HEADER IMMUNE SYSTEM 15-DEC-24 9L1S TITLE STRUCTURE OF THE HER2 (S310F) - PERTUZUMAB (T30S/D31A) COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-2; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: METASTATIC LYMPH NODE GENE 19 PROTEIN,MLN 19,PROTO-ONCOGENE COMPND 5 NEU,PROTO-ONCOGENE C-ERBB-2,TYROSINE KINASE-TYPE CELL SURFACE COMPND 6 RECEPTOR HER2,P185ERBB2; COMPND 7 EC: 2.7.10.1; COMPND 8 ENGINEERED: YES; COMPND 9 MUTATION: YES; COMPND 10 MOL_ID: 2; COMPND 11 MOLECULE: PERTUZUMAB FAB LIGHT CHAIN; COMPND 12 CHAIN: B; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 3; COMPND 15 MOLECULE: PERTUZUMAB FAB HEAVY CHAIN; COMPND 16 CHAIN: C; COMPND 17 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: ERBB2, HER2, MLN19, NEU, NGL; 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_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ANTIGEN, ANTIBODY, IMMUNE SYSTEM EXPDTA ELECTRON MICROSCOPY AUTHOR L.XU,J.GUO REVDAT 1 01-JAN-25 9L1S 0 JRNL AUTH X.BAI,L.XU,Z.WANG,X.ZHUANG,J.NING,Y.SUN,H.WANG,Y.GUO,Y.XU, JRNL AUTH 2 J.GUO,S.CHEN,L.PAN JRNL TITL COMPUTATIONAL-AIDED RATIONAL MUTATION DESIGN OF PERTUZUMAB JRNL TITL 2 TO OVERCOME ACTIVE HER2 MUTATION S310F THROUGH ANTIBODY-DRUG JRNL TITL 3 CONJUGATES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.00 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) : 3.000 REMARK 3 NUMBER OF PARTICLES : 167849 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 9L1S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 17-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1300054731. 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 : HER2 (S310F) - PERTUZUMAB REMARK 245 (T30S/D31A) COMPLEX 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 : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1500.00 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) : 6400.00 REMARK 245 ILLUMINATION MODE : OTHER 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 PRO A 122 REMARK 465 LEU A 123 REMARK 465 ASN A 124 REMARK 465 ASN A 125 REMARK 465 THR A 126 REMARK 465 THR A 127 REMARK 465 PRO A 128 REMARK 465 VAL A 129 REMARK 465 THR A 130 REMARK 465 GLY A 131 REMARK 465 ALA A 132 REMARK 465 CYS A 587 REMARK 465 ALA A 588 REMARK 465 HIS A 589 REMARK 465 TYR A 590 REMARK 465 LYS A 591 REMARK 465 ASP A 592 REMARK 465 PRO A 593 REMARK 465 PRO A 594 REMARK 465 PHE A 595 REMARK 465 CYS A 596 REMARK 465 VAL A 597 REMARK 465 ALA A 598 REMARK 465 ARG A 599 REMARK 465 CYS A 600 REMARK 465 PRO A 601 REMARK 465 SER A 602 REMARK 465 GLY A 603 REMARK 465 VAL A 604 REMARK 465 LYS A 605 REMARK 465 PRO A 606 REMARK 465 ASP A 607 REMARK 465 LEU A 608 REMARK 465 SER A 609 REMARK 465 TYR A 610 REMARK 465 MET A 611 REMARK 465 PRO A 612 REMARK 465 ILE A 613 REMARK 465 TRP A 614 REMARK 465 LYS A 615 REMARK 465 PHE A 616 REMARK 465 PRO A 617 REMARK 465 ASP A 618 REMARK 465 GLU A 619 REMARK 465 GLU A 620 REMARK 465 GLY A 621 REMARK 465 ALA A 622 REMARK 465 CYS A 623 REMARK 465 GLN A 624 REMARK 465 PRO A 625 REMARK 465 CYS A 626 REMARK 465 PRO A 627 REMARK 465 ILE A 628 REMARK 465 ASN A 629 REMARK 465 CYS A 630 REMARK 465 THR A 631 REMARK 465 HIS A 632 REMARK 465 SER A 633 REMARK 465 CYS A 634 REMARK 465 VAL A 635 REMARK 465 ASP A 636 REMARK 465 LEU A 637 REMARK 465 ASP A 638 REMARK 465 ASP A 639 REMARK 465 LYS A 640 REMARK 465 GLY A 641 REMARK 465 CYS A 642 REMARK 465 PRO A 643 REMARK 465 ALA A 644 REMARK 465 GLU A 645 REMARK 465 GLN A 646 REMARK 465 ARG A 647 REMARK 465 ALA A 648 REMARK 465 SER A 649 REMARK 465 PRO A 650 REMARK 465 LEU A 651 REMARK 465 THR A 652 REMARK 465 HIS A 653 REMARK 465 HIS A 654 REMARK 465 HIS A 655 REMARK 465 HIS A 656 REMARK 465 HIS A 657 REMARK 465 HIS A 658 REMARK 465 ASP C 217 REMARK 465 LYS C 218 REMARK 465 THR C 219 REMARK 465 HIS C 220 REMARK 465 THR C 221 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 O CYS A 504 CD1 LEU A 509 1.95 REMARK 500 OH TYR A 301 OE2 GLU A 460 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 THR A 41 52.21 -93.69 REMARK 500 TYR A 64 62.39 61.15 REMARK 500 ASP A 110 16.79 58.10 REMARK 500 ARG A 157 60.58 60.71 REMARK 500 ASN A 176 30.15 -94.70 REMARK 500 ALA A 241 -61.29 -92.22 REMARK 500 THR A 276 1.40 58.05 REMARK 500 HIS A 318 17.15 59.64 REMARK 500 ASN A 388 54.26 -93.70 REMARK 500 LEU A 422 38.28 -98.81 REMARK 500 SER A 423 4.51 -67.18 REMARK 500 ASN A 438 9.54 59.92 REMARK 500 TRP A 452 -74.50 -116.72 REMARK 500 LEU A 453 -40.58 -144.40 REMARK 500 HIS A 473 31.55 -96.99 REMARK 500 PRO A 481 75.46 -69.62 REMARK 500 ALA A 510 47.40 -145.32 REMARK 500 CYS A 511 73.20 59.07 REMARK 500 HIS A 512 130.28 -34.28 REMARK 500 GLN A 533 -66.11 -93.47 REMARK 500 GLU A 542 -165.61 -116.94 REMARK 500 GLU A 543 130.43 -38.85 REMARK 500 GLU A 566 49.87 -86.77 REMARK 500 SER B 50 19.41 58.56 REMARK 500 ALA B 51 -4.59 67.33 REMARK 500 PRO B 80 47.90 -69.78 REMARK 500 GLU B 81 -16.73 -141.43 REMARK 500 ASP B 151 -23.22 68.03 REMARK 500 ASN B 152 -20.67 -150.34 REMARK 500 ALA C 31 -12.71 -143.15 REMARK 500 ASP C 86 30.67 -94.64 REMARK 500 PRO C 98 48.56 -67.00 REMARK 500 ASN C 155 49.84 34.00 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-62753 RELATED DB: EMDB REMARK 900 STRUCTURE OF THE HER2 (S310F) - PERTUZUMAB (T30S/D31A) COMPLEX DBREF 9L1S A 23 652 UNP P04626 ERBB2_HUMAN 23 652 DBREF 9L1S B 1 214 PDB 9L1S 9L1S 1 214 DBREF 9L1S C 1 221 PDB 9L1S 9L1S 1 221 SEQADV 9L1S PHE A 310 UNP P04626 SER 310 ENGINEERED MUTATION SEQADV 9L1S VAL A 435 UNP P04626 ILE 435 CONFLICT SEQADV 9L1S HIS A 653 UNP P04626 EXPRESSION TAG SEQADV 9L1S HIS A 654 UNP P04626 EXPRESSION TAG SEQADV 9L1S HIS A 655 UNP P04626 EXPRESSION TAG SEQADV 9L1S HIS A 656 UNP P04626 EXPRESSION TAG SEQADV 9L1S HIS A 657 UNP P04626 EXPRESSION TAG SEQADV 9L1S HIS A 658 UNP P04626 EXPRESSION TAG SEQRES 1 A 636 THR GLN VAL CYS THR GLY THR ASP MET LYS LEU ARG LEU SEQRES 2 A 636 PRO ALA SER PRO GLU THR HIS LEU ASP MET LEU ARG HIS SEQRES 3 A 636 LEU TYR GLN GLY CYS GLN VAL VAL GLN GLY ASN LEU GLU SEQRES 4 A 636 LEU THR TYR LEU PRO THR ASN ALA SER LEU SER PHE LEU SEQRES 5 A 636 GLN ASP ILE GLN GLU VAL GLN GLY TYR VAL LEU ILE ALA SEQRES 6 A 636 HIS ASN GLN VAL ARG GLN VAL PRO LEU GLN ARG LEU ARG SEQRES 7 A 636 ILE VAL ARG GLY THR GLN LEU PHE GLU ASP ASN TYR ALA SEQRES 8 A 636 LEU ALA VAL LEU ASP ASN GLY ASP PRO LEU ASN ASN THR SEQRES 9 A 636 THR PRO VAL THR GLY ALA SER PRO GLY GLY LEU ARG GLU SEQRES 10 A 636 LEU GLN LEU ARG SER LEU THR GLU ILE LEU LYS GLY GLY SEQRES 11 A 636 VAL LEU ILE GLN ARG ASN PRO GLN LEU CYS TYR GLN ASP SEQRES 12 A 636 THR ILE LEU TRP LYS ASP ILE PHE HIS LYS ASN ASN GLN SEQRES 13 A 636 LEU ALA LEU THR LEU ILE ASP THR ASN ARG SER ARG ALA SEQRES 14 A 636 CYS HIS PRO CYS SER PRO MET CYS LYS GLY SER ARG CYS SEQRES 15 A 636 TRP GLY GLU SER SER GLU ASP CYS GLN SER LEU THR ARG SEQRES 16 A 636 THR VAL CYS ALA GLY GLY CYS ALA ARG CYS LYS GLY PRO SEQRES 17 A 636 LEU PRO THR ASP CYS CYS HIS GLU GLN CYS ALA ALA GLY SEQRES 18 A 636 CYS THR GLY PRO LYS HIS SER ASP CYS LEU ALA CYS LEU SEQRES 19 A 636 HIS PHE ASN HIS SER GLY ILE CYS GLU LEU HIS CYS PRO SEQRES 20 A 636 ALA LEU VAL THR TYR ASN THR ASP THR PHE GLU SER MET SEQRES 21 A 636 PRO ASN PRO GLU GLY ARG TYR THR PHE GLY ALA SER CYS SEQRES 22 A 636 VAL THR ALA CYS PRO TYR ASN TYR LEU SER THR ASP VAL SEQRES 23 A 636 GLY PHE CYS THR LEU VAL CYS PRO LEU HIS ASN GLN GLU SEQRES 24 A 636 VAL THR ALA GLU ASP GLY THR GLN ARG CYS GLU LYS CYS SEQRES 25 A 636 SER LYS PRO CYS ALA ARG VAL CYS TYR GLY LEU GLY MET SEQRES 26 A 636 GLU HIS LEU ARG GLU VAL ARG ALA VAL THR SER ALA ASN SEQRES 27 A 636 ILE GLN GLU PHE ALA GLY CYS LYS LYS ILE PHE GLY SER SEQRES 28 A 636 LEU ALA PHE LEU PRO GLU SER PHE ASP GLY ASP PRO ALA SEQRES 29 A 636 SER ASN THR ALA PRO LEU GLN PRO GLU GLN LEU GLN VAL SEQRES 30 A 636 PHE GLU THR LEU GLU GLU ILE THR GLY TYR LEU TYR ILE SEQRES 31 A 636 SER ALA TRP PRO ASP SER LEU PRO ASP LEU SER VAL PHE SEQRES 32 A 636 GLN ASN LEU GLN VAL ILE ARG GLY ARG VAL LEU HIS ASN SEQRES 33 A 636 GLY ALA TYR SER LEU THR LEU GLN GLY LEU GLY ILE SER SEQRES 34 A 636 TRP LEU GLY LEU ARG SER LEU ARG GLU LEU GLY SER GLY SEQRES 35 A 636 LEU ALA LEU ILE HIS HIS ASN THR HIS LEU CYS PHE VAL SEQRES 36 A 636 HIS THR VAL PRO TRP ASP GLN LEU PHE ARG ASN PRO HIS SEQRES 37 A 636 GLN ALA LEU LEU HIS THR ALA ASN ARG PRO GLU ASP GLU SEQRES 38 A 636 CYS VAL GLY GLU GLY LEU ALA CYS HIS GLN LEU CYS ALA SEQRES 39 A 636 ARG GLY HIS CYS TRP GLY PRO GLY PRO THR GLN CYS VAL SEQRES 40 A 636 ASN CYS SER GLN PHE LEU ARG GLY GLN GLU CYS VAL GLU SEQRES 41 A 636 GLU CYS ARG VAL LEU GLN GLY LEU PRO ARG GLU TYR VAL SEQRES 42 A 636 ASN ALA ARG HIS CYS LEU PRO CYS HIS PRO GLU CYS GLN SEQRES 43 A 636 PRO GLN ASN GLY SER VAL THR CYS PHE GLY PRO GLU ALA SEQRES 44 A 636 ASP GLN CYS VAL ALA CYS ALA HIS TYR LYS ASP PRO PRO SEQRES 45 A 636 PHE CYS VAL ALA ARG CYS PRO SER GLY VAL LYS PRO ASP SEQRES 46 A 636 LEU SER TYR MET PRO ILE TRP LYS PHE PRO ASP GLU GLU SEQRES 47 A 636 GLY ALA CYS GLN PRO CYS PRO ILE ASN CYS THR HIS SER SEQRES 48 A 636 CYS VAL ASP LEU ASP ASP LYS GLY CYS PRO ALA GLU GLN SEQRES 49 A 636 ARG ALA SER PRO LEU THR HIS HIS HIS HIS HIS HIS SEQRES 1 B 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 B 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS LYS ALA SER SEQRES 3 B 214 GLN ASP VAL SER ILE GLY VAL ALA TRP TYR GLN GLN LYS SEQRES 4 B 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 B 214 TYR ARG TYR THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 B 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 B 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 B 214 TYR ILE TYR PRO TYR THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 B 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 B 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 B 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 B 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 B 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 B 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 B 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 B 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 B 214 PHE ASN ARG GLY GLU CYS SEQRES 1 C 227 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 227 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 C 227 PHE THR PHE SER ALA TYR THR MET ASP TRP VAL ARG GLN SEQRES 4 C 227 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ASP VAL ASN SEQRES 5 C 227 PRO ASN SER GLY GLY SER ILE TYR ASN GLN ARG PHE LYS SEQRES 6 C 227 GLY ARG PHE THR LEU SER VAL ASP ARG SER LYS ASN THR SEQRES 7 C 227 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 C 227 ALA VAL TYR TYR CYS ALA ARG ASN LEU GLY PRO SER PHE SEQRES 9 C 227 TYR PHE ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 10 C 227 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11 C 227 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12 C 227 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 C 227 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14 C 227 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 C 227 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 C 227 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17 C 227 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 18 C 227 CYS ASP LYS THR HIS THR HELIX 1 AA1 HIS A 42 HIS A 48 1 7 HELIX 2 AA2 LEU A 71 GLN A 75 5 5 HELIX 3 AA3 LEU A 107 ASN A 111 5 5 HELIX 4 AA4 LEU A 168 PHE A 173 1 6 HELIX 5 AA5 SER A 208 CYS A 212 5 5 HELIX 6 AA6 LEU A 231 CYS A 235 5 5 HELIX 7 AA7 GLU A 395 GLU A 401 5 7 HELIX 8 AA8 LEU A 436 GLY A 439 5 4 HELIX 9 AA9 PRO A 500 GLY A 506 1 7 HELIX 10 AB1 CYS A 515 HIS A 519 5 5 HELIX 11 AB2 LYS B 183 GLU B 187 1 5 HELIX 12 AB3 THR C 28 TYR C 32 5 5 HELIX 13 AB4 SER C 156 ALA C 158 5 3 SHEET 1 AA1 5 VAL A 25 CYS A 26 0 SHEET 2 AA1 5 VAL A 55 VAL A 56 1 O VAL A 55 N CYS A 26 SHEET 3 AA1 5 GLU A 79 VAL A 80 1 O GLU A 79 N VAL A 56 SHEET 4 AA1 5 ILE A 101 VAL A 102 1 O ILE A 101 N VAL A 80 SHEET 5 AA1 5 GLU A 147 ILE A 148 1 O GLU A 147 N VAL A 102 SHEET 1 AA2 5 LEU A 60 LEU A 65 0 SHEET 2 AA2 5 VAL A 84 ASN A 89 1 O LEU A 85 N LEU A 62 SHEET 3 AA2 5 LEU A 114 LEU A 117 1 O ALA A 115 N ILE A 86 SHEET 4 AA2 5 VAL A 153 GLN A 156 1 O LEU A 154 N VAL A 116 SHEET 5 AA2 5 THR A 182 ILE A 184 1 O LEU A 183 N ILE A 155 SHEET 1 AA3 2 PHE A 258 HIS A 260 0 SHEET 2 AA3 2 ILE A 263 GLU A 265 -1 O ILE A 263 N HIS A 260 SHEET 1 AA4 2 VAL A 272 TYR A 274 0 SHEET 2 AA4 2 SER A 281 PRO A 283 -1 O MET A 282 N THR A 273 SHEET 1 AA5 2 TYR A 289 PHE A 291 0 SHEET 2 AA5 2 SER A 294 VAL A 296 -1 O VAL A 296 N TYR A 289 SHEET 1 AA6 2 LEU A 304 SER A 305 0 SHEET 2 AA6 2 CYS A 311 THR A 312 -1 O THR A 312 N LEU A 304 SHEET 1 AA7 2 ASN A 319 THR A 323 0 SHEET 2 AA7 2 GLN A 329 LYS A 333 -1 O GLU A 332 N GLN A 320 SHEET 1 AA8 2 CYS A 342 TYR A 343 0 SHEET 2 AA8 2 ILE A 370 PHE A 371 1 O PHE A 371 N CYS A 342 SHEET 1 AA9 5 LEU A 374 PHE A 376 0 SHEET 2 AA9 5 LEU A 410 ILE A 412 1 O TYR A 411 N PHE A 376 SHEET 3 AA9 5 TYR A 441 GLN A 446 1 O THR A 444 N ILE A 412 SHEET 4 AA9 5 LEU A 465 HIS A 469 1 O LEU A 465 N SER A 442 SHEET 5 AA9 5 LEU A 493 LEU A 494 1 O LEU A 494 N ALA A 466 SHEET 1 AB1 3 GLU A 405 ILE A 406 0 SHEET 2 AB1 3 VAL A 430 ILE A 431 1 O VAL A 430 N ILE A 406 SHEET 3 AB1 3 GLU A 460 LEU A 461 1 O GLU A 460 N ILE A 431 SHEET 1 AB2 3 GLU A 539 VAL A 541 0 SHEET 2 AB2 3 PHE A 534 ARG A 536 -1 N PHE A 534 O VAL A 541 SHEET 3 AB2 3 HIS A 559 CYS A 560 1 O CYS A 560 N LEU A 535 SHEET 1 AB3 2 ARG A 552 GLU A 553 0 SHEET 2 AB3 2 PRO A 562 CYS A 563 -1 O CYS A 563 N ARG A 552 SHEET 1 AB4 4 THR B 5 SER B 7 0 SHEET 2 AB4 4 VAL B 19 LYS B 24 -1 O LYS B 24 N THR B 5 SHEET 3 AB4 4 ASP B 70 ILE B 75 -1 O LEU B 73 N ILE B 21 SHEET 4 AB4 4 SER B 63 SER B 65 -1 N SER B 63 O THR B 74 SHEET 1 AB5 3 SER B 10 ALA B 13 0 SHEET 2 AB5 3 THR B 102 ILE B 106 1 O LYS B 103 N LEU B 11 SHEET 3 AB5 3 THR B 85 TYR B 86 -1 N TYR B 86 O THR B 102 SHEET 1 AB6 4 TYR B 53 ARG B 54 0 SHEET 2 AB6 4 LYS B 45 TYR B 49 -1 N TYR B 49 O TYR B 53 SHEET 3 AB6 4 VAL B 33 GLN B 37 -1 N TRP B 35 O ILE B 48 SHEET 4 AB6 4 CYS B 88 GLN B 90 -1 O GLN B 89 N ALA B 34 SHEET 1 AB7 3 THR B 129 VAL B 133 0 SHEET 2 AB7 3 THR B 178 SER B 182 -1 O LEU B 181 N ALA B 130 SHEET 3 AB7 3 SER B 159 GLN B 160 -1 N GLN B 160 O THR B 178 SHEET 1 AB8 3 LYS B 145 VAL B 150 0 SHEET 2 AB8 3 VAL B 191 THR B 197 -1 O GLU B 195 N GLN B 147 SHEET 3 AB8 3 THR B 206 ASN B 210 -1 O PHE B 209 N TYR B 192 SHEET 1 AB9 4 VAL C 5 SER C 7 0 SHEET 2 AB9 4 LEU C 18 ALA C 23 -1 O ALA C 23 N VAL C 5 SHEET 3 AB9 4 THR C 77 MET C 82 -1 O MET C 82 N LEU C 18 SHEET 4 AB9 4 PHE C 67 ASP C 72 -1 N THR C 68 O GLN C 81 SHEET 1 AC1 6 GLY C 10 VAL C 12 0 SHEET 2 AC1 6 THR C 107 VAL C 111 1 O THR C 110 N GLY C 10 SHEET 3 AC1 6 ALA C 88 TYR C 91 -1 N TYR C 90 O THR C 107 SHEET 4 AC1 6 MET C 34 GLN C 39 -1 N VAL C 37 O TYR C 91 SHEET 5 AC1 6 LEU C 45 VAL C 51 -1 O GLU C 46 N ARG C 38 SHEET 6 AC1 6 ILE C 58 TYR C 59 -1 O ILE C 58 N ASP C 50 SHEET 1 AC2 4 PHE C 122 LEU C 124 0 SHEET 2 AC2 4 THR C 135 LEU C 141 -1 O GLY C 139 N LEU C 124 SHEET 3 AC2 4 SER C 179 PRO C 185 -1 O VAL C 184 N ALA C 136 SHEET 4 AC2 4 VAL C 163 THR C 165 -1 N HIS C 164 O VAL C 181 SHEET 1 AC3 3 THR C 151 TRP C 154 0 SHEET 2 AC3 3 TYR C 194 ASN C 199 -1 O ASN C 197 N SER C 153 SHEET 3 AC3 3 ASP C 208 VAL C 211 -1 O VAL C 211 N TYR C 194 SHEET 1 AC4 2 VAL C 169 LEU C 170 0 SHEET 2 AC4 2 TYR C 176 SER C 177 -1 O SER C 177 N VAL C 169 SSBOND 1 CYS A 26 CYS A 53 1555 1555 2.03 SSBOND 2 CYS A 162 CYS A 192 1555 1555 2.03 SSBOND 3 CYS A 195 CYS A 204 1555 1555 2.03 SSBOND 4 CYS A 199 CYS A 212 1555 1555 2.03 SSBOND 5 CYS A 220 CYS A 227 1555 1555 2.03 SSBOND 6 CYS A 224 CYS A 235 1555 1555 2.03 SSBOND 7 CYS A 236 CYS A 244 1555 1555 2.03 SSBOND 8 CYS A 240 CYS A 252 1555 1555 2.03 SSBOND 9 CYS A 255 CYS A 264 1555 1555 2.03 SSBOND 10 CYS A 268 CYS A 295 1555 1555 2.03 SSBOND 11 CYS A 299 CYS A 311 1555 1555 2.03 SSBOND 12 CYS A 315 CYS A 331 1555 1555 2.03 SSBOND 13 CYS A 342 CYS A 367 1555 1555 2.03 SSBOND 14 CYS A 475 CYS A 504 1555 1555 2.03 SSBOND 15 CYS A 511 CYS A 520 1555 1555 2.03 SSBOND 16 CYS A 515 CYS A 528 1555 1555 2.03 SSBOND 17 CYS A 544 CYS A 560 1555 1555 2.03 SSBOND 18 CYS B 23 CYS B 88 1555 1555 2.04 SSBOND 19 CYS B 134 CYS B 194 1555 1555 2.03 SSBOND 20 CYS C 22 CYS C 92 1555 1555 2.03 SSBOND 21 CYS C 140 CYS C 196 1555 1555 2.03 CISPEP 1 SER B 7 PRO B 8 0 -1.99 CISPEP 2 TYR B 94 PRO B 95 0 -3.09 CISPEP 3 TYR B 140 PRO B 141 0 1.69 CISPEP 4 PHE C 146 PRO C 147 0 -1.85 CISPEP 5 GLU C 148 PRO C 149 0 -4.12 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