HEADER ANTITUMOR PROTEIN/IMMUNE SYSTEM 10-JUL-24 9IPB TITLE LOCAL REFINEMENT STRUCTURE OF SEGFR AND 528 FV (FROM LH-TYPE TITLE 2 BISPECIFIC DIABODY EX3) COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PROTO-ONCOGENE C-ERBB-1,RECEPTOR TYROSINE-PROTEIN KINASE COMPND 5 ERBB-1; COMPND 6 EC: 2.7.10.1; COMPND 7 ENGINEERED: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: 528 FV FROM LH-TYPE BISPECIFIC DIABODY EX3; COMPND 10 CHAIN: D; COMPND 11 ENGINEERED: YES; COMPND 12 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: EGFR, ERBB, ERBB1, HER1; SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 10 ORGANISM_TAXID: 32630; SOURCE 11 EXPRESSION_SYSTEM: BREVIBACILLUS CHOSHINENSIS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 54911 KEYWDS BISPECIFIC ANTIBODY, DIABODY, EGFR, LH, EX3, 528, LOCAL REFINEMENT, KEYWDS 2 ANTITUMOR PROTEIN, ANTITUMOR PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR K.SATO,S.UEHARA,A.TSUGITA,T.MATSUI,R.ASANO,K.MAKABE,T.YOKOYAMA, AUTHOR 2 Y.TANAKA REVDAT 1 28-MAY-25 9IPB 0 JRNL AUTH K.SATO,S.UEHARA,A.TSUGITA,M.ISHII,S.ISHIYAMA,A.MAEJIMA, JRNL AUTH 2 I.NAKAHARA,M.NAZUKA,T.MATSUI,G.CHRISTOS,T.YOKOYAMA, JRNL AUTH 3 I.KUMAGAI,K.MAKABE,R.ASANO,Y.TANAKA JRNL TITL BISPECIFIC ANTIBODY-ANTIGEN COMPLEX STRUCTURES REVEAL JRNL TITL 2 ACTIVITY ENHANCEMENT BY DOMAIN REARRANGEMENT JRNL REF CELL REP 2025 JRNL REFN ESSN 2211-1247 REMARK 2 REMARK 2 RESOLUTION. 2.93 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL 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) : 2.930 REMARK 3 NUMBER OF PARTICLES : 108521 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 9IPB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1300049128. 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 : LH-TYPE BISPECIFIC ANTIBODY EX3 REMARK 245 COMPOSED OF 528 AND OKT3 FVS IN REMARK 245 TERNARY COMPLEX WITH SEGFR AND REMARK 245 CD3GAMMA-EPSILON; SOLUBLE REMARK 245 EPIDERMAL GROWTH FACTOR REMARK 245 RECEPTOR (SEGFR); LH-TYPE REMARK 245 BISPECIFIC DIABODY EX3 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 : 7.40 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 : JEOL CRYO ARM 300 REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 900.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2400.00 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) : 6000.00 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, B, C 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 LEU A 1 REMARK 465 GLU A 2 REMARK 465 GLU A 3 REMARK 465 GLY A 9 REMARK 465 THR A 10 REMARK 465 SER A 11 REMARK 465 ASN A 12 REMARK 465 LYS A 13 REMARK 465 LEU A 14 REMARK 465 THR A 15 REMARK 465 GLN A 16 REMARK 465 LEU A 17 REMARK 465 GLY A 18 REMARK 465 TYR A 101 REMARK 465 ASP A 102 REMARK 465 ALA A 103 REMARK 465 ASN A 104 REMARK 465 LYS A 105 REMARK 465 THR A 106 REMARK 465 GLY A 107 REMARK 465 PHE A 156 REMARK 465 GLN A 157 REMARK 465 ASN A 158 REMARK 465 HIS A 159 REMARK 465 LEU A 160 REMARK 465 GLY A 161 REMARK 465 SER A 162 REMARK 465 CYS A 163 REMARK 465 GLN A 164 REMARK 465 LYS A 165 REMARK 465 CYS A 166 REMARK 465 ASP A 167 REMARK 465 PRO A 168 REMARK 465 SER A 169 REMARK 465 CYS A 170 REMARK 465 PRO A 171 REMARK 465 ASN A 172 REMARK 465 ILE A 190 REMARK 465 CYS A 191 REMARK 465 ALA A 192 REMARK 465 GLN A 193 REMARK 465 GLN A 194 REMARK 465 CYS A 195 REMARK 465 SER A 196 REMARK 465 GLY A 197 REMARK 465 ARG A 198 REMARK 465 CYS A 199 REMARK 465 ARG A 200 REMARK 465 GLY A 201 REMARK 465 LYS A 202 REMARK 465 SER A 203 REMARK 465 PRO A 204 REMARK 465 SER A 205 REMARK 465 ASP A 206 REMARK 465 CYS A 207 REMARK 465 CYS A 208 REMARK 465 HIS A 209 REMARK 465 HIS A 597 REMARK 465 PRO A 598 REMARK 465 ASN A 599 REMARK 465 CYS A 600 REMARK 465 THR A 601 REMARK 465 TYR A 602 REMARK 465 GLY A 603 REMARK 465 CYS A 604 REMARK 465 THR A 605 REMARK 465 GLY A 606 REMARK 465 PRO A 607 REMARK 465 GLY A 608 REMARK 465 LEU A 609 REMARK 465 GLU A 610 REMARK 465 GLY A 611 REMARK 465 CYS A 612 REMARK 465 PRO A 613 REMARK 465 THR A 614 REMARK 465 ASN A 615 REMARK 465 GLY A 616 REMARK 465 PRO A 617 REMARK 465 LYS A 618 REMARK 465 ILE A 619 REMARK 465 PRO A 620 REMARK 465 SER A 621 REMARK 465 HIS A 622 REMARK 465 HIS A 623 REMARK 465 HIS A 624 REMARK 465 HIS A 625 REMARK 465 HIS A 626 REMARK 465 HIS A 627 REMARK 465 GLY D 235 REMARK 465 GLY D 236 REMARK 465 GLY D 237 REMARK 465 GLY D 238 REMARK 465 SER D 239 REMARK 465 GLY D 240 REMARK 465 GLY D 241 REMARK 465 GLY D 242 REMARK 465 GLY D 243 REMARK 465 SER D 244 REMARK 465 GLY D 245 REMARK 465 GLY D 246 REMARK 465 GLY D 247 REMARK 465 GLY D 248 REMARK 465 SER D 249 REMARK 465 GLY D 250 REMARK 465 GLY D 251 REMARK 465 GLY D 252 REMARK 465 GLY D 253 REMARK 465 SER D 254 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 NH1 ARG A 114 OE1 GLU A 181 1.53 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 PHE A 31 -6.53 -143.18 REMARK 500 TYR A 45 58.39 70.55 REMARK 500 LEU A 77 35.96 -158.42 REMARK 500 ILE A 143 -66.85 -91.16 REMARK 500 GLU A 181 -63.71 69.43 REMARK 500 LYS A 185 68.61 39.31 REMARK 500 THR A 187 -16.82 -148.80 REMARK 500 ALA A 213 -60.06 -90.65 REMARK 500 PRO A 219 48.27 -78.64 REMARK 500 GLU A 233 -31.69 -146.86 REMARK 500 ALA A 234 -31.06 -153.91 REMARK 500 ARG A 273 -149.05 58.98 REMARK 500 GLU A 296 -74.62 -87.18 REMARK 500 ASP A 297 -168.23 -78.27 REMARK 500 LYS A 333 -21.60 90.75 REMARK 500 ASN A 337 41.64 37.97 REMARK 500 GLN A 411 -65.11 -149.78 REMARK 500 LEU A 426 53.64 -106.66 REMARK 500 SER A 433 -70.86 -72.18 REMARK 500 ASP A 434 -60.87 -90.21 REMARK 500 LYS A 463 -169.89 -125.86 REMARK 500 LYS A 465 53.35 -115.69 REMARK 500 PRO A 488 -10.98 -48.81 REMARK 500 ASP A 498 55.35 -91.82 REMARK 500 ASN A 544 -153.39 -128.21 REMARK 500 TYR D 291 53.23 -92.90 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-60768 RELATED DB: EMDB REMARK 900 LOCAL REFINEMENT STRUCTURE OF SEGFR AND 528 FV (FROM LH-TYPE REMARK 900 BISPECIFIC DIABODY EX3) COMPLEX DBREF 9IPB A 1 621 UNP P00533 EGFR_HUMAN 25 645 DBREF 9IPB D 117 366 PDB 9IPB 9IPB 117 366 SEQADV 9IPB HIS A 622 UNP P00533 EXPRESSION TAG SEQADV 9IPB HIS A 623 UNP P00533 EXPRESSION TAG SEQADV 9IPB HIS A 624 UNP P00533 EXPRESSION TAG SEQADV 9IPB HIS A 625 UNP P00533 EXPRESSION TAG SEQADV 9IPB HIS A 626 UNP P00533 EXPRESSION TAG SEQADV 9IPB HIS A 627 UNP P00533 EXPRESSION TAG SEQRES 1 A 627 LEU GLU GLU LYS LYS VAL CYS GLN GLY THR SER ASN LYS SEQRES 2 A 627 LEU THR GLN LEU GLY THR PHE GLU ASP HIS PHE LEU SER SEQRES 3 A 627 LEU GLN ARG MET PHE ASN ASN CYS GLU VAL VAL LEU GLY SEQRES 4 A 627 ASN LEU GLU ILE THR TYR VAL GLN ARG ASN TYR ASP LEU SEQRES 5 A 627 SER PHE LEU LYS THR ILE GLN GLU VAL ALA GLY TYR VAL SEQRES 6 A 627 LEU ILE ALA LEU ASN THR VAL GLU ARG ILE PRO LEU GLU SEQRES 7 A 627 ASN LEU GLN ILE ILE ARG GLY ASN MET TYR TYR GLU ASN SEQRES 8 A 627 SER TYR ALA LEU ALA VAL LEU SER ASN TYR ASP ALA ASN SEQRES 9 A 627 LYS THR GLY LEU LYS GLU LEU PRO MET ARG ASN LEU GLN SEQRES 10 A 627 GLU ILE LEU HIS GLY ALA VAL ARG PHE SER ASN ASN PRO SEQRES 11 A 627 ALA LEU CYS ASN VAL GLU SER ILE GLN TRP ARG ASP ILE SEQRES 12 A 627 VAL SER SER ASP PHE LEU SER ASN MET SER MET ASP PHE SEQRES 13 A 627 GLN ASN HIS LEU GLY SER CYS GLN LYS CYS ASP PRO SER SEQRES 14 A 627 CYS PRO ASN GLY SER CYS TRP GLY ALA GLY GLU GLU ASN SEQRES 15 A 627 CYS GLN LYS LEU THR LYS ILE ILE CYS ALA GLN GLN CYS SEQRES 16 A 627 SER GLY ARG CYS ARG GLY LYS SER PRO SER ASP CYS CYS SEQRES 17 A 627 HIS ASN GLN CYS ALA ALA GLY CYS THR GLY PRO ARG GLU SEQRES 18 A 627 SER ASP CYS LEU VAL CYS ARG LYS PHE ARG ASP GLU ALA SEQRES 19 A 627 THR CYS LYS ASP THR CYS PRO PRO LEU MET LEU TYR ASN SEQRES 20 A 627 PRO THR THR TYR GLN MET ASP VAL ASN PRO GLU GLY LYS SEQRES 21 A 627 TYR SER PHE GLY ALA THR CYS VAL LYS LYS CYS PRO ARG SEQRES 22 A 627 ASN TYR VAL VAL THR ASP HIS GLY SER CYS VAL ARG ALA SEQRES 23 A 627 CYS GLY ALA ASP SER TYR GLU MET GLU GLU ASP GLY VAL SEQRES 24 A 627 ARG LYS CYS LYS LYS CYS GLU GLY PRO CYS ARG LYS VAL SEQRES 25 A 627 CYS ASN GLY ILE GLY ILE GLY GLU PHE LYS ASP SER LEU SEQRES 26 A 627 SER ILE ASN ALA THR ASN ILE LYS HIS PHE LYS ASN CYS SEQRES 27 A 627 THR SER ILE SER GLY ASP LEU HIS ILE LEU PRO VAL ALA SEQRES 28 A 627 PHE ARG GLY ASP SER PHE THR HIS THR PRO PRO LEU ASP SEQRES 29 A 627 PRO GLN GLU LEU ASP ILE LEU LYS THR VAL LYS GLU ILE SEQRES 30 A 627 THR GLY PHE LEU LEU ILE GLN ALA TRP PRO GLU ASN ARG SEQRES 31 A 627 THR ASP LEU HIS ALA PHE GLU ASN LEU GLU ILE ILE ARG SEQRES 32 A 627 GLY ARG THR LYS GLN HIS GLY GLN PHE SER LEU ALA VAL SEQRES 33 A 627 VAL SER LEU ASN ILE THR SER LEU GLY LEU ARG SER LEU SEQRES 34 A 627 LYS GLU ILE SER ASP GLY ASP VAL ILE ILE SER GLY ASN SEQRES 35 A 627 LYS ASN LEU CYS TYR ALA ASN THR ILE ASN TRP LYS LYS SEQRES 36 A 627 LEU PHE GLY THR SER GLY GLN LYS THR LYS ILE ILE SER SEQRES 37 A 627 ASN ARG GLY GLU ASN SER CYS LYS ALA THR GLY GLN VAL SEQRES 38 A 627 CYS HIS ALA LEU CYS SER PRO GLU GLY CYS TRP GLY PRO SEQRES 39 A 627 GLU PRO ARG ASP CYS VAL SER CYS ARG ASN VAL SER ARG SEQRES 40 A 627 GLY ARG GLU CYS VAL ASP LYS CYS ASN LEU LEU GLU GLY SEQRES 41 A 627 GLU PRO ARG GLU PHE VAL GLU ASN SER GLU CYS ILE GLN SEQRES 42 A 627 CYS HIS PRO GLU CYS LEU PRO GLN ALA MET ASN ILE THR SEQRES 43 A 627 CYS THR GLY ARG GLY PRO ASP ASN CYS ILE GLN CYS ALA SEQRES 44 A 627 HIS TYR ILE ASP GLY PRO HIS CYS VAL LYS THR CYS PRO SEQRES 45 A 627 ALA GLY VAL MET GLY GLU ASN ASN THR LEU VAL TRP LYS SEQRES 46 A 627 TYR ALA ASP ALA GLY HIS VAL CYS HIS LEU CYS HIS PRO SEQRES 47 A 627 ASN CYS THR TYR GLY CYS THR GLY PRO GLY LEU GLU GLY SEQRES 48 A 627 CYS PRO THR ASN GLY PRO LYS ILE PRO SER HIS HIS HIS SEQRES 49 A 627 HIS HIS HIS SEQRES 1 D 250 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 D 250 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 D 250 TYR THR PHE THR SER TYR TRP MET HIS TRP VAL ARG GLN SEQRES 4 D 250 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY ASN ILE TRP SEQRES 5 D 250 PRO GLY SER GLY GLY THR ASN TYR ALA GLU LYS PHE LYS SEQRES 6 D 250 ASN ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 D 250 ALA TYR MET GLU LEU SER ARG LEU ARG SER ASP ASP THR SEQRES 8 D 250 ALA VAL TYR TYR CYS ALA ARG SER GLY GLY PRO TYR PHE SEQRES 9 D 250 PHE ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 D 250 SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY SEQRES 11 D 250 GLY GLY SER GLY GLY GLY GLY SER ASP ILE VAL MET THR SEQRES 12 D 250 GLN SER PRO LEU SER LEU PRO VAL THR PRO GLY GLU PRO SEQRES 13 D 250 ALA SER ILE SER CYS ARG SER SER GLN ASN ILE VAL HIS SEQRES 14 D 250 ASN ASN GLY ILE THR TYR LEU GLU TRP TYR LEU GLN LYS SEQRES 15 D 250 PRO GLY GLN SER PRO GLN LEU LEU ILE TYR LYS VAL SER SEQRES 16 D 250 ASP ARG PHE SER GLY VAL PRO ASP ARG PHE SER GLY SER SEQRES 17 D 250 GLY SER GLY THR ASP PHE THR LEU LYS ILE SER ARG VAL SEQRES 18 D 250 GLU ALA GLU ASP VAL GLY VAL TYR TYR CYS PHE GLN GLY SEQRES 19 D 250 SER HIS ILE PRO PRO THR PHE GLY GLN GLY THR LYS VAL SEQRES 20 D 250 GLU ILE LYS HET NAG B 1 14 HET NAG B 2 14 HET NAG C 1 14 HET NAG C 2 14 HET NAG A 701 14 HET NAG A 702 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE 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 FORMUL 3 NAG 6(C8 H15 N O6) HELIX 1 AA1 PHE A 20 MET A 30 1 11 HELIX 2 AA2 GLN A 139 VAL A 144 1 6 HELIX 3 AA3 ASP A 147 ASN A 151 5 5 HELIX 4 AA4 ILE A 318 LYS A 322 5 5 HELIX 5 AA5 LEU A 348 GLY A 354 1 7 HELIX 6 AA6 ASP A 364 VAL A 374 5 11 HELIX 7 AA7 LEU A 393 GLU A 397 5 5 HELIX 8 AA8 LYS A 407 GLY A 410 5 4 HELIX 9 AA9 ASN A 452 PHE A 457 1 6 HELIX 10 AB1 GLY A 471 THR A 478 1 8 HELIX 11 AB2 GLU A 495 CYS A 499 5 5 HELIX 12 AB3 GLU A 578 ASN A 580 5 3 HELIX 13 AB4 THR D 144 TYR D 148 5 5 HELIX 14 AB5 ARG D 203 THR D 207 5 5 HELIX 15 AB6 GLU D 338 VAL D 342 5 5 SHEET 1 AA1 5 VAL A 6 CYS A 7 0 SHEET 2 AA1 5 VAL A 36 VAL A 37 1 O VAL A 36 N CYS A 7 SHEET 3 AA1 5 GLU A 60 VAL A 61 1 O GLU A 60 N VAL A 37 SHEET 4 AA1 5 ILE A 82 ILE A 83 1 O ILE A 82 N VAL A 61 SHEET 5 AA1 5 GLU A 118 ILE A 119 1 O GLU A 118 N ILE A 83 SHEET 1 AA2 4 LEU A 41 VAL A 46 0 SHEET 2 AA2 4 VAL A 65 ASN A 70 1 O LEU A 66 N LEU A 41 SHEET 3 AA2 4 TYR A 93 LEU A 98 1 O ALA A 94 N VAL A 65 SHEET 4 AA2 4 ALA A 123 SER A 127 1 O ARG A 125 N LEU A 95 SHEET 1 AA3 2 PHE A 230 ARG A 231 0 SHEET 2 AA3 2 CYS A 236 LYS A 237 -1 O LYS A 237 N PHE A 230 SHEET 1 AA4 2 MET A 244 TYR A 246 0 SHEET 2 AA4 2 MET A 253 VAL A 255 -1 O ASP A 254 N LEU A 245 SHEET 1 AA5 2 TYR A 261 PHE A 263 0 SHEET 2 AA5 2 THR A 266 VAL A 268 -1 O THR A 266 N PHE A 263 SHEET 1 AA6 2 VAL A 276 VAL A 277 0 SHEET 2 AA6 2 CYS A 283 VAL A 284 -1 O VAL A 284 N VAL A 276 SHEET 1 AA7 2 SER A 291 GLU A 295 0 SHEET 2 AA7 2 ARG A 300 LYS A 304 -1 O LYS A 301 N MET A 294 SHEET 1 AA8 4 LEU A 345 ILE A 347 0 SHEET 2 AA8 4 LEU A 381 ILE A 383 1 O LEU A 382 N LEU A 345 SHEET 3 AA8 4 PHE A 412 VAL A 417 1 O SER A 413 N LEU A 381 SHEET 4 AA8 4 ASP A 436 SER A 440 1 O ILE A 438 N LEU A 414 SHEET 1 AA9 2 GLU A 376 ILE A 377 0 SHEET 2 AA9 2 ILE A 401 ILE A 402 1 O ILE A 401 N ILE A 377 SHEET 1 AB1 2 GLU A 524 VAL A 526 0 SHEET 2 AB1 2 CYS A 531 GLN A 533 -1 O ILE A 532 N PHE A 525 SHEET 1 AB2 5 HIS A 566 CYS A 567 0 SHEET 2 AB2 5 ILE A 562 ASP A 563 -1 N ASP A 563 O HIS A 566 SHEET 3 AB2 5 VAL A 592 LEU A 595 1 O CYS A 593 N ILE A 562 SHEET 4 AB2 5 LEU A 582 ALA A 587 -1 N TYR A 586 O HIS A 594 SHEET 5 AB2 5 ALA A 573 MET A 576 -1 N VAL A 575 O VAL A 583 SHEET 1 AB3 4 GLN D 119 GLN D 122 0 SHEET 2 AB3 4 VAL D 134 SER D 141 -1 O LYS D 139 N VAL D 121 SHEET 3 AB3 4 THR D 194 LEU D 199 -1 O LEU D 199 N VAL D 134 SHEET 4 AB3 4 VAL D 184 THR D 185 -1 N THR D 185 O GLU D 198 SHEET 1 AB4 4 GLN D 119 GLN D 122 0 SHEET 2 AB4 4 VAL D 134 SER D 141 -1 O LYS D 139 N VAL D 121 SHEET 3 AB4 4 THR D 194 LEU D 199 -1 O LEU D 199 N VAL D 134 SHEET 4 AB4 4 ARG D 188 ASP D 189 -1 N ASP D 189 O THR D 194 SHEET 1 AB5 5 GLU D 126 LYS D 128 0 SHEET 2 AB5 5 THR D 228 VAL D 232 1 O THR D 231 N GLU D 126 SHEET 3 AB5 5 ALA D 208 CYS D 212 -1 N TYR D 210 O THR D 228 SHEET 4 AB5 5 TRP D 152 GLN D 155 -1 N VAL D 153 O TYR D 211 SHEET 5 AB5 5 LEU D 161 TRP D 163 -1 O GLU D 162 N ARG D 154 SHEET 1 AB6 2 GLY D 165 ASN D 166 0 SHEET 2 AB6 2 ASN D 175 TYR D 176 -1 O ASN D 175 N ASN D 166 SHEET 1 AB7 4 MET D 258 THR D 259 0 SHEET 2 AB7 4 ALA D 273 SER D 279 -1 O ARG D 278 N THR D 259 SHEET 3 AB7 4 ASP D 329 ILE D 334 -1 O LEU D 332 N ILE D 275 SHEET 4 AB7 4 PHE D 321 SER D 326 -1 N SER D 324 O THR D 331 SHEET 1 AB8 5 PRO D 266 VAL D 267 0 SHEET 2 AB8 5 THR D 361 ILE D 365 1 O GLU D 364 N VAL D 267 SHEET 3 AB8 5 GLY D 343 GLN D 349 -1 N GLY D 343 O VAL D 363 SHEET 4 AB8 5 LEU D 292 GLN D 297 -1 N GLU D 293 O PHE D 348 SHEET 5 AB8 5 GLN D 304 ILE D 307 -1 O LEU D 306 N TRP D 294 SSBOND 1 CYS A 7 CYS A 34 1555 1555 2.03 SSBOND 2 CYS A 212 CYS A 224 1555 1555 2.03 SSBOND 3 CYS A 227 CYS A 236 1555 1555 2.03 SSBOND 4 CYS A 240 CYS A 267 1555 1555 2.03 SSBOND 5 CYS A 271 CYS A 283 1555 1555 2.03 SSBOND 6 CYS A 287 CYS A 302 1555 1555 2.04 SSBOND 7 CYS A 305 CYS A 309 1555 1555 2.03 SSBOND 8 CYS A 313 CYS A 338 1555 1555 2.03 SSBOND 9 CYS A 446 CYS A 475 1555 1555 2.02 SSBOND 10 CYS A 482 CYS A 491 1555 1555 2.03 SSBOND 11 CYS A 486 CYS A 499 1555 1555 2.03 SSBOND 12 CYS A 502 CYS A 511 1555 1555 2.03 SSBOND 13 CYS A 515 CYS A 531 1555 1555 2.03 SSBOND 14 CYS A 534 CYS A 547 1555 1555 2.03 SSBOND 15 CYS A 538 CYS A 555 1555 1555 2.03 SSBOND 16 CYS A 558 CYS A 567 1555 1555 2.04 SSBOND 17 CYS A 571 CYS A 593 1555 1555 2.03 SSBOND 18 CYS D 138 CYS D 212 1555 1555 2.03 SSBOND 19 CYS D 277 CYS D 347 1555 1555 2.03 LINK ND2 ASN A 328 C1 NAG B 1 1555 1555 1.46 LINK ND2 ASN A 337 C1 NAG A 701 1555 1555 1.44 LINK ND2 ASN A 420 C1 NAG C 1 1555 1555 1.44 LINK ND2 ASN A 504 C1 NAG A 702 1555 1555 1.45 LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.43 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44 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