HEADER VIRAL PROTEIN/IMMUNE SYSTEM 09-OCT-24 9DWE TITLE CRYO-EM STRUCTURE OF HEMAGGLUTININ H5 A/TEXAS/37/2024 IN COMPLEX WITH TITLE 2 LSTA AND ANTIBODY CR9114 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CR9114 FAB LIGHT CHAIN; COMPND 3 CHAIN: L, M, N; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: CR9114 FAB FAB HEAVY CHAIN; COMPND 7 CHAIN: H, I, J; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HEMAGGLUTININ; COMPND 11 CHAIN: A, B, C; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: EXPICHO; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: EXPICHO; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 15 ORGANISM_TAXID: 11320; SOURCE 16 GENE: HA; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM_CELL_LINE: 293F KEYWDS HEMAGGLUTININ, SIALIC ACID COMPLEX, ANTIBODY, VIRAL PROTEIN, H5N1, KEYWDS 2 VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR M.L.FERNANDEZ-QUINTERO,J.HAN,A.J.RODRIGUEZ,A.B.WARD REVDAT 1 04-DEC-24 9DWE 0 JRNL AUTH M.GOOD,M.L.FERNANDEZ-QUINTERO,W.JI,J.HAN,A.J.RODRIGUEZ, JRNL AUTH 2 A.B.WARD,J.J.GUTHMILLER JRNL TITL A SINGLE MUTATION IN DAIRY COW-ASSOCIATED H5N1 VIRUSES JRNL TITL 2 INCREASES RECEPTOR BINDING BREADTH JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, COOT, CRYOSPARC, PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 4FQH 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) : 2.800 REMARK 3 NUMBER OF PARTICLES : 260000 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9DWE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-24. REMARK 100 THE DEPOSITION ID IS D_1000288880. 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 : HEMAGGLUTININ H5 REMARK 245 A/TEXAS/37/2024 HOMOTRIMER REMARK 245 BOUND TO LSTA AND CR9114 FAB; REMARK 245 CR9114 FAB; HEMAGGLUTININ REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.70 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 : 4922 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS GLACIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1600.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4163.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 190000 REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 200 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: NONAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, A, M, I, B, N, J, C, P, REMARK 350 AND CHAINS: D, E 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 MET A -5 REMARK 465 GLU A -4 REMARK 465 ASN A -3 REMARK 465 ILE A -2 REMARK 465 VAL A -1 REMARK 465 LEU A 0 REMARK 465 LEU A 1 REMARK 465 LEU A 2 REMARK 465 ALA A 3 REMARK 465 ILE A 4 REMARK 465 VAL A 5 REMARK 465 SER A 6 REMARK 465 LEU A 7 REMARK 465 ARG A 333 REMARK 465 GLU A 334 REMARK 465 LYS A 335 REMARK 465 ARG A 336 REMARK 465 ARG A 337 REMARK 465 LYS A 338 REMARK 465 ARG A 339 REMARK 465 GLY A 514 REMARK 465 SER A 515 REMARK 465 GLY A 516 REMARK 465 TYR A 517 REMARK 465 ILE A 518 REMARK 465 PRO A 519 REMARK 465 GLU A 520 REMARK 465 ALA A 521 REMARK 465 PRO A 522 REMARK 465 ARG A 523 REMARK 465 ASP A 524 REMARK 465 GLY A 525 REMARK 465 GLN A 526 REMARK 465 ALA A 527 REMARK 465 TYR A 528 REMARK 465 VAL A 529 REMARK 465 ARG A 530 REMARK 465 LYS A 531 REMARK 465 ASP A 532 REMARK 465 GLY A 533 REMARK 465 GLU A 534 REMARK 465 TRP A 535 REMARK 465 VAL A 536 REMARK 465 LEU A 537 REMARK 465 LEU A 538 REMARK 465 SER A 539 REMARK 465 THR A 540 REMARK 465 PHE A 541 REMARK 465 LEU A 542 REMARK 465 GLY A 543 REMARK 465 SER A 544 REMARK 465 GLY A 545 REMARK 465 LEU A 546 REMARK 465 ASN A 547 REMARK 465 ASP A 548 REMARK 465 ILE A 549 REMARK 465 PHE A 550 REMARK 465 GLU A 551 REMARK 465 ALA A 552 REMARK 465 GLN A 553 REMARK 465 LYS A 554 REMARK 465 ILE A 555 REMARK 465 GLU A 556 REMARK 465 TRP A 557 REMARK 465 HIS A 558 REMARK 465 GLU A 559 REMARK 465 GLY A 560 REMARK 465 HIS A 561 REMARK 465 HIS A 562 REMARK 465 HIS A 563 REMARK 465 HIS A 564 REMARK 465 HIS A 565 REMARK 465 HIS A 566 REMARK 465 MET B -5 REMARK 465 GLU B -4 REMARK 465 ASN B -3 REMARK 465 ILE B -2 REMARK 465 VAL B -1 REMARK 465 LEU B 0 REMARK 465 LEU B 1 REMARK 465 LEU B 2 REMARK 465 ALA B 3 REMARK 465 ILE B 4 REMARK 465 VAL B 5 REMARK 465 SER B 6 REMARK 465 LEU B 7 REMARK 465 ARG B 333 REMARK 465 GLU B 334 REMARK 465 LYS B 335 REMARK 465 ARG B 336 REMARK 465 ARG B 337 REMARK 465 LYS B 338 REMARK 465 ARG B 339 REMARK 465 GLY B 514 REMARK 465 SER B 515 REMARK 465 GLY B 516 REMARK 465 TYR B 517 REMARK 465 ILE B 518 REMARK 465 PRO B 519 REMARK 465 GLU B 520 REMARK 465 ALA B 521 REMARK 465 PRO B 522 REMARK 465 ARG B 523 REMARK 465 ASP B 524 REMARK 465 GLY B 525 REMARK 465 GLN B 526 REMARK 465 ALA B 527 REMARK 465 TYR B 528 REMARK 465 VAL B 529 REMARK 465 ARG B 530 REMARK 465 LYS B 531 REMARK 465 ASP B 532 REMARK 465 GLY B 533 REMARK 465 GLU B 534 REMARK 465 TRP B 535 REMARK 465 VAL B 536 REMARK 465 LEU B 537 REMARK 465 LEU B 538 REMARK 465 SER B 539 REMARK 465 THR B 540 REMARK 465 PHE B 541 REMARK 465 LEU B 542 REMARK 465 GLY B 543 REMARK 465 SER B 544 REMARK 465 GLY B 545 REMARK 465 LEU B 546 REMARK 465 ASN B 547 REMARK 465 ASP B 548 REMARK 465 ILE B 549 REMARK 465 PHE B 550 REMARK 465 GLU B 551 REMARK 465 ALA B 552 REMARK 465 GLN B 553 REMARK 465 LYS B 554 REMARK 465 ILE B 555 REMARK 465 GLU B 556 REMARK 465 TRP B 557 REMARK 465 HIS B 558 REMARK 465 GLU B 559 REMARK 465 GLY B 560 REMARK 465 HIS B 561 REMARK 465 HIS B 562 REMARK 465 HIS B 563 REMARK 465 HIS B 564 REMARK 465 HIS B 565 REMARK 465 HIS B 566 REMARK 465 MET C -5 REMARK 465 GLU C -4 REMARK 465 ASN C -3 REMARK 465 ILE C -2 REMARK 465 VAL C -1 REMARK 465 LEU C 0 REMARK 465 LEU C 1 REMARK 465 LEU C 2 REMARK 465 ALA C 3 REMARK 465 ILE C 4 REMARK 465 VAL C 5 REMARK 465 SER C 6 REMARK 465 LEU C 7 REMARK 465 ARG C 333 REMARK 465 GLU C 334 REMARK 465 LYS C 335 REMARK 465 ARG C 336 REMARK 465 ARG C 337 REMARK 465 LYS C 338 REMARK 465 ARG C 339 REMARK 465 GLY C 514 REMARK 465 SER C 515 REMARK 465 GLY C 516 REMARK 465 TYR C 517 REMARK 465 ILE C 518 REMARK 465 PRO C 519 REMARK 465 GLU C 520 REMARK 465 ALA C 521 REMARK 465 PRO C 522 REMARK 465 ARG C 523 REMARK 465 ASP C 524 REMARK 465 GLY C 525 REMARK 465 GLN C 526 REMARK 465 ALA C 527 REMARK 465 TYR C 528 REMARK 465 VAL C 529 REMARK 465 ARG C 530 REMARK 465 LYS C 531 REMARK 465 ASP C 532 REMARK 465 GLY C 533 REMARK 465 GLU C 534 REMARK 465 TRP C 535 REMARK 465 VAL C 536 REMARK 465 LEU C 537 REMARK 465 LEU C 538 REMARK 465 SER C 539 REMARK 465 THR C 540 REMARK 465 PHE C 541 REMARK 465 LEU C 542 REMARK 465 GLY C 543 REMARK 465 SER C 544 REMARK 465 GLY C 545 REMARK 465 LEU C 546 REMARK 465 ASN C 547 REMARK 465 ASP C 548 REMARK 465 ILE C 549 REMARK 465 PHE C 550 REMARK 465 GLU C 551 REMARK 465 ALA C 552 REMARK 465 GLN C 553 REMARK 465 LYS C 554 REMARK 465 ILE C 555 REMARK 465 GLU C 556 REMARK 465 TRP C 557 REMARK 465 HIS C 558 REMARK 465 GLU C 559 REMARK 465 GLY C 560 REMARK 465 HIS C 561 REMARK 465 HIS C 562 REMARK 465 HIS C 563 REMARK 465 HIS C 564 REMARK 465 HIS C 565 REMARK 465 HIS C 566 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 SER B 513 CZ ARG C 506 1.49 REMARK 500 O SER B 513 NH1 ARG C 506 1.62 REMARK 500 O SER B 513 NE ARG C 506 1.92 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ALA L 3 -5.85 71.08 REMARK 500 ASN L 51 -46.09 73.24 REMARK 500 LYS A 63 -120.06 58.62 REMARK 500 ASP A 98 -158.81 -89.11 REMARK 500 LYS A 202 -3.95 66.73 REMARK 500 THR A 212 -165.08 -125.77 REMARK 500 THR A 400 36.05 -98.98 REMARK 500 ARG A 466 -125.59 58.34 REMARK 500 ALA M 3 -5.84 71.15 REMARK 500 ASN M 51 -45.86 73.30 REMARK 500 LYS B 63 -117.53 59.48 REMARK 500 ASP B 98 -159.37 -89.09 REMARK 500 CYS B 145 78.90 -119.29 REMARK 500 LYS B 202 -9.32 68.41 REMARK 500 THR B 212 -165.60 -124.15 REMARK 500 THR B 400 36.10 -98.75 REMARK 500 ARG B 466 -125.90 57.49 REMARK 500 ALA N 3 -5.85 71.26 REMARK 500 ASN N 51 -46.44 72.50 REMARK 500 TYR J 99 -163.15 -108.69 REMARK 500 LYS C 63 -120.39 58.72 REMARK 500 ASP C 98 -158.84 -89.11 REMARK 500 LYS C 202 -5.68 67.05 REMARK 500 THR C 212 -165.27 -124.63 REMARK 500 THR C 400 35.58 -99.28 REMARK 500 ARG C 466 -126.10 58.31 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 GAL P 1 REMARK 610 GAL D 1 REMARK 610 GAL E 1 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-47241 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF HEMAGGLUTININ H5 A/TEXAS/37/2024 IN COMPLEX REMARK 900 WITH LSTA AND ANTIBODY CR9114 DBREF 9DWE L 2 108 PDB 9DWE 9DWE 2 108 DBREF 9DWE H 1 112 PDB 9DWE 9DWE 1 112 DBREF1 9DWE A -5 514 UNP A0A8E4ZAK5_9INFA DBREF2 9DWE A A0A8E4ZAK5 1 520 DBREF 9DWE M 2 108 PDB 9DWE 9DWE 2 108 DBREF 9DWE I 1 112 PDB 9DWE 9DWE 1 112 DBREF1 9DWE B -5 514 UNP A0A8E4ZAK5_9INFA DBREF2 9DWE B A0A8E4ZAK5 1 520 DBREF 9DWE N 2 108 PDB 9DWE 9DWE 2 108 DBREF 9DWE J 1 112 PDB 9DWE 9DWE 1 112 DBREF1 9DWE C -5 514 UNP A0A8E4ZAK5_9INFA DBREF2 9DWE C A0A8E4ZAK5 1 520 SEQADV 9DWE MET A 114 UNP A0A8E4ZAK LEU 120 CONFLICT SEQADV 9DWE GLN A 125 UNP A0A8E4ZAK LEU 131 CONFLICT SEQADV 9DWE ILE A 205 UNP A0A8E4ZAK THR 211 CONFLICT SEQADV 9DWE ALA A 220 UNP A0A8E4ZAK VAL 226 CONFLICT SEQADV 9DWE SER A 515 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLY A 516 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE TYR A 517 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ILE A 518 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE PRO A 519 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLU A 520 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ALA A 521 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE PRO A 522 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ARG A 523 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ASP A 524 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLY A 525 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLN A 526 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ALA A 527 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE TYR A 528 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE VAL A 529 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ARG A 530 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE LYS A 531 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ASP A 532 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLY A 533 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLU A 534 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE TRP A 535 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE VAL A 536 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE LEU A 537 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE LEU A 538 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE SER A 539 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE THR A 540 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE PHE A 541 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE LEU A 542 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLY A 543 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE SER A 544 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLY A 545 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE LEU A 546 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ASN A 547 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ASP A 548 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ILE A 549 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE PHE A 550 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLU A 551 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ALA A 552 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLN A 553 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE LYS A 554 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ILE A 555 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLU A 556 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE TRP A 557 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE HIS A 558 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLU A 559 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLY A 560 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE HIS A 561 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE HIS A 562 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE HIS A 563 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE HIS A 564 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE HIS A 565 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE HIS A 566 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE MET B 114 UNP A0A8E4ZAK LEU 120 CONFLICT SEQADV 9DWE GLN B 125 UNP A0A8E4ZAK LEU 131 CONFLICT SEQADV 9DWE ILE B 205 UNP A0A8E4ZAK THR 211 CONFLICT SEQADV 9DWE ALA B 220 UNP A0A8E4ZAK VAL 226 CONFLICT SEQADV 9DWE SER B 515 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLY B 516 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE TYR B 517 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ILE B 518 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE PRO B 519 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLU B 520 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ALA B 521 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE PRO B 522 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ARG B 523 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ASP B 524 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLY B 525 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLN B 526 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ALA B 527 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE TYR B 528 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE VAL B 529 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ARG B 530 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE LYS B 531 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ASP B 532 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLY B 533 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLU B 534 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE TRP B 535 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE VAL B 536 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE LEU B 537 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE LEU B 538 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE SER B 539 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE THR B 540 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE PHE B 541 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE LEU B 542 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLY B 543 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE SER B 544 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLY B 545 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE LEU B 546 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ASN B 547 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ASP B 548 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ILE B 549 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE PHE B 550 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLU B 551 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ALA B 552 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLN B 553 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE LYS B 554 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ILE B 555 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLU B 556 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE TRP B 557 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE HIS B 558 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLU B 559 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLY B 560 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE HIS B 561 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE HIS B 562 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE HIS B 563 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE HIS B 564 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE HIS B 565 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE HIS B 566 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE MET C 114 UNP A0A8E4ZAK LEU 120 CONFLICT SEQADV 9DWE GLN C 125 UNP A0A8E4ZAK LEU 131 CONFLICT SEQADV 9DWE ILE C 205 UNP A0A8E4ZAK THR 211 CONFLICT SEQADV 9DWE ALA C 220 UNP A0A8E4ZAK VAL 226 CONFLICT SEQADV 9DWE SER C 515 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLY C 516 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE TYR C 517 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ILE C 518 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE PRO C 519 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLU C 520 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ALA C 521 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE PRO C 522 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ARG C 523 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ASP C 524 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLY C 525 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLN C 526 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ALA C 527 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE TYR C 528 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE VAL C 529 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ARG C 530 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE LYS C 531 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ASP C 532 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLY C 533 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLU C 534 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE TRP C 535 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE VAL C 536 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE LEU C 537 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE LEU C 538 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE SER C 539 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE THR C 540 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE PHE C 541 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE LEU C 542 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLY C 543 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE SER C 544 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLY C 545 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE LEU C 546 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ASN C 547 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ASP C 548 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ILE C 549 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE PHE C 550 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLU C 551 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ALA C 552 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLN C 553 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE LYS C 554 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE ILE C 555 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLU C 556 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE TRP C 557 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE HIS C 558 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLU C 559 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE GLY C 560 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE HIS C 561 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE HIS C 562 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE HIS C 563 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE HIS C 564 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE HIS C 565 UNP A0A8E4ZAK EXPRESSION TAG SEQADV 9DWE HIS C 566 UNP A0A8E4ZAK EXPRESSION TAG SEQRES 1 L 110 SER ALA LEU THR GLN PRO PRO ALA VAL SER GLY THR PRO SEQRES 2 L 110 GLY GLN ARG VAL THR ILE SER CYS SER GLY SER ASP SER SEQRES 3 L 110 ASN ILE GLY ARG ARG SER VAL ASN TRP TYR GLN GLN PHE SEQRES 4 L 110 PRO GLY THR ALA PRO LYS LEU LEU ILE TYR SER ASN ASP SEQRES 5 L 110 GLN ARG PRO SER VAL VAL PRO ASP ARG PHE SER GLY SER SEQRES 6 L 110 LYS SER GLY THR SER ALA SER LEU ALA ILE SER GLY LEU SEQRES 7 L 110 GLN SER GLU ASP GLU ALA GLU TYR TYR CYS ALA ALA TRP SEQRES 8 L 110 ASP ASP SER LEU LYS GLY ALA VAL PHE GLY GLY GLY THR SEQRES 9 L 110 GLN LEU THR VAL LEU GLY SEQRES 1 H 120 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 120 PRO GLY SER SER VAL LYS VAL SER CYS LYS SER SER GLY SEQRES 3 H 120 GLY THR SER ASN ASN TYR ALA ILE SER TRP VAL ARG GLN SEQRES 4 H 120 ALA PRO GLY GLN GLY LEU ASP TRP MET GLY GLY ILE SER SEQRES 5 H 120 PRO ILE PHE GLY SER THR ALA TYR ALA GLN LYS PHE GLN SEQRES 6 H 120 GLY ARG VAL THR ILE SER ALA ASP ILE PHE SER ASN THR SEQRES 7 H 120 ALA TYR MET GLU LEU ASN SER LEU THR SER GLU ASP THR SEQRES 8 H 120 ALA VAL TYR PHE CYS ALA ARG HIS GLY ASN TYR TYR TYR SEQRES 9 H 120 TYR SER GLY MET ASP VAL TRP GLY GLN GLY THR THR VAL SEQRES 10 H 120 THR VAL SER SEQRES 1 A 572 MET GLU ASN ILE VAL LEU LEU LEU ALA ILE VAL SER LEU SEQRES 2 A 572 VAL LYS SER ASP GLN ILE CYS ILE GLY TYR HIS ALA ASN SEQRES 3 A 572 ASN SER THR GLU GLN VAL ASP THR ILE MET GLU LYS ASN SEQRES 4 A 572 VAL THR VAL THR HIS ALA GLN ASP ILE LEU GLU LYS THR SEQRES 5 A 572 HIS ASN GLY LYS LEU CYS ASP LEU ASN GLY VAL LYS PRO SEQRES 6 A 572 LEU ILE LEU LYS ASP CYS SER VAL ALA GLY TRP LEU LEU SEQRES 7 A 572 GLY ASN PRO MET CYS ASP GLU PHE ILE ARG VAL PRO GLU SEQRES 8 A 572 TRP SER TYR ILE VAL GLU ARG ALA ASN PRO ALA ASN ASP SEQRES 9 A 572 LEU CYS TYR PRO GLY SER LEU ASN ASP TYR GLU GLU LEU SEQRES 10 A 572 LYS HIS MET LEU SER ARG ILE ASN HIS PHE GLU LYS ILE SEQRES 11 A 572 GLN ILE ILE PRO LYS SER SER TRP PRO ASN HIS GLU THR SEQRES 12 A 572 SER LEU GLY VAL SER ALA ALA CYS PRO TYR GLN GLY ALA SEQRES 13 A 572 PRO SER PHE PHE ARG ASN VAL VAL TRP LEU ILE LYS LYS SEQRES 14 A 572 ASN ASP ALA TYR PRO THR ILE LYS ILE SER TYR ASN ASN SEQRES 15 A 572 THR ASN ARG GLU ASP LEU LEU ILE LEU TRP GLY ILE HIS SEQRES 16 A 572 HIS SER ASN ASN ALA GLU GLU GLN THR ASN LEU TYR LYS SEQRES 17 A 572 ASN PRO ILE THR TYR ILE SER VAL GLY THR SER THR LEU SEQRES 18 A 572 ASN GLN ARG LEU ALA PRO LYS ILE ALA THR ARG SER GLN SEQRES 19 A 572 VAL ASN GLY GLN ARG GLY ARG MET ASP PHE PHE TRP THR SEQRES 20 A 572 ILE LEU LYS PRO ASP ASP ALA ILE HIS PHE GLU SER ASN SEQRES 21 A 572 GLY ASN PHE ILE ALA PRO GLU TYR ALA TYR LYS ILE VAL SEQRES 22 A 572 LYS LYS GLY ASP SER THR ILE MET LYS SER GLY VAL GLU SEQRES 23 A 572 TYR GLY HIS CYS ASN THR LYS CYS GLN THR PRO VAL GLY SEQRES 24 A 572 ALA ILE ASN SER SER MET PRO PHE HIS ASN ILE HIS PRO SEQRES 25 A 572 LEU THR ILE GLY GLU CYS PRO LYS TYR VAL LYS SER ASN SEQRES 26 A 572 LYS LEU VAL LEU ALA THR GLY LEU ARG ASN SER PRO LEU SEQRES 27 A 572 ARG GLU LYS ARG ARG LYS ARG GLY LEU PHE GLY ALA ILE SEQRES 28 A 572 ALA GLY PHE ILE GLU GLY GLY TRP GLN GLY MET VAL ASP SEQRES 29 A 572 GLY TRP TYR GLY TYR HIS HIS SER ASN GLU GLN GLY SER SEQRES 30 A 572 GLY TYR ALA ALA ASP LYS GLU SER THR GLN LYS ALA ILE SEQRES 31 A 572 ASP GLY VAL THR ASN LYS VAL ASN SER ILE ILE ASP LYS SEQRES 32 A 572 MET ASN THR GLN PHE GLU ALA VAL GLY ARG GLU PHE ASN SEQRES 33 A 572 ASN LEU GLU ARG ARG ILE GLU ASN LEU ASN LYS LYS MET SEQRES 34 A 572 GLU ASP GLY PHE LEU ASP VAL TRP THR TYR ASN ALA GLU SEQRES 35 A 572 LEU LEU VAL LEU MET GLU ASN GLU ARG THR LEU ASP PHE SEQRES 36 A 572 HIS ASP SER ASN VAL LYS ASN LEU TYR ASP LYS VAL ARG SEQRES 37 A 572 LEU GLN LEU ARG ASP ASN ALA LYS GLU LEU GLY ASN GLY SEQRES 38 A 572 CYS PHE GLU PHE TYR HIS LYS CYS ASP ASN GLU CYS MET SEQRES 39 A 572 GLU SER VAL ARG ASN GLY THR TYR ASP TYR PRO GLN TYR SEQRES 40 A 572 SER GLU GLU ALA ARG LEU LYS ARG GLU GLU ILE SER GLY SEQRES 41 A 572 SER GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY GLN ALA SEQRES 42 A 572 TYR VAL ARG LYS ASP GLY GLU TRP VAL LEU LEU SER THR SEQRES 43 A 572 PHE LEU GLY SER GLY LEU ASN ASP ILE PHE GLU ALA GLN SEQRES 44 A 572 LYS ILE GLU TRP HIS GLU GLY HIS HIS HIS HIS HIS HIS SEQRES 1 M 110 SER ALA LEU THR GLN PRO PRO ALA VAL SER GLY THR PRO SEQRES 2 M 110 GLY GLN ARG VAL THR ILE SER CYS SER GLY SER ASP SER SEQRES 3 M 110 ASN ILE GLY ARG ARG SER VAL ASN TRP TYR GLN GLN PHE SEQRES 4 M 110 PRO GLY THR ALA PRO LYS LEU LEU ILE TYR SER ASN ASP SEQRES 5 M 110 GLN ARG PRO SER VAL VAL PRO ASP ARG PHE SER GLY SER SEQRES 6 M 110 LYS SER GLY THR SER ALA SER LEU ALA ILE SER GLY LEU SEQRES 7 M 110 GLN SER GLU ASP GLU ALA GLU TYR TYR CYS ALA ALA TRP SEQRES 8 M 110 ASP ASP SER LEU LYS GLY ALA VAL PHE GLY GLY GLY THR SEQRES 9 M 110 GLN LEU THR VAL LEU GLY SEQRES 1 I 120 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 I 120 PRO GLY SER SER VAL LYS VAL SER CYS LYS SER SER GLY SEQRES 3 I 120 GLY THR SER ASN ASN TYR ALA ILE SER TRP VAL ARG GLN SEQRES 4 I 120 ALA PRO GLY GLN GLY LEU ASP TRP MET GLY GLY ILE SER SEQRES 5 I 120 PRO ILE PHE GLY SER THR ALA TYR ALA GLN LYS PHE GLN SEQRES 6 I 120 GLY ARG VAL THR ILE SER ALA ASP ILE PHE SER ASN THR SEQRES 7 I 120 ALA TYR MET GLU LEU ASN SER LEU THR SER GLU ASP THR SEQRES 8 I 120 ALA VAL TYR PHE CYS ALA ARG HIS GLY ASN TYR TYR TYR SEQRES 9 I 120 TYR SER GLY MET ASP VAL TRP GLY GLN GLY THR THR VAL SEQRES 10 I 120 THR VAL SER SEQRES 1 B 572 MET GLU ASN ILE VAL LEU LEU LEU ALA ILE VAL SER LEU SEQRES 2 B 572 VAL LYS SER ASP GLN ILE CYS ILE GLY TYR HIS ALA ASN SEQRES 3 B 572 ASN SER THR GLU GLN VAL ASP THR ILE MET GLU LYS ASN SEQRES 4 B 572 VAL THR VAL THR HIS ALA GLN ASP ILE LEU GLU LYS THR SEQRES 5 B 572 HIS ASN GLY LYS LEU CYS ASP LEU ASN GLY VAL LYS PRO SEQRES 6 B 572 LEU ILE LEU LYS ASP CYS SER VAL ALA GLY TRP LEU LEU SEQRES 7 B 572 GLY ASN PRO MET CYS ASP GLU PHE ILE ARG VAL PRO GLU SEQRES 8 B 572 TRP SER TYR ILE VAL GLU ARG ALA ASN PRO ALA ASN ASP SEQRES 9 B 572 LEU CYS TYR PRO GLY SER LEU ASN ASP TYR GLU GLU LEU SEQRES 10 B 572 LYS HIS MET LEU SER ARG ILE ASN HIS PHE GLU LYS ILE SEQRES 11 B 572 GLN ILE ILE PRO LYS SER SER TRP PRO ASN HIS GLU THR SEQRES 12 B 572 SER LEU GLY VAL SER ALA ALA CYS PRO TYR GLN GLY ALA SEQRES 13 B 572 PRO SER PHE PHE ARG ASN VAL VAL TRP LEU ILE LYS LYS SEQRES 14 B 572 ASN ASP ALA TYR PRO THR ILE LYS ILE SER TYR ASN ASN SEQRES 15 B 572 THR ASN ARG GLU ASP LEU LEU ILE LEU TRP GLY ILE HIS SEQRES 16 B 572 HIS SER ASN ASN ALA GLU GLU GLN THR ASN LEU TYR LYS SEQRES 17 B 572 ASN PRO ILE THR TYR ILE SER VAL GLY THR SER THR LEU SEQRES 18 B 572 ASN GLN ARG LEU ALA PRO LYS ILE ALA THR ARG SER GLN SEQRES 19 B 572 VAL ASN GLY GLN ARG GLY ARG MET ASP PHE PHE TRP THR SEQRES 20 B 572 ILE LEU LYS PRO ASP ASP ALA ILE HIS PHE GLU SER ASN SEQRES 21 B 572 GLY ASN PHE ILE ALA PRO GLU TYR ALA TYR LYS ILE VAL SEQRES 22 B 572 LYS LYS GLY ASP SER THR ILE MET LYS SER GLY VAL GLU SEQRES 23 B 572 TYR GLY HIS CYS ASN THR LYS CYS GLN THR PRO VAL GLY SEQRES 24 B 572 ALA ILE ASN SER SER MET PRO PHE HIS ASN ILE HIS PRO SEQRES 25 B 572 LEU THR ILE GLY GLU CYS PRO LYS TYR VAL LYS SER ASN SEQRES 26 B 572 LYS LEU VAL LEU ALA THR GLY LEU ARG ASN SER PRO LEU SEQRES 27 B 572 ARG GLU LYS ARG ARG LYS ARG GLY LEU PHE GLY ALA ILE SEQRES 28 B 572 ALA GLY PHE ILE GLU GLY GLY TRP GLN GLY MET VAL ASP SEQRES 29 B 572 GLY TRP TYR GLY TYR HIS HIS SER ASN GLU GLN GLY SER SEQRES 30 B 572 GLY TYR ALA ALA ASP LYS GLU SER THR GLN LYS ALA ILE SEQRES 31 B 572 ASP GLY VAL THR ASN LYS VAL ASN SER ILE ILE ASP LYS SEQRES 32 B 572 MET ASN THR GLN PHE GLU ALA VAL GLY ARG GLU PHE ASN SEQRES 33 B 572 ASN LEU GLU ARG ARG ILE GLU ASN LEU ASN LYS LYS MET SEQRES 34 B 572 GLU ASP GLY PHE LEU ASP VAL TRP THR TYR ASN ALA GLU SEQRES 35 B 572 LEU LEU VAL LEU MET GLU ASN GLU ARG THR LEU ASP PHE SEQRES 36 B 572 HIS ASP SER ASN VAL LYS ASN LEU TYR ASP LYS VAL ARG SEQRES 37 B 572 LEU GLN LEU ARG ASP ASN ALA LYS GLU LEU GLY ASN GLY SEQRES 38 B 572 CYS PHE GLU PHE TYR HIS LYS CYS ASP ASN GLU CYS MET SEQRES 39 B 572 GLU SER VAL ARG ASN GLY THR TYR ASP TYR PRO GLN TYR SEQRES 40 B 572 SER GLU GLU ALA ARG LEU LYS ARG GLU GLU ILE SER GLY SEQRES 41 B 572 SER GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY GLN ALA SEQRES 42 B 572 TYR VAL ARG LYS ASP GLY GLU TRP VAL LEU LEU SER THR SEQRES 43 B 572 PHE LEU GLY SER GLY LEU ASN ASP ILE PHE GLU ALA GLN SEQRES 44 B 572 LYS ILE GLU TRP HIS GLU GLY HIS HIS HIS HIS HIS HIS SEQRES 1 N 110 SER ALA LEU THR GLN PRO PRO ALA VAL SER GLY THR PRO SEQRES 2 N 110 GLY GLN ARG VAL THR ILE SER CYS SER GLY SER ASP SER SEQRES 3 N 110 ASN ILE GLY ARG ARG SER VAL ASN TRP TYR GLN GLN PHE SEQRES 4 N 110 PRO GLY THR ALA PRO LYS LEU LEU ILE TYR SER ASN ASP SEQRES 5 N 110 GLN ARG PRO SER VAL VAL PRO ASP ARG PHE SER GLY SER SEQRES 6 N 110 LYS SER GLY THR SER ALA SER LEU ALA ILE SER GLY LEU SEQRES 7 N 110 GLN SER GLU ASP GLU ALA GLU TYR TYR CYS ALA ALA TRP SEQRES 8 N 110 ASP ASP SER LEU LYS GLY ALA VAL PHE GLY GLY GLY THR SEQRES 9 N 110 GLN LEU THR VAL LEU GLY SEQRES 1 J 120 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 J 120 PRO GLY SER SER VAL LYS VAL SER CYS LYS SER SER GLY SEQRES 3 J 120 GLY THR SER ASN ASN TYR ALA ILE SER TRP VAL ARG GLN SEQRES 4 J 120 ALA PRO GLY GLN GLY LEU ASP TRP MET GLY GLY ILE SER SEQRES 5 J 120 PRO ILE PHE GLY SER THR ALA TYR ALA GLN LYS PHE GLN SEQRES 6 J 120 GLY ARG VAL THR ILE SER ALA ASP ILE PHE SER ASN THR SEQRES 7 J 120 ALA TYR MET GLU LEU ASN SER LEU THR SER GLU ASP THR SEQRES 8 J 120 ALA VAL TYR PHE CYS ALA ARG HIS GLY ASN TYR TYR TYR SEQRES 9 J 120 TYR SER GLY MET ASP VAL TRP GLY GLN GLY THR THR VAL SEQRES 10 J 120 THR VAL SER SEQRES 1 C 572 MET GLU ASN ILE VAL LEU LEU LEU ALA ILE VAL SER LEU SEQRES 2 C 572 VAL LYS SER ASP GLN ILE CYS ILE GLY TYR HIS ALA ASN SEQRES 3 C 572 ASN SER THR GLU GLN VAL ASP THR ILE MET GLU LYS ASN SEQRES 4 C 572 VAL THR VAL THR HIS ALA GLN ASP ILE LEU GLU LYS THR SEQRES 5 C 572 HIS ASN GLY LYS LEU CYS ASP LEU ASN GLY VAL LYS PRO SEQRES 6 C 572 LEU ILE LEU LYS ASP CYS SER VAL ALA GLY TRP LEU LEU SEQRES 7 C 572 GLY ASN PRO MET CYS ASP GLU PHE ILE ARG VAL PRO GLU SEQRES 8 C 572 TRP SER TYR ILE VAL GLU ARG ALA ASN PRO ALA ASN ASP SEQRES 9 C 572 LEU CYS TYR PRO GLY SER LEU ASN ASP TYR GLU GLU LEU SEQRES 10 C 572 LYS HIS MET LEU SER ARG ILE ASN HIS PHE GLU LYS ILE SEQRES 11 C 572 GLN ILE ILE PRO LYS SER SER TRP PRO ASN HIS GLU THR SEQRES 12 C 572 SER LEU GLY VAL SER ALA ALA CYS PRO TYR GLN GLY ALA SEQRES 13 C 572 PRO SER PHE PHE ARG ASN VAL VAL TRP LEU ILE LYS LYS SEQRES 14 C 572 ASN ASP ALA TYR PRO THR ILE LYS ILE SER TYR ASN ASN SEQRES 15 C 572 THR ASN ARG GLU ASP LEU LEU ILE LEU TRP GLY ILE HIS SEQRES 16 C 572 HIS SER ASN ASN ALA GLU GLU GLN THR ASN LEU TYR LYS SEQRES 17 C 572 ASN PRO ILE THR TYR ILE SER VAL GLY THR SER THR LEU SEQRES 18 C 572 ASN GLN ARG LEU ALA PRO LYS ILE ALA THR ARG SER GLN SEQRES 19 C 572 VAL ASN GLY GLN ARG GLY ARG MET ASP PHE PHE TRP THR SEQRES 20 C 572 ILE LEU LYS PRO ASP ASP ALA ILE HIS PHE GLU SER ASN SEQRES 21 C 572 GLY ASN PHE ILE ALA PRO GLU TYR ALA TYR LYS ILE VAL SEQRES 22 C 572 LYS LYS GLY ASP SER THR ILE MET LYS SER GLY VAL GLU SEQRES 23 C 572 TYR GLY HIS CYS ASN THR LYS CYS GLN THR PRO VAL GLY SEQRES 24 C 572 ALA ILE ASN SER SER MET PRO PHE HIS ASN ILE HIS PRO SEQRES 25 C 572 LEU THR ILE GLY GLU CYS PRO LYS TYR VAL LYS SER ASN SEQRES 26 C 572 LYS LEU VAL LEU ALA THR GLY LEU ARG ASN SER PRO LEU SEQRES 27 C 572 ARG GLU LYS ARG ARG LYS ARG GLY LEU PHE GLY ALA ILE SEQRES 28 C 572 ALA GLY PHE ILE GLU GLY GLY TRP GLN GLY MET VAL ASP SEQRES 29 C 572 GLY TRP TYR GLY TYR HIS HIS SER ASN GLU GLN GLY SER SEQRES 30 C 572 GLY TYR ALA ALA ASP LYS GLU SER THR GLN LYS ALA ILE SEQRES 31 C 572 ASP GLY VAL THR ASN LYS VAL ASN SER ILE ILE ASP LYS SEQRES 32 C 572 MET ASN THR GLN PHE GLU ALA VAL GLY ARG GLU PHE ASN SEQRES 33 C 572 ASN LEU GLU ARG ARG ILE GLU ASN LEU ASN LYS LYS MET SEQRES 34 C 572 GLU ASP GLY PHE LEU ASP VAL TRP THR TYR ASN ALA GLU SEQRES 35 C 572 LEU LEU VAL LEU MET GLU ASN GLU ARG THR LEU ASP PHE SEQRES 36 C 572 HIS ASP SER ASN VAL LYS ASN LEU TYR ASP LYS VAL ARG SEQRES 37 C 572 LEU GLN LEU ARG ASP ASN ALA LYS GLU LEU GLY ASN GLY SEQRES 38 C 572 CYS PHE GLU PHE TYR HIS LYS CYS ASP ASN GLU CYS MET SEQRES 39 C 572 GLU SER VAL ARG ASN GLY THR TYR ASP TYR PRO GLN TYR SEQRES 40 C 572 SER GLU GLU ALA ARG LEU LYS ARG GLU GLU ILE SER GLY SEQRES 41 C 572 SER GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY GLN ALA SEQRES 42 C 572 TYR VAL ARG LYS ASP GLY GLU TRP VAL LEU LEU SER THR SEQRES 43 C 572 PHE LEU GLY SER GLY LEU ASN ASP ILE PHE GLU ALA GLN SEQRES 44 C 572 LYS ILE GLU TRP HIS GLU GLY HIS HIS HIS HIS HIS HIS HET GAL P 1 11 HET SIA P 2 20 HET GAL D 1 11 HET SIA D 2 20 HET GAL E 1 11 HET SIA E 2 20 HET NAG A 601 14 HET NAG A 602 14 HET NAG A 603 14 HET NAG A 604 14 HET NAG A 605 14 HET NAG B 601 14 HET NAG B 602 14 HET NAG B 603 14 HET NAG B 604 14 HET NAG B 605 14 HET NAG C 601 14 HET NAG C 602 14 HET NAG C 603 14 HET NAG C 604 14 HET NAG C 605 14 HETNAM GAL BETA-D-GALACTOPYRANOSE HETNAM SIA N-ACETYL-ALPHA-NEURAMINIC ACID HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE HETSYN SIA N-ACETYLNEURAMINIC ACID; SIALIC ACID; ALPHA-SIALIC HETSYN 2 SIA ACID; O-SIALIC ACID 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 10 GAL 3(C6 H12 O6) FORMUL 10 SIA 3(C11 H19 N O9) FORMUL 13 NAG 15(C8 H15 N O6) HELIX 1 AA1 THR H 83 THR H 87 5 5 HELIX 2 AA2 SER A 66 GLY A 73 1 8 HELIX 3 AA3 ASN A 74 ILE A 81 5 8 HELIX 4 AA4 ASP A 107 LEU A 115 1 9 HELIX 5 AA5 PRO A 128 TRP A 132 5 5 HELIX 6 AA6 ASN A 193 LYS A 202 1 10 HELIX 7 AA7 ASP A 376 MET A 398 1 23 HELIX 8 AA8 GLU A 413 ARG A 466 1 54 HELIX 9 AA9 ASP A 484 ASN A 493 1 10 HELIX 10 AB1 ASP A 497 SER A 513 1 17 HELIX 11 AB2 THR I 83 THR I 87 5 5 HELIX 12 AB3 SER B 66 GLY B 73 1 8 HELIX 13 AB4 ASN B 74 ILE B 81 5 8 HELIX 14 AB5 ASP B 107 LEU B 115 1 9 HELIX 15 AB6 PRO B 128 TRP B 132 5 5 HELIX 16 AB7 ASN B 193 TYR B 201 1 9 HELIX 17 AB8 ASP B 376 MET B 398 1 23 HELIX 18 AB9 GLU B 413 ARG B 466 1 54 HELIX 19 AC1 ASP B 484 ASN B 493 1 10 HELIX 20 AC2 TYR B 501 SER B 513 1 13 HELIX 21 AC3 GLN N 79 GLU N 83 5 5 HELIX 22 AC4 THR J 83 THR J 87 5 5 HELIX 23 AC5 SER C 66 GLY C 73 1 8 HELIX 24 AC6 ASN C 74 ILE C 81 5 8 HELIX 25 AC7 ASP C 107 LEU C 115 1 9 HELIX 26 AC8 PRO C 128 TRP C 132 5 5 HELIX 27 AC9 ASN C 193 TYR C 201 1 9 HELIX 28 AD1 ASP C 376 MET C 398 1 23 HELIX 29 AD2 ASN C 410 LEU C 412 5 3 HELIX 30 AD3 GLU C 413 ARG C 466 1 54 HELIX 31 AD4 ASP C 484 ASN C 493 1 10 HELIX 32 AD5 ASP C 497 SER C 513 1 17 SHEET 1 AA1 5 ALA L 9 GLY L 13 0 SHEET 2 AA1 5 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11 SHEET 3 AA1 5 GLU L 85 ASP L 92 -1 N TYR L 86 O THR L 102 SHEET 4 AA1 5 VAL L 33 GLN L 38 -1 N ASN L 34 O ALA L 89 SHEET 5 AA1 5 LYS L 45 ILE L 48 -1 O ILE L 48 N TRP L 35 SHEET 1 AA2 4 ALA L 9 GLY L 13 0 SHEET 2 AA2 4 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11 SHEET 3 AA2 4 GLU L 85 ASP L 92 -1 N TYR L 86 O THR L 102 SHEET 4 AA2 4 GLY L 95B PHE L 98 -1 O GLY L 95B N ASP L 92 SHEET 1 AA3 3 VAL L 19 SER L 24 0 SHEET 2 AA3 3 SER L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 3 AA3 3 PHE L 62 SER L 67 -1 N SER L 63 O ALA L 74 SHEET 1 AA4 4 GLN H 3 GLN H 6 0 SHEET 2 AA4 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AA4 4 THR H 77 LEU H 82 -1 O MET H 80 N VAL H 20 SHEET 4 AA4 4 VAL H 67 ASP H 72 -1 N THR H 68 O GLU H 81 SHEET 1 AA5 6 GLU H 10 LYS H 12 0 SHEET 2 AA5 6 THR H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AA5 6 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 107 SHEET 4 AA5 6 ILE H 34 GLN H 39 -1 N VAL H 37 O PHE H 91 SHEET 5 AA5 6 LEU H 45 SER H 52 -1 O GLY H 49 N TRP H 36 SHEET 6 AA5 6 SER H 56 TYR H 59 -1 O SER H 56 N SER H 52 SHEET 1 AA6 4 GLU H 10 LYS H 12 0 SHEET 2 AA6 4 THR H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AA6 4 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 107 SHEET 4 AA6 4 VAL H 102 TRP H 103 -1 O VAL H 102 N ARG H 94 SHEET 1 AA7 5 GLY A 370 ALA A 375 0 SHEET 2 AA7 5 TYR A 361 ASN A 367 -1 N TYR A 363 O ALA A 374 SHEET 3 AA7 5 GLN A 12 TYR A 17 -1 N GLN A 12 O SER A 366 SHEET 4 AA7 5 CYS A 476 PHE A 479 -1 O PHE A 477 N ILE A 13 SHEET 5 AA7 5 ALA A 469 GLU A 471 -1 N LYS A 470 O GLU A 478 SHEET 1 AA8 2 GLN A 25 VAL A 26 0 SHEET 2 AA8 2 VAL A 34 THR A 35 -1 O VAL A 34 N VAL A 26 SHEET 1 AA9 2 ALA A 39 ASP A 41 0 SHEET 2 AA9 2 VAL A 322 ALA A 324 -1 O LEU A 323 N GLN A 40 SHEET 1 AB1 3 LEU A 43 GLU A 44 0 SHEET 2 AB1 3 PHE A 301 HIS A 302 1 O PHE A 301 N GLU A 44 SHEET 3 AB1 3 LYS A 314 TYR A 315 1 O LYS A 314 N HIS A 302 SHEET 1 AB2 2 LEU A 51 LEU A 54 0 SHEET 2 AB2 2 TYR A 281 THR A 286 1 O CYS A 284 N ASP A 53 SHEET 1 AB3 3 LEU A 60 ILE A 61 0 SHEET 2 AB3 3 ILE A 89 GLU A 91 1 O VAL A 90 N LEU A 60 SHEET 3 AB3 3 ILE A 274 LYS A 276 1 O MET A 275 N ILE A 89 SHEET 1 AB4 5 GLY A 103 LEU A 105 0 SHEET 2 AB4 5 ARG A 235 LEU A 243 1 O PHE A 238 N SER A 104 SHEET 3 AB4 5 LEU A 182 HIS A 190 -1 N LEU A 182 O LEU A 243 SHEET 4 AB4 5 TYR A 262 LYS A 269 -1 O TYR A 264 N LEU A 183 SHEET 5 AB4 5 ILE A 118 GLN A 125 -1 N ILE A 124 O ALA A 263 SHEET 1 AB5 5 GLY A 103 LEU A 105 0 SHEET 2 AB5 5 ARG A 235 LEU A 243 1 O PHE A 238 N SER A 104 SHEET 3 AB5 5 LEU A 182 HIS A 190 -1 N LEU A 182 O LEU A 243 SHEET 4 AB5 5 PHE A 257 PRO A 260 -1 O ILE A 258 N GLY A 187 SHEET 5 AB5 5 VAL A 157 TRP A 159 -1 N VAL A 158 O ALA A 259 SHEET 1 AB6 2 HIS A 135 GLU A 136 0 SHEET 2 AB6 2 ILE A 161 LYS A 162 -1 O ILE A 161 N GLU A 136 SHEET 1 AB7 2 SER A 142 TYR A 147 0 SHEET 2 AB7 2 ALA A 150 SER A 152 -1 O ALA A 150 N TYR A 147 SHEET 1 AB8 4 ILE A 170 ASN A 175 0 SHEET 2 AB8 4 ALA A 248 SER A 253 -1 O SER A 253 N ILE A 170 SHEET 3 AB8 4 ILE A 208 GLY A 211 -1 N SER A 209 O GLU A 252 SHEET 4 AB8 4 ASN A 216 LEU A 219 -1 O GLN A 217 N VAL A 210 SHEET 1 AB9 3 ALA A 294 ILE A 295 0 SHEET 2 AB9 3 CYS A 288 GLN A 289 -1 N CYS A 288 O ILE A 295 SHEET 3 AB9 3 ILE A 309 GLY A 310 -1 O ILE A 309 N GLN A 289 SHEET 1 AC1 5 ALA M 9 GLY M 13 0 SHEET 2 AC1 5 THR M 102 VAL M 106 1 O THR M 105 N VAL M 11 SHEET 3 AC1 5 GLU M 85 ASP M 92 -1 N TYR M 86 O THR M 102 SHEET 4 AC1 5 VAL M 33 GLN M 38 -1 N ASN M 34 O ALA M 89 SHEET 5 AC1 5 LYS M 45 ILE M 48 -1 O ILE M 48 N TRP M 35 SHEET 1 AC2 4 ALA M 9 GLY M 13 0 SHEET 2 AC2 4 THR M 102 VAL M 106 1 O THR M 105 N VAL M 11 SHEET 3 AC2 4 GLU M 85 ASP M 92 -1 N TYR M 86 O THR M 102 SHEET 4 AC2 4 GLY M 95B PHE M 98 -1 O GLY M 95B N ASP M 92 SHEET 1 AC3 3 VAL M 19 SER M 24 0 SHEET 2 AC3 3 SER M 70 ILE M 75 -1 O LEU M 73 N ILE M 21 SHEET 3 AC3 3 PHE M 62 SER M 67 -1 N SER M 63 O ALA M 74 SHEET 1 AC4 4 GLN I 3 GLN I 6 0 SHEET 2 AC4 4 VAL I 18 SER I 25 -1 O LYS I 23 N VAL I 5 SHEET 3 AC4 4 THR I 77 LEU I 82 -1 O MET I 80 N VAL I 20 SHEET 4 AC4 4 VAL I 67 ASP I 72 -1 N THR I 68 O GLU I 81 SHEET 1 AC5 6 GLU I 10 LYS I 12 0 SHEET 2 AC5 6 THR I 107 VAL I 111 1 O THR I 110 N LYS I 12 SHEET 3 AC5 6 ALA I 88 ARG I 94 -1 N TYR I 90 O THR I 107 SHEET 4 AC5 6 ILE I 34 GLN I 39 -1 N VAL I 37 O PHE I 91 SHEET 5 AC5 6 LEU I 45 SER I 52 -1 O GLY I 49 N TRP I 36 SHEET 6 AC5 6 SER I 56 TYR I 59 -1 O SER I 56 N SER I 52 SHEET 1 AC6 4 GLU I 10 LYS I 12 0 SHEET 2 AC6 4 THR I 107 VAL I 111 1 O THR I 110 N LYS I 12 SHEET 3 AC6 4 ALA I 88 ARG I 94 -1 N TYR I 90 O THR I 107 SHEET 4 AC6 4 VAL I 102 TRP I 103 -1 O VAL I 102 N ARG I 94 SHEET 1 AC7 5 GLY B 370 ALA B 375 0 SHEET 2 AC7 5 TYR B 361 ASN B 367 -1 N TYR B 363 O ALA B 374 SHEET 3 AC7 5 GLN B 12 TYR B 17 -1 N GLN B 12 O SER B 366 SHEET 4 AC7 5 CYS B 476 PHE B 479 -1 O PHE B 477 N ILE B 13 SHEET 5 AC7 5 ALA B 469 GLU B 471 -1 N LYS B 470 O GLU B 478 SHEET 1 AC8 2 GLN B 25 VAL B 26 0 SHEET 2 AC8 2 VAL B 34 THR B 35 -1 O VAL B 34 N VAL B 26 SHEET 1 AC9 2 ALA B 39 ASP B 41 0 SHEET 2 AC9 2 VAL B 322 ALA B 324 -1 O LEU B 323 N GLN B 40 SHEET 1 AD1 3 LEU B 43 GLU B 44 0 SHEET 2 AD1 3 PHE B 301 HIS B 302 1 O PHE B 301 N GLU B 44 SHEET 3 AD1 3 LYS B 314 TYR B 315 1 O LYS B 314 N HIS B 302 SHEET 1 AD2 2 LEU B 51 LEU B 54 0 SHEET 2 AD2 2 TYR B 281 THR B 286 1 O CYS B 284 N ASP B 53 SHEET 1 AD3 3 LEU B 60 ILE B 61 0 SHEET 2 AD3 3 ILE B 89 GLU B 91 1 O VAL B 90 N LEU B 60 SHEET 3 AD3 3 ILE B 274 LYS B 276 1 O MET B 275 N ILE B 89 SHEET 1 AD4 5 GLY B 103 LEU B 105 0 SHEET 2 AD4 5 ARG B 235 LEU B 243 1 O PHE B 238 N SER B 104 SHEET 3 AD4 5 LEU B 182 HIS B 190 -1 N LEU B 182 O LEU B 243 SHEET 4 AD4 5 TYR B 262 LYS B 269 -1 O TYR B 264 N LEU B 183 SHEET 5 AD4 5 ILE B 118 GLN B 125 -1 N ILE B 124 O ALA B 263 SHEET 1 AD5 5 GLY B 103 LEU B 105 0 SHEET 2 AD5 5 ARG B 235 LEU B 243 1 O PHE B 238 N SER B 104 SHEET 3 AD5 5 LEU B 182 HIS B 190 -1 N LEU B 182 O LEU B 243 SHEET 4 AD5 5 PHE B 257 PRO B 260 -1 O ILE B 258 N GLY B 187 SHEET 5 AD5 5 VAL B 157 TRP B 159 -1 N VAL B 158 O ALA B 259 SHEET 1 AD6 2 HIS B 135 GLU B 136 0 SHEET 2 AD6 2 ILE B 161 LYS B 162 -1 O ILE B 161 N GLU B 136 SHEET 1 AD7 2 SER B 142 TYR B 147 0 SHEET 2 AD7 2 ALA B 150 SER B 152 -1 O ALA B 150 N TYR B 147 SHEET 1 AD8 4 ILE B 170 ASN B 175 0 SHEET 2 AD8 4 ALA B 248 SER B 253 -1 O SER B 253 N ILE B 170 SHEET 3 AD8 4 ILE B 208 GLY B 211 -1 N SER B 209 O GLU B 252 SHEET 4 AD8 4 ASN B 216 LEU B 219 -1 O GLN B 217 N VAL B 210 SHEET 1 AD9 2 CYS B 288 GLN B 289 0 SHEET 2 AD9 2 ILE B 309 GLY B 310 -1 O ILE B 309 N GLN B 289 SHEET 1 AE1 5 ALA N 9 GLY N 13 0 SHEET 2 AE1 5 THR N 102 VAL N 106 1 O THR N 105 N VAL N 11 SHEET 3 AE1 5 GLU N 85 ASP N 92 -1 N TYR N 86 O THR N 102 SHEET 4 AE1 5 VAL N 33 GLN N 38 -1 N ASN N 34 O ALA N 89 SHEET 5 AE1 5 LYS N 45 ILE N 48 -1 O ILE N 48 N TRP N 35 SHEET 1 AE2 4 ALA N 9 GLY N 13 0 SHEET 2 AE2 4 THR N 102 VAL N 106 1 O THR N 105 N VAL N 11 SHEET 3 AE2 4 GLU N 85 ASP N 92 -1 N TYR N 86 O THR N 102 SHEET 4 AE2 4 GLY N 95B PHE N 98 -1 O GLY N 95B N ASP N 92 SHEET 1 AE3 3 VAL N 19 SER N 24 0 SHEET 2 AE3 3 SER N 70 ILE N 75 -1 O LEU N 73 N ILE N 21 SHEET 3 AE3 3 PHE N 62 SER N 67 -1 N SER N 63 O ALA N 74 SHEET 1 AE4 4 GLN J 3 GLN J 6 0 SHEET 2 AE4 4 VAL J 18 SER J 25 -1 O LYS J 23 N VAL J 5 SHEET 3 AE4 4 THR J 77 LEU J 82 -1 O MET J 80 N VAL J 20 SHEET 4 AE4 4 VAL J 67 ASP J 72 -1 N THR J 68 O GLU J 81 SHEET 1 AE5 6 GLU J 10 LYS J 12 0 SHEET 2 AE5 6 THR J 107 VAL J 111 1 O THR J 110 N LYS J 12 SHEET 3 AE5 6 ALA J 88 ARG J 94 -1 N TYR J 90 O THR J 107 SHEET 4 AE5 6 ILE J 34 GLN J 39 -1 N VAL J 37 O PHE J 91 SHEET 5 AE5 6 LEU J 45 SER J 52 -1 O GLY J 49 N TRP J 36 SHEET 6 AE5 6 SER J 56 TYR J 59 -1 O SER J 56 N SER J 52 SHEET 1 AE6 4 GLU J 10 LYS J 12 0 SHEET 2 AE6 4 THR J 107 VAL J 111 1 O THR J 110 N LYS J 12 SHEET 3 AE6 4 ALA J 88 ARG J 94 -1 N TYR J 90 O THR J 107 SHEET 4 AE6 4 VAL J 102 TRP J 103 -1 O VAL J 102 N ARG J 94 SHEET 1 AE7 5 GLY C 372 ALA C 375 0 SHEET 2 AE7 5 TYR C 361 HIS C 365 -1 N TYR C 363 O ALA C 374 SHEET 3 AE7 5 GLN C 12 TYR C 17 -1 N GLY C 16 O GLY C 362 SHEET 4 AE7 5 CYS C 476 PHE C 479 -1 O PHE C 477 N ILE C 13 SHEET 5 AE7 5 ALA C 469 GLU C 471 -1 N LYS C 470 O GLU C 478 SHEET 1 AE8 2 GLN C 25 VAL C 26 0 SHEET 2 AE8 2 VAL C 34 THR C 35 -1 O VAL C 34 N VAL C 26 SHEET 1 AE9 2 ALA C 39 ASP C 41 0 SHEET 2 AE9 2 VAL C 322 ALA C 324 -1 O LEU C 323 N GLN C 40 SHEET 1 AF1 3 LEU C 43 GLU C 44 0 SHEET 2 AF1 3 PHE C 301 HIS C 302 1 O PHE C 301 N GLU C 44 SHEET 3 AF1 3 LYS C 314 TYR C 315 1 O LYS C 314 N HIS C 302 SHEET 1 AF2 2 LEU C 51 LEU C 54 0 SHEET 2 AF2 2 TYR C 281 THR C 286 1 O CYS C 284 N ASP C 53 SHEET 1 AF3 3 LEU C 60 ILE C 61 0 SHEET 2 AF3 3 ILE C 89 GLU C 91 1 O VAL C 90 N LEU C 60 SHEET 3 AF3 3 ILE C 274 LYS C 276 1 O MET C 275 N ILE C 89 SHEET 1 AF4 5 GLY C 103 LEU C 105 0 SHEET 2 AF4 5 ARG C 235 LEU C 243 1 O PHE C 238 N SER C 104 SHEET 3 AF4 5 LEU C 182 HIS C 190 -1 N LEU C 182 O LEU C 243 SHEET 4 AF4 5 TYR C 262 LYS C 269 -1 O TYR C 264 N LEU C 183 SHEET 5 AF4 5 ILE C 118 GLN C 125 -1 N GLU C 122 O LYS C 265 SHEET 1 AF5 5 GLY C 103 LEU C 105 0 SHEET 2 AF5 5 ARG C 235 LEU C 243 1 O PHE C 238 N SER C 104 SHEET 3 AF5 5 LEU C 182 HIS C 190 -1 N LEU C 182 O LEU C 243 SHEET 4 AF5 5 PHE C 257 PRO C 260 -1 O ILE C 258 N GLY C 187 SHEET 5 AF5 5 VAL C 157 TRP C 159 -1 N VAL C 158 O ALA C 259 SHEET 1 AF6 2 HIS C 135 GLU C 136 0 SHEET 2 AF6 2 ILE C 161 LYS C 162 -1 O ILE C 161 N GLU C 136 SHEET 1 AF7 2 SER C 142 TYR C 147 0 SHEET 2 AF7 2 ALA C 150 SER C 152 -1 O ALA C 150 N TYR C 147 SHEET 1 AF8 4 ILE C 170 ASN C 175 0 SHEET 2 AF8 4 ALA C 248 SER C 253 -1 O SER C 253 N ILE C 170 SHEET 3 AF8 4 ILE C 208 GLY C 211 -1 N SER C 209 O GLU C 252 SHEET 4 AF8 4 ASN C 216 LEU C 219 -1 O GLN C 217 N VAL C 210 SHEET 1 AF9 2 CYS C 288 GLN C 289 0 SHEET 2 AF9 2 ILE C 309 GLY C 310 -1 O ILE C 309 N GLN C 289 SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 2 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 3 CYS A 14 CYS A 476 1555 1555 2.03 SSBOND 4 CYS A 52 CYS A 284 1555 1555 2.03 SSBOND 5 CYS A 65 CYS A 77 1555 1555 2.02 SSBOND 6 CYS A 100 CYS A 145 1555 1555 2.03 SSBOND 7 CYS A 288 CYS A 312 1555 1555 2.03 SSBOND 8 CYS A 483 CYS A 487 1555 1555 2.03 SSBOND 9 CYS M 23 CYS M 88 1555 1555 2.03 SSBOND 10 CYS I 22 CYS I 92 1555 1555 2.03 SSBOND 11 CYS B 14 CYS B 476 1555 1555 2.03 SSBOND 12 CYS B 52 CYS B 284 1555 1555 2.03 SSBOND 13 CYS B 65 CYS B 77 1555 1555 2.02 SSBOND 14 CYS B 100 CYS B 145 1555 1555 2.03 SSBOND 15 CYS B 288 CYS B 312 1555 1555 2.03 SSBOND 16 CYS B 483 CYS B 487 1555 1555 2.03 SSBOND 17 CYS N 23 CYS N 88 1555 1555 2.03 SSBOND 18 CYS J 22 CYS J 92 1555 1555 2.03 SSBOND 19 CYS C 14 CYS C 476 1555 1555 2.03 SSBOND 20 CYS C 52 CYS C 284 1555 1555 2.03 SSBOND 21 CYS C 65 CYS C 77 1555 1555 2.02 SSBOND 22 CYS C 100 CYS C 145 1555 1555 2.03 SSBOND 23 CYS C 288 CYS C 312 1555 1555 2.03 SSBOND 24 CYS C 483 CYS C 487 1555 1555 2.03 LINK ND2 ASN A 21 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 33 C1 NAG A 602 1555 1555 1.44 LINK ND2 ASN A 175 C1 NAG A 603 1555 1555 1.44 LINK ND2 ASN A 296 C1 NAG A 604 1555 1555 1.44 LINK ND2 ASN A 493 C1 NAG A 605 1555 1555 1.46 LINK ND2 ASN B 21 C1 NAG B 601 1555 1555 1.44 LINK ND2 ASN B 33 C1 NAG B 602 1555 1555 1.46 LINK ND2 ASN B 175 C1 NAG B 603 1555 1555 1.44 LINK ND2 ASN B 296 C1 NAG B 604 1555 1555 1.46 LINK ND2 ASN B 493 C1 NAG B 605 1555 1555 1.48 LINK ND2 ASN C 21 C1 NAG C 601 1555 1555 1.44 LINK ND2 ASN C 33 C1 NAG C 602 1555 1555 1.44 LINK ND2 ASN C 175 C1 NAG C 603 1555 1555 1.44 LINK ND2 ASN C 296 C1 NAG C 604 1555 1555 1.46 LINK ND2 ASN C 493 C1 NAG C 605 1555 1555 1.45 LINK O3 GAL P 1 C2 SIA P 2 1555 1555 1.50 LINK O3 GAL D 1 C2 SIA D 2 1555 1555 1.50 LINK O3 GAL E 1 C2 SIA E 2 1555 1555 1.51 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