HEADER VIRAL PROTEIN 16-APR-25 9O8M TITLE AB1983 IN COMPLEX WITH HIV-1 ENV VARIANT WIN332 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTIBODY AB1983 HEAVY CHAIN VARIABLE FRAGMENT; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: AB1983 LIGHT CHAIN VARIABLE FRAGMENT; COMPND 7 CHAIN: B, D; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ENVELOPE GLYCOPROTEIN GP160; COMPND 11 CHAIN: K, E, I; COMPND 12 SYNONYM: ENV POLYPROTEIN; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: ENVELOPE GLYCOPROTEIN GP160 OF TRANSMEMBRANE PROTEIN GP41; COMPND 16 CHAIN: J, F, L; COMPND 17 SYNONYM: TM, GLYCOPROTEIN 41, GP41; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 19 ORGANISM_TAXID: 11676; SOURCE 20 GENE: ENV; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 24 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 25 MOL_ID: 4; SOURCE 26 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 27 ORGANISM_TAXID: 11676; SOURCE 28 GENE: ENV; SOURCE 29 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 30 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 31 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 32 EXPRESSION_SYSTEM_CELL_LINE: HEK293F KEYWDS HIV-1 ENV, ANTIBODY, VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR Z.J.LIN,J.CUI,J.DU,I.RELANO-RODRIGUEZ,A.ESCOLANO,J.PALLESEN REVDAT 1 04-FEB-26 9O8M 0 JRNL AUTH I.RELANO-RODRIGUEZ,J.DU,Z.J.LIN,M.KERWIN,M.TARQUIS-MEDINA, JRNL AUTH 2 E.URBANO,J.CUI,M.WATKINS,P.ZHAO,R.HABIB,S.GHOSH,J.PARK, JRNL AUTH 3 C.BOROUGHS,A.A.WALSH,M.B.MELO,G.M.SHAW,B.H.HAHN,D.J.IRVINE, JRNL AUTH 4 L.WELLS,D.B.WEINER,D.W.KULP,R.S.VEAZEY,J.PALLESEN,A.ESCOLANO JRNL TITL RAPID ELICITATION OF A NEW CLASS OF 1 NEUTRALIZING JRNL TITL 2 N332-GLYCAN INDEPENDENT V3-GLYCAN ANTIBODIES AGAINST HIV-1 JRNL TITL 3 IN NONHUMAN PRIMATES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.79 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : COOT, CRYOSPARC, ROSETTA REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT 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) : 3.790 REMARK 3 NUMBER OF PARTICLES : 218900 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 9O8M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-25. REMARK 100 THE DEPOSITION ID IS D_1000294103. 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 : ANTIBODY AB1983 IN COMPLEX WITH REMARK 245 HIV-1 ENV WIN332 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 : 7.60 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 GLACIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00 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) : 5000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 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: DECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, K, J, E, F, I, L, REMARK 350 AND CHAINS: G, H, M, N, 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 ALA K 58 REMARK 465 LYS K 59 REMARK 465 ALA K 60 REMARK 465 TYR K 61 REMARK 465 GLU K 62 REMARK 465 THR K 63 REMARK 465 GLU K 64 REMARK 465 LYS K 65 REMARK 465 ASP K 78 REMARK 465 PRO K 79 REMARK 465 ASN K 80 REMARK 465 GLU K 185A REMARK 465 ASN K 185B REMARK 465 GLN K 185C REMARK 465 GLY K 185D REMARK 465 ASN K 185E REMARK 465 ARG K 185F REMARK 465 SER K 185G REMARK 465 ASN K 185H REMARK 465 ASN K 185I REMARK 465 THR K 400 REMARK 465 SER K 401 REMARK 465 VAL K 402 REMARK 465 GLN K 403 REMARK 465 GLY K 404 REMARK 465 SER K 405 REMARK 465 ASN K 406 REMARK 465 SER K 407 REMARK 465 THR K 408 REMARK 465 GLY K 409 REMARK 465 SER K 410 REMARK 465 GLY K 458 REMARK 465 GLY K 459 REMARK 465 SER K 460 REMARK 465 THR K 461 REMARK 465 VAL K 506 REMARK 465 GLY K 507 REMARK 465 ARG K 508 REMARK 465 ARG K 509 REMARK 465 ARG K 510 REMARK 465 ARG K 511 REMARK 465 ARG K 512 REMARK 465 ARG K 513 REMARK 465 ALA J 512 REMARK 465 VAL J 513 REMARK 465 GLY J 514 REMARK 465 ILE J 515 REMARK 465 GLY J 516 REMARK 465 ALA J 517 REMARK 465 VAL J 518 REMARK 465 GLY J 547 REMARK 465 ILE J 548 REMARK 465 VAL J 549 REMARK 465 GLN J 550 REMARK 465 GLN J 551 REMARK 465 GLN J 552 REMARK 465 SER J 553 REMARK 465 ASN J 554 REMARK 465 LEU J 555 REMARK 465 LEU J 556 REMARK 465 ARG J 557 REMARK 465 ALA J 558 REMARK 465 PRO J 559 REMARK 465 GLU J 560 REMARK 465 PRO J 561 REMARK 465 GLN J 562 REMARK 465 GLN J 563 REMARK 465 HIS J 564 REMARK 465 LEU J 565 REMARK 465 LEU J 566 REMARK 465 LYS J 567 REMARK 465 ASP J 568 REMARK 465 ASP J 664 REMARK 465 ALA E 58 REMARK 465 LYS E 59 REMARK 465 ALA E 60 REMARK 465 TYR E 61 REMARK 465 GLU E 62 REMARK 465 THR E 63 REMARK 465 GLU E 64 REMARK 465 LYS E 65 REMARK 465 ASP E 78 REMARK 465 PRO E 79 REMARK 465 ASN E 80 REMARK 465 GLU E 185A REMARK 465 ASN E 185B REMARK 465 GLN E 185C REMARK 465 GLY E 185D REMARK 465 ASN E 185E REMARK 465 ARG E 185F REMARK 465 SER E 185G REMARK 465 ASN E 185H REMARK 465 ASN E 185I REMARK 465 THR E 400 REMARK 465 SER E 401 REMARK 465 VAL E 402 REMARK 465 GLN E 403 REMARK 465 GLY E 404 REMARK 465 SER E 405 REMARK 465 ASN E 406 REMARK 465 SER E 407 REMARK 465 THR E 408 REMARK 465 GLY E 409 REMARK 465 SER E 410 REMARK 465 GLY E 458 REMARK 465 GLY E 459 REMARK 465 SER E 460 REMARK 465 THR E 461 REMARK 465 VAL E 506 REMARK 465 GLY E 507 REMARK 465 ARG E 508 REMARK 465 ARG E 509 REMARK 465 ARG E 510 REMARK 465 ARG E 511 REMARK 465 ARG E 512 REMARK 465 ARG E 513 REMARK 465 ALA F 512 REMARK 465 VAL F 513 REMARK 465 GLY F 514 REMARK 465 ILE F 515 REMARK 465 GLY F 516 REMARK 465 ALA F 517 REMARK 465 VAL F 518 REMARK 465 GLY F 547 REMARK 465 ILE F 548 REMARK 465 VAL F 549 REMARK 465 GLN F 550 REMARK 465 GLN F 551 REMARK 465 GLN F 552 REMARK 465 SER F 553 REMARK 465 ASN F 554 REMARK 465 LEU F 555 REMARK 465 LEU F 556 REMARK 465 ARG F 557 REMARK 465 ALA F 558 REMARK 465 PRO F 559 REMARK 465 GLU F 560 REMARK 465 PRO F 561 REMARK 465 GLN F 562 REMARK 465 GLN F 563 REMARK 465 HIS F 564 REMARK 465 LEU F 565 REMARK 465 LEU F 566 REMARK 465 LYS F 567 REMARK 465 ASP F 568 REMARK 465 ASP F 664 REMARK 465 ALA I 58 REMARK 465 LYS I 59 REMARK 465 ALA I 60 REMARK 465 TYR I 61 REMARK 465 GLU I 62 REMARK 465 THR I 63 REMARK 465 GLU I 64 REMARK 465 LYS I 65 REMARK 465 ASP I 78 REMARK 465 PRO I 79 REMARK 465 ASN I 80 REMARK 465 GLU I 185A REMARK 465 ASN I 185B REMARK 465 GLN I 185C REMARK 465 GLY I 185D REMARK 465 ASN I 185E REMARK 465 ARG I 185F REMARK 465 SER I 185G REMARK 465 ASN I 185H REMARK 465 ASN I 185I REMARK 465 THR I 400 REMARK 465 SER I 401 REMARK 465 VAL I 402 REMARK 465 GLN I 403 REMARK 465 GLY I 404 REMARK 465 SER I 405 REMARK 465 ASN I 406 REMARK 465 SER I 407 REMARK 465 THR I 408 REMARK 465 GLY I 409 REMARK 465 SER I 410 REMARK 465 GLY I 458 REMARK 465 GLY I 459 REMARK 465 SER I 460 REMARK 465 THR I 461 REMARK 465 VAL I 506 REMARK 465 GLY I 507 REMARK 465 ARG I 508 REMARK 465 ARG I 509 REMARK 465 ARG I 510 REMARK 465 ARG I 511 REMARK 465 ARG I 512 REMARK 465 ARG I 513 REMARK 465 ALA L 512 REMARK 465 VAL L 513 REMARK 465 GLY L 514 REMARK 465 ILE L 515 REMARK 465 GLY L 516 REMARK 465 ALA L 517 REMARK 465 VAL L 518 REMARK 465 GLY L 547 REMARK 465 ILE L 548 REMARK 465 VAL L 549 REMARK 465 GLN L 550 REMARK 465 GLN L 551 REMARK 465 GLN L 552 REMARK 465 SER L 553 REMARK 465 ASN L 554 REMARK 465 LEU L 555 REMARK 465 LEU L 556 REMARK 465 ARG L 557 REMARK 465 ALA L 558 REMARK 465 PRO L 559 REMARK 465 GLU L 560 REMARK 465 PRO L 561 REMARK 465 GLN L 562 REMARK 465 GLN L 563 REMARK 465 HIS L 564 REMARK 465 LEU L 565 REMARK 465 LEU L 566 REMARK 465 LYS L 567 REMARK 465 ASP L 568 REMARK 465 ASP L 664 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 SER A 15 -5.98 76.98 REMARK 500 TRP A 108 -109.33 27.10 REMARK 500 VAL B 47 -61.28 -108.64 REMARK 500 TRP C 108 -107.61 27.74 REMARK 500 VAL D 47 -63.54 -106.97 REMARK 500 ALA K 135 76.66 -150.55 REMARK 500 GLN K 258 -21.07 68.54 REMARK 500 THR K 387 -5.52 64.81 REMARK 500 ALA E 135 59.43 38.26 REMARK 500 MET E 150 61.15 -100.60 REMARK 500 GLN E 258 -22.12 67.42 REMARK 500 ASN E 276 93.98 -161.14 REMARK 500 GLN I 258 -22.57 68.20 REMARK 500 ASN I 276 92.60 -162.02 REMARK 500 THR I 387 -5.06 65.03 REMARK 500 LEU L 523 15.64 59.64 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-70231 RELATED DB: EMDB REMARK 900 AB1983 IN COMPLEX WITH HIV-1 ENV VARIANT WIN332 REMARK 900 RELATED ID: 9OED RELATED DB: PDB REMARK 900 AB1999 IN COMPLEX WITH HIV-1 ENV RC1 DBREF 9O8M A 1 123 PDB 9O8M 9O8M 1 123 DBREF 9O8M B 1 116 PDB 9O8M 9O8M 1 116 DBREF 9O8M C 1 123 PDB 9O8M 9O8M 1 123 DBREF 9O8M D 1 116 PDB 9O8M 9O8M 1 116 DBREF 9O8M K 33 513 UNP Q2N0S6 Q2N0S6_HV1 32 510 DBREF 9O8M J 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 9O8M E 33 513 UNP Q2N0S6 Q2N0S6_HV1 32 510 DBREF 9O8M F 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 9O8M I 33 513 UNP Q2N0S6 Q2N0S6_HV1 32 510 DBREF 9O8M L 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 SEQADV 9O8M GLU K 106 UNP Q2N0S6 THR 105 CONFLICT SEQADV 9O8M TYR K 134 UNP Q2N0S6 VAL 133 CONFLICT SEQADV 9O8M ALA K 135 UNP Q2N0S6 THR 134 CONFLICT SEQADV 9O8M PRO K 136 UNP Q2N0S6 ASN 135 CONFLICT SEQADV 9O8M LEU K 138 UNP Q2N0S6 ILE 137 CONFLICT SEQADV 9O8M LEU K 139 UNP Q2N0S6 THR 138 CONFLICT SEQADV 9O8M SER K 140 UNP Q2N0S6 ASP 139 CONFLICT SEQADV 9O8M ASN K 149 UNP Q2N0S6 ASP 140 CONFLICT SEQADV 9O8M GLN K 156 UNP Q2N0S6 ASN 147 CONFLICT SEQADV 9O8M ILE K 271 UNP Q2N0S6 MET 270 CONFLICT SEQADV 9O8M LEU K 288 UNP Q2N0S6 PHE 287 CONFLICT SEQADV 9O8M VAL K 304 UNP Q2N0S6 ARG 303 CONFLICT SEQADV 9O8M TYR K 319 UNP Q2N0S6 ALA 316 CONFLICT SEQADV 9O8M PHE K 320 UNP Q2N0S6 THR 317 CONFLICT SEQADV 9O8M MET K 328 UNP Q2N0S6 GLN 326 CONFLICT SEQADV 9O8M GLN K 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 9O8M GLN K 363 UNP Q2N0S6 ASN 361 CONFLICT SEQADV 9O8M VAL K 415 UNP Q2N0S6 THR 412 CONFLICT SEQADV 9O8M CYS K 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 9O8M ARG K 509 UNP Q2N0S6 GLU 506 CONFLICT SEQADV 9O8M ARG K 510 UNP Q2N0S6 LYS 507 CONFLICT SEQADV 9O8M ARG K 512 UNP Q2N0S6 ALA 509 CONFLICT SEQADV 9O8M ARG K 513 UNP Q2N0S6 VAL 510 CONFLICT SEQADV 9O8M SER J 519 UNP Q2N0S6 PHE 516 CONFLICT SEQADV 9O8M PRO J 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 9O8M PRO J 561 UNP Q2N0S6 ALA 558 CONFLICT SEQADV 9O8M ASP J 568 UNP Q2N0S6 LEU 565 CONFLICT SEQADV 9O8M HIS J 570 UNP Q2N0S6 VAL 567 CONFLICT SEQADV 9O8M HIS J 585 UNP Q2N0S6 ARG 582 CONFLICT SEQADV 9O8M CYS J 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 9O8M GLU E 106 UNP Q2N0S6 THR 105 CONFLICT SEQADV 9O8M TYR E 134 UNP Q2N0S6 VAL 133 CONFLICT SEQADV 9O8M ALA E 135 UNP Q2N0S6 THR 134 CONFLICT SEQADV 9O8M PRO E 136 UNP Q2N0S6 ASN 135 CONFLICT SEQADV 9O8M LEU E 138 UNP Q2N0S6 ILE 137 CONFLICT SEQADV 9O8M LEU E 139 UNP Q2N0S6 THR 138 CONFLICT SEQADV 9O8M SER E 140 UNP Q2N0S6 ASP 139 CONFLICT SEQADV 9O8M ASN E 149 UNP Q2N0S6 ASP 140 CONFLICT SEQADV 9O8M GLN E 156 UNP Q2N0S6 ASN 147 CONFLICT SEQADV 9O8M ILE E 271 UNP Q2N0S6 MET 270 CONFLICT SEQADV 9O8M LEU E 288 UNP Q2N0S6 PHE 287 CONFLICT SEQADV 9O8M VAL E 304 UNP Q2N0S6 ARG 303 CONFLICT SEQADV 9O8M TYR E 319 UNP Q2N0S6 ALA 316 CONFLICT SEQADV 9O8M PHE E 320 UNP Q2N0S6 THR 317 CONFLICT SEQADV 9O8M MET E 328 UNP Q2N0S6 GLN 326 CONFLICT SEQADV 9O8M GLN E 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 9O8M GLN E 363 UNP Q2N0S6 ASN 361 CONFLICT SEQADV 9O8M VAL E 415 UNP Q2N0S6 THR 412 CONFLICT SEQADV 9O8M CYS E 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 9O8M ARG E 509 UNP Q2N0S6 GLU 506 CONFLICT SEQADV 9O8M ARG E 510 UNP Q2N0S6 LYS 507 CONFLICT SEQADV 9O8M ARG E 512 UNP Q2N0S6 ALA 509 CONFLICT SEQADV 9O8M ARG E 513 UNP Q2N0S6 VAL 510 CONFLICT SEQADV 9O8M SER F 519 UNP Q2N0S6 PHE 516 CONFLICT SEQADV 9O8M PRO F 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 9O8M PRO F 561 UNP Q2N0S6 ALA 558 CONFLICT SEQADV 9O8M ASP F 568 UNP Q2N0S6 LEU 565 CONFLICT SEQADV 9O8M HIS F 570 UNP Q2N0S6 VAL 567 CONFLICT SEQADV 9O8M HIS F 585 UNP Q2N0S6 ARG 582 CONFLICT SEQADV 9O8M CYS F 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 9O8M GLU I 106 UNP Q2N0S6 THR 105 CONFLICT SEQADV 9O8M TYR I 134 UNP Q2N0S6 VAL 133 CONFLICT SEQADV 9O8M ALA I 135 UNP Q2N0S6 THR 134 CONFLICT SEQADV 9O8M PRO I 136 UNP Q2N0S6 ASN 135 CONFLICT SEQADV 9O8M LEU I 138 UNP Q2N0S6 ILE 137 CONFLICT SEQADV 9O8M LEU I 139 UNP Q2N0S6 THR 138 CONFLICT SEQADV 9O8M SER I 140 UNP Q2N0S6 ASP 139 CONFLICT SEQADV 9O8M ASN I 149 UNP Q2N0S6 ASP 140 CONFLICT SEQADV 9O8M GLN I 156 UNP Q2N0S6 ASN 147 CONFLICT SEQADV 9O8M ILE I 271 UNP Q2N0S6 MET 270 CONFLICT SEQADV 9O8M LEU I 288 UNP Q2N0S6 PHE 287 CONFLICT SEQADV 9O8M VAL I 304 UNP Q2N0S6 ARG 303 CONFLICT SEQADV 9O8M TYR I 319 UNP Q2N0S6 ALA 316 CONFLICT SEQADV 9O8M PHE I 320 UNP Q2N0S6 THR 317 CONFLICT SEQADV 9O8M MET I 328 UNP Q2N0S6 GLN 326 CONFLICT SEQADV 9O8M GLN I 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 9O8M GLN I 363 UNP Q2N0S6 ASN 361 CONFLICT SEQADV 9O8M VAL I 415 UNP Q2N0S6 THR 412 CONFLICT SEQADV 9O8M CYS I 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 9O8M ARG I 509 UNP Q2N0S6 GLU 506 CONFLICT SEQADV 9O8M ARG I 510 UNP Q2N0S6 LYS 507 CONFLICT SEQADV 9O8M ARG I 512 UNP Q2N0S6 ALA 509 CONFLICT SEQADV 9O8M ARG I 513 UNP Q2N0S6 VAL 510 CONFLICT SEQADV 9O8M SER L 519 UNP Q2N0S6 PHE 516 CONFLICT SEQADV 9O8M PRO L 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 9O8M PRO L 561 UNP Q2N0S6 ALA 558 CONFLICT SEQADV 9O8M ASP L 568 UNP Q2N0S6 LEU 565 CONFLICT SEQADV 9O8M HIS L 570 UNP Q2N0S6 VAL 567 CONFLICT SEQADV 9O8M HIS L 585 UNP Q2N0S6 ARG 582 CONFLICT SEQADV 9O8M CYS L 605 UNP Q2N0S6 THR 602 CONFLICT SEQRES 1 A 123 GLN LEU GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 A 123 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 A 123 GLY SER ILE SER SER ASP TYR TYR TYR TRP SER TRP ILE SEQRES 4 A 123 ARG GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY GLY SEQRES 5 A 123 ILE TYR SER ILE SER GLU SER THR ASN TYR ASN PRO SER SEQRES 6 A 123 LEU LYS SER ARG VAL THR ILE SER LYS ASP THR SER LYS SEQRES 7 A 123 ASN GLN PHE SER LEU LYS LEU SER SER VAL THR ALA ALA SEQRES 8 A 123 ASP THR ALA VAL TYR PHE CYS ALA ARG LYS ASP PRO TYR SEQRES 9 A 123 SER SER GLY TRP THR PRO ASP TYR TRP GLY GLN GLY VAL SEQRES 10 A 123 LEU VAL THR VAL SER SER SEQRES 1 B 116 GLN SER VAL LEU THR GLN PRO SER SER ALA SER ALA SER SEQRES 2 B 116 LEU GLY ALA SER VAL THR LEU THR CYS THR LEU SER SER SEQRES 3 B 116 GLY TYR SER ASN TYR ALA VAL ASP TRP HIS GLN GLN ARG SEQRES 4 B 116 PRO GLY LYS GLY PRO GLN PHE VAL MET ARG VAL GLY THR SEQRES 5 B 116 GLY GLY ILE VAL GLY SER LYS GLY ASP GLY ILE PRO ASP SEQRES 6 B 116 ARG PHE SER GLY SER GLY SER GLY LEU ASN ARG TYR LEU SEQRES 7 B 116 THR ILE LYS ASN ILE GLN GLU GLU ASP GLU SER ASP TYR SEQRES 8 B 116 HIS CYS GLY ALA ASP HIS GLY THR GLY SER SER PHE VAL SEQRES 9 B 116 TRP VAL PHE GLY GLY GLY THR ARG LEU THR VAL LEU SEQRES 1 C 123 GLN LEU GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 C 123 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 C 123 GLY SER ILE SER SER ASP TYR TYR TYR TRP SER TRP ILE SEQRES 4 C 123 ARG GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY GLY SEQRES 5 C 123 ILE TYR SER ILE SER GLU SER THR ASN TYR ASN PRO SER SEQRES 6 C 123 LEU LYS SER ARG VAL THR ILE SER LYS ASP THR SER LYS SEQRES 7 C 123 ASN GLN PHE SER LEU LYS LEU SER SER VAL THR ALA ALA SEQRES 8 C 123 ASP THR ALA VAL TYR PHE CYS ALA ARG LYS ASP PRO TYR SEQRES 9 C 123 SER SER GLY TRP THR PRO ASP TYR TRP GLY GLN GLY VAL SEQRES 10 C 123 LEU VAL THR VAL SER SER SEQRES 1 D 116 GLN SER VAL LEU THR GLN PRO SER SER ALA SER ALA SER SEQRES 2 D 116 LEU GLY ALA SER VAL THR LEU THR CYS THR LEU SER SER SEQRES 3 D 116 GLY TYR SER ASN TYR ALA VAL ASP TRP HIS GLN GLN ARG SEQRES 4 D 116 PRO GLY LYS GLY PRO GLN PHE VAL MET ARG VAL GLY THR SEQRES 5 D 116 GLY GLY ILE VAL GLY SER LYS GLY ASP GLY ILE PRO ASP SEQRES 6 D 116 ARG PHE SER GLY SER GLY SER GLY LEU ASN ARG TYR LEU SEQRES 7 D 116 THR ILE LYS ASN ILE GLN GLU GLU ASP GLU SER ASP TYR SEQRES 8 D 116 HIS CYS GLY ALA ASP HIS GLY THR GLY SER SER PHE VAL SEQRES 9 D 116 TRP VAL PHE GLY GLY GLY THR ARG LEU THR VAL LEU SEQRES 1 K 479 ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP SEQRES 2 K 479 LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA SEQRES 3 K 479 LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR SEQRES 4 K 479 HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE SEQRES 5 K 479 HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS SEQRES 6 K 479 ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE ILE SER SEQRES 7 K 479 LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR SEQRES 8 K 479 PRO LEU CYS VAL THR LEU GLN CYS THR ASN TYR ALA PRO SEQRES 9 K 479 ASN LEU LEU SER ASN MET ARG GLY GLU LEU LYS GLN CYS SEQRES 10 K 479 SER PHE ASN MET THR THR GLU LEU ARG ASP LYS LYS GLN SEQRES 11 K 479 LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL VAL GLN SEQRES 12 K 479 ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SER ASN SEQRES 13 K 479 LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER ALA ILE SEQRES 14 K 479 THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO SEQRES 15 K 479 ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS SEQRES 16 K 479 CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SEQRES 17 K 479 SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO SEQRES 18 K 479 VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA SEQRES 19 K 479 GLU GLU GLU VAL ILE ILE ARG SER GLU ASN ILE THR ASN SEQRES 20 K 479 ASN ALA LYS ASN ILE LEU VAL GLN LEU ASN THR PRO VAL SEQRES 21 K 479 GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR VAL LYS SEQRES 22 K 479 SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR TYR PHE SEQRES 23 K 479 GLY ASP ILE ILE GLY ASP ILE ARG MET ALA HIS CYS GLN SEQRES 24 K 479 VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL SEQRES 25 K 479 VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE SEQRES 26 K 479 ILE ARG PHE ALA GLN SER SER GLY GLY ASP LEU GLU VAL SEQRES 27 K 479 THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR SEQRES 28 K 479 CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SER SEQRES 29 K 479 ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER ASN SEQRES 30 K 479 ASP SER ILE VAL LEU PRO CYS ARG ILE LYS GLN ILE ILE SEQRES 31 K 479 ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO SEQRES 32 K 479 PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR SEQRES 33 K 479 GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SER SEQRES 34 K 479 THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG SEQRES 35 K 479 ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL SEQRES 36 K 479 LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS SEQRES 37 K 479 ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 J 153 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 J 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 J 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 J 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 J 153 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 J 153 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 J 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 J 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 J 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 J 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 J 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 J 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 E 479 ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP SEQRES 2 E 479 LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA SEQRES 3 E 479 LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR SEQRES 4 E 479 HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE SEQRES 5 E 479 HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS SEQRES 6 E 479 ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE ILE SER SEQRES 7 E 479 LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR SEQRES 8 E 479 PRO LEU CYS VAL THR LEU GLN CYS THR ASN TYR ALA PRO SEQRES 9 E 479 ASN LEU LEU SER ASN MET ARG GLY GLU LEU LYS GLN CYS SEQRES 10 E 479 SER PHE ASN MET THR THR GLU LEU ARG ASP LYS LYS GLN SEQRES 11 E 479 LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL VAL GLN SEQRES 12 E 479 ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SER ASN SEQRES 13 E 479 LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER ALA ILE SEQRES 14 E 479 THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO SEQRES 15 E 479 ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS SEQRES 16 E 479 CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SEQRES 17 E 479 SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO SEQRES 18 E 479 VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA SEQRES 19 E 479 GLU GLU GLU VAL ILE ILE ARG SER GLU ASN ILE THR ASN SEQRES 20 E 479 ASN ALA LYS ASN ILE LEU VAL GLN LEU ASN THR PRO VAL SEQRES 21 E 479 GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR VAL LYS SEQRES 22 E 479 SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR TYR PHE SEQRES 23 E 479 GLY ASP ILE ILE GLY ASP ILE ARG MET ALA HIS CYS GLN SEQRES 24 E 479 VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL SEQRES 25 E 479 VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE SEQRES 26 E 479 ILE ARG PHE ALA GLN SER SER GLY GLY ASP LEU GLU VAL SEQRES 27 E 479 THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR SEQRES 28 E 479 CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SER SEQRES 29 E 479 ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER ASN SEQRES 30 E 479 ASP SER ILE VAL LEU PRO CYS ARG ILE LYS GLN ILE ILE SEQRES 31 E 479 ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO SEQRES 32 E 479 PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR SEQRES 33 E 479 GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SER SEQRES 34 E 479 THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG SEQRES 35 E 479 ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL SEQRES 36 E 479 LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS SEQRES 37 E 479 ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 F 153 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 F 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 F 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 F 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 F 153 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 F 153 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 F 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 F 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 F 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 F 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 F 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 F 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 I 479 ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP SEQRES 2 I 479 LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA SEQRES 3 I 479 LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR SEQRES 4 I 479 HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE SEQRES 5 I 479 HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS SEQRES 6 I 479 ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE ILE SER SEQRES 7 I 479 LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR SEQRES 8 I 479 PRO LEU CYS VAL THR LEU GLN CYS THR ASN TYR ALA PRO SEQRES 9 I 479 ASN LEU LEU SER ASN MET ARG GLY GLU LEU LYS GLN CYS SEQRES 10 I 479 SER PHE ASN MET THR THR GLU LEU ARG ASP LYS LYS GLN SEQRES 11 I 479 LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL VAL GLN SEQRES 12 I 479 ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SER ASN SEQRES 13 I 479 LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER ALA ILE SEQRES 14 I 479 THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO SEQRES 15 I 479 ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS SEQRES 16 I 479 CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SEQRES 17 I 479 SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO SEQRES 18 I 479 VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA SEQRES 19 I 479 GLU GLU GLU VAL ILE ILE ARG SER GLU ASN ILE THR ASN SEQRES 20 I 479 ASN ALA LYS ASN ILE LEU VAL GLN LEU ASN THR PRO VAL SEQRES 21 I 479 GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR VAL LYS SEQRES 22 I 479 SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR TYR PHE SEQRES 23 I 479 GLY ASP ILE ILE GLY ASP ILE ARG MET ALA HIS CYS GLN SEQRES 24 I 479 VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL SEQRES 25 I 479 VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE SEQRES 26 I 479 ILE ARG PHE ALA GLN SER SER GLY GLY ASP LEU GLU VAL SEQRES 27 I 479 THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR SEQRES 28 I 479 CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SER SEQRES 29 I 479 ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER ASN SEQRES 30 I 479 ASP SER ILE VAL LEU PRO CYS ARG ILE LYS GLN ILE ILE SEQRES 31 I 479 ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO SEQRES 32 I 479 PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR SEQRES 33 I 479 GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SER SEQRES 34 I 479 THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG SEQRES 35 I 479 ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL SEQRES 36 I 479 LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS SEQRES 37 I 479 ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 L 153 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 L 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 L 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 L 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 L 153 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 L 153 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 L 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 L 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 L 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 L 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 L 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 L 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP HET NAG G 1 14 HET FUC G 2 10 HET NAG H 1 14 HET NAG H 2 14 HET BMA H 3 11 HET MAN H 4 11 HET MAN H 5 11 HET MAN H 6 11 HET NAG M 1 14 HET NAG M 2 14 HET NAG N 1 14 HET NAG N 2 14 HET BMA N 3 11 HET NAG O 1 14 HET NAG O 2 14 HET NAG P 1 14 HET FUC P 2 10 HET NAG Q 1 14 HET NAG Q 2 14 HET BMA Q 3 11 HET MAN Q 4 11 HET MAN Q 5 11 HET MAN Q 6 11 HET NAG R 1 14 HET NAG R 2 14 HET NAG S 1 14 HET NAG S 2 14 HET BMA S 3 11 HET NAG T 1 14 HET NAG T 2 14 HET NAG U 1 14 HET NAG U 2 14 HET BMA U 3 11 HET MAN U 4 11 HET MAN U 5 11 HET MAN U 6 11 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 K 601 14 HET NAG K 602 14 HET NAG K 603 14 HET NAG K 604 14 HET NAG K 605 14 HET NAG K 606 14 HET NAG K 607 14 HET NAG K 608 14 HET NAG E 601 14 HET NAG E 602 14 HET NAG E 603 14 HET NAG E 604 14 HET NAG E 605 14 HET NAG E 606 14 HET NAG E 607 14 HET NAG I 601 14 HET NAG I 602 14 HET NAG I 603 14 HET NAG I 604 14 HET NAG I 605 14 HET NAG I 606 14 HET NAG I 607 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 11 NAG 48(C8 H15 N O6) FORMUL 11 FUC 2(C6 H12 O5) FORMUL 12 BMA 6(C6 H12 O6) FORMUL 12 MAN 9(C6 H12 O6) HELIX 1 AA1 THR A 89 THR A 93 5 5 HELIX 2 AA2 SER B 25 SER B 29 5 5 HELIX 3 AA3 GLN B 84 GLU B 88 5 5 HELIX 4 AA4 THR B 99 PHE B 103 5 5 HELIX 5 AA5 SER C 28 ASP C 32 5 5 HELIX 6 AA6 LEU C 66 SER C 68 5 3 HELIX 7 AA7 THR C 89 THR C 93 5 5 HELIX 8 AA8 SER D 25 SER D 29 5 5 HELIX 9 AA9 GLN D 84 GLU D 88 5 5 HELIX 10 AB1 THR D 99 PHE D 103 5 5 HELIX 11 AB2 ALA K 70 CYS K 74 5 5 HELIX 12 AB3 TRP K 96 ASN K 98 5 3 HELIX 13 AB4 ASN K 99 LYS K 117 1 19 HELIX 14 AB5 LEU K 122 VAL K 127 5 6 HELIX 15 AB6 LYS K 335 GLY K 354 1 20 HELIX 16 AB7 ASP K 368 THR K 373 1 6 HELIX 17 AB8 ASP K 474 SER K 481 1 8 HELIX 18 AB9 LEU J 523 SER J 528 5 6 HELIX 19 AC1 GLY J 531 MET J 535 5 5 HELIX 20 AC2 THR J 536 LEU J 544 1 9 HELIX 21 AC3 HIS J 570 GLY J 597 1 28 HELIX 22 AC4 ASN J 611 SER J 615 5 5 HELIX 23 AC5 ASN J 618 MET J 626 1 9 HELIX 24 AC6 THR J 627 ILE J 635 1 9 HELIX 25 AC7 TYR J 638 ALA J 662 1 25 HELIX 26 AC8 ALA E 70 CYS E 74 5 5 HELIX 27 AC9 TRP E 96 ASN E 98 5 3 HELIX 28 AD1 ASN E 99 LYS E 117 1 19 HELIX 29 AD2 LEU E 122 VAL E 127 5 6 HELIX 30 AD3 LYS E 335 GLY E 354 1 20 HELIX 31 AD4 ASP E 368 THR E 373 1 6 HELIX 32 AD5 ASP E 474 TYR E 484 1 11 HELIX 33 AD6 LEU F 523 SER F 528 5 6 HELIX 34 AD7 THR F 529 SER F 534 1 6 HELIX 35 AD8 THR F 536 LEU F 544 1 9 HELIX 36 AD9 HIS F 570 TRP F 596 1 27 HELIX 37 AE1 ASN F 611 SER F 615 5 5 HELIX 38 AE2 ASN F 618 MET F 626 1 9 HELIX 39 AE3 THR F 627 ILE F 635 1 9 HELIX 40 AE4 TYR F 638 ALA F 662 1 25 HELIX 41 AE5 ALA I 70 CYS I 74 5 5 HELIX 42 AE6 TRP I 96 ASN I 98 5 3 HELIX 43 AE7 ASN I 99 LYS I 117 1 19 HELIX 44 AE8 LEU I 122 VAL I 127 5 6 HELIX 45 AE9 LYS I 335 GLY I 354 1 20 HELIX 46 AF1 ASP I 368 THR I 373 1 6 HELIX 47 AF2 MET I 475 TYR I 484 1 10 HELIX 48 AF3 LEU L 523 SER L 528 5 6 HELIX 49 AF4 GLY L 531 MET L 535 5 5 HELIX 50 AF5 THR L 536 LEU L 544 1 9 HELIX 51 AF6 HIS L 570 GLY L 597 1 28 HELIX 52 AF7 ASN L 611 SER L 615 5 5 HELIX 53 AF8 ASN L 618 MET L 626 1 9 HELIX 54 AF9 THR L 627 ILE L 635 1 9 HELIX 55 AG1 TYR L 638 ALA L 662 1 25 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O ALA A 23 N GLN A 5 SHEET 3 AA1 4 GLN A 80 LEU A 85 -1 O LEU A 85 N LEU A 18 SHEET 4 AA1 4 VAL A 70 ASP A 75 -1 N SER A 73 O SER A 82 SHEET 1 AA2 6 LEU A 11 VAL A 12 0 SHEET 2 AA2 6 VAL A 117 VAL A 121 1 O THR A 120 N VAL A 12 SHEET 3 AA2 6 ALA A 94 LYS A 101 -1 N TYR A 96 O VAL A 117 SHEET 4 AA2 6 TYR A 35 GLN A 41 -1 N ILE A 39 O PHE A 97 SHEET 5 AA2 6 GLU A 48 TYR A 54 -1 O GLY A 51 N TRP A 38 SHEET 6 AA2 6 THR A 60 TYR A 62 -1 O ASN A 61 N GLY A 52 SHEET 1 AA3 4 LEU A 11 VAL A 12 0 SHEET 2 AA3 4 VAL A 117 VAL A 121 1 O THR A 120 N VAL A 12 SHEET 3 AA3 4 ALA A 94 LYS A 101 -1 N TYR A 96 O VAL A 117 SHEET 4 AA3 4 TYR A 112 TRP A 113 -1 O TYR A 112 N ARG A 100 SHEET 1 AA4 6 SER B 9 SER B 13 0 SHEET 2 AA4 6 THR B 111 LEU B 116 1 O ARG B 112 N ALA B 10 SHEET 3 AA4 6 SER B 89 HIS B 97 -1 N TYR B 91 O THR B 111 SHEET 4 AA4 6 VAL B 33 GLN B 38 -1 N ASP B 34 O GLY B 94 SHEET 5 AA4 6 PRO B 44 GLY B 51 -1 O GLN B 45 N GLN B 37 SHEET 6 AA4 6 GLY B 54 ILE B 55 -1 O GLY B 54 N GLY B 51 SHEET 1 AA5 4 SER B 9 SER B 13 0 SHEET 2 AA5 4 THR B 111 LEU B 116 1 O ARG B 112 N ALA B 10 SHEET 3 AA5 4 SER B 89 HIS B 97 -1 N TYR B 91 O THR B 111 SHEET 4 AA5 4 VAL B 104 PHE B 107 -1 O VAL B 104 N HIS B 97 SHEET 1 AA6 3 VAL B 18 THR B 23 0 SHEET 2 AA6 3 ASN B 75 ILE B 80 -1 O LEU B 78 N LEU B 20 SHEET 3 AA6 3 PHE B 67 SER B 72 -1 N SER B 70 O TYR B 77 SHEET 1 AA7 4 GLN C 3 SER C 7 0 SHEET 2 AA7 4 LEU C 18 SER C 25 -1 O SER C 25 N GLN C 3 SHEET 3 AA7 4 GLN C 80 LEU C 85 -1 O PHE C 81 N CYS C 22 SHEET 4 AA7 4 VAL C 70 ASP C 75 -1 N SER C 73 O SER C 82 SHEET 1 AA8 6 LEU C 11 VAL C 12 0 SHEET 2 AA8 6 VAL C 117 VAL C 121 1 O THR C 120 N VAL C 12 SHEET 3 AA8 6 ALA C 94 LYS C 101 -1 N TYR C 96 O VAL C 117 SHEET 4 AA8 6 TYR C 35 GLN C 41 -1 N GLN C 41 O VAL C 95 SHEET 5 AA8 6 GLU C 48 TYR C 54 -1 O GLU C 48 N ARG C 40 SHEET 6 AA8 6 THR C 60 TYR C 62 -1 O ASN C 61 N GLY C 52 SHEET 1 AA9 4 LEU C 11 VAL C 12 0 SHEET 2 AA9 4 VAL C 117 VAL C 121 1 O THR C 120 N VAL C 12 SHEET 3 AA9 4 ALA C 94 LYS C 101 -1 N TYR C 96 O VAL C 117 SHEET 4 AA9 4 TYR C 112 TRP C 113 -1 O TYR C 112 N ARG C 100 SHEET 1 AB1 6 SER D 9 SER D 13 0 SHEET 2 AB1 6 THR D 111 LEU D 116 1 O LEU D 116 N ALA D 12 SHEET 3 AB1 6 SER D 89 HIS D 92 -1 N TYR D 91 O THR D 111 SHEET 4 AB1 6 VAL D 33 GLN D 38 -1 N GLN D 38 O ASP D 90 SHEET 5 AB1 6 PRO D 44 VAL D 50 -1 O GLN D 45 N GLN D 37 SHEET 6 AB1 6 ILE D 55 VAL D 56 -1 O VAL D 56 N ARG D 49 SHEET 1 AB2 3 VAL D 18 THR D 23 0 SHEET 2 AB2 3 ASN D 75 ILE D 80 -1 O LEU D 78 N LEU D 20 SHEET 3 AB2 3 PHE D 67 SER D 72 -1 N SER D 68 O THR D 79 SHEET 1 AB3 2 GLY D 94 HIS D 97 0 SHEET 2 AB3 2 VAL D 104 PHE D 107 -1 O VAL D 104 N HIS D 97 SHEET 1 AB4 3 LEU K 494 THR K 499 0 SHEET 2 AB4 3 TRP K 35 TYR K 40 -1 N TRP K 35 O THR K 499 SHEET 3 AB4 3 ILE J 603 PRO J 609 -1 O VAL J 608 N VAL K 36 SHEET 1 AB5 5 TRP K 45 ASP K 47 0 SHEET 2 AB5 5 TYR K 486 ILE K 491 -1 O LYS K 490 N LYS K 46 SHEET 3 AB5 5 PHE K 223 CYS K 228 -1 N LEU K 226 O LYS K 487 SHEET 4 AB5 5 VAL K 242 VAL K 245 -1 O SER K 243 N LYS K 227 SHEET 5 AB5 5 GLU K 83 HIS K 85 -1 N ILE K 84 O THR K 244 SHEET 1 AB6 3 VAL K 75 PRO K 76 0 SHEET 2 AB6 3 PHE K 53 SER K 56 1 N SER K 56 O VAL K 75 SHEET 3 AB6 3 HIS K 216 CYS K 218 -1 O HIS K 216 N ALA K 55 SHEET 1 AB7 2 GLU K 91 ASN K 94 0 SHEET 2 AB7 2 THR K 236 CYS K 239 -1 O CYS K 239 N GLU K 91 SHEET 1 AB8 5 LYS K 169 TYR K 177 0 SHEET 2 AB8 5 LEU K 154 THR K 162 -1 N CYS K 157 O SER K 174 SHEET 3 AB8 5 LEU K 129 ASN K 133 -1 N GLN K 130 O SER K 158 SHEET 4 AB8 5 LYS K 189 LEU K 193 -1 O TYR K 191 N LEU K 129 SHEET 5 AB8 5 VAL K 181 GLN K 183 -1 N VAL K 182 O ARG K 192 SHEET 1 AB9 3 ILE K 201 GLN K 203 0 SHEET 2 AB9 3 ALA K 433 TYR K 435 1 O TYR K 435 N THR K 202 SHEET 3 AB9 3 ILE K 423 ILE K 424 -1 N ILE K 424 O MET K 434 SHEET 1 AC1 7 LEU K 259 LEU K 261 0 SHEET 2 AC1 7 ILE K 443 ARG K 456 -1 O GLY K 451 N LEU K 260 SHEET 3 AC1 7 ASN K 283 ARG K 298 -1 N ILE K 284 O LEU K 454 SHEET 4 AC1 7 HIS K 330 SER K 334 -1 O GLN K 332 N ASN K 295 SHEET 5 AC1 7 SER K 413 ILE K 420 -1 O LEU K 416 N CYS K 331 SHEET 6 AC1 7 GLU K 381 CYS K 385 -1 N TYR K 384 O ARG K 419 SHEET 7 AC1 7 PHE K 376 CYS K 378 -1 N PHE K 376 O PHE K 383 SHEET 1 AC2 6 ILE K 271 ARG K 273 0 SHEET 2 AC2 6 ASN K 283 ARG K 298 -1 O LEU K 285 N ARG K 273 SHEET 3 AC2 6 ILE K 443 ARG K 456 -1 O LEU K 454 N ILE K 284 SHEET 4 AC2 6 THR K 465 PRO K 470 -1 O ARG K 469 N THR K 455 SHEET 5 AC2 6 ILE K 358 PHE K 361 1 N ILE K 358 O GLU K 466 SHEET 6 AC2 6 THR K 394 TRP K 395 -1 O TRP K 395 N ILE K 359 SHEET 1 AC3 2 ASN K 301 GLY K 312 0 SHEET 2 AC3 2 GLN K 315 ILE K 323 -1 O PHE K 317 N ILE K 307 SHEET 1 AC4 3 LEU E 494 THR E 499 0 SHEET 2 AC4 3 TRP E 35 TYR E 40 -1 N TYR E 39 O GLY E 495 SHEET 3 AC4 3 ILE F 603 PRO F 609 -1 O VAL F 608 N VAL E 36 SHEET 1 AC5 5 TRP E 45 ASP E 47 0 SHEET 2 AC5 5 TYR E 486 ILE E 491 -1 O LYS E 490 N LYS E 46 SHEET 3 AC5 5 PHE E 223 CYS E 228 -1 N LEU E 226 O LYS E 487 SHEET 4 AC5 5 VAL E 242 VAL E 245 -1 O SER E 243 N LYS E 227 SHEET 5 AC5 5 GLU E 83 HIS E 85 -1 N ILE E 84 O THR E 244 SHEET 1 AC6 3 VAL E 75 PRO E 76 0 SHEET 2 AC6 3 PHE E 53 SER E 56 1 N SER E 56 O VAL E 75 SHEET 3 AC6 3 HIS E 216 CYS E 218 -1 O CYS E 218 N PHE E 53 SHEET 1 AC7 2 GLU E 91 ASN E 94 0 SHEET 2 AC7 2 THR E 236 CYS E 239 -1 O CYS E 239 N GLU E 91 SHEET 1 AC8 5 LYS E 169 TYR E 177 0 SHEET 2 AC8 5 LEU E 154 THR E 162 -1 N MET E 161 O GLN E 170 SHEET 3 AC8 5 LEU E 129 ASN E 133 -1 N THR E 132 O GLN E 156 SHEET 4 AC8 5 GLU E 190 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 5 AC8 5 VAL E 181 GLN E 183 -1 N VAL E 182 O ARG E 192 SHEET 1 AC9 3 ILE E 201 GLN E 203 0 SHEET 2 AC9 3 ALA E 433 TYR E 435 1 O TYR E 435 N THR E 202 SHEET 3 AC9 3 ILE E 423 ILE E 424 -1 N ILE E 424 O MET E 434 SHEET 1 AD1 7 LEU E 259 LEU E 260 0 SHEET 2 AD1 7 ILE E 443 ARG E 456 -1 O THR E 450 N LEU E 260 SHEET 3 AD1 7 ASN E 283 ARG E 298 -1 N ILE E 284 O LEU E 454 SHEET 4 AD1 7 HIS E 330 SER E 334 -1 O HIS E 330 N THR E 297 SHEET 5 AD1 7 SER E 413 ILE E 420 -1 O LEU E 416 N CYS E 331 SHEET 6 AD1 7 GLU E 381 CYS E 385 -1 N TYR E 384 O ARG E 419 SHEET 7 AD1 7 PHE E 376 CYS E 378 -1 N PHE E 376 O PHE E 383 SHEET 1 AD2 6 ILE E 271 ARG E 273 0 SHEET 2 AD2 6 ASN E 283 ARG E 298 -1 O LEU E 285 N ARG E 273 SHEET 3 AD2 6 ILE E 443 ARG E 456 -1 O LEU E 454 N ILE E 284 SHEET 4 AD2 6 THR E 465 PRO E 470 -1 O ARG E 469 N THR E 455 SHEET 5 AD2 6 ILE E 358 PHE E 361 1 N ILE E 358 O GLU E 466 SHEET 6 AD2 6 THR E 394 ILE E 396 -1 O TRP E 395 N ILE E 359 SHEET 1 AD3 2 ASN E 301 GLY E 312 0 SHEET 2 AD3 2 GLN E 315 ILE E 323 -1 O PHE E 317 N ILE E 307 SHEET 1 AD4 3 LEU I 494 THR I 499 0 SHEET 2 AD4 3 TRP I 35 TYR I 40 -1 N TRP I 35 O THR I 499 SHEET 3 AD4 3 ILE L 603 PRO L 609 -1 O VAL L 608 N VAL I 36 SHEET 1 AD5 5 TRP I 45 ASP I 47 0 SHEET 2 AD5 5 TYR I 486 ILE I 491 -1 O LYS I 490 N LYS I 46 SHEET 3 AD5 5 PHE I 223 CYS I 228 -1 N LEU I 226 O LYS I 487 SHEET 4 AD5 5 VAL I 242 VAL I 245 -1 O SER I 243 N LYS I 227 SHEET 5 AD5 5 GLU I 83 HIS I 85 -1 N ILE I 84 O THR I 244 SHEET 1 AD6 3 VAL I 75 PRO I 76 0 SHEET 2 AD6 3 PHE I 53 SER I 56 1 N SER I 56 O VAL I 75 SHEET 3 AD6 3 HIS I 216 CYS I 218 -1 O CYS I 218 N PHE I 53 SHEET 1 AD7 2 GLU I 91 ASN I 94 0 SHEET 2 AD7 2 THR I 236 CYS I 239 -1 O CYS I 239 N GLU I 91 SHEET 1 AD8 5 LYS I 169 TYR I 177 0 SHEET 2 AD8 5 LEU I 154 THR I 162 -1 N CYS I 157 O SER I 174 SHEET 3 AD8 5 LEU I 129 ASN I 133 -1 N THR I 132 O GLN I 156 SHEET 4 AD8 5 LYS I 189 LEU I 193 -1 O TYR I 191 N LEU I 129 SHEET 5 AD8 5 VAL I 181 GLN I 183 -1 N VAL I 182 O ARG I 192 SHEET 1 AD9 3 ILE I 201 GLN I 203 0 SHEET 2 AD9 3 ALA I 433 TYR I 435 1 O TYR I 435 N THR I 202 SHEET 3 AD9 3 ILE I 423 ILE I 424 -1 N ILE I 424 O MET I 434 SHEET 1 AE1 7 LEU I 259 LEU I 261 0 SHEET 2 AE1 7 ILE I 443 ARG I 456 -1 O THR I 450 N LEU I 260 SHEET 3 AE1 7 ILE I 284 ARG I 298 -1 N ILE I 284 O LEU I 454 SHEET 4 AE1 7 HIS I 330 SER I 334 -1 O HIS I 330 N THR I 297 SHEET 5 AE1 7 SER I 413 ILE I 420 -1 O LEU I 416 N CYS I 331 SHEET 6 AE1 7 GLU I 381 CYS I 385 -1 N TYR I 384 O ARG I 419 SHEET 7 AE1 7 PHE I 376 CYS I 378 -1 N PHE I 376 O PHE I 383 SHEET 1 AE2 6 ILE I 271 ARG I 273 0 SHEET 2 AE2 6 ILE I 284 ARG I 298 -1 O LEU I 285 N ARG I 273 SHEET 3 AE2 6 ILE I 443 ARG I 456 -1 O LEU I 454 N ILE I 284 SHEET 4 AE2 6 THR I 465 PRO I 470 -1 O ARG I 469 N THR I 455 SHEET 5 AE2 6 ILE I 358 PHE I 361 1 N ILE I 358 O GLU I 466 SHEET 6 AE2 6 THR I 394 TRP I 395 -1 O TRP I 395 N ILE I 359 SHEET 1 AE3 2 ASN I 301 GLY I 312 0 SHEET 2 AE3 2 GLN I 315 ILE I 323 -1 O ILE I 323 N ASN I 301 SSBOND 1 CYS A 22 CYS A 98 1555 1555 2.04 SSBOND 2 CYS B 22 CYS B 93 1555 1555 2.03 SSBOND 3 CYS C 22 CYS C 98 1555 1555 2.04 SSBOND 4 CYS D 22 CYS D 93 1555 1555 2.03 SSBOND 5 CYS K 54 CYS K 74 1555 1555 2.03 SSBOND 6 CYS K 119 CYS K 205 1555 1555 2.05 SSBOND 7 CYS K 126 CYS K 196 1555 1555 2.06 SSBOND 8 CYS K 131 CYS K 157 1555 1555 2.03 SSBOND 9 CYS K 218 CYS K 247 1555 1555 2.04 SSBOND 10 CYS K 228 CYS K 239 1555 1555 2.05 SSBOND 11 CYS K 296 CYS K 331 1555 1555 2.03 SSBOND 12 CYS K 378 CYS K 445 1555 1555 2.03 SSBOND 13 CYS K 385 CYS K 418 1555 1555 2.04 SSBOND 14 CYS K 501 CYS J 605 1555 1555 2.04 SSBOND 15 CYS J 598 CYS J 604 1555 1555 2.05 SSBOND 16 CYS E 54 CYS E 74 1555 1555 2.03 SSBOND 17 CYS E 119 CYS E 205 1555 1555 2.05 SSBOND 18 CYS E 126 CYS E 196 1555 1555 2.10 SSBOND 19 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 20 CYS E 218 CYS E 247 1555 1555 2.04 SSBOND 21 CYS E 228 CYS E 239 1555 1555 2.04 SSBOND 22 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 23 CYS E 378 CYS E 445 1555 1555 2.03 SSBOND 24 CYS E 385 CYS E 418 1555 1555 2.03 SSBOND 25 CYS E 501 CYS F 605 1555 1555 2.04 SSBOND 26 CYS F 598 CYS F 604 1555 1555 2.04 SSBOND 27 CYS I 54 CYS I 74 1555 1555 2.03 SSBOND 28 CYS I 119 CYS I 205 1555 1555 2.05 SSBOND 29 CYS I 126 CYS I 196 1555 1555 2.12 SSBOND 30 CYS I 131 CYS I 157 1555 1555 2.04 SSBOND 31 CYS I 218 CYS I 247 1555 1555 2.04 SSBOND 32 CYS I 228 CYS I 239 1555 1555 2.05 SSBOND 33 CYS I 296 CYS I 331 1555 1555 2.03 SSBOND 34 CYS I 378 CYS I 445 1555 1555 2.03 SSBOND 35 CYS I 385 CYS I 418 1555 1555 2.03 SSBOND 36 CYS I 501 CYS L 605 1555 1555 2.04 SSBOND 37 CYS L 598 CYS L 604 1555 1555 2.04 LINK ND2 ASN K 88 C1 NAG K 601 1555 1555 1.51 LINK ND2 ASN K 160 C1 NAG K 602 1555 1555 1.52 LINK ND2 ASN K 197 C1 NAG K 603 1555 1555 1.52 LINK ND2 ASN K 234 C1 NAG G 1 1555 1555 1.52 LINK ND2 ASN K 262 C1 NAG H 1 1555 1555 1.52 LINK ND2 ASN K 276 C1 NAG K 604 1555 1555 1.50 LINK ND2 ASN K 295 C1 NAG K 605 1555 1555 1.51 LINK ND2 ASN K 301 C1 NAG N 1 1555 1555 1.50 LINK ND2 ASN K 339 C1 NAG K 606 1555 1555 1.51 LINK ND2 ASN K 355 C1 NAG K 607 1555 1555 1.51 LINK ND2 ASN K 386 C1 NAG O 1 1555 1555 1.49 LINK ND2 ASN K 392 C1 NAG K 608 1555 1555 1.49 LINK ND2 ASN K 448 C1 NAG M 1 1555 1555 1.50 LINK ND2 ASN E 88 C1 NAG E 601 1555 1555 1.51 LINK ND2 ASN E 160 C1 NAG E 602 1555 1555 1.51 LINK ND2 ASN E 197 C1 NAG E 603 1555 1555 1.52 LINK ND2 ASN E 234 C1 NAG P 1 1555 1555 1.52 LINK ND2 ASN E 262 C1 NAG Q 1 1555 1555 1.53 LINK ND2 ASN E 276 C1 NAG E 604 1555 1555 1.52 LINK ND2 ASN E 295 C1 NAG E 605 1555 1555 1.50 LINK ND2 ASN E 301 C1 NAG S 1 1555 1555 1.51 LINK ND2 ASN E 339 C1 NAG E 606 1555 1555 1.51 LINK ND2 ASN E 355 C1 NAG E 607 1555 1555 1.51 LINK ND2 ASN E 386 C1 NAG T 1 1555 1555 1.50 LINK ND2 ASN E 448 C1 NAG R 1 1555 1555 1.50 LINK ND2 ASN I 88 C1 NAG I 601 1555 1555 1.50 LINK ND2 ASN I 160 C1 NAG I 602 1555 1555 1.51 LINK ND2 ASN I 197 C1 NAG I 603 1555 1555 1.52 LINK ND2 ASN I 234 C1 NAG I 604 1555 1555 1.52 LINK ND2 ASN I 262 C1 NAG U 1 1555 1555 1.52 LINK ND2 ASN I 276 C1 NAG I 605 1555 1555 1.51 LINK ND2 ASN I 301 C1 NAG W 1 1555 1555 1.51 LINK ND2 ASN I 355 C1 NAG I 606 1555 1555 1.50 LINK ND2 ASN I 386 C1 NAG X 1 1555 1555 1.49 LINK ND2 ASN I 392 C1 NAG I 607 1555 1555 1.50 LINK ND2 ASN I 448 C1 NAG V 1 1555 1555 1.50 LINK O6 NAG G 1 C1 FUC G 2 1555 1555 1.45 LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.39 LINK O4 NAG H 2 C1 BMA H 3 1555 1555 1.39 LINK O3 BMA H 3 C1 MAN H 4 1555 1555 1.39 LINK O6 BMA H 3 C1 MAN H 6 1555 1555 1.40 LINK O2 MAN H 4 C1 MAN H 5 1555 1555 1.39 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.40 LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.39 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.43 LINK O6 NAG P 1 C1 FUC P 2 1555 1555 1.41 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.39 LINK O4 NAG Q 2 C1 BMA Q 3 1555 1555 1.39 LINK O3 BMA Q 3 C1 MAN Q 4 1555 1555 1.39 LINK O6 BMA Q 3 C1 MAN Q 6 1555 1555 1.40 LINK O2 MAN Q 4 C1 MAN Q 5 1555 1555 1.39 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.39 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.39 LINK O4 NAG S 2 C1 BMA S 3 1555 1555 1.39 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.39 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.39 LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.39 LINK O3 BMA U 3 C1 MAN U 4 1555 1555 1.39 LINK O6 BMA U 3 C1 MAN U 6 1555 1555 1.40 LINK O2 MAN U 4 C1 MAN U 5 1555 1555 1.39 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.39 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.39 LINK O4 NAG W 2 C1 BMA W 3 1555 1555 1.39 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.40 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