HEADER IMMUNE SYSTEM 15-NOV-24 9KMC TITLE CRYO-EM STRUCTURE OF THE HETEROTRIMERIC INTERLEUKIN-2 RECEPTOR IN TITLE 2 COMPLEX WITH INTERLEUKIN-2 AND ANTI-CD25 FAB S417 COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTERLEUKIN-2 RECEPTOR SUBUNIT ALPHA; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: IL-2 RECEPTOR SUBUNIT ALPHA,IL-2-RA,IL-2R SUBUNIT ALPHA,IL2- COMPND 5 RA,TAC ANTIGEN,P55; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: INTERLEUKIN-2 RECEPTOR SUBUNIT BETA; COMPND 9 CHAIN: B; COMPND 10 SYNONYM: IL-2 RECEPTOR SUBUNIT BETA,IL-2R SUBUNIT BETA,IL-2RB,HIGH COMPND 11 AFFINITY IL-2 RECEPTOR SUBUNIT BETA,INTERLEUKIN-15 RECEPTOR SUBUNIT COMPND 12 BETA,P70-75,P75; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 3; COMPND 15 MOLECULE: CYTOKINE RECEPTOR COMMON SUBUNIT GAMMA; COMPND 16 CHAIN: C; COMPND 17 SYNONYM: INTERLEUKIN-2 RECEPTOR SUBUNIT GAMMA,IL-2 RECEPTOR SUBUNIT COMPND 18 GAMMA,IL-2R SUBUNIT GAMMA,IL-2RG,GAMMAC,P64; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 4; COMPND 21 MOLECULE: INTERLEUKIN-2; COMPND 22 CHAIN: D; COMPND 23 SYNONYM: IL-2,T-CELL GROWTH FACTOR,TCGF; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 5; COMPND 26 MOLECULE: FAB S417 HEAVY CHAIN; COMPND 27 CHAIN: E; COMPND 28 ENGINEERED: YES; COMPND 29 MOL_ID: 6; COMPND 30 MOLECULE: FAB S417 LIGHT CHAIN; COMPND 31 CHAIN: F; COMPND 32 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: IL2RA; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: IL2RB, IL15RB; SOURCE 13 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 GENE: IL2RG; SOURCE 20 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 GENE: IL2; SOURCE 27 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 31 ORGANISM_TAXID: 32630; SOURCE 32 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 34 MOL_ID: 6; SOURCE 35 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 36 ORGANISM_TAXID: 32630; SOURCE 37 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 38 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS CYTOKINE, IMMUNE SYSTEM EXPDTA ELECTRON MICROSCOPY AUTHOR K.KATSURA,T.MATSUMOTO,M.SHIROUZU REVDAT 1 19-NOV-25 9KMC 0 JRNL AUTH A.ITOH-NAKADAI,M.LIANG,F.ISHIKAWA JRNL TITL CXCR4 INDUCES MEMORY FORMATION OVER EXHAUSTION IN CAR-T JRNL TITL 2 CELLS TO ACHIEVE DURABLE LEUKEMIA TARGETING JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.97 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 2.970 REMARK 3 NUMBER OF PARTICLES : 353002 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9KMC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1300053843. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : HETEROTRIMERIC INTERLEUKIN-2 REMARK 245 RECEPTOR IN COMPLEX WITH REMARK 245 INTERLEUKIN-2 AND FAB S417; REMARK 245 INTERLEUKIN-2 RECEPTOR SUBUNIT REMARK 245 ALPHA; INTERLEUKIN-2 RECEPTOR REMARK 245 SUBUNIT BETA; CYTOKINE RECEPTOR REMARK 245 COMMON SUBUNIT GAMMA; REMARK 245 INTERLEUKIN-2; FAB S417 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 8.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5040.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J, REMARK 350 AND CHAINS: K 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 THR A 87 REMARK 465 ARG A 88 REMARK 465 ASN A 89 REMARK 465 THR A 90 REMARK 465 THR A 91 REMARK 465 LYS A 92 REMARK 465 GLN A 93 REMARK 465 VAL A 94 REMARK 465 THR A 95 REMARK 465 PRO A 96 REMARK 465 GLN A 97 REMARK 465 PRO A 98 REMARK 465 GLU A 99 REMARK 465 GLU A 100 REMARK 465 GLN A 101 REMARK 465 LYS A 102 REMARK 465 GLU A 103 REMARK 465 ARG A 104 REMARK 465 LYS A 105 REMARK 465 THR A 106 REMARK 465 THR A 107 REMARK 465 GLU A 108 REMARK 465 MET A 109 REMARK 465 GLN A 110 REMARK 465 SER A 111 REMARK 465 PRO A 112 REMARK 465 MET A 113 REMARK 465 GLN A 114 REMARK 465 PRO A 115 REMARK 465 VAL A 116 REMARK 465 ASP A 117 REMARK 465 GLN A 118 REMARK 465 GLU A 187 REMARK 465 MET A 188 REMARK 465 GLU A 189 REMARK 465 THR A 190 REMARK 465 SER A 191 REMARK 465 GLN A 192 REMARK 465 PHE A 193 REMARK 465 PRO A 194 REMARK 465 GLY A 195 REMARK 465 GLU A 196 REMARK 465 GLU A 197 REMARK 465 LYS A 198 REMARK 465 PRO A 199 REMARK 465 GLN A 200 REMARK 465 ALA A 201 REMARK 465 SER A 202 REMARK 465 PRO A 203 REMARK 465 GLU A 204 REMARK 465 GLY A 205 REMARK 465 ARG A 206 REMARK 465 PRO A 207 REMARK 465 GLU A 208 REMARK 465 SER A 209 REMARK 465 GLU A 210 REMARK 465 THR A 211 REMARK 465 SER A 212 REMARK 465 CYS A 213 REMARK 465 LEU A 214 REMARK 465 VAL A 215 REMARK 465 THR A 216 REMARK 465 THR A 217 REMARK 465 THR A 218 REMARK 465 ASP A 219 REMARK 465 PHE A 220 REMARK 465 GLN A 221 REMARK 465 ILE A 222 REMARK 465 GLN A 223 REMARK 465 THR A 224 REMARK 465 GLU A 225 REMARK 465 MET A 226 REMARK 465 ALA A 227 REMARK 465 ALA A 228 REMARK 465 THR A 229 REMARK 465 MET A 230 REMARK 465 GLU A 231 REMARK 465 THR A 232 REMARK 465 SER A 233 REMARK 465 ILE A 234 REMARK 465 PHE A 235 REMARK 465 THR A 236 REMARK 465 THR A 237 REMARK 465 GLU A 238 REMARK 465 TYR A 239 REMARK 465 GLN A 240 REMARK 465 GLY A 241 REMARK 465 GLY A 242 REMARK 465 GLY A 243 REMARK 465 GLY A 244 REMARK 465 SER A 245 REMARK 465 GLY A 246 REMARK 465 GLY A 247 REMARK 465 GLY A 248 REMARK 465 GLY A 249 REMARK 465 SER A 250 REMARK 465 GLY A 251 REMARK 465 GLY A 252 REMARK 465 GLY A 253 REMARK 465 GLY A 254 REMARK 465 SER A 255 REMARK 465 HIS A 256 REMARK 465 HIS A 257 REMARK 465 HIS A 258 REMARK 465 HIS A 259 REMARK 465 HIS A 260 REMARK 465 HIS A 261 REMARK 465 ALA B 235 REMARK 465 LEU B 236 REMARK 465 GLY B 237 REMARK 465 LYS B 238 REMARK 465 ASP B 239 REMARK 465 THR B 240 REMARK 465 HIS B 241 REMARK 465 HIS B 242 REMARK 465 HIS B 243 REMARK 465 HIS B 244 REMARK 465 HIS B 245 REMARK 465 HIS B 246 REMARK 465 HIS B 247 REMARK 465 HIS B 248 REMARK 465 LEU C 23 REMARK 465 ASN C 24 REMARK 465 THR C 25 REMARK 465 THR C 26 REMARK 465 ILE C 27 REMARK 465 LEU C 28 REMARK 465 THR C 29 REMARK 465 PRO C 30 REMARK 465 ASN C 31 REMARK 465 GLY C 32 REMARK 465 ASN C 33 REMARK 465 GLU C 34 REMARK 465 ASP C 35 REMARK 465 THR C 36 REMARK 465 THR C 37 REMARK 465 ALA C 38 REMARK 465 ASP C 39 REMARK 465 PHE C 40 REMARK 465 PHE C 41 REMARK 465 LEU C 42 REMARK 465 THR C 43 REMARK 465 THR C 44 REMARK 465 MET C 45 REMARK 465 PRO C 46 REMARK 465 THR C 47 REMARK 465 ASP C 48 REMARK 465 SER C 49 REMARK 465 LEU C 50 REMARK 465 SER C 51 REMARK 465 VAL C 52 REMARK 465 SER C 53 REMARK 465 ASN C 249 REMARK 465 THR C 250 REMARK 465 SER C 251 REMARK 465 LYS C 252 REMARK 465 GLU C 253 REMARK 465 ASN C 254 REMARK 465 PRO C 255 REMARK 465 HIS C 256 REMARK 465 HIS C 257 REMARK 465 HIS C 258 REMARK 465 HIS C 259 REMARK 465 HIS C 260 REMARK 465 HIS C 261 REMARK 465 HIS C 262 REMARK 465 HIS C 263 REMARK 465 SER E 221 REMARK 465 CYS E 222 REMARK 465 GLU E 223 REMARK 465 ASN E 224 REMARK 465 LEU E 225 REMARK 465 TYR E 226 REMARK 465 PHE E 227 REMARK 465 GLN E 228 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 ASN A 70 -167.90 -117.80 REMARK 500 LEU A 159 53.67 -94.04 REMARK 500 SER B 40 -9.04 81.98 REMARK 500 ALA B 42 14.92 -147.79 REMARK 500 ALA B 85 139.81 -171.70 REMARK 500 ASN B 129 50.20 -119.32 REMARK 500 CYS B 148 116.48 -160.65 REMARK 500 GLU B 162 -127.27 62.44 REMARK 500 GLU B 180 -4.25 77.09 REMARK 500 GLU B 191 35.41 -94.86 REMARK 500 GLN C 118 36.50 -97.72 REMARK 500 LYS C 119 -8.40 72.44 REMARK 500 ASN C 159 66.39 39.03 REMARK 500 ASP C 203 -163.19 -76.48 REMARK 500 HIS C 206 50.19 35.11 REMARK 500 SER C 212 66.39 61.36 REMARK 500 THR D 27 -15.12 74.93 REMARK 500 LEU D 60 0.44 -68.15 REMARK 500 ALA E 92 -178.42 -172.28 REMARK 500 THR F 50 -12.00 72.46 REMARK 500 GLU F 142 95.31 -67.69 REMARK 500 THR F 163 -166.36 -77.94 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-62427 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE HETEROTRIMERIC INTERLEUKIN-2 RECEPTOR REMARK 900 COMPLEX WITH INTERLEUKIN-2 AND CD25 FAB DBREF 9KMC A 22 240 UNP P01589 IL2RA_HUMAN 22 240 DBREF 9KMC B 27 240 UNP P14784 IL2RB_HUMAN 27 240 DBREF 9KMC C 23 255 UNP P31785 IL2RG_HUMAN 23 255 DBREF 9KMC D 21 153 UNP P60568 IL2_HUMAN 21 153 DBREF 9KMC E 1 228 PDB 9KMC 9KMC 1 228 DBREF 9KMC F 1 213 PDB 9KMC 9KMC 1 213 SEQADV 9KMC GLY A 241 UNP P01589 EXPRESSION TAG SEQADV 9KMC GLY A 242 UNP P01589 EXPRESSION TAG SEQADV 9KMC GLY A 243 UNP P01589 EXPRESSION TAG SEQADV 9KMC GLY A 244 UNP P01589 EXPRESSION TAG SEQADV 9KMC SER A 245 UNP P01589 EXPRESSION TAG SEQADV 9KMC GLY A 246 UNP P01589 EXPRESSION TAG SEQADV 9KMC GLY A 247 UNP P01589 EXPRESSION TAG SEQADV 9KMC GLY A 248 UNP P01589 EXPRESSION TAG SEQADV 9KMC GLY A 249 UNP P01589 EXPRESSION TAG SEQADV 9KMC SER A 250 UNP P01589 EXPRESSION TAG SEQADV 9KMC GLY A 251 UNP P01589 EXPRESSION TAG SEQADV 9KMC GLY A 252 UNP P01589 EXPRESSION TAG SEQADV 9KMC GLY A 253 UNP P01589 EXPRESSION TAG SEQADV 9KMC GLY A 254 UNP P01589 EXPRESSION TAG SEQADV 9KMC SER A 255 UNP P01589 EXPRESSION TAG SEQADV 9KMC HIS A 256 UNP P01589 EXPRESSION TAG SEQADV 9KMC HIS A 257 UNP P01589 EXPRESSION TAG SEQADV 9KMC HIS A 258 UNP P01589 EXPRESSION TAG SEQADV 9KMC HIS A 259 UNP P01589 EXPRESSION TAG SEQADV 9KMC HIS A 260 UNP P01589 EXPRESSION TAG SEQADV 9KMC HIS A 261 UNP P01589 EXPRESSION TAG SEQADV 9KMC HIS B 241 UNP P14784 EXPRESSION TAG SEQADV 9KMC HIS B 242 UNP P14784 EXPRESSION TAG SEQADV 9KMC HIS B 243 UNP P14784 EXPRESSION TAG SEQADV 9KMC HIS B 244 UNP P14784 EXPRESSION TAG SEQADV 9KMC HIS B 245 UNP P14784 EXPRESSION TAG SEQADV 9KMC HIS B 246 UNP P14784 EXPRESSION TAG SEQADV 9KMC HIS B 247 UNP P14784 EXPRESSION TAG SEQADV 9KMC HIS B 248 UNP P14784 EXPRESSION TAG SEQADV 9KMC GLN C 75 UNP P31785 ASN 75 CONFLICT SEQADV 9KMC HIS C 256 UNP P31785 EXPRESSION TAG SEQADV 9KMC HIS C 257 UNP P31785 EXPRESSION TAG SEQADV 9KMC HIS C 258 UNP P31785 EXPRESSION TAG SEQADV 9KMC HIS C 259 UNP P31785 EXPRESSION TAG SEQADV 9KMC HIS C 260 UNP P31785 EXPRESSION TAG SEQADV 9KMC HIS C 261 UNP P31785 EXPRESSION TAG SEQADV 9KMC HIS C 262 UNP P31785 EXPRESSION TAG SEQADV 9KMC HIS C 263 UNP P31785 EXPRESSION TAG SEQRES 1 A 240 GLU LEU CYS ASP ASP ASP PRO PRO GLU ILE PRO HIS ALA SEQRES 2 A 240 THR PHE LYS ALA MET ALA TYR LYS GLU GLY THR MET LEU SEQRES 3 A 240 ASN CYS GLU CYS LYS ARG GLY PHE ARG ARG ILE LYS SER SEQRES 4 A 240 GLY SER LEU TYR MET LEU CYS THR GLY ASN SER SER HIS SEQRES 5 A 240 SER SER TRP ASP ASN GLN CYS GLN CYS THR SER SER ALA SEQRES 6 A 240 THR ARG ASN THR THR LYS GLN VAL THR PRO GLN PRO GLU SEQRES 7 A 240 GLU GLN LYS GLU ARG LYS THR THR GLU MET GLN SER PRO SEQRES 8 A 240 MET GLN PRO VAL ASP GLN ALA SER LEU PRO GLY HIS CYS SEQRES 9 A 240 ARG GLU PRO PRO PRO TRP GLU ASN GLU ALA THR GLU ARG SEQRES 10 A 240 ILE TYR HIS PHE VAL VAL GLY GLN MET VAL TYR TYR GLN SEQRES 11 A 240 CYS VAL GLN GLY TYR ARG ALA LEU HIS ARG GLY PRO ALA SEQRES 12 A 240 GLU SER VAL CYS LYS MET THR HIS GLY LYS THR ARG TRP SEQRES 13 A 240 THR GLN PRO GLN LEU ILE CYS THR GLY GLU MET GLU THR SEQRES 14 A 240 SER GLN PHE PRO GLY GLU GLU LYS PRO GLN ALA SER PRO SEQRES 15 A 240 GLU GLY ARG PRO GLU SER GLU THR SER CYS LEU VAL THR SEQRES 16 A 240 THR THR ASP PHE GLN ILE GLN THR GLU MET ALA ALA THR SEQRES 17 A 240 MET GLU THR SER ILE PHE THR THR GLU TYR GLN GLY GLY SEQRES 18 A 240 GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 19 A 240 HIS HIS HIS HIS HIS HIS SEQRES 1 B 222 ALA VAL ASN GLY THR SER GLN PHE THR CYS PHE TYR ASN SEQRES 2 B 222 SER ARG ALA ASN ILE SER CYS VAL TRP SER GLN ASP GLY SEQRES 3 B 222 ALA LEU GLN ASP THR SER CYS GLN VAL HIS ALA TRP PRO SEQRES 4 B 222 ASP ARG ARG ARG TRP ASN GLN THR CYS GLU LEU LEU PRO SEQRES 5 B 222 VAL SER GLN ALA SER TRP ALA CYS ASN LEU ILE LEU GLY SEQRES 6 B 222 ALA PRO ASP SER GLN LYS LEU THR THR VAL ASP ILE VAL SEQRES 7 B 222 THR LEU ARG VAL LEU CYS ARG GLU GLY VAL ARG TRP ARG SEQRES 8 B 222 VAL MET ALA ILE GLN ASP PHE LYS PRO PHE GLU ASN LEU SEQRES 9 B 222 ARG LEU MET ALA PRO ILE SER LEU GLN VAL VAL HIS VAL SEQRES 10 B 222 GLU THR HIS ARG CYS ASN ILE SER TRP GLU ILE SER GLN SEQRES 11 B 222 ALA SER HIS TYR PHE GLU ARG HIS LEU GLU PHE GLU ALA SEQRES 12 B 222 ARG THR LEU SER PRO GLY HIS THR TRP GLU GLU ALA PRO SEQRES 13 B 222 LEU LEU THR LEU LYS GLN LYS GLN GLU TRP ILE CYS LEU SEQRES 14 B 222 GLU THR LEU THR PRO ASP THR GLN TYR GLU PHE GLN VAL SEQRES 15 B 222 ARG VAL LYS PRO LEU GLN GLY GLU PHE THR THR TRP SER SEQRES 16 B 222 PRO TRP SER GLN PRO LEU ALA PHE ARG THR LYS PRO ALA SEQRES 17 B 222 ALA LEU GLY LYS ASP THR HIS HIS HIS HIS HIS HIS HIS SEQRES 18 B 222 HIS SEQRES 1 C 241 LEU ASN THR THR ILE LEU THR PRO ASN GLY ASN GLU ASP SEQRES 2 C 241 THR THR ALA ASP PHE PHE LEU THR THR MET PRO THR ASP SEQRES 3 C 241 SER LEU SER VAL SER THR LEU PRO LEU PRO GLU VAL GLN SEQRES 4 C 241 CYS PHE VAL PHE ASN VAL GLU TYR MET ASN CYS THR TRP SEQRES 5 C 241 GLN SER SER SER GLU PRO GLN PRO THR ASN LEU THR LEU SEQRES 6 C 241 HIS TYR TRP TYR LYS ASN SER ASP ASN ASP LYS VAL GLN SEQRES 7 C 241 LYS CYS SER HIS TYR LEU PHE SER GLU GLU ILE THR SER SEQRES 8 C 241 GLY CYS GLN LEU GLN LYS LYS GLU ILE HIS LEU TYR GLN SEQRES 9 C 241 THR PHE VAL VAL GLN LEU GLN ASP PRO ARG GLU PRO ARG SEQRES 10 C 241 ARG GLN ALA THR GLN MET LEU LYS LEU GLN ASN LEU VAL SEQRES 11 C 241 ILE PRO TRP ALA PRO GLU ASN LEU THR LEU HIS LYS LEU SEQRES 12 C 241 SER GLU SER GLN LEU GLU LEU ASN TRP ASN ASN ARG PHE SEQRES 13 C 241 LEU ASN HIS CYS LEU GLU HIS LEU VAL GLN TYR ARG THR SEQRES 14 C 241 ASP TRP ASP HIS SER TRP THR GLU GLN SER VAL ASP TYR SEQRES 15 C 241 ARG HIS LYS PHE SER LEU PRO SER VAL ASP GLY GLN LYS SEQRES 16 C 241 ARG TYR THR PHE ARG VAL ARG SER ARG PHE ASN PRO LEU SEQRES 17 C 241 CYS GLY SER ALA GLN HIS TRP SER GLU TRP SER HIS PRO SEQRES 18 C 241 ILE HIS TRP GLY SER ASN THR SER LYS GLU ASN PRO HIS SEQRES 19 C 241 HIS HIS HIS HIS HIS HIS HIS SEQRES 1 D 133 ALA PRO THR SER SER SER THR LYS LYS THR GLN LEU GLN SEQRES 2 D 133 LEU GLU HIS LEU LEU LEU ASP LEU GLN MET ILE LEU ASN SEQRES 3 D 133 GLY ILE ASN ASN TYR LYS ASN PRO LYS LEU THR ARG MET SEQRES 4 D 133 LEU THR PHE LYS PHE TYR MET PRO LYS LYS ALA THR GLU SEQRES 5 D 133 LEU LYS HIS LEU GLN CYS LEU GLU GLU GLU LEU LYS PRO SEQRES 6 D 133 LEU GLU GLU VAL LEU ASN LEU ALA GLN SER LYS ASN PHE SEQRES 7 D 133 HIS LEU ARG PRO ARG ASP LEU ILE SER ASN ILE ASN VAL SEQRES 8 D 133 ILE VAL LEU GLU LEU LYS GLY SER GLU THR THR PHE MET SEQRES 9 D 133 CYS GLU TYR ALA ASP GLU THR ALA THR ILE VAL GLU PHE SEQRES 10 D 133 LEU ASN ARG TRP ILE THR PHE CYS GLN SER ILE ILE SER SEQRES 11 D 133 THR LEU THR SEQRES 1 E 228 GLN VAL GLN LEU HIS GLN SER GLY ASP ASP LEU VAL LYS SEQRES 2 E 228 PRO GLY ALA SER VAL LYS LEU SER CYS ARG ALA SER GLY SEQRES 3 E 228 TYR THR PHE THR SER TYR TRP ILE ASN TRP VAL LYS GLN SEQRES 4 E 228 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ARG ILE LEU SEQRES 5 E 228 PRO GLY THR ASN SER ILE TYR TYR SER GLU ILE PHE LYS SEQRES 6 E 228 GLY LYS ALA SER LEU THR VAL ASP THR SER SER ASN THR SEQRES 7 E 228 ALA TYR ILE GLN LEU SER SER LEU SER SER GLU ASP SER SEQRES 8 E 228 ALA VAL TYR PHE CYS ALA ARG LEU LEU TRP ASN LYS GLY SEQRES 9 E 228 ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SEQRES 10 E 228 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11 E 228 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12 E 228 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 E 228 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14 E 228 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 E 228 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 E 228 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17 E 228 SER ASN THR LYS VAL ASP LYS LYS ALA GLU PRO LYS SER SEQRES 18 E 228 CYS GLU ASN LEU TYR PHE GLN SEQRES 1 F 213 GLN ILE VAL LEU SER GLN SER PRO VAL ILE LEU SER ALA SEQRES 2 F 213 SER PRO GLY GLU LYS VAL THR MET THR CYS ARG ALA SER SEQRES 3 F 213 SER GLY VAL SER SER ILE HIS TRP TYR GLN GLN GLN PRO SEQRES 4 F 213 GLY SER SER PRO LYS PRO TRP ILE TYR ASP THR SER SER SEQRES 5 F 213 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6 F 213 SER GLY THR SER TYR SER LEU THR ILE SER ARG VAL GLU SEQRES 7 F 213 ALA GLU ASP ALA ALA THR TYR TYR CYS GLN GLN TRP SER SEQRES 8 F 213 SER ASN PRO PRO THR PHE GLY ALA GLY THR LYS LEU GLU SEQRES 9 F 213 LEU LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 F 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 F 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 F 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 F 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 F 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 F 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 F 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 F 213 ASN ARG GLY GLU CYS HET NAG G 1 26 HET NAG G 2 28 HET FUC G 3 21 HET NAG H 1 26 HET NAG H 2 28 HET FUC H 3 21 HET NAG I 1 27 HET NAG I 2 27 HET BMA I 3 22 HET NAG J 1 27 HET NAG J 2 28 HET NAG K 1 27 HET NAG K 2 28 HET NAG C 301 28 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 7 NAG 11(C8 H15 N O6) FORMUL 7 FUC 2(C6 H12 O5) FORMUL 9 BMA C6 H12 O6 HELIX 1 AA1 THR D 27 ASN D 49 1 23 HELIX 2 AA2 LYS D 55 LEU D 60 1 6 HELIX 3 AA3 GLU D 72 HIS D 75 5 4 HELIX 4 AA4 LEU D 76 GLN D 94 1 19 HELIX 5 AA5 ARG D 101 GLY D 118 1 18 HELIX 6 AA6 THR D 133 THR D 153 1 21 HELIX 7 AA7 THR E 28 TYR E 32 5 5 HELIX 8 AA8 SER E 87 SER E 91 5 5 HELIX 9 AA9 SER E 133 THR E 137 5 5 HELIX 10 AB1 SER E 193 THR E 197 5 5 HELIX 11 AB2 GLU F 78 ALA F 82 5 5 HELIX 12 AB3 LYS F 182 HIS F 188 1 7 SHEET 1 AA1 3 ALA A 34 LYS A 37 0 SHEET 2 AA1 3 MET A 147 CYS A 152 -1 O TYR A 149 N LYS A 37 SHEET 3 AA1 3 GLU A 165 VAL A 167 -1 O SER A 166 N VAL A 148 SHEET 1 AA2 2 TYR A 41 LYS A 42 0 SHEET 2 AA2 2 HIS A 124 CYS A 125 -1 O CYS A 125 N TYR A 41 SHEET 1 AA3 4 HIS A 73 TRP A 76 0 SHEET 2 AA3 4 TYR A 64 ASN A 70 -1 N THR A 68 O SER A 75 SHEET 3 AA3 4 MET A 46 ASN A 48 -1 N LEU A 47 O MET A 65 SHEET 4 AA3 4 TYR A 140 HIS A 141 -1 O HIS A 141 N MET A 46 SHEET 1 AA4 2 PHE A 55 ARG A 57 0 SHEET 2 AA4 2 CYS A 82 SER A 84 -1 O THR A 83 N ARG A 56 SHEET 1 AA5 2 ARG A 157 ALA A 158 0 SHEET 2 AA5 2 CYS A 184 THR A 185 -1 O THR A 185 N ARG A 157 SHEET 1 AA6 4 SER B 32 TYR B 38 0 SHEET 2 AA6 4 ASN B 43 GLN B 50 -1 O VAL B 47 N THR B 35 SHEET 3 AA6 4 SER B 83 ILE B 89 -1 O LEU B 88 N ILE B 44 SHEET 4 AA6 4 LEU B 77 SER B 80 -1 N LEU B 77 O ALA B 85 SHEET 1 AA7 4 GLN B 72 GLU B 75 0 SHEET 2 AA7 4 CYS B 59 PRO B 65 -1 N ALA B 63 O GLN B 72 SHEET 3 AA7 4 VAL B 104 GLU B 112 -1 O LEU B 109 N GLN B 60 SHEET 4 AA7 4 ARG B 115 PHE B 124 -1 O PHE B 124 N VAL B 104 SHEET 1 AA8 3 ILE B 136 VAL B 143 0 SHEET 2 AA8 3 CYS B 148 GLU B 153 -1 O GLU B 153 N ILE B 136 SHEET 3 AA8 3 TRP B 192 LEU B 195 -1 O LEU B 195 N CYS B 148 SHEET 1 AA9 4 LEU B 184 LEU B 186 0 SHEET 2 AA9 4 LEU B 165 LEU B 172 -1 N ALA B 169 O LEU B 184 SHEET 3 AA9 4 GLN B 203 PRO B 212 -1 O GLN B 207 N ARG B 170 SHEET 4 AA9 4 LEU B 227 ARG B 230 -1 O PHE B 229 N TYR B 204 SHEET 1 AB1 5 TYR C 105 SER C 108 0 SHEET 2 AB1 5 ILE C 111 LEU C 117 -1 O SER C 113 N LEU C 106 SHEET 3 AB1 5 MET C 70 TRP C 74 -1 N CYS C 72 O CYS C 115 SHEET 4 AB1 5 VAL C 60 PHE C 65 -1 N PHE C 63 O ASN C 71 SHEET 5 AB1 5 VAL C 152 ILE C 153 1 O ILE C 153 N VAL C 64 SHEET 1 AB2 4 GLN C 100 LYS C 101 0 SHEET 2 AB2 4 THR C 86 LYS C 92 -1 N TYR C 89 O GLN C 100 SHEET 3 AB2 4 THR C 127 GLN C 133 -1 O GLN C 131 N HIS C 88 SHEET 4 AB2 4 GLN C 141 LYS C 147 -1 O ALA C 142 N LEU C 132 SHEET 1 AB3 3 GLU C 158 SER C 166 0 SHEET 2 AB3 3 GLN C 169 ASN C 175 -1 O ASN C 175 N GLU C 158 SHEET 3 AB3 3 LYS C 207 PRO C 211 -1 O PHE C 208 N LEU C 172 SHEET 1 AB4 3 THR C 198 VAL C 202 0 SHEET 2 AB4 3 GLU C 184 THR C 191 -1 N TYR C 189 O THR C 198 SHEET 3 AB4 3 VAL C 223 ARG C 226 -1 O ARG C 226 N GLU C 184 SHEET 1 AB5 4 THR C 198 VAL C 202 0 SHEET 2 AB5 4 GLU C 184 THR C 191 -1 N TYR C 189 O THR C 198 SHEET 3 AB5 4 ARG C 218 PHE C 221 -1 O THR C 220 N ARG C 190 SHEET 4 AB5 4 ILE C 244 GLY C 247 -1 O TRP C 246 N TYR C 219 SHEET 1 AB6 2 PHE D 64 PRO D 67 0 SHEET 2 AB6 2 TYR D 127 ALA D 132 -1 O ALA D 128 N MET D 66 SHEET 1 AB7 4 GLN E 3 GLN E 6 0 SHEET 2 AB7 4 VAL E 18 SER E 25 -1 O ARG E 23 N HIS E 5 SHEET 3 AB7 4 THR E 78 LEU E 83 -1 O ILE E 81 N LEU E 20 SHEET 4 AB7 4 ALA E 68 ASP E 73 -1 N THR E 71 O TYR E 80 SHEET 1 AB8 6 ASP E 10 VAL E 12 0 SHEET 2 AB8 6 THR E 113 VAL E 117 1 O SER E 114 N ASP E 10 SHEET 3 AB8 6 ALA E 92 LEU E 99 -1 N ALA E 92 O VAL E 115 SHEET 4 AB8 6 ILE E 34 GLN E 39 -1 N VAL E 37 O PHE E 95 SHEET 5 AB8 6 LEU E 45 ILE E 51 -1 O ILE E 48 N TRP E 36 SHEET 6 AB8 6 ILE E 58 TYR E 60 -1 O TYR E 59 N ARG E 50 SHEET 1 AB9 4 ASP E 10 VAL E 12 0 SHEET 2 AB9 4 THR E 113 VAL E 117 1 O SER E 114 N ASP E 10 SHEET 3 AB9 4 ALA E 92 LEU E 99 -1 N ALA E 92 O VAL E 115 SHEET 4 AB9 4 MET E 106 TRP E 109 -1 O TYR E 108 N ARG E 98 SHEET 1 AC1 4 SER E 126 LEU E 130 0 SHEET 2 AC1 4 THR E 141 TYR E 151 -1 O LYS E 149 N SER E 126 SHEET 3 AC1 4 TYR E 182 PRO E 191 -1 O LEU E 184 N VAL E 148 SHEET 4 AC1 4 VAL E 175 LEU E 176 -1 N VAL E 175 O SER E 183 SHEET 1 AC2 3 THR E 157 VAL E 158 0 SHEET 2 AC2 3 VAL E 204 HIS E 206 -1 O ASN E 205 N THR E 157 SHEET 3 AC2 3 THR E 211 VAL E 213 -1 O THR E 211 N HIS E 206 SHEET 1 AC3 2 TYR E 200 ILE E 201 0 SHEET 2 AC3 2 LYS E 216 ALA E 217 -1 O ALA E 217 N TYR E 200 SHEET 1 AC4 4 LEU F 4 SER F 7 0 SHEET 2 AC4 4 VAL F 19 ALA F 25 -1 O ARG F 24 N SER F 5 SHEET 3 AC4 4 SER F 69 ILE F 74 -1 O ILE F 74 N VAL F 19 SHEET 4 AC4 4 PHE F 61 SER F 66 -1 N SER F 62 O THR F 73 SHEET 1 AC5 6 ILE F 10 ALA F 13 0 SHEET 2 AC5 6 THR F 101 LEU F 105 1 O GLU F 104 N ALA F 13 SHEET 3 AC5 6 THR F 84 GLN F 89 -1 N TYR F 85 O THR F 101 SHEET 4 AC5 6 HIS F 33 GLN F 37 -1 N HIS F 33 O GLN F 88 SHEET 5 AC5 6 LYS F 44 TYR F 48 -1 O TRP F 46 N TRP F 34 SHEET 6 AC5 6 SER F 52 LEU F 53 -1 O SER F 52 N TYR F 48 SHEET 1 AC6 4 ILE F 10 ALA F 13 0 SHEET 2 AC6 4 THR F 101 LEU F 105 1 O GLU F 104 N ALA F 13 SHEET 3 AC6 4 THR F 84 GLN F 89 -1 N TYR F 85 O THR F 101 SHEET 4 AC6 4 THR F 96 PHE F 97 -1 O THR F 96 N GLN F 89 SHEET 1 AC7 4 SER F 113 PHE F 117 0 SHEET 2 AC7 4 THR F 128 PHE F 138 -1 O VAL F 132 N PHE F 117 SHEET 3 AC7 4 TYR F 172 SER F 181 -1 O SER F 176 N CYS F 133 SHEET 4 AC7 4 SER F 158 VAL F 162 -1 N SER F 161 O SER F 175 SHEET 1 AC8 3 ALA F 143 VAL F 149 0 SHEET 2 AC8 3 VAL F 190 HIS F 197 -1 O THR F 196 N LYS F 144 SHEET 3 AC8 3 VAL F 204 ASN F 209 -1 O VAL F 204 N VAL F 195 SSBOND 1 CYS A 24 CYS A 168 1555 1555 2.03 SSBOND 2 CYS A 49 CYS A 80 1555 1555 2.03 SSBOND 3 CYS A 51 CYS A 82 1555 1555 2.03 SSBOND 4 CYS A 67 CYS A 125 1555 1555 2.03 SSBOND 5 CYS A 152 CYS A 184 1555 1555 2.03 SSBOND 6 CYS B 36 CYS B 46 1555 1555 2.03 SSBOND 7 CYS B 59 CYS B 110 1555 1555 2.03 SSBOND 8 CYS B 74 CYS B 86 1555 1555 2.04 SSBOND 9 CYS C 102 CYS C 115 1555 1555 2.03 SSBOND 10 CYS C 182 CYS C 231 1555 1555 2.03 SSBOND 11 CYS D 78 CYS D 125 1555 1555 2.03 SSBOND 12 CYS E 22 CYS E 96 1555 1555 2.03 SSBOND 13 CYS E 146 CYS E 202 1555 1555 2.03 SSBOND 14 CYS F 23 CYS F 87 1555 1555 2.03 SSBOND 15 CYS F 133 CYS F 193 1555 1555 2.03 LINK ND2 ASN B 43 C1 NAG G 1 1555 1555 1.44 LINK ND2 ASN B 71 C1 NAG H 1 1555 1555 1.43 LINK ND2 ASN B 149 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN C 71 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN C 84 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN C 159 C1 NAG C 301 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44 LINK O6 NAG G 1 C1 FUC G 3 1555 1555 1.44 LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44 LINK O6 NAG H 1 C1 FUC H 3 1555 1555 1.45 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.45 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 CISPEP 1 ASN C 228 PRO C 229 0 -2.70 CISPEP 2 PHE E 152 PRO E 153 0 -4.24 CISPEP 3 GLU E 154 PRO E 155 0 -3.07 CISPEP 4 SER F 7 PRO F 8 0 -2.07 CISPEP 5 ASN F 93 PRO F 94 0 -5.90 CISPEP 6 TYR F 139 PRO F 140 0 -0.17 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000