1 NAG D 1301 2.16 REMARK 500 ND2 ASN D 301 O5 NAG D 1301 2.18 REMARK 500 ND2 ASN D 301 C2 NAG D 1301 2.16 REMARK 500 CG ASN D 332 C1 NAG D 1332 2.17 REMARK 500 ND2 ASN D 332 C2 NAG D 1332 2.08 REMARK 500 REMARK 500 THIS ENTRY HAS 66 CLOSE CONTACTS REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 ILE A 84 C HIS A 85 N 0.148 REMARK 500 GLU A 92 C PHE A 93 N -0.138 REMARK 500 GLN B 658 C ASP B 659 N 0.287 REMARK 500 ILE C 84 C HIS C 85 N 0.148 REMARK 500 GLU C 92 C PHE C 93 N -0.139 REMARK 500 ILE D 84 C HIS D 85 N 0.148 REMARK 500 GLU D 92 C PHE D 93 N -0.139 REMARK 500 GLN E 658 C ASP E 659 N 0.286 REMARK 500 GLN F 658 C ASP F 659 N 0.287 REMARK 500 PRO J 8 C SER J 9 N 0.258 REMARK 500 PRO K 8 C SER K 9 N 0.258 REMARK 500 PRO L 8 C SER L 9 N 0.258 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ILE A 84 CA - C - N ANGL. DEV. = -23.6 DEGREES REMARK 500 ILE A 84 O - C - N ANGL. DEV. = 20.3 DEGREES REMARK 500 HIS A 85 C - N - CA ANGL. DEV. = -22.2 DEGREES REMARK 500 LEU A 86 CA - C - N ANGL. DEV. = 14.9 DEGREES REMARK 500 LEU A 86 O - C - N ANGL. DEV. = -20.2 DEGREES REMARK 500 GLU A 87 C - N - CA ANGL. DEV. = 16.5 DEGREES REMARK 500 GLN A 348 CA - C - N ANGL. DEV. = -17.6 DEGREES REMARK 500 GLN A 348 O - C - N ANGL. DEV. = 16.9 DEGREES REMARK 500 LEU A 349 C - N - CA ANGL. DEV. = -16.8 DEGREES REMARK 500 LYS A 351 CA - C - N ANGL. DEV. = 15.9 DEGREES REMARK 500 LYS A 351 O - C - N ANGL. DEV. = -16.2 DEGREES REMARK 500 SER A 393 CA - C - N ANGL. DEV. = -18.4 DEGREES REMARK 500 SER A 393 O - C - N ANGL. DEV. = 17.8 DEGREES REMARK 500 GLU B 648 N - CA - C ANGL. DEV. = 38.2 DEGREES REMARK 500 GLU B 648 N - CA - CB ANGL. DEV. = -12.6 DEGREES REMARK 500 GLN B 658 CA - C - N ANGL. DEV. = -17.5 DEGREES REMARK 500 GLN B 658 O - C - N ANGL. DEV. = 16.5 DEGREES REMARK 500 ILE C 84 CA - C - N ANGL. DEV. = -23.7 DEGREES REMARK 500 ILE C 84 O - C - N ANGL. DEV. = 20.3 DEGREES REMARK 500 HIS C 85 C - N - CA ANGL. DEV. = -22.2 DEGREES REMARK 500 LEU C 86 CA - C - N ANGL. DEV. = 14.9 DEGREES REMARK 500 LEU C 86 O - C - N ANGL. DEV. = -20.2 DEGREES REMARK 500 GLU C 87 C - N - CA ANGL. DEV. = 16.5 DEGREES REMARK 500 GLN C 348 CA - C - N ANGL. DEV. = -17.7 DEGREES REMARK 500 GLN C 348 O - C - N ANGL. DEV. = 16.9 DEGREES REMARK 500 LEU C 349 C - N - CA ANGL. DEV. = -16.8 DEGREES REMARK 500 LYS C 351 CA - C - N ANGL. DEV. = 16.0 DEGREES REMARK 500 LYS C 351 O - C - N ANGL. DEV. = -16.2 DEGREES REMARK 500 SER C 393 CA - C - N ANGL. DEV. = -18.4 DEGREES REMARK 500 SER C 393 O - C - N ANGL. DEV. = 17.9 DEGREES REMARK 500 ILE D 84 CA - C - N ANGL. DEV. = -23.6 DEGREES REMARK 500 ILE D 84 O - C - N ANGL. DEV. = 20.3 DEGREES REMARK 500 HIS D 85 C - N - CA ANGL. DEV. = -22.2 DEGREES REMARK 500 LEU D 86 CA - C - N ANGL. DEV. = 14.9 DEGREES REMARK 500 LEU D 86 O - C - N ANGL. DEV. = -20.2 DEGREES REMARK 500 GLU D 87 C - N - CA ANGL. DEV. = 16.6 DEGREES REMARK 500 GLN D 348 CA - C - N ANGL. DEV. = -17.7 DEGREES REMARK 500 GLN D 348 O - C - N ANGL. DEV. = 16.9 DEGREES REMARK 500 LEU D 349 C - N - CA ANGL. DEV. = -16.8 DEGREES REMARK 500 LYS D 351 CA - C - N ANGL. DEV. = 15.9 DEGREES REMARK 500 LYS D 351 O - C - N ANGL. DEV. = -16.2 DEGREES REMARK 500 SER D 393 CA - C - N ANGL. DEV. = -18.4 DEGREES REMARK 500 SER D 393 O - C - N ANGL. DEV. = 17.9 DEGREES REMARK 500 GLU E 648 N - CA - C ANGL. DEV. = 38.2 DEGREES REMARK 500 GLU E 648 N - CA - CB ANGL. DEV. = -12.6 DEGREES REMARK 500 GLN E 658 CA - C - N ANGL. DEV. = -17.5 DEGREES REMARK 500 GLN E 658 O - C - N ANGL. DEV. = 16.5 DEGREES REMARK 500 GLU F 648 N - CA - C ANGL. DEV. = 38.2 DEGREES REMARK 500 GLU F 648 N - CA - CB ANGL. DEV. = -12.6 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 61 ANGLE DEVIATIONS. 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 SER A 56 106.12 -171.93 REMARK 500 ASP A 57 -149.09 47.39 REMARK 500 TRP A 69 -71.45 -93.69 REMARK 500 ALA A 70 -1.62 -163.61 REMARK 500 HIS A 72 -45.47 -155.88 REMARK 500 ILE A 84 119.31 -171.63 REMARK 500 ASN A 88 -3.56 74.57 REMARK 500 GLU A 91 -179.15 -172.99 REMARK 500 CYS A 126 83.27 -68.07 REMARK 500 ASN A 137 117.05 -32.17 REMARK 500 THR A 139 -74.20 -79.79 REMARK 500 ASP A 140 93.73 -170.47 REMARK 500 GLU A 153 -20.44 72.15 REMARK 500 THR A 163 -164.44 -109.67 REMARK 500 ARG A 166 100.05 -49.85 REMARK 500 ASP A 167 -93.69 156.16 REMARK 500 SER A 199 -179.38 -173.03 REMARK 500 PHE A 233 127.90 -170.09 REMARK 500 GLN A 258 -67.17 67.57 REMARK 500 GLU A 268 -107.37 62.22 REMARK 500 ASN A 276 95.90 -162.91 REMARK 500 LYS A 305 77.95 -68.72 REMARK 500 ILE A 326 78.83 -66.42 REMARK 500 LYS A 351 -10.98 -49.33 REMARK 500 PHE A 353 -21.87 -143.48 REMARK 500 ASN A 356 48.12 -150.55 REMARK 500 ILE A 396 -136.60 -75.14 REMARK 500 SER A 463 14.22 -140.02 REMARK 500 THR A 464 -74.16 -173.61 REMARK 500 ARG A 500 95.49 -67.09 REMARK 500 SER B 546 -75.43 74.25 REMARK 500 ILE B 548 -107.40 55.18 REMARK 500 VAL B 549 -66.02 64.54 REMARK 500 LEU B 568 -105.88 46.02 REMARK 500 THR B 569 155.24 77.18 REMARK 500 TRP B 571 -22.52 85.98 REMARK 500 CYS B 598 -65.84 -137.07 REMARK 500 SER B 599 -55.90 70.48 REMARK 500 LYS B 601 -147.03 -87.14 REMARK 500 LEU B 602 -51.15 67.38 REMARK 500 SER B 615 88.98 60.30 REMARK 500 ILE B 622 -77.35 -96.05 REMARK 500 ASN B 625 46.44 -152.88 REMARK 500 MET B 626 136.30 -173.14 REMARK 500 GLU B 648 -69.61 -101.17 REMARK 500 SER B 649 -73.25 -19.89 REMARK 500 ASN B 656 -63.46 87.81 REMARK 500 SER C 56 106.05 -171.93 REMARK 500 ASP C 57 -149.06 47.43 REMARK 500 TRP C 69 -71.39 -93.70 REMARK 500 REMARK 500 THIS ENTRY HAS 177 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 LEU A 86 -17.24 REMARK 500 LEU C 86 -17.21 REMARK 500 LEU D 86 -17.32 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 GLU B 648 15.9 L L OUTSIDE RANGE REMARK 500 GLU E 648 15.9 L L OUTSIDE RANGE REMARK 500 GLU F 648 15.9 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1088 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1089 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A1090 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1133 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1134 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1156 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1157 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A1158 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1160 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1161 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A1162 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1197 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1198 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1234 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1235 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1262 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1263 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A1264 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1265 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1266 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1267 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1268 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1276 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1277 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A1278 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1295 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1296 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A1297 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1298 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1299 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1301 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1302 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A1303 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1304 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1305 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1306 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1308 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1332 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1333 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A1334 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1335 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1336 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1337 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1339 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1340 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1341 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1342 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1343 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1355 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1356 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1363 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1364 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A1365 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1386 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1387 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A1388 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1392 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1393 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1448 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1449 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1611 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1612 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1618 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1637 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1088 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1089 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA C1090 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1133 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1134 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1156 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1157 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA C1158 REMARK 800 REMARK 800 SITE_IDENTIFIER: IC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1160 REMARK 800 REMARK 800 SITE_IDENTIFIER: IC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1161 REMARK 800 REMARK 800 SITE_IDENTIFIER: IC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA C1162 REMARK 800 REMARK 800 SITE_IDENTIFIER: IC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1197 REMARK 800 REMARK 800 SITE_IDENTIFIER: IC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1198 REMARK 800 REMARK 800 SITE_IDENTIFIER: IC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1234 REMARK 800 REMARK 800 SITE_IDENTIFIER: IC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1235 REMARK 800 REMARK 800 SITE_IDENTIFIER: IC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1262 REMARK 800 REMARK 800 SITE_IDENTIFIER: IC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1263 REMARK 800 REMARK 800 SITE_IDENTIFIER: JC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA C1264 REMARK 800 REMARK 800 SITE_IDENTIFIER: JC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C1265 REMARK 800 REMARK 800 SITE_IDENTIFIER: JC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C1266 REMARK 800 REMARK 800 SITE_IDENTIFIER: JC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C1267 REMARK 800 REMARK 800 SITE_IDENTIFIER: JC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C1268 REMARK 800 REMARK 800 SITE_IDENTIFIER: JC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1276 REMARK 800 REMARK 800 SITE_IDENTIFIER: JC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1277 REMARK 800 REMARK 800 SITE_IDENTIFIER: JC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA C1278 REMARK 800 REMARK 800 SITE_IDENTIFIER: JC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1295 REMARK 800 REMARK 800 SITE_IDENTIFIER: KC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1296 REMARK 800 REMARK 800 SITE_IDENTIFIER: KC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA C1297 REMARK 800 REMARK 800 SITE_IDENTIFIER: KC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C1298 REMARK 800 REMARK 800 SITE_IDENTIFIER: KC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C1299 REMARK 800 REMARK 800 SITE_IDENTIFIER: KC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1301 REMARK 800 REMARK 800 SITE_IDENTIFIER: KC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1302 REMARK 800 REMARK 800 SITE_IDENTIFIER: KC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA C1303 REMARK 800 REMARK 800 SITE_IDENTIFIER: KC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C1304 REMARK 800 REMARK 800 SITE_IDENTIFIER: KC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C1305 REMARK 800 REMARK 800 SITE_IDENTIFIER: LC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C1306 REMARK 800 REMARK 800 SITE_IDENTIFIER: LC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C1308 REMARK 800 REMARK 800 SITE_IDENTIFIER: LC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1332 REMARK 800 REMARK 800 SITE_IDENTIFIER: LC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1333 REMARK 800 REMARK 800 SITE_IDENTIFIER: LC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA C1334 REMARK 800 REMARK 800 SITE_IDENTIFIER: LC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C1335 REMARK 800 REMARK 800 SITE_IDENTIFIER: LC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C1336 REMARK 800 REMARK 800 SITE_IDENTIFIER: LC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C1337 REMARK 800 REMARK 800 SITE_IDENTIFIER: LC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C1339 REMARK 800 REMARK 800 SITE_IDENTIFIER: MC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C1340 REMARK 800 REMARK 800 SITE_IDENTIFIER: MC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C1341 REMARK 800 REMARK 800 SITE_IDENTIFIER: MC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C1342 REMARK 800 REMARK 800 SITE_IDENTIFIER: MC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1343 REMARK 800 REMARK 800 SITE_IDENTIFIER: MC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1355 REMARK 800 REMARK 800 SITE_IDENTIFIER: MC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1356 REMARK 800 REMARK 800 SITE_IDENTIFIER: MC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1363 REMARK 800 REMARK 800 SITE_IDENTIFIER: MC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1364 REMARK 800 REMARK 800 SITE_IDENTIFIER: MC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA C1365 REMARK 800 REMARK 800 SITE_IDENTIFIER: NC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1386 REMARK 800 REMARK 800 SITE_IDENTIFIER: NC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1387 REMARK 800 REMARK 800 SITE_IDENTIFIER: NC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA C1388 REMARK 800 REMARK 800 SITE_IDENTIFIER: NC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1392 REMARK 800 REMARK 800 SITE_IDENTIFIER: NC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1393 REMARK 800 REMARK 800 SITE_IDENTIFIER: NC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1448 REMARK 800 REMARK 800 SITE_IDENTIFIER: NC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1449 REMARK 800 REMARK 800 SITE_IDENTIFIER: NC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1088 REMARK 800 REMARK 800 SITE_IDENTIFIER: NC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1089 REMARK 800 REMARK 800 SITE_IDENTIFIER: OC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA D1090 REMARK 800 REMARK 800 SITE_IDENTIFIER: OC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1133 REMARK 800 REMARK 800 SITE_IDENTIFIER: OC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1134 REMARK 800 REMARK 800 SITE_IDENTIFIER: OC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1156 REMARK 800 REMARK 800 SITE_IDENTIFIER: OC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1157 REMARK 800 REMARK 800 SITE_IDENTIFIER: OC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA D1158 REMARK 800 REMARK 800 SITE_IDENTIFIER: OC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1160 REMARK 800 REMARK 800 SITE_IDENTIFIER: OC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1161 REMARK 800 REMARK 800 SITE_IDENTIFIER: OC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA D1162 REMARK 800 REMARK 800 SITE_IDENTIFIER: PC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1197 REMARK 800 REMARK 800 SITE_IDENTIFIER: PC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1198 REMARK 800 REMARK 800 SITE_IDENTIFIER: PC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1234 REMARK 800 REMARK 800 SITE_IDENTIFIER: PC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1235 REMARK 800 REMARK 800 SITE_IDENTIFIER: PC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1262 REMARK 800 REMARK 800 SITE_IDENTIFIER: PC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1263 REMARK 800 REMARK 800 SITE_IDENTIFIER: PC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA D1264 REMARK 800 REMARK 800 SITE_IDENTIFIER: PC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D1265 REMARK 800 REMARK 800 SITE_IDENTIFIER: PC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D1266 REMARK 800 REMARK 800 SITE_IDENTIFIER: QC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D1267 REMARK 800 REMARK 800 SITE_IDENTIFIER: QC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D1268 REMARK 800 REMARK 800 SITE_IDENTIFIER: QC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1276 REMARK 800 REMARK 800 SITE_IDENTIFIER: QC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1277 REMARK 800 REMARK 800 SITE_IDENTIFIER: QC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA D1278 REMARK 800 REMARK 800 SITE_IDENTIFIER: QC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1295 REMARK 800 REMARK 800 SITE_IDENTIFIER: QC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1296 REMARK 800 REMARK 800 SITE_IDENTIFIER: QC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA D1297 REMARK 800 REMARK 800 SITE_IDENTIFIER: QC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D1298 REMARK 800 REMARK 800 SITE_IDENTIFIER: RC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D1299 REMARK 800 REMARK 800 SITE_IDENTIFIER: RC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1301 REMARK 800 REMARK 800 SITE_IDENTIFIER: RC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1302 REMARK 800 REMARK 800 SITE_IDENTIFIER: RC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA D1303 REMARK 800 REMARK 800 SITE_IDENTIFIER: RC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D1304 REMARK 800 REMARK 800 SITE_IDENTIFIER: RC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D1305 REMARK 800 REMARK 800 SITE_IDENTIFIER: RC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D1306 REMARK 800 REMARK 800 SITE_IDENTIFIER: RC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D1308 REMARK 800 REMARK 800 SITE_IDENTIFIER: RC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1332 REMARK 800 REMARK 800 SITE_IDENTIFIER: SC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1333 REMARK 800 REMARK 800 SITE_IDENTIFIER: SC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA D1334 REMARK 800 REMARK 800 SITE_IDENTIFIER: SC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D1335 REMARK 800 REMARK 800 SITE_IDENTIFIER: SC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D1336 REMARK 800 REMARK 800 SITE_IDENTIFIER: SC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D1337 REMARK 800 REMARK 800 SITE_IDENTIFIER: SC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D1339 REMARK 800 REMARK 800 SITE_IDENTIFIER: SC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D1340 REMARK 800 REMARK 800 SITE_IDENTIFIER: SC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D1341 REMARK 800 REMARK 800 SITE_IDENTIFIER: SC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D1342 REMARK 800 REMARK 800 SITE_IDENTIFIER: TC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1343 REMARK 800 REMARK 800 SITE_IDENTIFIER: TC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1355 REMARK 800 REMARK 800 SITE_IDENTIFIER: TC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1356 REMARK 800 REMARK 800 SITE_IDENTIFIER: TC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1363 REMARK 800 REMARK 800 SITE_IDENTIFIER: TC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1364 REMARK 800 REMARK 800 SITE_IDENTIFIER: TC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA D1365 REMARK 800 REMARK 800 SITE_IDENTIFIER: TC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1386 REMARK 800 REMARK 800 SITE_IDENTIFIER: TC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1387 REMARK 800 REMARK 800 SITE_IDENTIFIER: TC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA D1388 REMARK 800 REMARK 800 SITE_IDENTIFIER: UC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1392 REMARK 800 REMARK 800 SITE_IDENTIFIER: UC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1393 REMARK 800 REMARK 800 SITE_IDENTIFIER: UC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1448 REMARK 800 REMARK 800 SITE_IDENTIFIER: UC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1449 REMARK 800 REMARK 800 SITE_IDENTIFIER: UC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E1611 REMARK 800 REMARK 800 SITE_IDENTIFIER: UC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E1612 REMARK 800 REMARK 800 SITE_IDENTIFIER: UC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E1618 REMARK 800 REMARK 800 SITE_IDENTIFIER: UC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E1637 REMARK 800 REMARK 800 SITE_IDENTIFIER: UC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG F1611 REMARK 800 REMARK 800 SITE_IDENTIFIER: VC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG F1612 REMARK 800 REMARK 800 SITE_IDENTIFIER: VC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG F1618 REMARK 800 REMARK 800 SITE_IDENTIFIER: VC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG F1637 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-3121 RELATED DB: EMDB DBREF 5ACO A 31 508 UNP Q2N0S6 Q2N0S6_9HIV1 30 505 DBREF 5ACO B 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 5ACO C 31 508 UNP Q2N0S6 Q2N0S6_9HIV1 30 505 DBREF 5ACO D 31 508 UNP Q2N0S6 Q2N0S6_9HIV1 30 505 DBREF 5ACO E 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 5ACO F 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 5ACO G 1 217 PDB 5ACO 5ACO 1 217 DBREF 5ACO H 1 217 PDB 5ACO 5ACO 1 217 DBREF 5ACO I 1 217 PDB 5ACO 5ACO 1 217 DBREF 5ACO J 1 213 PDB 5ACO 5ACO 1 213 DBREF 5ACO K 1 213 PDB 5ACO 5ACO 1 213 DBREF 5ACO L 1 213 PDB 5ACO 5ACO 1 213 SEQADV 5ACO ASN A 332 UNP Q2N0S6 THR 330 ENGINEERED MUTATION SEQADV 5ACO CYS A 501 UNP Q2N0S6 ALA 498 ENGINEERED MUTATION SEQADV 5ACO PRO B 559 UNP Q2N0S6 ILE 556 ENGINEERED MUTATION SEQADV 5ACO CYS B 605 UNP Q2N0S6 THR 602 ENGINEERED MUTATION SEQADV 5ACO ASN C 332 UNP Q2N0S6 THR 330 ENGINEERED MUTATION SEQADV 5ACO CYS C 501 UNP Q2N0S6 ALA 498 ENGINEERED MUTATION SEQADV 5ACO ASN D 332 UNP Q2N0S6 THR 330 ENGINEERED MUTATION SEQADV 5ACO CYS D 501 UNP Q2N0S6 ALA 498 ENGINEERED MUTATION SEQADV 5ACO PRO E 559 UNP Q2N0S6 ILE 556 ENGINEERED MUTATION SEQADV 5ACO CYS E 605 UNP Q2N0S6 THR 602 ENGINEERED MUTATION SEQADV 5ACO PRO F 559 UNP Q2N0S6 ILE 556 ENGINEERED MUTATION SEQADV 5ACO CYS F 605 UNP Q2N0S6 THR 602 ENGINEERED MUTATION SEQRES 1 A 476 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 A 476 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 A 476 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 A 476 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 A 476 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 A 476 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 A 476 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 A 476 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 A 476 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 A 476 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 A 476 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 A 476 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 A 476 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 A 476 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 A 476 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 A 476 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 A 476 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 A 476 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 A 476 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 A 476 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 A 476 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 A 476 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 A 476 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 A 476 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 A 476 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 A 476 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 A 476 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 A 476 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 A 476 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 A 476 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 A 476 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 A 476 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 A 476 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 A 476 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 A 476 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 A 476 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 A 476 CYS LYS ARG ARG VAL VAL GLY ARG SEQRES 1 C 476 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 C 476 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 C 476 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 C 476 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 C 476 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 C 476 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 C 476 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 C 476 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 C 476 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 C 476 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 C 476 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 C 476 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 C 476 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 C 476 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 C 476 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 C 476 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 C 476 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 C 476 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 C 476 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 C 476 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 C 476 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 C 476 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 C 476 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 C 476 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 C 476 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 C 476 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 C 476 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 C 476 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 C 476 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 C 476 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 C 476 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 C 476 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 C 476 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 C 476 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 C 476 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 C 476 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 C 476 CYS LYS ARG ARG VAL VAL GLY ARG SEQRES 1 D 476 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 D 476 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 D 476 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 D 476 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 D 476 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 D 476 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 D 476 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 D 476 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 D 476 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 D 476 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 D 476 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 D 476 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 D 476 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 D 476 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 D 476 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 D 476 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 D 476 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 D 476 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 D 476 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 D 476 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 D 476 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 D 476 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 D 476 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 D 476 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 D 476 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 D 476 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 D 476 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 D 476 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 D 476 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 D 476 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 D 476 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 D 476 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 D 476 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 D 476 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 D 476 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 D 476 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 D 476 CYS LYS ARG ARG VAL VAL GLY ARG SEQRES 1 B 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 B 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 B 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 B 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 B 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 B 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 B 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 B 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 B 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 B 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 B 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 B 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 E 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 E 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 E 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 E 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 E 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 E 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 E 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 E 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 E 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 E 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 E 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 E 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 F 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 F 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 F 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 F 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 F 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 F 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 F 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 F 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 F 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 F 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 F 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 F 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 G 239 GLU PRO GLN LEU GLN GLU SER GLY PRO THR LEU VAL GLU SEQRES 2 G 239 ALA SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 G 239 ASP SER THR ALA ALA CYS ASN SER PHE TRP GLY TRP VAL SEQRES 4 G 239 ARG GLN PRO PRO GLY LYS GLY LEU GLU TRP VAL GLY SER SEQRES 5 G 239 LEU SER HIS CYS ALA SER TYR TRP ASN ARG GLY TRP THR SEQRES 6 G 239 TYR HIS ASN PRO SER LEU LYS SER ARG LEU THR LEU ALA SEQRES 7 G 239 LEU ASP THR PRO LYS ASN LEU VAL PHE LEU LYS LEU ASN SEQRES 8 G 239 SER VAL THR ALA ALA ASP THR ALA THR TYR TYR CYS ALA SEQRES 9 G 239 ARG PHE GLY GLY GLU VAL LEU ARG TYR THR ASP TRP PRO SEQRES 10 G 239 LYS PRO ALA TRP VAL ASP LEU TRP GLY ARG GLY THR LEU SEQRES 11 G 239 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 12 G 239 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 13 G 239 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 14 G 239 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 15 G 239 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 16 G 239 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 17 G 239 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 18 G 239 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 19 G 239 PRO LYS SER CYS ASP SEQRES 1 H 239 GLU PRO GLN LEU GLN GLU SER GLY PRO THR LEU VAL GLU SEQRES 2 H 239 ALA SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 H 239 ASP SER THR ALA ALA CYS ASN SER PHE TRP GLY TRP VAL SEQRES 4 H 239 ARG GLN PRO PRO GLY LYS GLY LEU GLU TRP VAL GLY SER SEQRES 5 H 239 LEU SER HIS CYS ALA SER TYR TRP ASN ARG GLY TRP THR SEQRES 6 H 239 TYR HIS ASN PRO SER LEU LYS SER ARG LEU THR LEU ALA SEQRES 7 H 239 LEU ASP THR PRO LYS ASN LEU VAL PHE LEU LYS LEU ASN SEQRES 8 H 239 SER VAL THR ALA ALA ASP THR ALA THR TYR TYR CYS ALA SEQRES 9 H 239 ARG PHE GLY GLY GLU VAL LEU ARG TYR THR ASP TRP PRO SEQRES 10 H 239 LYS PRO ALA TRP VAL ASP LEU TRP GLY ARG GLY THR LEU SEQRES 11 H 239 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 12 H 239 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 13 H 239 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 14 H 239 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 15 H 239 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 16 H 239 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 17 H 239 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 18 H 239 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 19 H 239 PRO LYS SER CYS ASP SEQRES 1 I 239 GLU PRO GLN LEU GLN GLU SER GLY PRO THR LEU VAL GLU SEQRES 2 I 239 ALA SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 I 239 ASP SER THR ALA ALA CYS ASN SER PHE TRP GLY TRP VAL SEQRES 4 I 239 ARG GLN PRO PRO GLY LYS GLY LEU GLU TRP VAL GLY SER SEQRES 5 I 239 LEU SER HIS CYS ALA SER TYR TRP ASN ARG GLY TRP THR SEQRES 6 I 239 TYR HIS ASN PRO SER LEU LYS SER ARG LEU THR LEU ALA SEQRES 7 I 239 LEU ASP THR PRO LYS ASN LEU VAL PHE LEU LYS LEU ASN SEQRES 8 I 239 SER VAL THR ALA ALA ASP THR ALA THR TYR TYR CYS ALA SEQRES 9 I 239 ARG PHE GLY GLY GLU VAL LEU ARG TYR THR ASP TRP PRO SEQRES 10 I 239 LYS PRO ALA TRP VAL ASP LEU TRP GLY ARG GLY THR LEU SEQRES 11 I 239 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 12 I 239 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 13 I 239 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 14 I 239 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 15 I 239 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 16 I 239 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 17 I 239 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 18 I 239 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 19 I 239 PRO LYS SER CYS ASP SEQRES 1 J 211 GLU SER ALA LEU THR GLN PRO PRO SER ALA SER GLY SER SEQRES 2 J 211 PRO GLY GLN SER ILE THR ILE SER CYS THR GLY THR SER SEQRES 3 J 211 ASN ASN PHE VAL SER TRP TYR GLN GLN HIS ALA GLY LYS SEQRES 4 J 211 ALA PRO LYS LEU VAL ILE TYR ASP VAL ASN LYS ARG PRO SEQRES 5 J 211 SER GLY VAL PRO ASP ARG PHE SER GLY SER LYS SER GLY SEQRES 6 J 211 ASN THR ALA SER LEU THR VAL SER GLY LEU GLN THR ASP SEQRES 7 J 211 ASP GLU ALA VAL TYR TYR CYS GLY SER LEU VAL GLY ASN SEQRES 8 J 211 TRP ASP VAL ILE PHE GLY GLY GLY THR LYS LEU THR VAL SEQRES 9 J 211 LEU GLY GLN PRO LYS ALA ALA PRO SER VAL THR LEU PHE SEQRES 10 J 211 PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA THR SEQRES 11 J 211 LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA VAL SEQRES 12 J 211 THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL LYS ALA SEQRES 13 J 211 GLY VAL GLU THR THR THR PRO SER LYS GLN SER ASN ASN SEQRES 14 J 211 LYS TYR ALA ALA SER SER TYR LEU SER LEU THR PRO GLU SEQRES 15 J 211 GLN TRP LYS SER HIS ARG SER TYR SER CYS GLN VAL THR SEQRES 16 J 211 HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO THR SEQRES 17 J 211 GLU CYS SER SEQRES 1 K 211 GLU SER ALA LEU THR GLN PRO PRO SER ALA SER GLY SER SEQRES 2 K 211 PRO GLY GLN SER ILE THR ILE SER CYS THR GLY THR SER SEQRES 3 K 211 ASN ASN PHE VAL SER TRP TYR GLN GLN HIS ALA GLY LYS SEQRES 4 K 211 ALA PRO LYS LEU VAL ILE TYR ASP VAL ASN LYS ARG PRO SEQRES 5 K 211 SER GLY VAL PRO ASP ARG PHE SER GLY SER LYS SER GLY SEQRES 6 K 211 ASN THR ALA SER LEU THR VAL SER GLY LEU GLN THR ASP SEQRES 7 K 211 ASP GLU ALA VAL TYR TYR CYS GLY SER LEU VAL GLY ASN SEQRES 8 K 211 TRP ASP VAL ILE PHE GLY GLY GLY THR LYS LEU THR VAL SEQRES 9 K 211 LEU GLY GLN PRO LYS ALA ALA PRO SER VAL THR LEU PHE SEQRES 10 K 211 PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA THR SEQRES 11 K 211 LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA VAL SEQRES 12 K 211 THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL LYS ALA SEQRES 13 K 211 GLY VAL GLU THR THR THR PRO SER LYS GLN SER ASN ASN SEQRES 14 K 211 LYS TYR ALA ALA SER SER TYR LEU SER LEU THR PRO GLU SEQRES 15 K 211 GLN TRP LYS SER HIS ARG SER TYR SER CYS GLN VAL THR SEQRES 16 K 211 HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO THR SEQRES 17 K 211 GLU CYS SER SEQRES 1 L 211 GLU SER ALA LEU THR GLN PRO PRO SER ALA SER GLY SER SEQRES 2 L 211 PRO GLY GLN SER ILE THR ILE SER CYS THR GLY THR SER SEQRES 3 L 211 ASN ASN PHE VAL SER TRP TYR GLN GLN HIS ALA GLY LYS SEQRES 4 L 211 ALA PRO LYS LEU VAL ILE TYR ASP VAL ASN LYS ARG PRO SEQRES 5 L 211 SER GLY VAL PRO ASP ARG PHE SER GLY SER LYS SER GLY SEQRES 6 L 211 ASN THR ALA SER LEU THR VAL SER GLY LEU GLN THR ASP SEQRES 7 L 211 ASP GLU ALA VAL TYR TYR CYS GLY SER LEU VAL GLY ASN SEQRES 8 L 211 TRP ASP VAL ILE PHE GLY GLY GLY THR LYS LEU THR VAL SEQRES 9 L 211 LEU GLY GLN PRO LYS ALA ALA PRO SER VAL THR LEU PHE SEQRES 10 L 211 PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA THR SEQRES 11 L 211 LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA VAL SEQRES 12 L 211 THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL LYS ALA SEQRES 13 L 211 GLY VAL GLU THR THR THR PRO SER LYS GLN SER ASN ASN SEQRES 14 L 211 LYS TYR ALA ALA SER SER TYR LEU SER LEU THR PRO GLU SEQRES 15 L 211 GLN TRP LYS SER HIS ARG SER TYR SER CYS GLN VAL THR SEQRES 16 L 211 HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO THR SEQRES 17 L 211 GLU CYS SER HET NAG A1088 14 HET NAG A1089 14 HET BMA A1090 11 HET NAG A1133 14 HET NAG A1134 14 HET NAG A1156 14 HET NAG A1157 14 HET BMA A1158 11 HET NAG A1160 14 HET NAG A1161 14 HET BMA A1162 11 HET NAG A1197 14 HET NAG A1198 14 HET NAG A1234 14 HET NAG A1235 14 HET NAG A1262 14 HET NAG A1263 14 HET BMA A1264 11 HET MAN A1265 11 HET MAN A1266 11 HET MAN A1267 11 HET MAN A1268 11 HET NAG A1276 14 HET NAG A1277 14 HET BMA A1278 11 HET NAG A1295 14 HET NAG A1296 14 HET BMA A1297 11 HET MAN A1298 11 HET MAN A1299 11 HET NAG A1301 14 HET NAG A1302 14 HET BMA A1303 11 HET MAN A1304 11 HET MAN A1305 11 HET MAN A1306 11 HET MAN A1308 11 HET NAG A1332 14 HET NAG A1333 14 HET BMA A1334 11 HET MAN A1335 11 HET MAN A1336 11 HET MAN A1337 11 HET MAN A1339 11 HET MAN A1340 11 HET MAN A1341 11 HET MAN A1342 11 HET NAG A1343 14 HET NAG A1355 14 HET NAG A1356 14 HET NAG A1363 14 HET NAG A1364 14 HET BMA A1365 11 HET NAG A1386 14 HET NAG A1387 14 HET BMA A1388 11 HET NAG A1392 14 HET NAG A1393 14 HET NAG A1448 14 HET NAG A1449 14 HET NAG B1611 14 HET NAG B1612 14 HET NAG B1618 14 HET NAG B1637 14 HET NAG C1088 14 HET NAG C1089 14 HET BMA C1090 11 HET NAG C1133 14 HET NAG C1134 14 HET NAG C1156 14 HET NAG C1157 14 HET BMA C1158 11 HET NAG C1160 14 HET NAG C1161 14 HET BMA C1162 11 HET NAG C1197 14 HET NAG C1198 14 HET NAG C1234 14 HET NAG C1235 14 HET NAG C1262 14 HET NAG C1263 14 HET BMA C1264 11 HET MAN C1265 11 HET MAN C1266 11 HET MAN C1267 11 HET MAN C1268 11 HET NAG C1276 14 HET NAG C1277 14 HET BMA C1278 11 HET NAG C1295 14 HET NAG C1296 14 HET BMA C1297 11 HET MAN C1298 11 HET MAN C1299 11 HET NAG C1301 14 HET NAG C1302 14 HET BMA C1303 11 HET MAN C1304 11 HET MAN C1305 11 HET MAN C1306 11 HET MAN C1308 11 HET NAG C1332 14 HET NAG C1333 14 HET BMA C1334 11 HET MAN C1335 11 HET MAN C1336 11 HET MAN C1337 11 HET MAN C1339 11 HET MAN C1340 11 HET MAN C1341 11 HET MAN C1342 11 HET NAG C1343 14 HET NAG C1355 14 HET NAG C1356 14 HET NAG C1363 14 HET NAG C1364 14 HET BMA C1365 11 HET NAG C1386 14 HET NAG C1387 14 HET BMA C1388 11 HET NAG C1392 14 HET NAG C1393 14 HET NAG C1448 14 HET NAG C1449 14 HET NAG D1088 14 HET NAG D1089 14 HET BMA D1090 11 HET NAG D1133 14 HET NAG D1134 14 HET NAG D1156 14 HET NAG D1157 14 HET BMA D1158 11 HET NAG D1160 14 HET NAG D1161 14 HET BMA D1162 11 HET NAG D1197 14 HET NAG D1198 14 HET NAG D1234 14 HET NAG D1235 14 HET NAG D1262 14 HET NAG D1263 14 HET BMA D1264 11 HET MAN D1265 11 HET MAN D1266 11 HET MAN D1267 11 HET MAN D1268 11 HET NAG D1276 14 HET NAG D1277 14 HET BMA D1278 11 HET NAG D1295 14 HET NAG D1296 14 HET BMA D1297 11 HET MAN D1298 11 HET MAN D1299 11 HET NAG D1301 14 HET NAG D1302 14 HET BMA D1303 11 HET MAN D1304 11 HET MAN D1305 11 HET MAN D1306 11 HET MAN D1308 11 HET NAG D1332 14 HET NAG D1333 14 HET BMA D1334 11 HET MAN D1335 11 HET MAN D1336 11 HET MAN D1337 11 HET MAN D1339 11 HET MAN D1340 11 HET MAN D1341 11 HET MAN D1342 11 HET NAG D1343 14 HET NAG D1355 14 HET NAG D1356 14 HET NAG D1363 14 HET NAG D1364 14 HET BMA D1365 11 HET NAG D1386 14 HET NAG D1387 14 HET BMA D1388 11 HET NAG D1392 14 HET NAG D1393 14 HET NAG D1448 14 HET NAG D1449 14 HET NAG E1611 14 HET NAG E1612 14 HET NAG E1618 14 HET NAG E1637 14 HET NAG F1611 14 HET NAG F1612 14 HET NAG F1618 14 HET NAG F1637 14 HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE HETNAM NAG N-ACETYL-D-GLUCOSAMINE FORMUL 13 BMA 30(C6 H12 O6) FORMUL 14 MAN 51(C6 H12 O6) FORMUL 15 NAG 111(C8 H15 N O6) HELIX 1 1 ASN A 99 SER A 115 1 17 HELIX 2 2 LEU A 122 CYS A 126 5 5 HELIX 3 3 ASN A 195 THR A 198 5 4 HELIX 4 4 LYS A 335 LYS A 351 1 17 HELIX 5 5 ASP A 368 THR A 373 1 6 HELIX 6 6 THR A 387 LEU A 390 5 4 HELIX 7 7 ASN A 425 ARG A 429 5 5 HELIX 8 8 MET A 475 TYR A 484 1 10 HELIX 9 9 THR B 529 SER B 534 1 6 HELIX 10 10 THR B 536 SER B 546 1 11 HELIX 11 11 ILE B 573 TRP B 596 1 24 HELIX 12 12 ASN B 618 TRP B 623 1 6 HELIX 13 13 THR B 627 SER B 636 1 10 HELIX 14 14 TYR B 638 GLU B 648 1 11 HELIX 15 15 GLU B 648 GLU B 654 1 7 HELIX 16 16 ASN B 656 ALA B 662 1 7 HELIX 17 17 ASN C 99 SER C 115 1 17 HELIX 18 18 LEU C 122 CYS C 126 5 5 HELIX 19 19 ASN C 195 THR C 198 5 4 HELIX 20 20 LYS C 335 LYS C 351 1 17 HELIX 21 21 ASP C 368 THR C 373 1 6 HELIX 22 22 THR C 387 LEU C 390 5 4 HELIX 23 23 ASN C 425 ARG C 429 5 5 HELIX 24 24 MET C 475 TYR C 484 1 10 HELIX 25 25 ASN D 99 SER D 115 1 17 HELIX 26 26 LEU D 122 CYS D 126 5 5 HELIX 27 27 ASN D 195 THR D 198 5 4 HELIX 28 28 LYS D 335 LYS D 351 1 17 HELIX 29 29 ASP D 368 THR D 373 1 6 HELIX 30 30 THR D 387 LEU D 390 5 4 HELIX 31 31 ASN D 425 ARG D 429 5 5 HELIX 32 32 MET D 475 TYR D 484 1 10 HELIX 33 33 THR E 529 SER E 534 1 6 HELIX 34 34 THR E 536 SER E 546 1 11 HELIX 35 35 ILE E 573 TRP E 596 1 24 HELIX 36 36 ASN E 618 TRP E 623 1 6 HELIX 37 37 THR E 627 SER E 636 1 10 HELIX 38 38 TYR E 638 GLU E 648 1 11 HELIX 39 39 GLU E 648 GLU E 654 1 7 HELIX 40 40 ASN E 656 ALA E 662 1 7 HELIX 41 41 THR F 529 SER F 534 1 6 HELIX 42 42 THR F 536 SER F 546 1 11 HELIX 43 43 ILE F 573 TRP F 596 1 24 HELIX 44 44 ASN F 618 TRP F 623 1 6 HELIX 45 45 THR F 627 SER F 636 1 10 HELIX 46 46 TYR F 638 GLU F 648 1 11 HELIX 47 47 GLU F 648 GLU F 654 1 7 HELIX 48 48 ASN F 656 ALA F 662 1 7 HELIX 49 49 LEU G 63 SER G 65 5 3 HELIX 50 50 THR G 83 THR G 87 5 5 HELIX 51 51 LEU H 63 SER H 65 5 3 HELIX 52 52 THR H 83 THR H 87 5 5 HELIX 53 53 LEU I 63 SER I 65 5 3 HELIX 54 54 THR I 83 THR I 87 5 5 HELIX 55 55 GLN J 79 GLU J 83 5 5 HELIX 56 56 GLN K 79 GLU K 83 5 5 HELIX 57 57 GLN L 79 GLU L 83 5 5 SHEET 1 AA 3 LEU A 494 THR A 499 0 SHEET 2 AA 3 TRP A 35 TYR A 40 -1 O TRP A 35 N THR A 499 SHEET 3 AA 3 ILE B 603 CYS B 604 -1 O CYS B 604 N VAL A 38 SHEET 1 AB 5 TRP A 45 ASP A 47 0 SHEET 2 AB 5 TYR A 486 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AB 5 PHE A 223 CYS A 228 -1 O ALA A 224 N VAL A 489 SHEET 4 AB 5 VAL A 242 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 5 AB 5 GLU A 83 HIS A 85 -1 O ILE A 84 N THR A 244 SHEET 1 AC 2 PHE A 53 ALA A 55 0 SHEET 2 AC 2 HIS A 216 CYS A 218 -1 O HIS A 216 N ALA A 55 SHEET 1 AD 2 GLU A 92 ASN A 94 0 SHEET 2 AD 2 THR A 236 PRO A 238 -1 O GLY A 237 N PHE A 93 SHEET 1 AE 3 LEU A 129 CYS A 131 0 SHEET 2 AE 3 LYS A 189 LEU A 193 -1 O LYS A 189 N CYS A 131 SHEET 3 AE 3 VAL A 181 GLN A 183 -1 O VAL A 182 N ARG A 192 SHEET 1 AF 2 LEU A 154 MET A 161 0 SHEET 2 AF 2 GLN A 170 TYR A 177 -1 O GLN A 170 N MET A 161 SHEET 1 AG 3 ILE A 201 GLN A 203 0 SHEET 2 AG 3 ALA A 433 TYR A 435 1 O ALA A 433 N THR A 202 SHEET 3 AG 3 ILE A 423 ILE A 424 -1 O ILE A 424 N MET A 434 SHEET 1 AH 2 LEU A 259 LEU A 261 0 SHEET 2 AH 2 ILE A 443 ARG A 456 -1 N THR A 450 O LEU A 260 SHEET 1 AI 2 MET A 271 ARG A 273 0 SHEET 2 AI 2 ASN A 283 ARG A 298 -1 O LEU A 285 N ARG A 273 SHEET 1 AJ 9 HIS A 374 CYS A 378 0 SHEET 2 AJ 9 GLU A 381 CYS A 385 -1 O GLU A 381 N CYS A 378 SHEET 3 AJ 9 SER A 413 LYS A 421 -1 O ARG A 419 N TYR A 384 SHEET 4 AJ 9 HIS A 330 SER A 334 -1 O CYS A 331 N LEU A 416 SHEET 5 AJ 9 ASN A 283 ARG A 298 -1 O GLN A 293 N SER A 334 SHEET 6 AJ 9 ILE A 443 ARG A 456 -1 O ILE A 443 N ARG A 298 SHEET 7 AJ 9 THR A 465 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 8 AJ 9 ILE A 358 PHE A 361 1 O ILE A 358 N GLU A 466 SHEET 9 AJ 9 SER A 393 TRP A 395 -1 O SER A 393 N PHE A 361 SHEET 1 AK 6 HIS A 374 CYS A 378 0 SHEET 2 AK 6 GLU A 381 CYS A 385 -1 O GLU A 381 N CYS A 378 SHEET 3 AK 6 SER A 413 LYS A 421 -1 O ARG A 419 N TYR A 384 SHEET 4 AK 6 HIS A 330 SER A 334 -1 O CYS A 331 N LEU A 416 SHEET 5 AK 6 ASN A 283 ARG A 298 -1 O GLN A 293 N SER A 334 SHEET 6 AK 6 MET A 271 ARG A 273 -1 O MET A 271 N GLN A 287 SHEET 1 AL 2 SER A 306 ILE A 307 0 SHEET 2 AL 2 PHE A 317 TYR A 318 -1 O PHE A 317 N ILE A 307 SHEET 1 AM 2 GLY A 324 ASP A 325 0 SHEET 2 AM 2 ARG H 100A TYR H 100B 1 N TYR H 100B O GLY A 324 SHEET 1 CA 3 LEU C 494 THR C 499 0 SHEET 2 CA 3 TRP C 35 TYR C 40 -1 O TRP C 35 N THR C 499 SHEET 3 CA 3 ILE E 603 CYS E 604 -1 O CYS E 604 N VAL C 38 SHEET 1 CB 5 TRP C 45 ASP C 47 0 SHEET 2 CB 5 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 CB 5 PHE C 223 CYS C 228 -1 O ALA C 224 N VAL C 489 SHEET 4 CB 5 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 CB 5 GLU C 83 HIS C 85 -1 O ILE C 84 N THR C 244 SHEET 1 CC 2 PHE C 53 ALA C 55 0 SHEET 2 CC 2 HIS C 216 CYS C 218 -1 O HIS C 216 N ALA C 55 SHEET 1 CD 2 GLU C 92 ASN C 94 0 SHEET 2 CD 2 THR C 236 PRO C 238 -1 O GLY C 237 N PHE C 93 SHEET 1 CE 3 LEU C 129 CYS C 131 0 SHEET 2 CE 3 LYS C 189 LEU C 193 -1 O LYS C 189 N CYS C 131 SHEET 3 CE 3 VAL C 181 GLN C 183 -1 O VAL C 182 N ARG C 192 SHEET 1 CF 2 LEU C 154 MET C 161 0 SHEET 2 CF 2 GLN C 170 TYR C 177 -1 O GLN C 170 N MET C 161 SHEET 1 CG 3 ILE C 201 GLN C 203 0 SHEET 2 CG 3 ALA C 433 TYR C 435 1 O ALA C 433 N THR C 202 SHEET 3 CG 3 ILE C 423 ILE C 424 -1 O ILE C 424 N MET C 434 SHEET 1 CH 2 LEU C 259 LEU C 261 0 SHEET 2 CH 2 ILE C 443 ARG C 456 -1 N THR C 450 O LEU C 260 SHEET 1 CI 2 MET C 271 ARG C 273 0 SHEET 2 CI 2 ASN C 283 ARG C 298 1 O LEU C 285 N ARG C 273 SHEET 1 CJ 9 HIS C 374 CYS C 378 0 SHEET 2 CJ 9 GLU C 381 CYS C 385 -1 O GLU C 381 N CYS C 378 SHEET 3 CJ 9 SER C 413 LYS C 421 -1 O ARG C 419 N TYR C 384 SHEET 4 CJ 9 HIS C 330 SER C 334 -1 O CYS C 331 N LEU C 416 SHEET 5 CJ 9 ASN C 283 ARG C 298 -1 O GLN C 293 N SER C 334 SHEET 6 CJ 9 ILE C 443 ARG C 456 -1 O ILE C 443 N ARG C 298 SHEET 7 CJ 9 THR C 465 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 8 CJ 9 ILE C 358 PHE C 361 1 O ILE C 358 N GLU C 466 SHEET 9 CJ 9 SER C 393 TRP C 395 -1 O SER C 393 N PHE C 361 SHEET 1 CK 6 HIS C 374 CYS C 378 0 SHEET 2 CK 6 GLU C 381 CYS C 385 -1 O GLU C 381 N CYS C 378 SHEET 3 CK 6 SER C 413 LYS C 421 -1 O ARG C 419 N TYR C 384 SHEET 4 CK 6 HIS C 330 SER C 334 -1 O CYS C 331 N LEU C 416 SHEET 5 CK 6 ASN C 283 ARG C 298 -1 O GLN C 293 N SER C 334 SHEET 6 CK 6 MET C 271 ARG C 273 1 O MET C 271 N GLN C 287 SHEET 1 CL 2 SER C 306 ILE C 307 0 SHEET 2 CL 2 PHE C 317 TYR C 318 -1 O PHE C 317 N ILE C 307 SHEET 1 CM 2 GLY C 324 ASP C 325 0 SHEET 2 CM 2 ARG G 100A TYR G 100B 1 N TYR G 100B O GLY C 324 SHEET 1 DA 3 LEU D 494 THR D 499 0 SHEET 2 DA 3 TRP D 35 TYR D 40 -1 O TRP D 35 N THR D 499 SHEET 3 DA 3 ILE F 603 CYS F 604 -1 O CYS F 604 N VAL D 38 SHEET 1 DB 5 TRP D 45 ASP D 47 0 SHEET 2 DB 5 TYR D 486 ILE D 491 -1 O LYS D 490 N LYS D 46 SHEET 3 DB 5 PHE D 223 CYS D 228 -1 O ALA D 224 N VAL D 489 SHEET 4 DB 5 VAL D 242 VAL D 245 -1 O SER D 243 N LYS D 227 SHEET 5 DB 5 GLU D 83 HIS D 85 -1 O ILE D 84 N THR D 244 SHEET 1 DC 2 PHE D 53 ALA D 55 0 SHEET 2 DC 2 HIS D 216 CYS D 218 -1 O HIS D 216 N ALA D 55 SHEET 1 DD 2 GLU D 92 ASN D 94 0 SHEET 2 DD 2 THR D 236 PRO D 238 -1 O GLY D 237 N PHE D 93 SHEET 1 DE 3 LEU D 129 CYS D 131 0 SHEET 2 DE 3 LYS D 189 LEU D 193 -1 O LYS D 189 N CYS D 131 SHEET 3 DE 3 VAL D 181 GLN D 183 -1 O VAL D 182 N ARG D 192 SHEET 1 DF 2 LEU D 154 MET D 161 0 SHEET 2 DF 2 GLN D 170 TYR D 177 -1 O GLN D 170 N MET D 161 SHEET 1 DG 3 ILE D 201 GLN D 203 0 SHEET 2 DG 3 ALA D 433 TYR D 435 1 O ALA D 433 N THR D 202 SHEET 3 DG 3 ILE D 423 ILE D 424 -1 O ILE D 424 N MET D 434 SHEET 1 DH 2 LEU D 259 LEU D 261 0 SHEET 2 DH 2 ILE D 443 ARG D 456 -1 N THR D 450 O LEU D 260 SHEET 1 DI 2 MET D 271 ARG D 273 0 SHEET 2 DI 2 ASN D 283 ARG D 298 1 O LEU D 285 N ARG D 273 SHEET 1 DJ 9 HIS D 374 CYS D 378 0 SHEET 2 DJ 9 GLU D 381 CYS D 385 -1 O GLU D 381 N CYS D 378 SHEET 3 DJ 9 SER D 413 LYS D 421 -1 O ARG D 419 N TYR D 384 SHEET 4 DJ 9 HIS D 330 SER D 334 -1 O CYS D 331 N LEU D 416 SHEET 5 DJ 9 ASN D 283 ARG D 298 -1 O GLN D 293 N SER D 334 SHEET 6 DJ 9 ILE D 443 ARG D 456 -1 O ILE D 443 N ARG D 298 SHEET 7 DJ 9 THR D 465 PRO D 470 -1 O ARG D 469 N THR D 455 SHEET 8 DJ 9 ILE D 358 PHE D 361 1 O ILE D 358 N GLU D 466 SHEET 9 DJ 9 SER D 393 TRP D 395 -1 O SER D 393 N PHE D 361 SHEET 1 DK 6 HIS D 374 CYS D 378 0 SHEET 2 DK 6 GLU D 381 CYS D 385 -1 O GLU D 381 N CYS D 378 SHEET 3 DK 6 SER D 413 LYS D 421 -1 O ARG D 419 N TYR D 384 SHEET 4 DK 6 HIS D 330 SER D 334 -1 O CYS D 331 N LEU D 416 SHEET 5 DK 6 ASN D 283 ARG D 298 -1 O GLN D 293 N SER D 334 SHEET 6 DK 6 MET D 271 ARG D 273 1 O MET D 271 N GLN D 287 SHEET 1 DL 2 SER D 306 ILE D 307 0 SHEET 2 DL 2 PHE D 317 TYR D 318 -1 O PHE D 317 N ILE D 307 SHEET 1 DM 2 GLY D 324 ASP D 325 0 SHEET 2 DM 2 ARG I 100A TYR I 100B 1 N TYR I 100B O GLY D 324 SHEET 1 GA 3 LEU G 18 ALA G 23 0 SHEET 2 GA 3 LEU G 77 LEU G 82 -1 O VAL G 78 N CYS G 22 SHEET 3 GA 3 LEU G 67 ASP G 72 -1 O THR G 68 N LYS G 81 SHEET 1 GB 5 TRP G 56 HIS G 59 0 SHEET 2 GB 5 TRP G 47 SER G 52 -1 O SER G 50 N TYR G 58 SHEET 3 GB 5 PHE G 35 GLN G 39 -1 O TRP G 35A N LEU G 51 SHEET 4 GB 5 ALA G 88 GLU G 98 -1 O THR G 89 N GLN G 39 SHEET 5 GB 5 LYS G 100G TRP G 103 -1 O LYS G 100G N GLU G 98 SHEET 1 GC 5 TRP G 56 HIS G 59 0 SHEET 2 GC 5 TRP G 47 SER G 52 -1 O SER G 50 N TYR G 58 SHEET 3 GC 5 PHE G 35 GLN G 39 -1 O TRP G 35A N LEU G 51 SHEET 4 GC 5 ALA G 88 GLU G 98 -1 O THR G 89 N GLN G 39 SHEET 5 GC 5 THR G 107 VAL G 109 -1 O THR G 107 N TYR G 90 SHEET 1 GD 2 LYS G 100G TRP G 103 0 SHEET 2 GD 2 ALA G 88 GLU G 98 -1 O ARG G 94 N ASP G 101 SHEET 1 HA 3 LEU H 18 ALA H 23 0 SHEET 2 HA 3 LEU H 77 LEU H 82 -1 O VAL H 78 N CYS H 22 SHEET 3 HA 3 LEU H 67 ASP H 72 -1 O THR H 68 N LYS H 81 SHEET 1 HB 5 TRP H 56 HIS H 59 0 SHEET 2 HB 5 TRP H 47 SER H 52 -1 O SER H 50 N TYR H 58 SHEET 3 HB 5 PHE H 35 GLN H 39 -1 O TRP H 35A N LEU H 51 SHEET 4 HB 5 ALA H 88 GLU H 98 -1 O THR H 89 N GLN H 39 SHEET 5 HB 5 LYS H 100G TRP H 103 -1 O LYS H 100G N GLU H 98 SHEET 1 HC 5 TRP H 56 HIS H 59 0 SHEET 2 HC 5 TRP H 47 SER H 52 -1 O SER H 50 N TYR H 58 SHEET 3 HC 5 PHE H 35 GLN H 39 -1 O TRP H 35A N LEU H 51 SHEET 4 HC 5 ALA H 88 GLU H 98 -1 O THR H 89 N GLN H 39 SHEET 5 HC 5 THR H 107 VAL H 109 -1 O THR H 107 N TYR H 90 SHEET 1 HD 2 LYS H 100G TRP H 103 0 SHEET 2 HD 2 ALA H 88 GLU H 98 -1 O ARG H 94 N ASP H 101 SHEET 1 IA 3 LEU I 18 ALA I 23 0 SHEET 2 IA 3 LEU I 77 LEU I 82 -1 O VAL I 78 N CYS I 22 SHEET 3 IA 3 LEU I 67 ASP I 72 -1 O THR I 68 N LYS I 81 SHEET 1 IB 5 TRP I 56 HIS I 59 0 SHEET 2 IB 5 TRP I 47 SER I 52 -1 O SER I 50 N TYR I 58 SHEET 3 IB 5 PHE I 35 GLN I 39 -1 O TRP I 35A N LEU I 51 SHEET 4 IB 5 ALA I 88 GLU I 98 -1 O THR I 89 N GLN I 39 SHEET 5 IB 5 LYS I 100G TRP I 103 -1 O LYS I 100G N GLU I 98 SHEET 1 IC 5 TRP I 56 HIS I 59 0 SHEET 2 IC 5 TRP I 47 SER I 52 -1 O SER I 50 N TYR I 58 SHEET 3 IC 5 PHE I 35 GLN I 39 -1 O TRP I 35A N LEU I 51 SHEET 4 IC 5 ALA I 88 GLU I 98 -1 O THR I 89 N GLN I 39 SHEET 5 IC 5 THR I 107 VAL I 109 -1 O THR I 107 N TYR I 90 SHEET 1 ID 2 LYS I 100G TRP I 103 0 SHEET 2 ID 2 ALA I 88 GLU I 98 -1 O ARG I 94 N ASP I 101 SHEET 1 JA 4 SER J 9 SER J 12 0 SHEET 2 JA 4 THR J 102 THR J 105 1 O LYS J 103 N ALA J 11 SHEET 3 JA 4 ALA J 84 VAL J 92 -1 O ALA J 84 N LEU J 104 SHEET 4 JA 4 ASP J 95A PHE J 98 1 O ASP J 95A N VAL J 92 SHEET 1 JB 5 SER J 9 SER J 12 0 SHEET 2 JB 5 THR J 102 THR J 105 1 O LYS J 103 N ALA J 11 SHEET 3 JB 5 ALA J 84 VAL J 92 -1 O ALA J 84 N LEU J 104 SHEET 4 JB 5 VAL J 33 GLN J 38 -1 O SER J 34 N GLY J 89 SHEET 5 JB 5 LYS J 45 ILE J 48 -1 O LYS J 45 N GLN J 37 SHEET 1 JC 2 ASP J 95A PHE J 98 0 SHEET 2 JC 2 ALA J 84 VAL J 92 1 O SER J 90 N ILE J 97 SHEET 1 JD 3 SER J 18 THR J 24 0 SHEET 2 JD 3 THR J 70 SER J 76 -1 O ALA J 71 N CYS J 23 SHEET 3 JD 3 PHE J 62 SER J 67 -1 O SER J 63 N THR J 74 SHEET 1 KA 4 SER K 9 SER K 12 0 SHEET 2 KA 4 THR K 102 THR K 105 1 O LYS K 103 N ALA K 11 SHEET 3 KA 4 ALA K 84 VAL K 92 -1 O ALA K 84 N LEU K 104 SHEET 4 KA 4 ASP K 95A PHE K 98 1 O ASP K 95A N VAL K 92 SHEET 1 KB 5 SER K 9 SER K 12 0 SHEET 2 KB 5 THR K 102 THR K 105 1 O LYS K 103 N ALA K 11 SHEET 3 KB 5 ALA K 84 VAL K 92 -1 O ALA K 84 N LEU K 104 SHEET 4 KB 5 VAL K 33 GLN K 38 -1 O SER K 34 N GLY K 89 SHEET 5 KB 5 LYS K 45 ILE K 48 -1 O LYS K 45 N GLN K 37 SHEET 1 KC 2 ASP K 95A PHE K 98 0 SHEET 2 KC 2 ALA K 84 VAL K 92 1 O SER K 90 N ILE K 97 SHEET 1 KD 3 SER K 18 THR K 24 0 SHEET 2 KD 3 THR K 70 SER K 76 -1 O ALA K 71 N CYS K 23 SHEET 3 KD 3 PHE K 62 SER K 67 -1 O SER K 63 N THR K 74 SHEET 1 LA 4 SER L 9 SER L 12 0 SHEET 2 LA 4 THR L 102 THR L 105 1 O LYS L 103 N ALA L 11 SHEET 3 LA 4 ALA L 84 VAL L 92 -1 O ALA L 84 N LEU L 104 SHEET 4 LA 4 ASP L 95A PHE L 98 1 O ASP L 95A N VAL L 92 SHEET 1 LB 5 SER L 9 SER L 12 0 SHEET 2 LB 5 THR L 102 THR L 105 1 O LYS L 103 N ALA L 11 SHEET 3 LB 5 ALA L 84 VAL L 92 -1 O ALA L 84 N LEU L 104 SHEET 4 LB 5 VAL L 33 GLN L 38 -1 O SER L 34 N GLY L 89 SHEET 5 LB 5 LYS L 45 ILE L 48 -1 O LYS L 45 N GLN L 37 SHEET 1 LC 2 ASP L 95A PHE L 98 0 SHEET 2 LC 2 ALA L 84 VAL L 92 1 O SER L 90 N ILE L 97 SHEET 1 LD 3 SER L 18 THR L 24 0 SHEET 2 LD 3 THR L 70 SER L 76 -1 O ALA L 71 N CYS L 23 SHEET 3 LD 3 PHE L 62 SER L 67 -1 O SER L 63 N THR L 74 SSBOND 1 CYS A 54 CYS A 74 1555 1555 2.10 SSBOND 2 CYS A 119 CYS A 205 1555 1555 2.11 SSBOND 3 CYS A 126 CYS A 196 1555 1555 2.11 SSBOND 4 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 5 CYS A 218 CYS A 247 1555 1555 2.04 SSBOND 6 CYS A 228 CYS A 239 1555 1555 1.62 SSBOND 7 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 8 CYS A 378 CYS A 445 1555 1555 2.11 SSBOND 9 CYS A 385 CYS A 418 1555 1555 2.09 SSBOND 10 CYS A 501 CYS B 605 1555 1555 2.22 SSBOND 11 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 12 CYS C 54 CYS C 74 1555 1555 2.10 SSBOND 13 CYS C 119 CYS C 205 1555 1555 2.11 SSBOND 14 CYS C 126 CYS C 196 1555 1555 2.11 SSBOND 15 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 16 CYS C 218 CYS C 247 1555 1555 2.04 SSBOND 17 CYS C 228 CYS C 239 1555 1555 1.62 SSBOND 18 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 19 CYS C 378 CYS C 445 1555 1555 2.11 SSBOND 20 CYS C 385 CYS C 418 1555 1555 2.09 SSBOND 21 CYS C 501 CYS E 605 1555 1555 2.22 SSBOND 22 CYS D 54 CYS D 74 1555 1555 2.10 SSBOND 23 CYS D 119 CYS D 205 1555 1555 2.11 SSBOND 24 CYS D 126 CYS D 196 1555 1555 2.11 SSBOND 25 CYS D 131 CYS D 157 1555 1555 2.03 SSBOND 26 CYS D 218 CYS D 247 1555 1555 2.04 SSBOND 27 CYS D 228 CYS D 239 1555 1555 1.62 SSBOND 28 CYS D 296 CYS D 331 1555 1555 2.03 SSBOND 29 CYS D 378 CYS D 445 1555 1555 2.11 SSBOND 30 CYS D 385 CYS D 418 1555 1555 2.09 SSBOND 31 CYS D 501 CYS F 605 1555 1555 2.22 SSBOND 32 CYS E 598 CYS E 604 1555 1555 2.03 SSBOND 33 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 34 CYS G 22 CYS G 92 1555 1555 2.03 SSBOND 35 CYS G 32 CYS G 52B 1555 1555 2.14 SSBOND 36 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 37 CYS H 32 CYS H 52B 1555 1555 2.14 SSBOND 38 CYS I 22 CYS I 92 1555 1555 2.03 SSBOND 39 CYS I 32 CYS I 52B 1555 1555 2.14 SSBOND 40 CYS J 23 CYS J 88 1555 1555 2.05 SSBOND 41 CYS K 23 CYS K 88 1555 1555 2.05 SSBOND 42 CYS L 23 CYS L 88 1555 1555 2.05 LINK ND2 ASN A 88 C1 NAG A1088 1555 1555 1.42 LINK ND2 ASN A 133 C1 NAG A1133 1555 1555 1.40 LINK ND2 ASN A 156 C1 NAG A1156 1555 1555 1.34 LINK ND2 ASN A 160 C1 NAG A1160 1555 1555 1.33 LINK ND2 ASN A 197 C1 NAG A1197 1555 1555 1.29 LINK ND2 ASN A 234 C1 NAG A1234 1555 1555 1.15 LINK ND2 ASN A 262 C1 NAG A1262 1555 1555 1.62 LINK ND2 ASN A 276 C1 NAG A1276 1555 1555 1.42 LINK ND2 ASN A 295 C1 NAG A1295 1555 1555 1.45 LINK ND2 ASN A 301 C1 NAG A1301 1555 1555 1.41 LINK ND2 ASN A 332 C1 NAG A1332 1555 1555 1.03 LINK ND2 ASN A 339 C1 NAG A1343 1555 1555 1.55 LINK ND2 ASN A 355 C1 NAG A1355 1555 1555 1.45 LINK ND2 ASN A 363 C1 NAG A1363 1555 1555 1.54 LINK ND2 ASN A 386 C1 NAG A1386 1555 1555 1.50 LINK ND2 ASN A 392 C1 NAG A1392 1555 1555 1.50 LINK ND2 ASN A 448 C1 NAG A1448 1555 1555 1.36 LINK O4 NAG A1088 C1 NAG A1089 1555 1555 1.39 LINK O4 NAG A1089 C1 BMA A1090 1555 1555 1.41 LINK O4 NAG A1133 C1 NAG A1134 1555 1555 1.39 LINK O4 NAG A1156 C1 NAG A1157 1555 1555 1.39 LINK O4 NAG A1157 C1 BMA A1158 1555 1555 1.41 LINK O4 NAG A1160 C1 NAG A1161 1555 1555 1.39 LINK O4 NAG A1161 C1 BMA A1162 1555 1555 1.41 LINK O4 NAG A1197 C1 NAG A1198 1555 1555 1.39 LINK O4 NAG A1234 C1 NAG A1235 1555 1555 1.39 LINK O4 NAG A1262 C1 NAG A1263 1555 1555 1.44 LINK O4 NAG A1263 C1 BMA A1264 1555 1555 1.44 LINK O3 BMA A1264 C1 MAN A1267 1555 1555 1.44 LINK O6 BMA A1264 C1 MAN A1265 1555 1555 1.44 LINK O3 MAN A1265 C1 MAN A1266 1555 1555 1.38 LINK O2 MAN A1267 C1 MAN A1268 1555 1555 1.44 LINK O4 NAG A1276 C1 NAG A1277 1555 1555 1.39 LINK O4 NAG A1277 C1 BMA A1278 1555 1555 1.41 LINK O4 NAG A1295 C1 NAG A1296 1555 1555 1.39 LINK O4 NAG A1296 C1 BMA A1297 1555 1555 1.41 LINK O3 BMA A1297 C1 MAN A1298 1555 1555 1.41 LINK O6 BMA A1297 C1 MAN A1299 1555 1555 1.40 LINK O4 NAG A1301 C1 NAG A1302 1555 1555 1.39 LINK O4 NAG A1302 C1 BMA A1303 1555 1555 1.40 LINK O3 BMA A1303 C1 MAN A1304 1555 1555 1.34 LINK O6 BMA A1303 C1 MAN A1305 1555 1555 1.41 LINK O3 MAN A1305 C1 MAN A1306 1555 1555 1.43 LINK O6 MAN A1305 C1 MAN A1308 1555 1555 1.50 LINK O4 NAG A1332 C1 NAG A1333 1555 1555 1.43 LINK O4 NAG A1333 C1 BMA A1334 1555 1555 1.43 LINK O3 BMA A1334 C1 MAN A1335 1555 1555 1.43 LINK O6 BMA A1334 C1 MAN A1336 1555 1555 1.40 LINK O2 MAN A1335 C1 MAN A1339 1555 1555 1.43 LINK O3 MAN A1336 C1 MAN A1337 1555 1555 1.42 LINK O6 MAN A1336 C1 MAN A1341 1555 1555 1.40 LINK O2 MAN A1339 C1 MAN A1340 1555 1555 1.40 LINK O2 MAN A1341 C1 MAN A1342 1555 1555 1.44 LINK O4 NAG A1355 C1 NAG A1356 1555 1555 1.39 LINK O4 NAG A1363 C1 NAG A1364 1555 1555 1.39 LINK O4 NAG A1364 C1 BMA A1365 1555 1555 1.41 LINK O4 NAG A1386 C1 NAG A1387 1555 1555 1.39 LINK O4 NAG A1387 C1 BMA A1388 1555 1555 1.41 LINK O4 NAG A1392 C1 NAG A1393 1555 1555 1.39 LINK O4 NAG A1448 C1 NAG A1449 1555 1555 1.39 LINK ND2 ASN B 611 C1 NAG B1611 1555 1555 1.29 LINK ND2 ASN B 618 C1 NAG B1618 1555 1555 1.33 LINK ND2 ASN B 637 C1 NAG B1637 1555 1555 1.52 LINK O4 NAG B1611 C1 NAG B1612 1555 1555 1.39 LINK ND2 ASN C 88 C1 NAG C1088 1555 1555 1.42 LINK ND2 ASN C 133 C1 NAG C1133 1555 1555 1.40 LINK ND2 ASN C 156 C1 NAG C1156 1555 1555 1.34 LINK ND2 ASN C 160 C1 NAG C1160 1555 1555 1.33 LINK ND2 ASN C 197 C1 NAG C1197 1555 1555 1.29 LINK ND2 ASN C 234 C1 NAG C1234 1555 1555 1.15 LINK ND2 ASN C 262 C1 NAG C1262 1555 1555 1.62 LINK ND2 ASN C 276 C1 NAG C1276 1555 1555 1.42 LINK ND2 ASN C 295 C1 NAG C1295 1555 1555 1.45 LINK ND2 ASN C 301 C1 NAG C1301 1555 1555 1.41 LINK ND2 ASN C 332 C1 NAG C1332 1555 1555 1.03 LINK ND2 ASN C 339 C1 NAG C1343 1555 1555 1.55 LINK ND2 ASN C 355 C1 NAG C1355 1555 1555 1.45 LINK ND2 ASN C 363 C1 NAG C1363 1555 1555 1.54 LINK ND2 ASN C 386 C1 NAG C1386 1555 1555 1.50 LINK ND2 ASN C 392 C1 NAG C1392 1555 1555 1.50 LINK ND2 ASN C 448 C1 NAG C1448 1555 1555 1.36 LINK O4 NAG C1088 C1 NAG C1089 1555 1555 1.39 LINK O4 NAG C1089 C1 BMA C1090 1555 1555 1.41 LINK O4 NAG C1133 C1 NAG C1134 1555 1555 1.39 LINK O4 NAG C1156 C1 NAG C1157 1555 1555 1.39 LINK O4 NAG C1157 C1 BMA C1158 1555 1555 1.41 LINK O4 NAG C1160 C1 NAG C1161 1555 1555 1.39 LINK O4 NAG C1161 C1 BMA C1162 1555 1555 1.41 LINK O4 NAG C1197 C1 NAG C1198 1555 1555 1.39 LINK O4 NAG C1234 C1 NAG C1235 1555 1555 1.39 LINK O4 NAG C1262 C1 NAG C1263 1555 1555 1.44 LINK O4 NAG C1263 C1 BMA C1264 1555 1555 1.44 LINK O3 BMA C1264 C1 MAN C1267 1555 1555 1.44 LINK O6 BMA C1264 C1 MAN C1265 1555 1555 1.44 LINK O3 MAN C1265 C1 MAN C1266 1555 1555 1.38 LINK O2 MAN C1267 C1 MAN C1268 1555 1555 1.44 LINK O4 NAG C1276 C1 NAG C1277 1555 1555 1.39 LINK O4 NAG C1277 C1 BMA C1278 1555 1555 1.41 LINK O4 NAG C1295 C1 NAG C1296 1555 1555 1.39 LINK O4 NAG C1296 C1 BMA C1297 1555 1555 1.41 LINK O3 BMA C1297 C1 MAN C1298 1555 1555 1.40 LINK O6 BMA C1297 C1 MAN C1299 1555 1555 1.40 LINK O4 NAG C1301 C1 NAG C1302 1555 1555 1.39 LINK O4 NAG C1302 C1 BMA C1303 1555 1555 1.40 LINK O3 BMA C1303 C1 MAN C1304 1555 1555 1.34 LINK O6 BMA C1303 C1 MAN C1305 1555 1555 1.41 LINK O6 MAN C1305 C1 MAN C1308 1555 1555 1.50 LINK O3 MAN C1305 C1 MAN C1306 1555 1555 1.43 LINK O4 NAG C1332 C1 NAG C1333 1555 1555 1.43 LINK O4 NAG C1333 C1 BMA C1334 1555 1555 1.43 LINK O3 BMA C1334 C1 MAN C1335 1555 1555 1.43 LINK O6 BMA C1334 C1 MAN C1336 1555 1555 1.40 LINK O2 MAN C1335 C1 MAN C1339 1555 1555 1.43 LINK O6 MAN C1336 C1 MAN C1341 1555 1555 1.40 LINK O3 MAN C1336 C1 MAN C1337 1555 1555 1.42 LINK O2 MAN C1339 C1 MAN C1340 1555 1555 1.40 LINK O2 MAN C1341 C1 MAN C1342 1555 1555 1.44 LINK O4 NAG C1355 C1 NAG C1356 1555 1555 1.39 LINK O4 NAG C1363 C1 NAG C1364 1555 1555 1.39 LINK O4 NAG C1364 C1 BMA C1365 1555 1555 1.41 LINK O4 NAG C1386 C1 NAG C1387 1555 1555 1.39 LINK O4 NAG C1387 C1 BMA C1388 1555 1555 1.41 LINK O4 NAG C1392 C1 NAG C1393 1555 1555 1.39 LINK O4 NAG C1448 C1 NAG C1449 1555 1555 1.39 LINK ND2 ASN D 88 C1 NAG D1088 1555 1555 1.42 LINK ND2 ASN D 133 C1 NAG D1133 1555 1555 1.40 LINK ND2 ASN D 156 C1 NAG D1156 1555 1555 1.34 LINK ND2 ASN D 160 C1 NAG D1160 1555 1555 1.33 LINK ND2 ASN D 197 C1 NAG D1197 1555 1555 1.29 LINK ND2 ASN D 234 C1 NAG D1234 1555 1555 1.15 LINK ND2 ASN D 262 C1 NAG D1262 1555 1555 1.61 LINK ND2 ASN D 276 C1 NAG D1276 1555 1555 1.42 LINK ND2 ASN D 295 C1 NAG D1295 1555 1555 1.45 LINK ND2 ASN D 301 C1 NAG D1301 1555 1555 1.41 LINK ND2 ASN D 332 C1 NAG D1332 1555 1555 1.03 LINK ND2 ASN D 339 C1 NAG D1343 1555 1555 1.55 LINK ND2 ASN D 355 C1 NAG D1355 1555 1555 1.45 LINK ND2 ASN D 363 C1 NAG D1363 1555 1555 1.54 LINK ND2 ASN D 386 C1 NAG D1386 1555 1555 1.50 LINK ND2 ASN D 392 C1 NAG D1392 1555 1555 1.50 LINK ND2 ASN D 448 C1 NAG D1448 1555 1555 1.36 LINK O4 NAG D1088 C1 NAG D1089 1555 1555 1.39 LINK O4 NAG D1089 C1 BMA D1090 1555 1555 1.41 LINK O4 NAG D1133 C1 NAG D1134 1555 1555 1.39 LINK O4 NAG D1156 C1 NAG D1157 1555 1555 1.39 LINK O4 NAG D1157 C1 BMA D1158 1555 1555 1.41 LINK O4 NAG D1160 C1 NAG D1161 1555 1555 1.39 LINK O4 NAG D1161 C1 BMA D1162 1555 1555 1.41 LINK O4 NAG D1197 C1 NAG D1198 1555 1555 1.39 LINK O4 NAG D1234 C1 NAG D1235 1555 1555 1.39 LINK O4 NAG D1262 C1 NAG D1263 1555 1555 1.44 LINK O4 NAG D1263 C1 BMA D1264 1555 1555 1.44 LINK O6 BMA D1264 C1 MAN D1265 1555 1555 1.44 LINK O3 BMA D1264 C1 MAN D1267 1555 1555 1.44 LINK O3 MAN D1265 C1 MAN D1266 1555 1555 1.38 LINK O2 MAN D1267 C1 MAN D1268 1555 1555 1.44 LINK O4 NAG D1276 C1 NAG D1277 1555 1555 1.39 LINK O4 NAG D1277 C1 BMA D1278 1555 1555 1.41 LINK O4 NAG D1295 C1 NAG D1296 1555 1555 1.39 LINK O4 NAG D1296 C1 BMA D1297 1555 1555 1.41 LINK O6 BMA D1297 C1 MAN D1299 1555 1555 1.40 LINK O3 BMA D1297 C1 MAN D1298 1555 1555 1.41 LINK O4 NAG D1301 C1 NAG D1302 1555 1555 1.39 LINK O4 NAG D1302 C1 BMA D1303 1555 1555 1.40 LINK O6 BMA D1303 C1 MAN D1305 1555 1555 1.41 LINK O3 BMA D1303 C1 MAN D1304 1555 1555 1.34 LINK O6 MAN D1305 C1 MAN D1308 1555 1555 1.50 LINK O3 MAN D1305 C1 MAN D1306 1555 1555 1.43 LINK O4 NAG D1332 C1 NAG D1333 1555 1555 1.43 LINK O4 NAG D1333 C1 BMA D1334 1555 1555 1.43 LINK O6 BMA D1334 C1 MAN D1336 1555 1555 1.40 LINK O3 BMA D1334 C1 MAN D1335 1555 1555 1.43 LINK O2 MAN D1335 C1 MAN D1339 1555 1555 1.43 LINK O6 MAN D1336 C1 MAN D1341 1555 1555 1.40 LINK O3 MAN D1336 C1 MAN D1337 1555 1555 1.42 LINK O2 MAN D1339 C1 MAN D1340 1555 1555 1.40 LINK O2 MAN D1341 C1 MAN D1342 1555 1555 1.44 LINK O4 NAG D1355 C1 NAG D1356 1555 1555 1.39 LINK O4 NAG D1363 C1 NAG D1364 1555 1555 1.39 LINK O4 NAG D1364 C1 BMA D1365 1555 1555 1.41 LINK O4 NAG D1386 C1 NAG D1387 1555 1555 1.39 LINK O4 NAG D1387 C1 BMA D1388 1555 1555 1.41 LINK O4 NAG D1392 C1 NAG D1393 1555 1555 1.39 LINK O4 NAG D1448 C1 NAG D1449 1555 1555 1.39 LINK ND2 ASN E 611 C1 NAG E1611 1555 1555 1.29 LINK ND2 ASN E 618 C1 NAG E1618 1555 1555 1.33 LINK ND2 ASN E 637 C1 NAG E1637 1555 1555 1.52 LINK O4 NAG E1611 C1 NAG E1612 1555 1555 1.39 LINK ND2 ASN F 611 C1 NAG F1611 1555 1555 1.29 LINK ND2 ASN F 618 C1 NAG F1618 1555 1555 1.33 LINK ND2 ASN F 637 C1 NAG F1637 1555 1555 1.52 LINK O4 NAG F1611 C1 NAG F1612 1555 1555 1.39 CISPEP 1 ILE A 138 THR A 139 0 -0.99 CISPEP 2 GLY A 312 PRO A 313 0 2.91 CISPEP 3 ASN A 411 ASP A 412 0 -21.07 CISPEP 4 ILE C 138 THR C 139 0 -0.98 CISPEP 5 GLY C 312 PRO C 313 0 2.87 CISPEP 6 ASN C 411 ASP C 412 0 -21.04 CISPEP 7 ILE D 138 THR D 139 0 -0.99 CISPEP 8 GLY D 312 PRO D 313 0 2.82 CISPEP 9 ASN D 411 ASP D 412 0 -21.03 CISPEP 10 SER J 27 ASN J 30 0 6.02 CISPEP 11 SER K 27 ASN K 30 0 6.12 CISPEP 12 SER L 27 ASN L 30 0 6.06 SITE 1 AC1 4 ASN A 88 NAG A1089 GLY B 527 SER B 528 SITE 1 AC2 2 NAG A1088 BMA A1090 SITE 1 AC3 1 NAG A1089 SITE 1 AC4 2 ASN A 133 NAG A1134 SITE 1 AC5 1 NAG A1133 SITE 1 AC6 3 ASN A 156 TYR A 173 NAG A1157 SITE 1 AC7 2 NAG A1156 BMA A1158 SITE 1 AC8 1 NAG A1157 SITE 1 AC9 3 GLN A 130 ASN A 160 NAG A1161 SITE 1 BC1 2 NAG A1160 BMA A1162 SITE 1 BC2 1 NAG A1161 SITE 1 BC3 3 ILE A 194 ASN A 197 NAG A1198 SITE 1 BC4 1 NAG A1197 SITE 1 BC5 3 ASN A 234 SER A 274 NAG A1235 SITE 1 BC6 1 NAG A1234 SITE 1 BC7 5 ASN A 262 VAL A 446 SER A 447 NAG A1263 SITE 2 BC7 5 NAG A1448 SITE 1 BC8 2 NAG A1262 BMA A1264 SITE 1 BC9 3 NAG A1263 MAN A1265 MAN A1267 SITE 1 CC1 2 BMA A1264 MAN A1266 SITE 1 CC2 1 MAN A1265 SITE 1 CC3 2 BMA A1264 MAN A1268 SITE 1 CC4 1 MAN A1267 SITE 1 CC5 3 ASN A 276 ASN A 279 NAG A1277 SITE 1 CC6 2 NAG A1276 BMA A1278 SITE 1 CC7 1 NAG A1277 SITE 1 CC8 2 ASN A 295 NAG A1296 SITE 1 CC9 2 NAG A1295 BMA A1297 SITE 1 DC1 3 NAG A1296 MAN A1298 MAN A1299 SITE 1 DC2 1 BMA A1297 SITE 1 DC3 1 BMA A1297 SITE 1 DC4 5 ASN A 301 NAG A1302 HIS H 52A CYS H 52B SITE 2 DC4 5 ALA H 52C SITE 1 DC5 7 NAG A1301 BMA A1303 MAN A1305 MAN A1308 SITE 2 DC5 7 ALA H 30 ALA H 31 HIS H 52A SITE 1 DC6 4 NAG A1302 MAN A1304 MAN A1305 THR H 73 SITE 1 DC7 2 BMA A1303 HIS H 52A SITE 1 DC8 4 NAG A1302 BMA A1303 MAN A1306 MAN A1308 SITE 1 DC9 1 MAN A1305 SITE 1 EC1 3 NAG A1302 MAN A1305 SER H 28 SITE 1 EC2 4 THR A 297 ASN A 332 ARG A 444 NAG A1333 SITE 1 EC3 2 NAG A1332 BMA A1334 SITE 1 EC4 4 NAG A1333 MAN A1335 MAN A1336 MAN A1339 SITE 1 EC5 2 BMA A1334 MAN A1339 SITE 1 EC6 4 BMA A1334 MAN A1337 MAN A1341 ASN L 94 SITE 1 EC7 1 MAN A1336 SITE 1 EC8 4 BMA A1334 MAN A1335 MAN A1340 THR H 57 SITE 1 EC9 6 MAN A1339 MAN A1342 TYR H 58 HIS H 59 SITE 2 EC9 6 LYS H 64 TRP L 95 SITE 1 FC1 3 MAN A1336 MAN A1342 ASN L 94 SITE 1 FC2 5 MAN A1340 MAN A1341 PRO H 61 ASN L 94 SITE 2 FC2 5 TRP L 95 SITE 1 FC3 2 ASN A 339 TRP A 395 SITE 1 FC4 2 ASN A 355 NAG A1356 SITE 1 FC5 1 NAG A1355 SITE 1 FC6 5 ASN A 363 THR A 372 NAG A1364 NAG A1386 SITE 2 FC6 5 NAG A1387 SITE 1 FC7 3 NAG A1363 BMA A1365 NAG A1387 SITE 1 FC8 1 NAG A1364 SITE 1 FC9 4 ASN A 386 NAG A1363 NAG A1387 NAG A1392 SITE 1 GC1 4 NAG A1363 NAG A1364 NAG A1386 BMA A1388 SITE 1 GC2 1 NAG A1387 SITE 1 GC3 3 ASN A 392 NAG A1386 NAG A1393 SITE 1 GC4 1 NAG A1392 SITE 1 GC5 5 LEU A 265 PRO A 291 ASN A 448 NAG A1262 SITE 2 GC5 5 NAG A1449 SITE 1 GC6 1 NAG A1448 SITE 1 GC7 3 ASN B 611 SER B 613 NAG B1612 SITE 1 GC8 1 NAG B1611 SITE 1 GC9 1 ASN B 618 SITE 1 HC1 1 ASN B 637 SITE 1 HC2 4 ASN C 88 NAG C1089 GLY E 527 SER E 528 SITE 1 HC3 2 NAG C1088 BMA C1090 SITE 1 HC4 1 NAG C1089 SITE 1 HC5 2 ASN C 133 NAG C1134 SITE 1 HC6 1 NAG C1133 SITE 1 HC7 3 ASN C 156 TYR C 173 NAG C1157 SITE 1 HC8 2 NAG C1156 BMA C1158 SITE 1 HC9 1 NAG C1157 SITE 1 IC1 3 GLN C 130 ASN C 160 NAG C1161 SITE 1 IC2 2 NAG C1160 BMA C1162 SITE 1 IC3 1 NAG C1161 SITE 1 IC4 3 ILE C 194 ASN C 197 NAG C1198 SITE 1 IC5 1 NAG C1197 SITE 1 IC6 3 ASN C 234 SER C 274 NAG C1235 SITE 1 IC7 1 NAG C1234 SITE 1 IC8 5 ASN C 262 VAL C 446 SER C 447 NAG C1263 SITE 2 IC8 5 NAG C1448 SITE 1 IC9 2 NAG C1262 BMA C1264 SITE 1 JC1 3 NAG C1263 MAN C1265 MAN C1267 SITE 1 JC2 2 BMA C1264 MAN C1266 SITE 1 JC3 1 MAN C1265 SITE 1 JC4 2 BMA C1264 MAN C1268 SITE 1 JC5 1 MAN C1267 SITE 1 JC6 3 ASN C 276 ASN C 279 NAG C1277 SITE 1 JC7 2 NAG C1276 BMA C1278 SITE 1 JC8 1 NAG C1277 SITE 1 JC9 2 ASN C 295 NAG C1296 SITE 1 KC1 2 NAG C1295 BMA C1297 SITE 1 KC2 3 NAG C1296 MAN C1298 MAN C1299 SITE 1 KC3 1 BMA C1297 SITE 1 KC4 1 BMA C1297 SITE 1 KC5 5 ASN C 301 NAG C1302 HIS G 52A CYS G 52B SITE 2 KC5 5 ALA G 52C SITE 1 KC6 7 NAG C1301 BMA C1303 MAN C1305 MAN C1308 SITE 2 KC6 7 ALA G 30 ALA G 31 HIS G 52A SITE 1 KC7 4 NAG C1302 MAN C1304 MAN C1305 THR G 73 SITE 1 KC8 2 BMA C1303 HIS G 52A SITE 1 KC9 4 NAG C1302 BMA C1303 MAN C1306 MAN C1308 SITE 1 LC1 1 MAN C1305 SITE 1 LC2 3 NAG C1302 MAN C1305 SER G 28 SITE 1 LC3 4 THR C 297 ASN C 332 ARG C 444 NAG C1333 SITE 1 LC4 2 NAG C1332 BMA C1334 SITE 1 LC5 4 NAG C1333 MAN C1335 MAN C1336 MAN C1339 SITE 1 LC6 2 BMA C1334 MAN C1339 SITE 1 LC7 4 BMA C1334 MAN C1337 MAN C1341 ASN J 94 SITE 1 LC8 1 MAN C1336 SITE 1 LC9 4 BMA C1334 MAN C1335 MAN C1340 THR G 57 SITE 1 MC1 6 MAN C1339 MAN C1342 TYR G 58 HIS G 59 SITE 2 MC1 6 LYS G 64 TRP J 95 SITE 1 MC2 3 MAN C1336 MAN C1342 ASN J 94 SITE 1 MC3 5 MAN C1340 MAN C1341 PRO G 61 ASN J 94 SITE 2 MC3 5 TRP J 95 SITE 1 MC4 2 ASN C 339 TRP C 395 SITE 1 MC5 2 ASN C 355 NAG C1356 SITE 1 MC6 1 NAG C1355 SITE 1 MC7 5 ASN C 363 THR C 372 NAG C1364 NAG C1386 SITE 2 MC7 5 NAG C1387 SITE 1 MC8 3 NAG C1363 BMA C1365 NAG C1387 SITE 1 MC9 1 NAG C1364 SITE 1 NC1 4 ASN C 386 NAG C1363 NAG C1387 NAG C1392 SITE 1 NC2 4 NAG C1363 NAG C1364 NAG C1386 BMA C1388 SITE 1 NC3 1 NAG C1387 SITE 1 NC4 3 ASN C 392 NAG C1386 NAG C1393 SITE 1 NC5 1 NAG C1392 SITE 1 NC6 5 LEU C 265 PRO C 291 ASN C 448 NAG C1262 SITE 2 NC6 5 NAG C1449 SITE 1 NC7 1 NAG C1448 SITE 1 NC8 4 ASN D 88 NAG D1089 GLY F 527 SER F 528 SITE 1 NC9 2 NAG D1088 BMA D1090 SITE 1 OC1 1 NAG D1089 SITE 1 OC2 2 ASN D 133 NAG D1134 SITE 1 OC3 1 NAG D1133 SITE 1 OC4 3 ASN D 156 TYR D 173 NAG D1157 SITE 1 OC5 2 NAG D1156 BMA D1158 SITE 1 OC6 1 NAG D1157 SITE 1 OC7 3 GLN D 130 ASN D 160 NAG D1161 SITE 1 OC8 2 NAG D1160 BMA D1162 SITE 1 OC9 1 NAG D1161 SITE 1 PC1 3 ILE D 194 ASN D 197 NAG D1198 SITE 1 PC2 1 NAG D1197 SITE 1 PC3 3 ASN D 234 SER D 274 NAG D1235 SITE 1 PC4 1 NAG D1234 SITE 1 PC5 5 ASN D 262 VAL D 446 SER D 447 NAG D1263 SITE 2 PC5 5 NAG D1448 SITE 1 PC6 2 NAG D1262 BMA D1264 SITE 1 PC7 3 NAG D1263 MAN D1265 MAN D1267 SITE 1 PC8 2 BMA D1264 MAN D1266 SITE 1 PC9 1 MAN D1265 SITE 1 QC1 2 BMA D1264 MAN D1268 SITE 1 QC2 1 MAN D1267 SITE 1 QC3 3 ASN D 276 ASN D 279 NAG D1277 SITE 1 QC4 2 NAG D1276 BMA D1278 SITE 1 QC5 1 NAG D1277 SITE 1 QC6 2 ASN D 295 NAG D1296 SITE 1 QC7 2 NAG D1295 BMA D1297 SITE 1 QC8 3 NAG D1296 MAN D1298 MAN D1299 SITE 1 QC9 1 BMA D1297 SITE 1 RC1 1 BMA D1297 SITE 1 RC2 5 ASN D 301 NAG D1302 HIS I 52A CYS I 52B SITE 2 RC2 5 ALA I 52C SITE 1 RC3 7 NAG D1301 BMA D1303 MAN D1305 MAN D1308 SITE 2 RC3 7 ALA I 30 ALA I 31 HIS I 52A SITE 1 RC4 4 NAG D1302 MAN D1304 MAN D1305 THR I 73 SITE 1 RC5 2 BMA D1303 HIS I 52A SITE 1 RC6 4 NAG D1302 BMA D1303 MAN D1306 MAN D1308 SITE 1 RC7 1 MAN D1305 SITE 1 RC8 3 NAG D1302 MAN D1305 SER I 28 SITE 1 RC9 4 THR D 297 ASN D 332 ARG D 444 NAG D1333 SITE 1 SC1 2 NAG D1332 BMA D1334 SITE 1 SC2 4 NAG D1333 MAN D1335 MAN D1336 MAN D1339 SITE 1 SC3 2 BMA D1334 MAN D1339 SITE 1 SC4 4 BMA D1334 MAN D1337 MAN D1341 ASN K 94 SITE 1 SC5 1 MAN D1336 SITE 1 SC6 4 BMA D1334 MAN D1335 MAN D1340 THR I 57 SITE 1 SC7 6 MAN D1339 MAN D1342 TYR I 58 HIS I 59 SITE 2 SC7 6 LYS I 64 TRP K 95 SITE 1 SC8 3 MAN D1336 MAN D1342 ASN K 94 SITE 1 SC9 5 MAN D1340 MAN D1341 PRO I 61 ASN K 94 SITE 2 SC9 5 TRP K 95 SITE 1 TC1 2 ASN D 339 TRP D 395 SITE 1 TC2 2 ASN D 355 NAG D1356 SITE 1 TC3 1 NAG D1355 SITE 1 TC4 5 ASN D 363 THR D 372 NAG D1364 NAG D1386 SITE 2 TC4 5 NAG D1387 SITE 1 TC5 3 NAG D1363 BMA D1365 NAG D1387 SITE 1 TC6 1 NAG D1364 SITE 1 TC7 4 ASN D 386 NAG D1363 NAG D1387 NAG D1392 SITE 1 TC8 4 NAG D1363 NAG D1364 NAG D1386 BMA D1388 SITE 1 TC9 1 NAG D1387 SITE 1 UC1 3 ASN D 392 NAG D1386 NAG D1393 SITE 1 UC2 1 NAG D1392 SITE 1 UC3 5 LEU D 265 PRO D 291 ASN D 448 NAG D1262 SITE 2 UC3 5 NAG D1449 SITE 1 UC4 1 NAG D1448 SITE 1 UC5 3 ASN E 611 SER E 613 NAG E1612 SITE 1 UC6 1 NAG E1611 SITE 1 UC7 1 ASN E 618 SITE 1 UC8 1 ASN E 637 SITE 1 UC9 3 ASN F 611 SER F 613 NAG F1612 SITE 1 VC1 1 NAG F1611 SITE 1 VC2 1 ASN F 618 SITE 1 VC3 1 ASN F 637 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