HEADER VIRAL PROTEIN/IMMUNE SYSTEM 16-SEP-24 9DN2 TITLE TJ5-1 FAB IN COMPLEX WITH NG2 COBRA HEMAGGLUTININ COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMAGGLUTININ; COMPND 3 CHAIN: A, B, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: TJ5-1 HEAVY CHAIN FAB FRAGMENT; COMPND 7 CHAIN: H, I, J; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: TJ5-1 LIGHT CHAIN FAB FRAGMENT; COMPND 11 CHAIN: L, M, N; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 3 ORGANISM_TAXID: 11320; SOURCE 4 GENE: HA; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ANTIBODY, FAB, HEMAGGLUTININ, COBRA, VIRAL PROTEIN, VIRAL PROTEIN- KEYWDS 2 IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR K.NAGASHIMA,J.MOUSA REVDAT 1 30-JUL-25 9DN2 0 JRNL AUTH K.NAGASHIMA,J.MOUSA JRNL TITL TJ5-1 FAB IN COMPLEX WITH NG2 COBRA HEMAGGLUTININ JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.24 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, CRYOSPARC 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) : 3.240 REMARK 3 NUMBER OF PARTICLES : 248400 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING ONLY REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9DN2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1000288441. 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 : COMPLEX OF TJ5-1 FAB FRAGMENT REMARK 245 WITH NG2 COBRA HEMAGGLUTININ 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 : 7.50 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) : 800.00 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) : 6021.60 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: NONAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, I, J, L, M, N, B, C, D, REMARK 350 AND CHAINS: E, F, G, K, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V, W, X 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 -15 REMARK 465 LYS A -14 REMARK 465 THR A -13 REMARK 465 ILE A -12 REMARK 465 ILE A -11 REMARK 465 ALA A -10 REMARK 465 LEU A -9 REMARK 465 SER A -8 REMARK 465 TYR A -7 REMARK 465 ILE A -6 REMARK 465 LEU A -5 REMARK 465 CYS A -4 REMARK 465 LEU A -3 REMARK 465 VAL A -2 REMARK 465 PHE A -1 REMARK 465 ALA A 0 REMARK 465 ILE A 502 REMARK 465 LYS A 503 REMARK 465 GLY A 504 REMARK 465 VAL A 505 REMARK 465 GLU A 506 REMARK 465 GLY A 507 REMARK 465 TYR A 508 REMARK 465 ILE A 509 REMARK 465 PRO A 510 REMARK 465 GLU A 511 REMARK 465 ALA A 512 REMARK 465 PRO A 513 REMARK 465 ARG A 514 REMARK 465 ASP A 515 REMARK 465 GLY A 516 REMARK 465 GLN A 517 REMARK 465 ALA A 518 REMARK 465 TYR A 519 REMARK 465 VAL A 520 REMARK 465 ARG A 521 REMARK 465 LYS A 522 REMARK 465 ASP A 523 REMARK 465 GLY A 524 REMARK 465 GLU A 525 REMARK 465 TRP A 526 REMARK 465 VAL A 527 REMARK 465 LEU A 528 REMARK 465 LEU A 529 REMARK 465 SER A 530 REMARK 465 THR A 531 REMARK 465 PHE A 532 REMARK 465 LEU A 533 REMARK 465 GLY A 534 REMARK 465 SER A 535 REMARK 465 GLY A 536 REMARK 465 LEU A 537 REMARK 465 ASN A 538 REMARK 465 ASP A 539 REMARK 465 ILE A 540 REMARK 465 PHE A 541 REMARK 465 GLU A 542 REMARK 465 ALA A 543 REMARK 465 GLN A 544 REMARK 465 LYS A 545 REMARK 465 ILE A 546 REMARK 465 GLU A 547 REMARK 465 TRP A 548 REMARK 465 HIS A 549 REMARK 465 GLU A 550 REMARK 465 GLY A 551 REMARK 465 HIS A 552 REMARK 465 HIS A 553 REMARK 465 HIS A 554 REMARK 465 HIS A 555 REMARK 465 HIS A 556 REMARK 465 HIS A 557 REMARK 465 GLU H 1 REMARK 465 GLN H 120 REMARK 465 GLY H 121 REMARK 465 THR H 122 REMARK 465 THR H 123 REMARK 465 VAL H 124 REMARK 465 ILE H 125 REMARK 465 VAL H 126 REMARK 465 SER H 127 REMARK 465 SER H 128 REMARK 465 GLU I 1 REMARK 465 GLN I 120 REMARK 465 GLY I 121 REMARK 465 THR I 122 REMARK 465 THR I 123 REMARK 465 VAL I 124 REMARK 465 ILE I 125 REMARK 465 VAL I 126 REMARK 465 SER I 127 REMARK 465 SER I 128 REMARK 465 GLU J 1 REMARK 465 GLN J 120 REMARK 465 GLY J 121 REMARK 465 THR J 122 REMARK 465 THR J 123 REMARK 465 VAL J 124 REMARK 465 ILE J 125 REMARK 465 VAL J 126 REMARK 465 SER J 127 REMARK 465 SER J 128 REMARK 465 GLN L 1 REMARK 465 SER L 2 REMARK 465 VAL L 3 REMARK 465 LEU L 127 REMARK 465 GLN M 1 REMARK 465 SER M 2 REMARK 465 VAL M 3 REMARK 465 LEU M 127 REMARK 465 GLN N 1 REMARK 465 SER N 2 REMARK 465 VAL N 3 REMARK 465 LEU N 127 REMARK 465 MET B -15 REMARK 465 LYS B -14 REMARK 465 THR B -13 REMARK 465 ILE B -12 REMARK 465 ILE B -11 REMARK 465 ALA B -10 REMARK 465 LEU B -9 REMARK 465 SER B -8 REMARK 465 TYR B -7 REMARK 465 ILE B -6 REMARK 465 LEU B -5 REMARK 465 CYS B -4 REMARK 465 LEU B -3 REMARK 465 VAL B -2 REMARK 465 PHE B -1 REMARK 465 ALA B 0 REMARK 465 ILE B 502 REMARK 465 LYS B 503 REMARK 465 GLY B 504 REMARK 465 VAL B 505 REMARK 465 GLU B 506 REMARK 465 GLY B 507 REMARK 465 TYR B 508 REMARK 465 ILE B 509 REMARK 465 PRO B 510 REMARK 465 GLU B 511 REMARK 465 ALA B 512 REMARK 465 PRO B 513 REMARK 465 ARG B 514 REMARK 465 ASP B 515 REMARK 465 GLY B 516 REMARK 465 GLN B 517 REMARK 465 ALA B 518 REMARK 465 TYR B 519 REMARK 465 VAL B 520 REMARK 465 ARG B 521 REMARK 465 LYS B 522 REMARK 465 ASP B 523 REMARK 465 GLY B 524 REMARK 465 GLU B 525 REMARK 465 TRP B 526 REMARK 465 VAL B 527 REMARK 465 LEU B 528 REMARK 465 LEU B 529 REMARK 465 SER B 530 REMARK 465 THR B 531 REMARK 465 PHE B 532 REMARK 465 LEU B 533 REMARK 465 GLY B 534 REMARK 465 SER B 535 REMARK 465 GLY B 536 REMARK 465 LEU B 537 REMARK 465 ASN B 538 REMARK 465 ASP B 539 REMARK 465 ILE B 540 REMARK 465 PHE B 541 REMARK 465 GLU B 542 REMARK 465 ALA B 543 REMARK 465 GLN B 544 REMARK 465 LYS B 545 REMARK 465 ILE B 546 REMARK 465 GLU B 547 REMARK 465 TRP B 548 REMARK 465 HIS B 549 REMARK 465 GLU B 550 REMARK 465 GLY B 551 REMARK 465 HIS B 552 REMARK 465 HIS B 553 REMARK 465 HIS B 554 REMARK 465 HIS B 555 REMARK 465 HIS B 556 REMARK 465 HIS B 557 REMARK 465 MET C -15 REMARK 465 LYS C -14 REMARK 465 THR C -13 REMARK 465 ILE C -12 REMARK 465 ILE C -11 REMARK 465 ALA C -10 REMARK 465 LEU C -9 REMARK 465 SER C -8 REMARK 465 TYR C -7 REMARK 465 ILE C -6 REMARK 465 LEU C -5 REMARK 465 CYS C -4 REMARK 465 LEU C -3 REMARK 465 VAL C -2 REMARK 465 PHE C -1 REMARK 465 ALA C 0 REMARK 465 ILE C 502 REMARK 465 LYS C 503 REMARK 465 GLY C 504 REMARK 465 VAL C 505 REMARK 465 GLU C 506 REMARK 465 GLY C 507 REMARK 465 TYR C 508 REMARK 465 ILE C 509 REMARK 465 PRO C 510 REMARK 465 GLU C 511 REMARK 465 ALA C 512 REMARK 465 PRO C 513 REMARK 465 ARG C 514 REMARK 465 ASP C 515 REMARK 465 GLY C 516 REMARK 465 GLN C 517 REMARK 465 ALA C 518 REMARK 465 TYR C 519 REMARK 465 VAL C 520 REMARK 465 ARG C 521 REMARK 465 LYS C 522 REMARK 465 ASP C 523 REMARK 465 GLY C 524 REMARK 465 GLU C 525 REMARK 465 TRP C 526 REMARK 465 VAL C 527 REMARK 465 LEU C 528 REMARK 465 LEU C 529 REMARK 465 SER C 530 REMARK 465 THR C 531 REMARK 465 PHE C 532 REMARK 465 LEU C 533 REMARK 465 GLY C 534 REMARK 465 SER C 535 REMARK 465 GLY C 536 REMARK 465 LEU C 537 REMARK 465 ASN C 538 REMARK 465 ASP C 539 REMARK 465 ILE C 540 REMARK 465 PHE C 541 REMARK 465 GLU C 542 REMARK 465 ALA C 543 REMARK 465 GLN C 544 REMARK 465 LYS C 545 REMARK 465 ILE C 546 REMARK 465 GLU C 547 REMARK 465 TRP C 548 REMARK 465 HIS C 549 REMARK 465 GLU C 550 REMARK 465 GLY C 551 REMARK 465 HIS C 552 REMARK 465 HIS C 553 REMARK 465 HIS C 554 REMARK 465 HIS C 555 REMARK 465 HIS C 556 REMARK 465 HIS C 557 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLN A 1 CG CD OE1 NE2 REMARK 470 GLN B 1 CG CD OE1 NE2 REMARK 470 GLN C 1 CG CD OE1 NE2 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 PRO A 4 172.10 -58.60 REMARK 500 ASN A 22 55.65 -90.16 REMARK 500 GLN A 173 54.80 -93.17 REMARK 500 PHE A 338 -11.42 73.41 REMARK 500 ASN A 357 -169.04 -162.02 REMARK 500 LEU A 447 -10.60 73.18 REMARK 500 ARG A 456 -113.89 53.78 REMARK 500 ASP A 474 -169.93 -126.36 REMARK 500 THR L 48 -65.27 -93.20 REMARK 500 ASN L 54 -174.45 62.93 REMARK 500 PRO L 68 40.83 -79.43 REMARK 500 SER L 83 -169.57 -122.14 REMARK 500 THR M 48 -65.23 -93.17 REMARK 500 ASN M 54 -174.44 62.84 REMARK 500 PRO M 68 40.82 -79.45 REMARK 500 SER M 83 -169.49 -122.10 REMARK 500 THR N 48 -65.28 -93.22 REMARK 500 ASN N 54 -174.46 62.93 REMARK 500 PRO N 68 40.78 -79.44 REMARK 500 SER N 83 -169.56 -122.15 REMARK 500 PRO B 4 172.18 -58.68 REMARK 500 ASN B 22 55.60 -90.26 REMARK 500 GLN B 173 54.82 -93.22 REMARK 500 PHE B 338 -11.42 73.42 REMARK 500 ASN B 357 -169.02 -161.95 REMARK 500 LEU B 447 -10.62 73.19 REMARK 500 ARG B 456 -113.96 53.88 REMARK 500 ASP B 474 -169.94 -126.36 REMARK 500 PRO C 4 172.18 -58.69 REMARK 500 ASN C 22 55.61 -90.17 REMARK 500 GLN C 173 54.81 -93.24 REMARK 500 PHE C 338 -11.39 73.46 REMARK 500 ASN C 357 -169.06 -162.06 REMARK 500 LEU C 447 -10.54 73.20 REMARK 500 ARG C 456 -113.98 53.87 REMARK 500 ASP C 474 -169.94 -126.27 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-47024 RELATED DB: EMDB REMARK 900 TJ5-1 FAB IN COMPLEX WITH NG2 COBRA HEMAGGLUTININ DBREF1 9DN2 A -15 506 UNP A0A2P1ADT1_9INFA DBREF2 9DN2 A A0A2P1ADT1 1 522 DBREF 9DN2 H 1 128 PDB 9DN2 9DN2 1 128 DBREF 9DN2 I 1 128 PDB 9DN2 9DN2 1 128 DBREF 9DN2 J 1 128 PDB 9DN2 9DN2 1 128 DBREF 9DN2 L 1 127 PDB 9DN2 9DN2 1 127 DBREF 9DN2 M 1 127 PDB 9DN2 9DN2 1 127 DBREF 9DN2 N 1 127 PDB 9DN2 9DN2 1 127 DBREF1 9DN2 B -15 506 UNP A0A2P1ADT1_9INFA DBREF2 9DN2 B A0A2P1ADT1 1 522 DBREF1 9DN2 C -15 506 UNP A0A2P1ADT1_9INFA DBREF2 9DN2 C A0A2P1ADT1 1 522 SEQADV 9DN2 GLY A 142 UNP A0A2P1ADT ARG 158 CONFLICT SEQADV 9DN2 SER A 144 UNP A0A2P1ADT LYS 160 CONFLICT SEQADV 9DN2 GLN A 311 UNP A0A2P1ADT HIS 327 CONFLICT SEQADV 9DN2 GLY A 507 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 TYR A 508 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ILE A 509 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 PRO A 510 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLU A 511 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ALA A 512 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 PRO A 513 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ARG A 514 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ASP A 515 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLY A 516 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLN A 517 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ALA A 518 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 TYR A 519 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 VAL A 520 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ARG A 521 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 LYS A 522 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ASP A 523 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLY A 524 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLU A 525 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 TRP A 526 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 VAL A 527 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 LEU A 528 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 LEU A 529 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 SER A 530 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 THR A 531 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 PHE A 532 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 LEU A 533 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLY A 534 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 SER A 535 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLY A 536 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 LEU A 537 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ASN A 538 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ASP A 539 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ILE A 540 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 PHE A 541 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLU A 542 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ALA A 543 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLN A 544 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 LYS A 545 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ILE A 546 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLU A 547 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 TRP A 548 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 HIS A 549 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLU A 550 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLY A 551 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 HIS A 552 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 HIS A 553 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 HIS A 554 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 HIS A 555 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 HIS A 556 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 HIS A 557 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLY B 142 UNP A0A2P1ADT ARG 158 CONFLICT SEQADV 9DN2 SER B 144 UNP A0A2P1ADT LYS 160 CONFLICT SEQADV 9DN2 GLN B 311 UNP A0A2P1ADT HIS 327 CONFLICT SEQADV 9DN2 GLY B 507 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 TYR B 508 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ILE B 509 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 PRO B 510 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLU B 511 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ALA B 512 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 PRO B 513 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ARG B 514 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ASP B 515 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLY B 516 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLN B 517 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ALA B 518 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 TYR B 519 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 VAL B 520 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ARG B 521 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 LYS B 522 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ASP B 523 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLY B 524 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLU B 525 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 TRP B 526 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 VAL B 527 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 LEU B 528 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 LEU B 529 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 SER B 530 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 THR B 531 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 PHE B 532 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 LEU B 533 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLY B 534 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 SER B 535 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLY B 536 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 LEU B 537 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ASN B 538 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ASP B 539 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ILE B 540 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 PHE B 541 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLU B 542 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ALA B 543 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLN B 544 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 LYS B 545 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ILE B 546 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLU B 547 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 TRP B 548 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 HIS B 549 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLU B 550 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLY B 551 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 HIS B 552 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 HIS B 553 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 HIS B 554 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 HIS B 555 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 HIS B 556 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 HIS B 557 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLY C 142 UNP A0A2P1ADT ARG 158 CONFLICT SEQADV 9DN2 SER C 144 UNP A0A2P1ADT LYS 160 CONFLICT SEQADV 9DN2 GLN C 311 UNP A0A2P1ADT HIS 327 CONFLICT SEQADV 9DN2 GLY C 507 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 TYR C 508 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ILE C 509 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 PRO C 510 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLU C 511 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ALA C 512 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 PRO C 513 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ARG C 514 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ASP C 515 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLY C 516 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLN C 517 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ALA C 518 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 TYR C 519 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 VAL C 520 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ARG C 521 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 LYS C 522 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ASP C 523 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLY C 524 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLU C 525 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 TRP C 526 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 VAL C 527 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 LEU C 528 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 LEU C 529 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 SER C 530 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 THR C 531 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 PHE C 532 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 LEU C 533 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLY C 534 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 SER C 535 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLY C 536 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 LEU C 537 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ASN C 538 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ASP C 539 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ILE C 540 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 PHE C 541 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLU C 542 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ALA C 543 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLN C 544 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 LYS C 545 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 ILE C 546 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLU C 547 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 TRP C 548 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 HIS C 549 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLU C 550 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 GLY C 551 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 HIS C 552 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 HIS C 553 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 HIS C 554 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 HIS C 555 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 HIS C 556 UNP A0A2P1ADT EXPRESSION TAG SEQADV 9DN2 HIS C 557 UNP A0A2P1ADT EXPRESSION TAG SEQRES 1 A 573 MET LYS THR ILE ILE ALA LEU SER TYR ILE LEU CYS LEU SEQRES 2 A 573 VAL PHE ALA GLN LYS ILE PRO GLY ASN ASP ASN SER THR SEQRES 3 A 573 ALA THR LEU CYS LEU GLY HIS HIS ALA VAL PRO ASN GLY SEQRES 4 A 573 THR ILE VAL LYS THR ILE THR ASN ASP ARG ILE GLU VAL SEQRES 5 A 573 THR ASN ALA THR GLU LEU VAL GLN ASN SER SER ILE GLY SEQRES 6 A 573 GLU ILE CYS ASP SER PRO HIS GLN ILE LEU ASP GLY GLU SEQRES 7 A 573 ASN CYS THR LEU ILE ASP ALA LEU LEU GLY ASP PRO GLN SEQRES 8 A 573 CYS ASP GLY PHE GLN ASN LYS LYS TRP ASP LEU PHE VAL SEQRES 9 A 573 GLU ARG SER LYS ALA TYR SER ASN CYS TYR PRO TYR ASP SEQRES 10 A 573 VAL PRO ASP TYR ALA SER LEU ARG SER LEU VAL ALA SER SEQRES 11 A 573 SER GLY THR LEU GLU PHE LYS ASN GLU SER PHE ASN TRP SEQRES 12 A 573 THR GLY VAL THR GLN ASN GLY THR SER SER ALA CYS ILE SEQRES 13 A 573 ARG GLY SER SER SER SER PHE PHE SER ARG LEU ASN TRP SEQRES 14 A 573 LEU THR HIS LEU ASN TYR THR TYR PRO ALA LEU ASN VAL SEQRES 15 A 573 THR MET PRO ASN ASN GLU GLN PHE ASP LYS LEU TYR ILE SEQRES 16 A 573 TRP GLY VAL HIS HIS PRO GLY THR ASP LYS ASP GLN ILE SEQRES 17 A 573 PHE LEU TYR ALA GLN SER SER GLY ARG ILE THR VAL SER SEQRES 18 A 573 THR LYS ARG SER GLN GLN ALA VAL ILE PRO ASN ILE GLY SEQRES 19 A 573 SER ARG PRO ARG ILE ARG ASP ILE PRO SER ARG ILE SER SEQRES 20 A 573 ILE TYR TRP THR ILE VAL LYS PRO GLY ASP ILE LEU LEU SEQRES 21 A 573 ILE ASN SER THR GLY ASN LEU ILE ALA PRO ARG GLY TYR SEQRES 22 A 573 PHE LYS ILE ARG SER GLY LYS SER SER ILE MET ARG SER SEQRES 23 A 573 ASP ALA PRO ILE GLY LYS CYS LYS SER GLU CYS ILE THR SEQRES 24 A 573 PRO ASN GLY SER ILE PRO ASN ASP LYS PRO PHE GLN ASN SEQRES 25 A 573 VAL ASN ARG ILE THR TYR GLY ALA CYS PRO ARG TYR VAL SEQRES 26 A 573 LYS GLN SER THR LEU LYS LEU ALA THR GLY MET ARG ASN SEQRES 27 A 573 VAL PRO GLU LYS GLN THR ARG GLY ILE PHE GLY ALA ILE SEQRES 28 A 573 ALA GLY PHE ILE GLU ASN GLY TRP GLU GLY MET VAL ASP SEQRES 29 A 573 GLY TRP TYR GLY PHE ARG HIS GLN ASN SER GLU GLY ARG SEQRES 30 A 573 GLY GLN ALA ALA ASP LEU LYS SER THR GLN ALA ALA ILE SEQRES 31 A 573 ASP GLN ILE ASN GLY LYS LEU ASN ARG LEU ILE GLY LYS SEQRES 32 A 573 THR ASN GLU LYS PHE HIS GLN ILE GLU LYS GLU PHE SER SEQRES 33 A 573 GLU VAL GLU GLY ARG ILE GLN ASP LEU GLU LYS TYR VAL SEQRES 34 A 573 GLU ASP THR LYS ILE ASP LEU TRP SER TYR ASN ALA GLU SEQRES 35 A 573 LEU LEU VAL ALA LEU GLU ASN GLN HIS THR ILE ASP LEU SEQRES 36 A 573 THR ASP SER GLU MET ASN LYS LEU PHE GLU LYS THR LYS SEQRES 37 A 573 LYS GLN LEU ARG GLU ASN ALA GLU ASP MET GLY ASN GLY SEQRES 38 A 573 CYS PHE LYS ILE TYR HIS LYS CYS ASP ASN ALA CYS ILE SEQRES 39 A 573 GLY SER ILE ARG ASN GLY THR TYR ASP HIS ASN VAL TYR SEQRES 40 A 573 ARG ASP GLU ALA LEU ASN ASN ARG PHE GLN ILE LYS GLY SEQRES 41 A 573 VAL GLU GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY GLN SEQRES 42 A 573 ALA TYR VAL ARG LYS ASP GLY GLU TRP VAL LEU LEU SER SEQRES 43 A 573 THR PHE LEU GLY SER GLY LEU ASN ASP ILE PHE GLU ALA SEQRES 44 A 573 GLN LYS ILE GLU TRP HIS GLU GLY HIS HIS HIS HIS HIS SEQRES 45 A 573 HIS SEQRES 1 H 118 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 118 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 118 TYR THR PHE THR GLY PHE TYR LEU HIS TRP VAL ARG GLN SEQRES 4 H 118 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 H 118 PRO HIS SER GLY ASP THR ASP PHE ALA GLN LYS PHE GLN SEQRES 6 H 118 GLY LYS VAL THR MET THR ARG ASP THR SER SER ASN THR SEQRES 7 H 118 VAL TYR MET ASP VAL ASN ARG LEU THR SER ASP ASP THR SEQRES 8 H 118 ALA VAL TYR TYR CYS VAL LYS ASN ASP ILE VAL LEU GLY SEQRES 9 H 118 MET GLY VAL TRP GLY GLN GLY THR THR VAL ILE VAL SER SEQRES 10 H 118 SER SEQRES 1 I 118 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 I 118 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 I 118 TYR THR PHE THR GLY PHE TYR LEU HIS TRP VAL ARG GLN SEQRES 4 I 118 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 I 118 PRO HIS SER GLY ASP THR ASP PHE ALA GLN LYS PHE GLN SEQRES 6 I 118 GLY LYS VAL THR MET THR ARG ASP THR SER SER ASN THR SEQRES 7 I 118 VAL TYR MET ASP VAL ASN ARG LEU THR SER ASP ASP THR SEQRES 8 I 118 ALA VAL TYR TYR CYS VAL LYS ASN ASP ILE VAL LEU GLY SEQRES 9 I 118 MET GLY VAL TRP GLY GLN GLY THR THR VAL ILE VAL SER SEQRES 10 I 118 SER SEQRES 1 J 118 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 J 118 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 J 118 TYR THR PHE THR GLY PHE TYR LEU HIS TRP VAL ARG GLN SEQRES 4 J 118 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 J 118 PRO HIS SER GLY ASP THR ASP PHE ALA GLN LYS PHE GLN SEQRES 6 J 118 GLY LYS VAL THR MET THR ARG ASP THR SER SER ASN THR SEQRES 7 J 118 VAL TYR MET ASP VAL ASN ARG LEU THR SER ASP ASP THR SEQRES 8 J 118 ALA VAL TYR TYR CYS VAL LYS ASN ASP ILE VAL LEU GLY SEQRES 9 J 118 MET GLY VAL TRP GLY GLN GLY THR THR VAL ILE VAL SER SEQRES 10 J 118 SER SEQRES 1 L 111 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 L 111 PRO GLY GLN ARG VAL THR ILE SER CYS THR GLY SER SER SEQRES 3 L 111 SER ASN ILE GLY ALA GLY TYR ASN VAL TYR TRP PHE GLN SEQRES 4 L 111 GLN LEU PRO PRO THR ALA PRO LYS LEU LEU ASN TYR GLY SEQRES 5 L 111 ASP ASN ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 L 111 ALA SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR SEQRES 7 L 111 GLY LEU GLN ALA GLU ASP GLU ALA GLU TYR TYR CYS GLN SEQRES 8 L 111 SER TYR ASP SER SER LEU ASN ALA TYR VAL PHE GLY THR SEQRES 9 L 111 GLY THR LYS VAL THR VAL LEU SEQRES 1 M 111 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 M 111 PRO GLY GLN ARG VAL THR ILE SER CYS THR GLY SER SER SEQRES 3 M 111 SER ASN ILE GLY ALA GLY TYR ASN VAL TYR TRP PHE GLN SEQRES 4 M 111 GLN LEU PRO PRO THR ALA PRO LYS LEU LEU ASN TYR GLY SEQRES 5 M 111 ASP ASN ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 M 111 ALA SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR SEQRES 7 M 111 GLY LEU GLN ALA GLU ASP GLU ALA GLU TYR TYR CYS GLN SEQRES 8 M 111 SER TYR ASP SER SER LEU ASN ALA TYR VAL PHE GLY THR SEQRES 9 M 111 GLY THR LYS VAL THR VAL LEU SEQRES 1 N 111 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 N 111 PRO GLY GLN ARG VAL THR ILE SER CYS THR GLY SER SER SEQRES 3 N 111 SER ASN ILE GLY ALA GLY TYR ASN VAL TYR TRP PHE GLN SEQRES 4 N 111 GLN LEU PRO PRO THR ALA PRO LYS LEU LEU ASN TYR GLY SEQRES 5 N 111 ASP ASN ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 N 111 ALA SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR SEQRES 7 N 111 GLY LEU GLN ALA GLU ASP GLU ALA GLU TYR TYR CYS GLN SEQRES 8 N 111 SER TYR ASP SER SER LEU ASN ALA TYR VAL PHE GLY THR SEQRES 9 N 111 GLY THR LYS VAL THR VAL LEU SEQRES 1 B 573 MET LYS THR ILE ILE ALA LEU SER TYR ILE LEU CYS LEU SEQRES 2 B 573 VAL PHE ALA GLN LYS ILE PRO GLY ASN ASP ASN SER THR SEQRES 3 B 573 ALA THR LEU CYS LEU GLY HIS HIS ALA VAL PRO ASN GLY SEQRES 4 B 573 THR ILE VAL LYS THR ILE THR ASN ASP ARG ILE GLU VAL SEQRES 5 B 573 THR ASN ALA THR GLU LEU VAL GLN ASN SER SER ILE GLY SEQRES 6 B 573 GLU ILE CYS ASP SER PRO HIS GLN ILE LEU ASP GLY GLU SEQRES 7 B 573 ASN CYS THR LEU ILE ASP ALA LEU LEU GLY ASP PRO GLN SEQRES 8 B 573 CYS ASP GLY PHE GLN ASN LYS LYS TRP ASP LEU PHE VAL SEQRES 9 B 573 GLU ARG SER LYS ALA TYR SER ASN CYS TYR PRO TYR ASP SEQRES 10 B 573 VAL PRO ASP TYR ALA SER LEU ARG SER LEU VAL ALA SER SEQRES 11 B 573 SER GLY THR LEU GLU PHE LYS ASN GLU SER PHE ASN TRP SEQRES 12 B 573 THR GLY VAL THR GLN ASN GLY THR SER SER ALA CYS ILE SEQRES 13 B 573 ARG GLY SER SER SER SER PHE PHE SER ARG LEU ASN TRP SEQRES 14 B 573 LEU THR HIS LEU ASN TYR THR TYR PRO ALA LEU ASN VAL SEQRES 15 B 573 THR MET PRO ASN ASN GLU GLN PHE ASP LYS LEU TYR ILE SEQRES 16 B 573 TRP GLY VAL HIS HIS PRO GLY THR ASP LYS ASP GLN ILE SEQRES 17 B 573 PHE LEU TYR ALA GLN SER SER GLY ARG ILE THR VAL SER SEQRES 18 B 573 THR LYS ARG SER GLN GLN ALA VAL ILE PRO ASN ILE GLY SEQRES 19 B 573 SER ARG PRO ARG ILE ARG ASP ILE PRO SER ARG ILE SER SEQRES 20 B 573 ILE TYR TRP THR ILE VAL LYS PRO GLY ASP ILE LEU LEU SEQRES 21 B 573 ILE ASN SER THR GLY ASN LEU ILE ALA PRO ARG GLY TYR SEQRES 22 B 573 PHE LYS ILE ARG SER GLY LYS SER SER ILE MET ARG SER SEQRES 23 B 573 ASP ALA PRO ILE GLY LYS CYS LYS SER GLU CYS ILE THR SEQRES 24 B 573 PRO ASN GLY SER ILE PRO ASN ASP LYS PRO PHE GLN ASN SEQRES 25 B 573 VAL ASN ARG ILE THR TYR GLY ALA CYS PRO ARG TYR VAL SEQRES 26 B 573 LYS GLN SER THR LEU LYS LEU ALA THR GLY MET ARG ASN SEQRES 27 B 573 VAL PRO GLU LYS GLN THR ARG GLY ILE PHE GLY ALA ILE SEQRES 28 B 573 ALA GLY PHE ILE GLU ASN GLY TRP GLU GLY MET VAL ASP SEQRES 29 B 573 GLY TRP TYR GLY PHE ARG HIS GLN ASN SER GLU GLY ARG SEQRES 30 B 573 GLY GLN ALA ALA ASP LEU LYS SER THR GLN ALA ALA ILE SEQRES 31 B 573 ASP GLN ILE ASN GLY LYS LEU ASN ARG LEU ILE GLY LYS SEQRES 32 B 573 THR ASN GLU LYS PHE HIS GLN ILE GLU LYS GLU PHE SER SEQRES 33 B 573 GLU VAL GLU GLY ARG ILE GLN ASP LEU GLU LYS TYR VAL SEQRES 34 B 573 GLU ASP THR LYS ILE ASP LEU TRP SER TYR ASN ALA GLU SEQRES 35 B 573 LEU LEU VAL ALA LEU GLU ASN GLN HIS THR ILE ASP LEU SEQRES 36 B 573 THR ASP SER GLU MET ASN LYS LEU PHE GLU LYS THR LYS SEQRES 37 B 573 LYS GLN LEU ARG GLU ASN ALA GLU ASP MET GLY ASN GLY SEQRES 38 B 573 CYS PHE LYS ILE TYR HIS LYS CYS ASP ASN ALA CYS ILE SEQRES 39 B 573 GLY SER ILE ARG ASN GLY THR TYR ASP HIS ASN VAL TYR SEQRES 40 B 573 ARG ASP GLU ALA LEU ASN ASN ARG PHE GLN ILE LYS GLY SEQRES 41 B 573 VAL GLU GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY GLN SEQRES 42 B 573 ALA TYR VAL ARG LYS ASP GLY GLU TRP VAL LEU LEU SER SEQRES 43 B 573 THR PHE LEU GLY SER GLY LEU ASN ASP ILE PHE GLU ALA SEQRES 44 B 573 GLN LYS ILE GLU TRP HIS GLU GLY HIS HIS HIS HIS HIS SEQRES 45 B 573 HIS SEQRES 1 C 573 MET LYS THR ILE ILE ALA LEU SER TYR ILE LEU CYS LEU SEQRES 2 C 573 VAL PHE ALA GLN LYS ILE PRO GLY ASN ASP ASN SER THR SEQRES 3 C 573 ALA THR LEU CYS LEU GLY HIS HIS ALA VAL PRO ASN GLY SEQRES 4 C 573 THR ILE VAL LYS THR ILE THR ASN ASP ARG ILE GLU VAL SEQRES 5 C 573 THR ASN ALA THR GLU LEU VAL GLN ASN SER SER ILE GLY SEQRES 6 C 573 GLU ILE CYS ASP SER PRO HIS GLN ILE LEU ASP GLY GLU SEQRES 7 C 573 ASN CYS THR LEU ILE ASP ALA LEU LEU GLY ASP PRO GLN SEQRES 8 C 573 CYS ASP GLY PHE GLN ASN LYS LYS TRP ASP LEU PHE VAL SEQRES 9 C 573 GLU ARG SER LYS ALA TYR SER ASN CYS TYR PRO TYR ASP SEQRES 10 C 573 VAL PRO ASP TYR ALA SER LEU ARG SER LEU VAL ALA SER SEQRES 11 C 573 SER GLY THR LEU GLU PHE LYS ASN GLU SER PHE ASN TRP SEQRES 12 C 573 THR GLY VAL THR GLN ASN GLY THR SER SER ALA CYS ILE SEQRES 13 C 573 ARG GLY SER SER SER SER PHE PHE SER ARG LEU ASN TRP SEQRES 14 C 573 LEU THR HIS LEU ASN TYR THR TYR PRO ALA LEU ASN VAL SEQRES 15 C 573 THR MET PRO ASN ASN GLU GLN PHE ASP LYS LEU TYR ILE SEQRES 16 C 573 TRP GLY VAL HIS HIS PRO GLY THR ASP LYS ASP GLN ILE SEQRES 17 C 573 PHE LEU TYR ALA GLN SER SER GLY ARG ILE THR VAL SER SEQRES 18 C 573 THR LYS ARG SER GLN GLN ALA VAL ILE PRO ASN ILE GLY SEQRES 19 C 573 SER ARG PRO ARG ILE ARG ASP ILE PRO SER ARG ILE SER SEQRES 20 C 573 ILE TYR TRP THR ILE VAL LYS PRO GLY ASP ILE LEU LEU SEQRES 21 C 573 ILE ASN SER THR GLY ASN LEU ILE ALA PRO ARG GLY TYR SEQRES 22 C 573 PHE LYS ILE ARG SER GLY LYS SER SER ILE MET ARG SER SEQRES 23 C 573 ASP ALA PRO ILE GLY LYS CYS LYS SER GLU CYS ILE THR SEQRES 24 C 573 PRO ASN GLY SER ILE PRO ASN ASP LYS PRO PHE GLN ASN SEQRES 25 C 573 VAL ASN ARG ILE THR TYR GLY ALA CYS PRO ARG TYR VAL SEQRES 26 C 573 LYS GLN SER THR LEU LYS LEU ALA THR GLY MET ARG ASN SEQRES 27 C 573 VAL PRO GLU LYS GLN THR ARG GLY ILE PHE GLY ALA ILE SEQRES 28 C 573 ALA GLY PHE ILE GLU ASN GLY TRP GLU GLY MET VAL ASP SEQRES 29 C 573 GLY TRP TYR GLY PHE ARG HIS GLN ASN SER GLU GLY ARG SEQRES 30 C 573 GLY GLN ALA ALA ASP LEU LYS SER THR GLN ALA ALA ILE SEQRES 31 C 573 ASP GLN ILE ASN GLY LYS LEU ASN ARG LEU ILE GLY LYS SEQRES 32 C 573 THR ASN GLU LYS PHE HIS GLN ILE GLU LYS GLU PHE SER SEQRES 33 C 573 GLU VAL GLU GLY ARG ILE GLN ASP LEU GLU LYS TYR VAL SEQRES 34 C 573 GLU ASP THR LYS ILE ASP LEU TRP SER TYR ASN ALA GLU SEQRES 35 C 573 LEU LEU VAL ALA LEU GLU ASN GLN HIS THR ILE ASP LEU SEQRES 36 C 573 THR ASP SER GLU MET ASN LYS LEU PHE GLU LYS THR LYS SEQRES 37 C 573 LYS GLN LEU ARG GLU ASN ALA GLU ASP MET GLY ASN GLY SEQRES 38 C 573 CYS PHE LYS ILE TYR HIS LYS CYS ASP ASN ALA CYS ILE SEQRES 39 C 573 GLY SER ILE ARG ASN GLY THR TYR ASP HIS ASN VAL TYR SEQRES 40 C 573 ARG ASP GLU ALA LEU ASN ASN ARG PHE GLN ILE LYS GLY SEQRES 41 C 573 VAL GLU GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY GLN SEQRES 42 C 573 ALA TYR VAL ARG LYS ASP GLY GLU TRP VAL LEU LEU SER SEQRES 43 C 573 THR PHE LEU GLY SER GLY LEU ASN ASP ILE PHE GLU ALA SEQRES 44 C 573 GLN LYS ILE GLU TRP HIS GLU GLY HIS HIS HIS HIS HIS SEQRES 45 C 573 HIS HET NAG D 1 14 HET NAG D 2 14 HET NAG E 1 14 HET NAG E 2 14 HET NAG F 1 14 HET NAG F 2 14 HET NAG G 1 14 HET NAG G 2 14 HET BMA G 3 11 HET NAG K 1 14 HET NAG K 2 14 HET NAG O 1 14 HET NAG O 2 14 HET NAG P 1 14 HET NAG P 2 14 HET NAG Q 1 14 HET NAG Q 2 14 HET NAG R 1 14 HET NAG R 2 14 HET BMA R 3 11 HET NAG S 1 14 HET NAG S 2 14 HET NAG T 1 14 HET NAG T 2 14 HET NAG U 1 14 HET NAG U 2 14 HET NAG V 1 14 HET NAG V 2 14 HET NAG W 1 14 HET NAG W 2 14 HET BMA W 3 11 HET NAG X 1 14 HET NAG X 2 14 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 NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE 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 BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 10 NAG 45(C8 H15 N O6) FORMUL 13 BMA 3(C6 H12 O6) HELIX 1 AA1 THR A 65 GLY A 72 1 8 HELIX 2 AA2 ASP A 73 GLN A 80 5 8 HELIX 3 AA3 ASP A 104 SER A 114 1 11 HELIX 4 AA4 THR A 187 TYR A 195 1 9 HELIX 5 AA5 ASP A 366 ILE A 385 1 20 HELIX 6 AA6 GLY A 404 LYS A 446 1 43 HELIX 7 AA7 PHE A 448 ARG A 456 1 9 HELIX 8 AA8 ASP A 474 GLY A 484 1 11 HELIX 9 AA9 TYR A 491 PHE A 500 1 10 HELIX 10 AB1 THR H 29 PHE H 37 5 5 HELIX 11 AB2 THR H 95 THR H 99 5 5 HELIX 12 AB3 THR I 29 PHE I 37 5 5 HELIX 13 AB4 THR I 95 THR I 99 5 5 HELIX 14 AB5 THR J 29 PHE J 37 5 5 HELIX 15 AB6 THR J 95 THR J 99 5 5 HELIX 16 AB7 THR B 65 GLY B 72 1 8 HELIX 17 AB8 ASP B 73 GLN B 80 5 8 HELIX 18 AB9 ASP B 104 SER B 114 1 11 HELIX 19 AC1 THR B 187 TYR B 195 1 9 HELIX 20 AC2 ASP B 366 ILE B 385 1 20 HELIX 21 AC3 GLY B 404 LYS B 446 1 43 HELIX 22 AC4 PHE B 448 ARG B 456 1 9 HELIX 23 AC5 ASP B 474 GLY B 484 1 11 HELIX 24 AC6 TYR B 491 PHE B 500 1 10 HELIX 25 AC7 THR C 65 GLY C 72 1 8 HELIX 26 AC8 ASP C 73 GLN C 80 5 8 HELIX 27 AC9 ASP C 104 SER C 114 1 11 HELIX 28 AD1 THR C 187 TYR C 195 1 9 HELIX 29 AD2 ASP C 366 ILE C 385 1 20 HELIX 30 AD3 GLY C 404 LYS C 446 1 43 HELIX 31 AD4 PHE C 448 ARG C 456 1 9 HELIX 32 AD5 ASP C 474 GLY C 484 1 11 HELIX 33 AD6 TYR C 491 PHE C 500 1 10 SHEET 1 AA1 3 CYS A 14 HIS A 17 0 SHEET 2 AA1 3 TYR A 351 HIS A 355 -1 O ARG A 354 N CYS A 14 SHEET 3 AA1 3 GLY A 362 ALA A 365 -1 O ALA A 364 N PHE A 353 SHEET 1 AA2 2 THR A 24 VAL A 26 0 SHEET 2 AA2 2 ILE A 34 VAL A 36 -1 O VAL A 36 N THR A 24 SHEET 1 AA3 2 THR A 40 GLU A 41 0 SHEET 2 AA3 2 LYS A 315 LEU A 316 -1 O LEU A 316 N THR A 40 SHEET 1 AA4 3 VAL A 43 GLN A 44 0 SHEET 2 AA4 3 PHE A 294 GLN A 295 1 O PHE A 294 N GLN A 44 SHEET 3 AA4 3 ARG A 307 TYR A 308 1 O ARG A 307 N GLN A 295 SHEET 1 AA5 3 ILE A 58 GLY A 61 0 SHEET 2 AA5 3 LEU A 86 ARG A 90 1 O LEU A 86 N LEU A 59 SHEET 3 AA5 3 ILE A 267 SER A 270 1 O MET A 268 N GLU A 89 SHEET 1 AA6 5 TYR A 100 ASP A 101 0 SHEET 2 AA6 5 ARG A 229 VAL A 237 1 O ILE A 230 N ASP A 101 SHEET 3 AA6 5 LYS A 176 HIS A 184 -1 N TYR A 178 O THR A 235 SHEET 4 AA6 5 LEU A 251 PRO A 254 -1 O ILE A 252 N GLY A 181 SHEET 5 AA6 5 LEU A 151 TRP A 153 -1 N ASN A 152 O ALA A 253 SHEET 1 AA7 2 LYS A 121 ASN A 122 0 SHEET 2 AA7 2 GLY A 256 TYR A 257 -1 O TYR A 257 N LYS A 121 SHEET 1 AA8 2 SER A 136 ILE A 140 0 SHEET 2 AA8 2 SER A 145 SER A 146 -1 O SER A 146 N CYS A 139 SHEET 1 AA9 4 LEU A 164 PRO A 169 0 SHEET 2 AA9 4 ILE A 242 SER A 247 -1 O SER A 247 N LEU A 164 SHEET 3 AA9 4 ILE A 202 SER A 205 -1 N SER A 205 O LEU A 244 SHEET 4 AA9 4 GLN A 210 VAL A 213 -1 O GLN A 211 N VAL A 204 SHEET 1 AB1 2 CYS A 281 THR A 283 0 SHEET 2 AB1 2 GLY A 286 ILE A 288 -1 O GLY A 286 N THR A 283 SHEET 1 AB2 2 ALA A 459 ASP A 461 0 SHEET 2 AB2 2 PHE A 467 ILE A 469 -1 O LYS A 468 N GLU A 460 SHEET 1 AB3 4 GLN H 3 SER H 7 0 SHEET 2 AB3 4 VAL H 19 SER H 26 -1 O SER H 26 N GLN H 3 SHEET 3 AB3 4 THR H 86 VAL H 91 -1 O VAL H 87 N CYS H 23 SHEET 4 AB3 4 VAL H 76 ASP H 81 -1 N ASP H 81 O THR H 86 SHEET 1 AB4 5 THR H 65 PHE H 67 0 SHEET 2 AB4 5 GLU H 51 ILE H 56 -1 N TRP H 55 O ASP H 66 SHEET 3 AB4 5 LEU H 39 GLN H 44 -1 N ARG H 43 O GLU H 51 SHEET 4 AB4 5 VAL H 101 ASP H 108 -1 O VAL H 101 N GLN H 44 SHEET 5 AB4 5 GLY H 114 VAL H 117 -1 O GLY H 114 N ASP H 108 SHEET 1 AB5 4 GLN I 3 SER I 7 0 SHEET 2 AB5 4 VAL I 19 SER I 26 -1 O SER I 26 N GLN I 3 SHEET 3 AB5 4 THR I 86 VAL I 91 -1 O VAL I 87 N CYS I 23 SHEET 4 AB5 4 VAL I 76 ASP I 81 -1 N ASP I 81 O THR I 86 SHEET 1 AB6 5 THR I 65 PHE I 67 0 SHEET 2 AB6 5 GLU I 51 ILE I 56 -1 N TRP I 55 O ASP I 66 SHEET 3 AB6 5 LEU I 39 GLN I 44 -1 N ARG I 43 O GLU I 51 SHEET 4 AB6 5 VAL I 101 ASP I 108 -1 O VAL I 101 N GLN I 44 SHEET 5 AB6 5 GLY I 114 VAL I 117 -1 O GLY I 114 N ASP I 108 SHEET 1 AB7 4 GLN J 3 SER J 7 0 SHEET 2 AB7 4 VAL J 19 SER J 26 -1 O SER J 26 N GLN J 3 SHEET 3 AB7 4 THR J 86 VAL J 91 -1 O VAL J 87 N CYS J 23 SHEET 4 AB7 4 VAL J 76 ASP J 81 -1 N ASP J 81 O THR J 86 SHEET 1 AB8 5 THR J 65 PHE J 67 0 SHEET 2 AB8 5 GLU J 51 ILE J 56 -1 N TRP J 55 O ASP J 66 SHEET 3 AB8 5 LEU J 39 GLN J 44 -1 N ARG J 43 O GLU J 51 SHEET 4 AB8 5 VAL J 101 ASP J 108 -1 O VAL J 101 N GLN J 44 SHEET 5 AB8 5 GLY J 114 VAL J 117 -1 O GLY J 114 N ASP J 108 SHEET 1 AB9 3 VAL L 19 CYS L 23 0 SHEET 2 AB9 3 ALA L 87 ILE L 91 -1 O ALA L 87 N CYS L 23 SHEET 3 AB9 3 PHE L 76 LYS L 80 -1 N SER L 77 O ALA L 90 SHEET 1 AC1 4 ALA L 49 LEU L 53 0 SHEET 2 AC1 4 TYR L 40 LEU L 45 -1 N GLN L 43 O LYS L 51 SHEET 3 AC1 4 TYR L 102 TYR L 107 -1 O GLN L 105 N TYR L 40 SHEET 4 AC1 4 TYR L 116 PHE L 118 -1 O VAL L 117 N SER L 106 SHEET 1 AC2 3 VAL M 19 CYS M 23 0 SHEET 2 AC2 3 ALA M 87 ILE M 91 -1 O ALA M 87 N CYS M 23 SHEET 3 AC2 3 PHE M 76 LYS M 80 -1 N SER M 77 O ALA M 90 SHEET 1 AC3 4 ALA M 49 LEU M 53 0 SHEET 2 AC3 4 TYR M 40 LEU M 45 -1 N GLN M 43 O LYS M 51 SHEET 3 AC3 4 TYR M 102 TYR M 107 -1 O GLN M 105 N TYR M 40 SHEET 4 AC3 4 TYR M 116 PHE M 118 -1 O VAL M 117 N SER M 106 SHEET 1 AC4 3 VAL N 19 CYS N 23 0 SHEET 2 AC4 3 ALA N 87 ILE N 91 -1 O ALA N 87 N CYS N 23 SHEET 3 AC4 3 PHE N 76 LYS N 80 -1 N SER N 77 O ALA N 90 SHEET 1 AC5 4 ALA N 49 LEU N 53 0 SHEET 2 AC5 4 TYR N 40 LEU N 45 -1 N GLN N 43 O LYS N 51 SHEET 3 AC5 4 TYR N 102 TYR N 107 -1 O GLN N 105 N TYR N 40 SHEET 4 AC5 4 TYR N 116 PHE N 118 -1 O VAL N 117 N SER N 106 SHEET 1 AC6 3 CYS B 14 HIS B 17 0 SHEET 2 AC6 3 TYR B 351 HIS B 355 -1 O ARG B 354 N CYS B 14 SHEET 3 AC6 3 GLY B 362 ALA B 365 -1 O ALA B 364 N PHE B 353 SHEET 1 AC7 2 THR B 24 VAL B 26 0 SHEET 2 AC7 2 ILE B 34 VAL B 36 -1 O VAL B 36 N THR B 24 SHEET 1 AC8 2 THR B 40 GLU B 41 0 SHEET 2 AC8 2 LYS B 315 LEU B 316 -1 O LEU B 316 N THR B 40 SHEET 1 AC9 3 VAL B 43 GLN B 44 0 SHEET 2 AC9 3 PHE B 294 GLN B 295 1 O PHE B 294 N GLN B 44 SHEET 3 AC9 3 ARG B 307 TYR B 308 1 O ARG B 307 N GLN B 295 SHEET 1 AD1 3 ILE B 58 GLY B 61 0 SHEET 2 AD1 3 LEU B 86 ARG B 90 1 O LEU B 86 N LEU B 59 SHEET 3 AD1 3 ILE B 267 SER B 270 1 O MET B 268 N GLU B 89 SHEET 1 AD2 5 TYR B 100 ASP B 101 0 SHEET 2 AD2 5 ARG B 229 VAL B 237 1 O ILE B 230 N ASP B 101 SHEET 3 AD2 5 LYS B 176 HIS B 184 -1 N TYR B 178 O THR B 235 SHEET 4 AD2 5 LEU B 251 PRO B 254 -1 O ILE B 252 N GLY B 181 SHEET 5 AD2 5 LEU B 151 TRP B 153 -1 N ASN B 152 O ALA B 253 SHEET 1 AD3 2 LYS B 121 ASN B 122 0 SHEET 2 AD3 2 GLY B 256 TYR B 257 -1 O TYR B 257 N LYS B 121 SHEET 1 AD4 2 SER B 136 ILE B 140 0 SHEET 2 AD4 2 SER B 145 SER B 146 -1 O SER B 146 N CYS B 139 SHEET 1 AD5 4 LEU B 164 PRO B 169 0 SHEET 2 AD5 4 ILE B 242 SER B 247 -1 O SER B 247 N LEU B 164 SHEET 3 AD5 4 ILE B 202 SER B 205 -1 N SER B 205 O LEU B 244 SHEET 4 AD5 4 GLN B 210 VAL B 213 -1 O GLN B 211 N VAL B 204 SHEET 1 AD6 2 CYS B 281 THR B 283 0 SHEET 2 AD6 2 GLY B 286 ILE B 288 -1 O GLY B 286 N THR B 283 SHEET 1 AD7 2 ALA B 459 ASP B 461 0 SHEET 2 AD7 2 PHE B 467 ILE B 469 -1 O LYS B 468 N GLU B 460 SHEET 1 AD8 3 CYS C 14 HIS C 17 0 SHEET 2 AD8 3 TYR C 351 HIS C 355 -1 O ARG C 354 N CYS C 14 SHEET 3 AD8 3 GLY C 362 ALA C 365 -1 O ALA C 364 N PHE C 353 SHEET 1 AD9 2 THR C 24 VAL C 26 0 SHEET 2 AD9 2 ILE C 34 VAL C 36 -1 O VAL C 36 N THR C 24 SHEET 1 AE1 2 THR C 40 GLU C 41 0 SHEET 2 AE1 2 LYS C 315 LEU C 316 -1 O LEU C 316 N THR C 40 SHEET 1 AE2 3 VAL C 43 GLN C 44 0 SHEET 2 AE2 3 PHE C 294 GLN C 295 1 O PHE C 294 N GLN C 44 SHEET 3 AE2 3 ARG C 307 TYR C 308 1 O ARG C 307 N GLN C 295 SHEET 1 AE3 3 ILE C 58 GLY C 61 0 SHEET 2 AE3 3 LEU C 86 ARG C 90 1 O LEU C 86 N LEU C 59 SHEET 3 AE3 3 ILE C 267 SER C 270 1 O MET C 268 N GLU C 89 SHEET 1 AE4 5 TYR C 100 ASP C 101 0 SHEET 2 AE4 5 ARG C 229 VAL C 237 1 O ILE C 230 N ASP C 101 SHEET 3 AE4 5 LYS C 176 HIS C 184 -1 N TYR C 178 O THR C 235 SHEET 4 AE4 5 LEU C 251 PRO C 254 -1 O ILE C 252 N GLY C 181 SHEET 5 AE4 5 LEU C 151 TRP C 153 -1 N ASN C 152 O ALA C 253 SHEET 1 AE5 2 LYS C 121 ASN C 122 0 SHEET 2 AE5 2 GLY C 256 TYR C 257 -1 O TYR C 257 N LYS C 121 SHEET 1 AE6 2 SER C 136 ILE C 140 0 SHEET 2 AE6 2 SER C 145 SER C 146 -1 O SER C 146 N CYS C 139 SHEET 1 AE7 4 LEU C 164 PRO C 169 0 SHEET 2 AE7 4 ILE C 242 SER C 247 -1 O SER C 247 N LEU C 164 SHEET 3 AE7 4 ILE C 202 SER C 205 -1 N SER C 205 O LEU C 244 SHEET 4 AE7 4 GLN C 210 VAL C 213 -1 O GLN C 211 N VAL C 204 SHEET 1 AE8 2 CYS C 281 THR C 283 0 SHEET 2 AE8 2 GLY C 286 ILE C 288 -1 O GLY C 286 N THR C 283 SHEET 1 AE9 2 ALA C 459 ASP C 461 0 SHEET 2 AE9 2 PHE C 467 ILE C 469 -1 O LYS C 468 N GLU C 460 SSBOND 1 CYS A 14 CYS A 466 1555 1555 2.03 SSBOND 2 CYS A 52 CYS A 277 1555 1555 2.03 SSBOND 3 CYS A 64 CYS A 76 1555 1555 2.03 SSBOND 4 CYS A 97 CYS A 139 1555 1555 2.03 SSBOND 5 CYS A 281 CYS A 305 1555 1555 2.03 SSBOND 6 CYS A 473 CYS A 477 1555 1555 2.03 SSBOND 7 CYS H 23 CYS H 104 1555 1555 2.04 SSBOND 8 CYS I 23 CYS I 104 1555 1555 2.04 SSBOND 9 CYS J 23 CYS J 104 1555 1555 2.04 SSBOND 10 CYS L 23 CYS L 104 1555 1555 2.03 SSBOND 11 CYS M 23 CYS M 104 1555 1555 2.03 SSBOND 12 CYS N 23 CYS N 104 1555 1555 2.03 SSBOND 13 CYS B 14 CYS B 466 1555 1555 2.03 SSBOND 14 CYS B 52 CYS B 277 1555 1555 2.03 SSBOND 15 CYS B 64 CYS B 76 1555 1555 2.03 SSBOND 16 CYS B 97 CYS B 139 1555 1555 2.03 SSBOND 17 CYS B 281 CYS B 305 1555 1555 2.03 SSBOND 18 CYS B 473 CYS B 477 1555 1555 2.03 SSBOND 19 CYS C 14 CYS C 466 1555 1555 2.03 SSBOND 20 CYS C 52 CYS C 277 1555 1555 2.03 SSBOND 21 CYS C 64 CYS C 76 1555 1555 2.03 SSBOND 22 CYS C 97 CYS C 139 1555 1555 2.03 SSBOND 23 CYS C 281 CYS C 305 1555 1555 2.03 SSBOND 24 CYS C 473 CYS C 477 1555 1555 2.03 LINK ND2 ASN A 8 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 38 C1 NAG F 1 1555 1555 1.44 LINK ND2 ASN A 63 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN A 126 C1 NAG A 604 1555 1555 1.45 LINK ND2 ASN A 133 C1 NAG A 602 1555 1555 1.44 LINK ND2 ASN A 158 C1 NAG A 603 1555 1555 1.44 LINK ND2 ASN A 165 C1 NAG G 1 1555 1555 1.44 LINK ND2 ASN A 246 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN A 285 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN A 483 C1 NAG A 605 1555 1555 1.44 LINK ND2 ASN B 8 C1 NAG B 601 1555 1555 1.44 LINK ND2 ASN B 38 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN B 63 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN B 126 C1 NAG B 604 1555 1555 1.45 LINK ND2 ASN B 133 C1 NAG B 602 1555 1555 1.44 LINK ND2 ASN B 158 C1 NAG B 603 1555 1555 1.44 LINK ND2 ASN B 165 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN B 246 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN B 285 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN B 483 C1 NAG B 605 1555 1555 1.44 LINK ND2 ASN C 8 C1 NAG C 601 1555 1555 1.44 LINK ND2 ASN C 38 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN C 63 C1 NAG X 1 1555 1555 1.44 LINK ND2 ASN C 126 C1 NAG C 604 1555 1555 1.45 LINK ND2 ASN C 133 C1 NAG C 602 1555 1555 1.44 LINK ND2 ASN C 158 C1 NAG C 603 1555 1555 1.44 LINK ND2 ASN C 165 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN C 246 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN C 285 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN C 483 C1 NAG C 605 1555 1555 1.44 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45 LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.45 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.45 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.44 LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.45 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.45 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.44 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.44 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.44 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.44 LINK O4 NAG W 2 C1 BMA W 3 1555 1555 1.45 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.45 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