HEADER VIRAL PROTEIN 02-APR-24 9EVZ TITLE HIV-1 ENVELOPE GLYCOPROTEIN (BG505 GP140 SOSIP.664) TRIMER IN COMPLEX TITLE 2 WITH ELC07 BROADLY NEUTRALIZING ANTIBODY. COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 3 CHAIN: A, B, F; COMPND 4 SYNONYM: ENV POLYPROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: ENVELOPE GLYCOPROTEIN GP120; COMPND 8 CHAIN: C, G, I; COMPND 9 SYNONYM: ENV POLYPROTEIN; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: ELC07 HEAVY CHAIN; COMPND 13 CHAIN: H; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: ELC07 LIGHT CHAIN; COMPND 17 CHAIN: L; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 STRAIN: BG505 SOSIP.664; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: 293F; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 10 ORGANISM_TAXID: 11676; SOURCE 11 STRAIN: BG505 SOSIP.664; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM_STRAIN: 293F; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 20 EXPRESSION_SYSTEM_STRAIN: 293F; SOURCE 21 MOL_ID: 4; SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 23 ORGANISM_TAXID: 9606; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM_STRAIN: 293F KEYWDS HIV-1, ENVELOPE GLYCOPROTEIN, GP140, NEUTRALIZING ANTIBODY, VIRAL KEYWDS 2 PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR J.HOPE,Y.ALGUEL,A.NANS,P.CHEREPANOV REVDAT 1 16-APR-25 9EVZ 0 JRNL AUTH S.GRIFFITH,L.MUIR,O.SUCHANEK,J.HOPE,C.PADE,G.GIBBONS, JRNL AUTH 2 K.TUONG,A.FUNG,E.TOUIZER,C.REES-SPEAR,A.NANS,C.ROUSTAN, JRNL AUTH 3 Y.ALGUEL,D.FINK,C.ORKIN,J.DEAYTON,J.ANDERSON,R.K.GUPTA, JRNL AUTH 4 K.J.DOORES,P.CHEREPANOV,A.MCKNIGHT,M.CLATWORTHY,L.E.MCCOY JRNL TITL TITLE: PRESERVATION OF MEMORY B CELL HOMEOSTASIS IN AN JRNL TITL 2 INDIVIDUAL PRODUCING BROADLY NEUTRALIZING ANTIBODIES AGAINST JRNL TITL 3 HIV-1 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.92 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : EPU, PHENIX, CRYOSPARC, CRYOSPARC, REMARK 3 CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : FOURIER SPACE REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 8FR6 REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : RIGID BODY 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) : 2.920 REMARK 3 NUMBER OF PARTICLES : 275291 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9EVZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-APR-24. REMARK 100 THE DEPOSITION ID IS D_1292137674. 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 : HIV-1 ENVELOPE GLYCOPROTEIN REMARK 245 (BG505 GP140 SOSIP.664) TRIMER REMARK 245 IN COMPLEX WITH ELC07 BROADLY REMARK 245 NEUTRALIZING ANTIBODY REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00 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 : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1300.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 3100.00 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) : 3300.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, F, G, I, H, L, q, u, REMARK 350 AND CHAINS: D, E, J, K, M, N, O, P, Q, REMARK 350 AND CHAINS: R, S, T, U, V, W, e, j, k 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 A 512 REMARK 465 VAL A 513 REMARK 465 GLY A 514 REMARK 465 ILE A 515 REMARK 465 GLY A 516 REMARK 465 ALA A 517 REMARK 465 VAL A 518 REMARK 465 PHE A 519 REMARK 465 LEU A 520 REMARK 465 ILE A 548 REMARK 465 VAL A 549 REMARK 465 GLN A 550 REMARK 465 GLN A 551 REMARK 465 GLN A 552 REMARK 465 SER A 553 REMARK 465 ASN A 554 REMARK 465 LEU A 555 REMARK 465 LEU A 556 REMARK 465 ARG A 557 REMARK 465 ALA A 558 REMARK 465 PRO A 559 REMARK 465 GLU A 560 REMARK 465 ALA A 561 REMARK 465 GLN A 562 REMARK 465 GLN A 563 REMARK 465 HIS A 564 REMARK 465 LEU A 565 REMARK 465 LEU A 566 REMARK 465 LYS A 567 REMARK 465 LEU A 660 REMARK 465 LEU A 661 REMARK 465 ALA A 662 REMARK 465 LEU A 663 REMARK 465 ASP A 664 REMARK 465 GLY A 665 REMARK 465 SER A 666 REMARK 465 GLY A 667 REMARK 465 LEU A 668 REMARK 465 ASN A 669 REMARK 465 ASP A 670 REMARK 465 ILE A 671 REMARK 465 PHE A 672 REMARK 465 GLU A 673 REMARK 465 ALA A 674 REMARK 465 GLN A 675 REMARK 465 LYS A 676 REMARK 465 ILE A 677 REMARK 465 GLU A 678 REMARK 465 TRP A 679 REMARK 465 HIS A 680 REMARK 465 GLU A 681 REMARK 465 ALA B 512 REMARK 465 VAL B 513 REMARK 465 GLY B 514 REMARK 465 ILE B 515 REMARK 465 GLY B 516 REMARK 465 ALA B 517 REMARK 465 VAL B 518 REMARK 465 PHE B 519 REMARK 465 LEU B 520 REMARK 465 ILE B 548 REMARK 465 VAL B 549 REMARK 465 GLN B 550 REMARK 465 GLN B 551 REMARK 465 GLN B 552 REMARK 465 SER B 553 REMARK 465 ASN B 554 REMARK 465 LEU B 555 REMARK 465 LEU B 556 REMARK 465 ARG B 557 REMARK 465 ALA B 558 REMARK 465 PRO B 559 REMARK 465 GLU B 560 REMARK 465 ALA B 561 REMARK 465 GLN B 562 REMARK 465 GLN B 563 REMARK 465 HIS B 564 REMARK 465 LEU B 565 REMARK 465 LEU B 566 REMARK 465 LYS B 567 REMARK 465 GLU B 657 REMARK 465 GLN B 658 REMARK 465 ASP B 659 REMARK 465 LEU B 660 REMARK 465 LEU B 661 REMARK 465 ALA B 662 REMARK 465 LEU B 663 REMARK 465 ASP B 664 REMARK 465 GLY B 665 REMARK 465 SER B 666 REMARK 465 GLY B 667 REMARK 465 LEU B 668 REMARK 465 ASN B 669 REMARK 465 ASP B 670 REMARK 465 ILE B 671 REMARK 465 PHE B 672 REMARK 465 GLU B 673 REMARK 465 ALA B 674 REMARK 465 GLN B 675 REMARK 465 LYS B 676 REMARK 465 ILE B 677 REMARK 465 GLU B 678 REMARK 465 TRP B 679 REMARK 465 HIS B 680 REMARK 465 GLU B 681 REMARK 465 MET C -4 REMARK 465 ASP C -3 REMARK 465 ALA C -2 REMARK 465 MET C -1 REMARK 465 LYS C 0 REMARK 465 ARG C 1 REMARK 465 GLY C 2 REMARK 465 LEU C 3 REMARK 465 CYS C 4 REMARK 465 CYS C 5 REMARK 465 VAL C 6 REMARK 465 LEU C 7 REMARK 465 LEU C 8 REMARK 465 LEU C 9 REMARK 465 CYS C 10 REMARK 465 GLY C 11 REMARK 465 ALA C 12 REMARK 465 VAL C 13 REMARK 465 PHE C 14 REMARK 465 VAL C 15 REMARK 465 SER C 16 REMARK 465 PRO C 17 REMARK 465 SER C 18 REMARK 465 GLN C 19 REMARK 465 GLU C 20 REMARK 465 ILE C 21 REMARK 465 HIS C 22 REMARK 465 ALA C 23 REMARK 465 ARG C 24 REMARK 465 PHE C 25 REMARK 465 ARG C 26 REMARK 465 ARG C 27 REMARK 465 GLY C 28 REMARK 465 ALA C 29 REMARK 465 ARG C 30 REMARK 465 ALA C 31 REMARK 465 GLU C 32 REMARK 465 LYS C 59 REMARK 465 ALA C 60 REMARK 465 TYR C 61 REMARK 465 GLU C 62 REMARK 465 THR C 63 REMARK 465 GLU C 64 REMARK 465 GLU C 185A REMARK 465 ASN C 185B REMARK 465 GLN C 185C REMARK 465 GLY C 185D REMARK 465 ASN C 185E REMARK 465 ARG C 185F REMARK 465 SER C 185G REMARK 465 ASN C 185H REMARK 465 ASN C 185I REMARK 465 SER C 185J REMARK 465 ASN C 399 REMARK 465 THR C 400 REMARK 465 SER C 401 REMARK 465 VAL C 402 REMARK 465 GLN C 403 REMARK 465 GLY C 404 REMARK 465 SER C 405 REMARK 465 ASN C 406 REMARK 465 SER C 407 REMARK 465 THR C 408 REMARK 465 GLY C 409 REMARK 465 SER C 410 REMARK 465 VAL C 505 REMARK 465 VAL C 506 REMARK 465 GLY C 507 REMARK 465 ARG C 508 REMARK 465 ARG C 509 REMARK 465 ARG C 510 REMARK 465 ARG C 511 REMARK 465 ARG C 512 REMARK 465 ARG C 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 PHE F 519 REMARK 465 LEU F 520 REMARK 465 GLY F 521 REMARK 465 VAL F 539 REMARK 465 GLN F 540 REMARK 465 ALA F 541 REMARK 465 ARG F 542 REMARK 465 ASN F 543 REMARK 465 LEU F 544 REMARK 465 LEU F 545 REMARK 465 SER F 546 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 ALA 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 664 REMARK 465 GLY F 665 REMARK 465 SER F 666 REMARK 465 GLY F 667 REMARK 465 LEU F 668 REMARK 465 ASN F 669 REMARK 465 ASP F 670 REMARK 465 ILE F 671 REMARK 465 PHE F 672 REMARK 465 GLU F 673 REMARK 465 ALA F 674 REMARK 465 GLN F 675 REMARK 465 LYS F 676 REMARK 465 ILE F 677 REMARK 465 GLU F 678 REMARK 465 TRP F 679 REMARK 465 HIS F 680 REMARK 465 GLU F 681 REMARK 465 MET G -4 REMARK 465 ASP G -3 REMARK 465 ALA G -2 REMARK 465 MET G -1 REMARK 465 LYS G 0 REMARK 465 ARG G 1 REMARK 465 GLY G 2 REMARK 465 LEU G 3 REMARK 465 CYS G 4 REMARK 465 CYS G 5 REMARK 465 VAL G 6 REMARK 465 LEU G 7 REMARK 465 LEU G 8 REMARK 465 LEU G 9 REMARK 465 CYS G 10 REMARK 465 GLY G 11 REMARK 465 ALA G 12 REMARK 465 VAL G 13 REMARK 465 PHE G 14 REMARK 465 VAL G 15 REMARK 465 SER G 16 REMARK 465 PRO G 17 REMARK 465 SER G 18 REMARK 465 GLN G 19 REMARK 465 GLU G 20 REMARK 465 ILE G 21 REMARK 465 HIS G 22 REMARK 465 ALA G 23 REMARK 465 ARG G 24 REMARK 465 PHE G 25 REMARK 465 ARG G 26 REMARK 465 ARG G 27 REMARK 465 GLY G 28 REMARK 465 ALA G 29 REMARK 465 ARG G 30 REMARK 465 ALA G 31 REMARK 465 GLU G 32 REMARK 465 ASN G 33 REMARK 465 ASP G 57 REMARK 465 ALA G 58 REMARK 465 LYS G 59 REMARK 465 ALA G 60 REMARK 465 TYR G 61 REMARK 465 GLU G 62 REMARK 465 THR G 63 REMARK 465 GLU G 64 REMARK 465 LYS G 65 REMARK 465 GLU G 185A REMARK 465 ASN G 185B REMARK 465 GLN G 185C REMARK 465 GLY G 185D REMARK 465 ASN G 185E REMARK 465 ARG G 185F REMARK 465 SER G 185G REMARK 465 ASN G 185H REMARK 465 ASN G 185I REMARK 465 SER G 185J REMARK 465 ASN G 399 REMARK 465 THR G 400 REMARK 465 SER G 401 REMARK 465 VAL G 402 REMARK 465 GLN G 403 REMARK 465 GLY G 404 REMARK 465 SER G 405 REMARK 465 ASN G 406 REMARK 465 SER G 407 REMARK 465 THR G 408 REMARK 465 GLY G 409 REMARK 465 SER G 410 REMARK 465 VAL G 505 REMARK 465 VAL G 506 REMARK 465 GLY G 507 REMARK 465 ARG G 508 REMARK 465 ARG G 509 REMARK 465 ARG G 510 REMARK 465 ARG G 511 REMARK 465 ARG G 512 REMARK 465 ARG G 513 REMARK 465 MET I -4 REMARK 465 ASP I -3 REMARK 465 ALA I -2 REMARK 465 MET I -1 REMARK 465 LYS I 0 REMARK 465 ARG I 1 REMARK 465 GLY I 2 REMARK 465 LEU I 3 REMARK 465 CYS I 4 REMARK 465 CYS I 5 REMARK 465 VAL I 6 REMARK 465 LEU I 7 REMARK 465 LEU I 8 REMARK 465 LEU I 9 REMARK 465 CYS I 10 REMARK 465 GLY I 11 REMARK 465 ALA I 12 REMARK 465 VAL I 13 REMARK 465 PHE I 14 REMARK 465 VAL I 15 REMARK 465 SER I 16 REMARK 465 PRO I 17 REMARK 465 SER I 18 REMARK 465 GLN I 19 REMARK 465 GLU I 20 REMARK 465 ILE I 21 REMARK 465 HIS I 22 REMARK 465 ALA I 23 REMARK 465 ARG I 24 REMARK 465 PHE I 25 REMARK 465 ARG I 26 REMARK 465 ARG I 27 REMARK 465 GLY I 28 REMARK 465 ALA I 29 REMARK 465 ARG I 30 REMARK 465 ALA I 31 REMARK 465 GLU I 32 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 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 SER I 185J REMARK 465 ASN I 399 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 VAL I 505 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 MET H -19 REMARK 465 GLU H -18 REMARK 465 THR H -17 REMARK 465 ASP H -16 REMARK 465 THR H -15 REMARK 465 LEU H -14 REMARK 465 LEU H -13 REMARK 465 LEU H -12 REMARK 465 TRP H -11 REMARK 465 VAL H -10 REMARK 465 LEU H -9 REMARK 465 LEU H -8 REMARK 465 LEU H -7 REMARK 465 TRP H -6 REMARK 465 VAL H -5 REMARK 465 PRO H -4 REMARK 465 GLY H -3 REMARK 465 SER H -2 REMARK 465 THR H -1 REMARK 465 GLY H 0 REMARK 465 GLY H 217 REMARK 465 SER H 218 REMARK 465 GLY H 219 REMARK 465 GLU H 220 REMARK 465 ASN H 221 REMARK 465 LEU H 222 REMARK 465 TYR H 223 REMARK 465 PHE H 224 REMARK 465 GLN H 225 REMARK 465 SER H 226 REMARK 465 ALA H 227 REMARK 465 GLY H 228 REMARK 465 HIS H 229 REMARK 465 HIS H 230 REMARK 465 HIS H 231 REMARK 465 HIS H 232 REMARK 465 HIS H 233 REMARK 465 HIS H 234 REMARK 465 MET L -20 REMARK 465 THR L -19 REMARK 465 GLN L -18 REMARK 465 THR L -17 REMARK 465 PRO L -16 REMARK 465 ALA L -15 REMARK 465 SER L -14 REMARK 465 LEU L -13 REMARK 465 LEU L -12 REMARK 465 PHE L -11 REMARK 465 LEU L -10 REMARK 465 LEU L -9 REMARK 465 LEU L -8 REMARK 465 LEU L -7 REMARK 465 TRP L -6 REMARK 465 LEU L -5 REMARK 465 PRO L -4 REMARK 465 GLY L -3 REMARK 465 ALA L -2 REMARK 465 LYS L -1 REMARK 465 CYS L 0 REMARK 465 ASP L 1 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 LYS A 655 CG CD CE NZ REMARK 470 LEU B 568 CG CD1 CD2 REMARK 470 LYS B 655 CG CD CE NZ REMARK 470 ARG C 504 CG CD NE CZ NH1 NH2 REMARK 470 ARG G 504 CG CD NE CZ NH1 NH2 REMARK 470 ASN I 33 CG OD1 ND2 REMARK 470 ARG I 504 CG CD NE CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS C 378 CA - CB - SG ANGL. DEV. = 6.9 DEGREES REMARK 500 CYS C 445 CA - CB - SG ANGL. DEV. = 6.8 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU A 523 19.36 57.92 REMARK 500 ASN A 543 51.88 -91.91 REMARK 500 ALA B 525 31.04 -96.51 REMARK 500 LEU B 619 48.56 -85.15 REMARK 500 SER B 620 -52.54 -122.21 REMARK 500 LEU C 122 52.04 -92.87 REMARK 500 GLN C 258 -10.63 72.08 REMARK 500 LEU G 122 56.19 -92.90 REMARK 500 THR G 135 -159.62 -126.86 REMARK 500 ASN G 136 75.64 67.14 REMARK 500 ASN G 137 54.51 72.02 REMARK 500 GLN G 258 -9.10 71.60 REMARK 500 ARG G 500 40.99 -109.48 REMARK 500 THR I 135 -158.44 -125.72 REMARK 500 ASN I 136 75.90 67.86 REMARK 500 ASN I 137 32.91 79.96 REMARK 500 ASP I 167 -15.84 -142.61 REMARK 500 CYS I 196 45.81 -82.66 REMARK 500 GLN I 258 -11.56 72.53 REMARK 500 ASP H 144 61.81 61.48 REMARK 500 SER L 30 -120.17 54.82 REMARK 500 SER L 67 -174.23 -170.99 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG O 1 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 8FR6 RELATED DB: PDB REMARK 900 STARTING MODEL REMARK 900 RELATED ID: EMD-50020 RELATED DB: EMDB REMARK 900 HIV-1 ENVELOPE GLYCOPROTEIN (BG505 GP140 SOSIP.664) TRIMER IN REMARK 900 COMPLEX WITH ELC07 BROADLY NEUTRALIZING ANTIBODY. DBREF 9EVZ A 512 681 PDB 9EVZ 9EVZ 512 681 DBREF 9EVZ B 512 681 PDB 9EVZ 9EVZ 512 681 DBREF 9EVZ C -4 513 PDB 9EVZ 9EVZ -4 513 DBREF 9EVZ F 512 681 PDB 9EVZ 9EVZ 512 681 DBREF 9EVZ G -4 513 PDB 9EVZ 9EVZ -4 513 DBREF 9EVZ I -4 513 PDB 9EVZ 9EVZ -4 513 DBREF 9EVZ H -19 234 PDB 9EVZ 9EVZ -19 234 DBREF 9EVZ L -20 214 PDB 9EVZ 9EVZ -20 214 SEQRES 1 A 170 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 A 170 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 A 170 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 A 170 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 A 170 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 A 170 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 A 170 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 A 170 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 A 170 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 A 170 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 A 170 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 A 170 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP GLY SER GLY SEQRES 13 A 170 LEU ASN ASP ILE PHE GLU ALA GLN LYS ILE GLU TRP HIS SEQRES 14 A 170 GLU SEQRES 1 B 170 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 B 170 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 B 170 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 B 170 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 B 170 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 B 170 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 B 170 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 B 170 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 B 170 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 B 170 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 B 170 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 B 170 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP GLY SER GLY SEQRES 13 B 170 LEU ASN ASP ILE PHE GLU ALA GLN LYS ILE GLU TRP HIS SEQRES 14 B 170 GLU SEQRES 1 C 516 MET ASP ALA MET LYS ARG GLY LEU CYS CYS VAL LEU LEU SEQRES 2 C 516 LEU CYS GLY ALA VAL PHE VAL SER PRO SER GLN GLU ILE SEQRES 3 C 516 HIS ALA ARG PHE ARG ARG GLY ALA ARG ALA GLU ASN LEU SEQRES 4 C 516 TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP LYS ASP SEQRES 5 C 516 ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA LYS ALA SEQRES 6 C 516 TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR HIS ALA SEQRES 7 C 516 CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE HIS LEU SEQRES 8 C 516 GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS ASN ASN SEQRES 9 C 516 MET VAL GLU GLN MET HIS THR ASP ILE ILE SER LEU TRP SEQRES 10 C 516 ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR PRO LEU SEQRES 11 C 516 CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN ASN ILE SEQRES 12 C 516 THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SER PHE SEQRES 13 C 516 ASN MET THR THR GLU LEU ARG ASP LYS LYS GLN LYS VAL SEQRES 14 C 516 TYR SER LEU PHE TYR ARG LEU ASP VAL VAL GLN ILE ASN SEQRES 15 C 516 GLU ASN GLN GLY ASN ARG SER ASN ASN SER ASN LYS GLU SEQRES 16 C 516 TYR ARG LEU ILE ASN CYS ASN THR SER ALA ILE THR GLN SEQRES 17 C 516 ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE HIS SEQRES 18 C 516 TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS SEQRES 19 C 516 ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SER VAL SEQRES 20 C 516 SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SEQRES 21 C 516 SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU GLU SEQRES 22 C 516 GLU VAL MET ILE ARG SER GLU ASN ILE THR ASN ASN ALA SEQRES 23 C 516 LYS ASN ILE LEU VAL GLN PHE ASN THR PRO VAL GLN ILE SEQRES 24 C 516 ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SER ILE SEQRES 25 C 516 ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA THR GLY ASP SEQRES 26 C 516 ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN VAL SER SEQRES 27 C 516 LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL VAL LYS SEQRES 28 C 516 GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE ILE ARG SEQRES 29 C 516 PHE ALA ASN SER SER GLY GLY ASP LEU GLU VAL THR THR SEQRES 30 C 516 HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN SEQRES 31 C 516 THR SER GLY LEU PHE ASN SER THR TRP ILE SER ASN THR SEQRES 32 C 516 SER VAL GLN GLY SER ASN SER THR GLY SER ASN ASP SER SEQRES 33 C 516 ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE ASN MET SEQRES 34 C 516 TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO PRO ILE SEQRES 35 C 516 GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR GLY LEU SEQRES 36 C 516 ILE LEU THR ARG ASP GLY GLY SER THR ASN SER THR THR SEQRES 37 C 516 GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG ASP ASN SEQRES 38 C 516 TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE SEQRES 39 C 516 GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS ARG ARG SEQRES 40 C 516 VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 F 170 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 F 170 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 F 170 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 F 170 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 F 170 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 F 170 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 F 170 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 F 170 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 F 170 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 F 170 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 F 170 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 F 170 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP GLY SER GLY SEQRES 13 F 170 LEU ASN ASP ILE PHE GLU ALA GLN LYS ILE GLU TRP HIS SEQRES 14 F 170 GLU SEQRES 1 G 516 MET ASP ALA MET LYS ARG GLY LEU CYS CYS VAL LEU LEU SEQRES 2 G 516 LEU CYS GLY ALA VAL PHE VAL SER PRO SER GLN GLU ILE SEQRES 3 G 516 HIS ALA ARG PHE ARG ARG GLY ALA ARG ALA GLU ASN LEU SEQRES 4 G 516 TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP LYS ASP SEQRES 5 G 516 ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA LYS ALA SEQRES 6 G 516 TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR HIS ALA SEQRES 7 G 516 CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE HIS LEU SEQRES 8 G 516 GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS ASN ASN SEQRES 9 G 516 MET VAL GLU GLN MET HIS THR ASP ILE ILE SER LEU TRP SEQRES 10 G 516 ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR PRO LEU SEQRES 11 G 516 CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN ASN ILE SEQRES 12 G 516 THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SER PHE SEQRES 13 G 516 ASN MET THR THR GLU LEU ARG ASP LYS LYS GLN LYS VAL SEQRES 14 G 516 TYR SER LEU PHE TYR ARG LEU ASP VAL VAL GLN ILE ASN SEQRES 15 G 516 GLU ASN GLN GLY ASN ARG SER ASN ASN SER ASN LYS GLU SEQRES 16 G 516 TYR ARG LEU ILE ASN CYS ASN THR SER ALA ILE THR GLN SEQRES 17 G 516 ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE HIS SEQRES 18 G 516 TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS SEQRES 19 G 516 ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SER VAL SEQRES 20 G 516 SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SEQRES 21 G 516 SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU GLU SEQRES 22 G 516 GLU VAL MET ILE ARG SER GLU ASN ILE THR ASN ASN ALA SEQRES 23 G 516 LYS ASN ILE LEU VAL GLN PHE ASN THR PRO VAL GLN ILE SEQRES 24 G 516 ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SER ILE SEQRES 25 G 516 ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA THR GLY ASP SEQRES 26 G 516 ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN VAL SER SEQRES 27 G 516 LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL VAL LYS SEQRES 28 G 516 GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE ILE ARG SEQRES 29 G 516 PHE ALA ASN SER SER GLY GLY ASP LEU GLU VAL THR THR SEQRES 30 G 516 HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN SEQRES 31 G 516 THR SER GLY LEU PHE ASN SER THR TRP ILE SER ASN THR SEQRES 32 G 516 SER VAL GLN GLY SER ASN SER THR GLY SER ASN ASP SER SEQRES 33 G 516 ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE ASN MET SEQRES 34 G 516 TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO PRO ILE SEQRES 35 G 516 GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR GLY LEU SEQRES 36 G 516 ILE LEU THR ARG ASP GLY GLY SER THR ASN SER THR THR SEQRES 37 G 516 GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG ASP ASN SEQRES 38 G 516 TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE SEQRES 39 G 516 GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS ARG ARG SEQRES 40 G 516 VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 I 516 MET ASP ALA MET LYS ARG GLY LEU CYS CYS VAL LEU LEU SEQRES 2 I 516 LEU CYS GLY ALA VAL PHE VAL SER PRO SER GLN GLU ILE SEQRES 3 I 516 HIS ALA ARG PHE ARG ARG GLY ALA ARG ALA GLU ASN LEU SEQRES 4 I 516 TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP LYS ASP SEQRES 5 I 516 ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA LYS ALA SEQRES 6 I 516 TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR HIS ALA SEQRES 7 I 516 CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE HIS LEU SEQRES 8 I 516 GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS ASN ASN SEQRES 9 I 516 MET VAL GLU GLN MET HIS THR ASP ILE ILE SER LEU TRP SEQRES 10 I 516 ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR PRO LEU SEQRES 11 I 516 CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN ASN ILE SEQRES 12 I 516 THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SER PHE SEQRES 13 I 516 ASN MET THR THR GLU LEU ARG ASP LYS LYS GLN LYS VAL SEQRES 14 I 516 TYR SER LEU PHE TYR ARG LEU ASP VAL VAL GLN ILE ASN SEQRES 15 I 516 GLU ASN GLN GLY ASN ARG SER ASN ASN SER ASN LYS GLU SEQRES 16 I 516 TYR ARG LEU ILE ASN CYS ASN THR SER ALA ILE THR GLN SEQRES 17 I 516 ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE HIS SEQRES 18 I 516 TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS SEQRES 19 I 516 ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SER VAL SEQRES 20 I 516 SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SEQRES 21 I 516 SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU GLU SEQRES 22 I 516 GLU VAL MET ILE ARG SER GLU ASN ILE THR ASN ASN ALA SEQRES 23 I 516 LYS ASN ILE LEU VAL GLN PHE ASN THR PRO VAL GLN ILE SEQRES 24 I 516 ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SER ILE SEQRES 25 I 516 ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA THR GLY ASP SEQRES 26 I 516 ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN VAL SER SEQRES 27 I 516 LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL VAL LYS SEQRES 28 I 516 GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE ILE ARG SEQRES 29 I 516 PHE ALA ASN SER SER GLY GLY ASP LEU GLU VAL THR THR SEQRES 30 I 516 HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN SEQRES 31 I 516 THR SER GLY LEU PHE ASN SER THR TRP ILE SER ASN THR SEQRES 32 I 516 SER VAL GLN GLY SER ASN SER THR GLY SER ASN ASP SER SEQRES 33 I 516 ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE ASN MET SEQRES 34 I 516 TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO PRO ILE SEQRES 35 I 516 GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR GLY LEU SEQRES 36 I 516 ILE LEU THR ARG ASP GLY GLY SER THR ASN SER THR THR SEQRES 37 I 516 GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG ASP ASN SEQRES 38 I 516 TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE SEQRES 39 I 516 GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS ARG ARG SEQRES 40 I 516 VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 H 268 MET GLU THR ASP THR LEU LEU LEU TRP VAL LEU LEU LEU SEQRES 2 H 268 TRP VAL PRO GLY SER THR GLY GLU VAL GLN LEU VAL GLN SEQRES 3 H 268 SER GLY ALA GLU LEU LYS LYS ALA GLY SER SER VAL LYS SEQRES 4 H 268 LEU SER CYS GLN ALA TYR GLY VAL ALA PHE SER THR TYR SEQRES 5 H 268 SER PHE HIS TRP VAL ARG GLN ALA PRO GLY GLN GLY LEU SEQRES 6 H 268 GLU TRP LEU GLY GLY PHE ILE PRO LEU VAL GLY LYS PRO SEQRES 7 H 268 ASN TYR THR ASN LYS PHE ARG GLY ARG LEU THR ILE THR SEQRES 8 H 268 ALA ASP GLU SER ALA ARG THR THR TYR MET GLU LEU ARG SEQRES 9 H 268 SER LEU ARG SER ASP ASP THR ALA ILE TYR TYR CYS ALA SEQRES 10 H 268 GLY GLY GLY ALA TYR SER SER GLY GLY GLY ARG PHE HIS SEQRES 11 H 268 TYR PHE GLY MET ALA VAL TRP GLY GLN GLY SER THR VAL SEQRES 12 H 268 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 13 H 268 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 14 H 268 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 15 H 268 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 16 H 268 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 17 H 268 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 18 H 268 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 19 H 268 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 20 H 268 LYS SER CYS GLY SER GLY GLU ASN LEU TYR PHE GLN SER SEQRES 21 H 268 ALA GLY HIS HIS HIS HIS HIS HIS SEQRES 1 L 235 MET THR GLN THR PRO ALA SER LEU LEU PHE LEU LEU LEU SEQRES 2 L 235 LEU TRP LEU PRO GLY ALA LYS CYS ASP ILE GLN LEU THR SEQRES 3 L 235 GLN SER PRO SER THR LEU SER ALA PRO VAL GLY ALA GLY SEQRES 4 L 235 VAL THR ILE THR CYS GLN ALA SER GLN SER ILE SER ASN SEQRES 5 L 235 GLY LEU ALA TRP TYR GLN GLN LYS PRO GLY ARG ALA PRO SEQRES 6 L 235 LYS MET LEU ILE THR GLU GLY SER SER LEU LYS SER GLY SEQRES 7 L 235 VAL PRO ASP ARG PHE ARG GLY SER GLY SER GLY THR HIS SEQRES 8 L 235 PHE ILE LEU THR ILE SER ASP LEU GLN PRO ASP ASP SER SEQRES 9 L 235 ALA THR TYR PHE CYS GLN GLN TYR ASN THR PHE PRO TRP SEQRES 10 L 235 THR PHE GLY ARG GLY THR LYS VAL GLU ILE LYS ARG THR SEQRES 11 L 235 VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP SEQRES 12 L 235 GLU GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU SEQRES 13 L 235 LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP SEQRES 14 L 235 LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SEQRES 15 L 235 SER VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SER SEQRES 16 L 235 LEU SER SER THR LEU THR LEU SER LYS ALA ASP TYR GLU SEQRES 17 L 235 LYS HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY SEQRES 18 L 235 LEU SER SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU SEQRES 19 L 235 CYS HET NAG q 1 14 HET NAG q 2 14 HET BMA q 3 11 HET NAG u 1 14 HET NAG u 2 14 HET NAG D 1 14 HET NAG D 2 14 HET NAG E 1 14 HET NAG E 2 14 HET NAG J 1 14 HET NAG J 2 14 HET NAG K 1 14 HET NAG K 2 14 HET NAG M 1 14 HET NAG M 2 14 HET NAG N 1 14 HET NAG N 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 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 NAG e 1 14 HET NAG e 2 14 HET BMA e 3 11 HET MAN e 4 11 HET MAN e 5 11 HET NAG j 1 14 HET NAG j 2 14 HET BMA j 3 11 HET MAN j 4 11 HET NAG k 1 14 HET NAG k 2 14 HET BMA k 3 11 HET MAN k 4 11 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 HET NAG C 606 14 HET NAG C 607 14 HET NAG C 608 14 HET NAG C 609 14 HET NAG F 701 14 HET NAG G 601 14 HET NAG G 602 14 HET NAG G 603 14 HET NAG G 604 14 HET NAG G 605 14 HET NAG G 606 14 HET NAG G 607 14 HET NAG G 608 14 HET NAG G 609 14 HET NAG G 610 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 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 BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 9 NAG 67(C8 H15 N O6) FORMUL 9 BMA 4(C6 H12 O6) FORMUL 26 MAN 4(C6 H12 O6) HELIX 1 AA1 GLY A 531 MET A 535 5 5 HELIX 2 AA2 THR A 536 ASN A 543 1 8 HELIX 3 AA3 GLN A 575 ILE A 595 1 21 HELIX 4 AA4 ASN A 618 ILE A 622 5 5 HELIX 5 AA5 THR A 627 SER A 636 1 10 HELIX 6 AA6 TYR A 638 ASP A 659 1 22 HELIX 7 AA7 GLY B 531 MET B 535 5 5 HELIX 8 AA8 THR B 536 ARG B 542 1 7 HELIX 9 AA9 GLY B 572 TRP B 596 1 25 HELIX 10 AB1 THR B 627 ILE B 635 1 9 HELIX 11 AB2 TYR B 638 ASN B 656 1 19 HELIX 12 AB3 ASN C 98 SER C 115 1 18 HELIX 13 AB4 LEU C 122 CYS C 126 5 5 HELIX 14 AB5 LYS C 335 GLY C 354 1 20 HELIX 15 AB6 ASP C 368 THR C 373 1 6 HELIX 16 AB7 MET C 475 SER C 481 1 7 HELIX 17 AB8 THR F 529 SER F 534 1 6 HELIX 18 AB9 THR F 569 TRP F 596 1 28 HELIX 19 AC1 LEU F 619 ASP F 624 1 6 HELIX 20 AC2 THR F 627 ILE F 635 1 9 HELIX 21 AC3 TYR F 638 LEU F 663 1 26 HELIX 22 AC4 ASN G 98 SER G 115 1 18 HELIX 23 AC5 LEU G 122 CYS G 126 5 5 HELIX 24 AC6 THR G 139 ARG G 151 5 5 HELIX 25 AC7 LYS G 335 GLY G 354 1 20 HELIX 26 AC8 ASP G 368 THR G 373 1 6 HELIX 27 AC9 MET G 475 SER G 481 1 7 HELIX 28 AD1 ALA I 70 CYS I 74 5 5 HELIX 29 AD2 ASN I 98 SER I 115 1 18 HELIX 30 AD3 THR I 123 CYS I 126 5 4 HELIX 31 AD4 LYS I 335 ARG I 350 1 16 HELIX 32 AD5 LYS I 351 PHE I 353 5 3 HELIX 33 AD6 ASP I 368 THR I 373 1 6 HELIX 34 AD7 MET I 475 ARG I 480 1 6 HELIX 35 AD8 ASN H 61 ARG H 64 5 4 HELIX 36 AD9 ARG H 83 THR H 87 5 5 HELIX 37 AE1 SER H 127 LYS H 129 5 3 HELIX 38 AE2 SER H 156 ALA H 158 5 3 HELIX 39 AE3 SER H 187 LEU H 189 5 3 HELIX 40 AE4 LYS H 201 ASN H 204 5 4 HELIX 41 AE5 GLN L 79 SER L 83 5 5 HELIX 42 AE6 SER L 121 LYS L 126 1 6 HELIX 43 AE7 LYS L 183 LYS L 188 1 6 SHEET 1 AA1 3 ILE A 603 PRO A 609 0 SHEET 2 AA1 3 TRP C 35 TYR C 40 -1 O VAL C 38 N CYS A 604 SHEET 3 AA1 3 LEU C 494 THR C 499 -1 O GLY C 495 N TYR C 39 SHEET 1 AA2 3 ILE B 603 PRO B 609 0 SHEET 2 AA2 3 TRP G 35 TYR G 40 -1 O VAL G 38 N CYS B 604 SHEET 3 AA2 3 LEU G 494 THR G 499 -1 O GLY G 495 N TYR G 39 SHEET 1 AA3 5 TRP C 45 ASP C 47 0 SHEET 2 AA3 5 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AA3 5 PHE C 223 CYS C 228 -1 N ALA C 224 O VAL C 489 SHEET 4 AA3 5 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 AA3 5 ILE C 84 LEU C 86 -1 N LEU C 86 O VAL C 242 SHEET 1 AA4 3 VAL C 75 PRO C 76 0 SHEET 2 AA4 3 PHE C 53 SER C 56 1 N SER C 56 O VAL C 75 SHEET 3 AA4 3 HIS C 216 CYS C 218 -1 O CYS C 218 N PHE C 53 SHEET 1 AA5 2 GLU C 91 ASN C 94 0 SHEET 2 AA5 2 THR C 236 CYS C 239 -1 O GLY C 237 N PHE C 93 SHEET 1 AA6 5 LYS C 169 TYR C 177 0 SHEET 2 AA6 5 LEU C 154 THR C 162 -1 N CYS C 157 O SER C 174 SHEET 3 AA6 5 LEU C 129 ASN C 133 -1 N THR C 132 O ASN C 156 SHEET 4 AA6 5 LYS C 189 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AA6 5 VAL C 181 ILE C 184 -1 N ILE C 184 O GLU C 190 SHEET 1 AA7 3 ALA C 200 GLN C 203 0 SHEET 2 AA7 3 GLN C 432 TYR C 435 1 O TYR C 435 N THR C 202 SHEET 3 AA7 3 ILE C 423 ILE C 424 -1 N ILE C 424 O MET C 434 SHEET 1 AA8 7 LEU C 259 LEU C 261 0 SHEET 2 AA8 7 ILE C 443 ARG C 456 -1 O THR C 450 N LEU C 260 SHEET 3 AA8 7 ILE C 284 ARG C 298 -1 N VAL C 292 O ILE C 449 SHEET 4 AA8 7 HIS C 330 SER C 334 -1 O HIS C 330 N THR C 297 SHEET 5 AA8 7 SER C 413 LYS C 421 -1 O LEU C 416 N CYS C 331 SHEET 6 AA8 7 GLU C 381 CYS C 385 -1 N TYR C 384 O ARG C 419 SHEET 7 AA8 7 HIS C 374 CYS C 378 -1 N HIS C 374 O CYS C 385 SHEET 1 AA9 6 MET C 271 ARG C 273 0 SHEET 2 AA9 6 ILE C 284 ARG C 298 -1 O LEU C 285 N ARG C 273 SHEET 3 AA9 6 ILE C 443 ARG C 456 -1 O ILE C 449 N VAL C 292 SHEET 4 AA9 6 THR C 465 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 5 AA9 6 ILE C 358 PHE C 361 1 N ARG C 360 O GLU C 466 SHEET 6 AA9 6 SER C 393 TRP C 395 -1 O SER C 393 N PHE C 361 SHEET 1 AB1 2 ARG C 304 GLY C 312 0 SHEET 2 AB1 2 GLN C 315 THR C 320 -1 O ALA C 319 N LYS C 305 SHEET 1 AB2 3 ILE F 603 PRO F 609 0 SHEET 2 AB2 3 TRP I 35 TYR I 40 -1 O VAL I 38 N CYS F 604 SHEET 3 AB2 3 LEU I 494 THR I 499 -1 O GLY I 495 N TYR I 39 SHEET 1 AB3 5 TRP G 45 ASP G 47 0 SHEET 2 AB3 5 TYR G 486 ILE G 491 -1 O LYS G 490 N LYS G 46 SHEET 3 AB3 5 PHE G 223 CYS G 228 -1 N ALA G 224 O VAL G 489 SHEET 4 AB3 5 VAL G 242 VAL G 245 -1 O SER G 243 N LYS G 227 SHEET 5 AB3 5 GLU G 83 LEU G 86 -1 N LEU G 86 O VAL G 242 SHEET 1 AB4 2 GLU G 91 ASN G 94 0 SHEET 2 AB4 2 THR G 236 CYS G 239 -1 O GLY G 237 N PHE G 93 SHEET 1 AB5 5 LYS G 169 TYR G 177 0 SHEET 2 AB5 5 LEU G 154 THR G 162 -1 N CYS G 157 O SER G 174 SHEET 3 AB5 5 LEU G 129 ASN G 133 -1 N THR G 132 O ASN G 156 SHEET 4 AB5 5 GLU G 190 LEU G 193 -1 O TYR G 191 N LEU G 129 SHEET 5 AB5 5 VAL G 181 ILE G 184 -1 N VAL G 182 O ARG G 192 SHEET 1 AB6 3 ALA G 200 GLN G 203 0 SHEET 2 AB6 3 GLN G 432 TYR G 435 1 O TYR G 435 N THR G 202 SHEET 3 AB6 3 ILE G 423 ILE G 424 -1 N ILE G 424 O MET G 434 SHEET 1 AB7 7 LEU G 259 LEU G 261 0 SHEET 2 AB7 7 GLY G 441 ARG G 456 -1 O THR G 450 N LEU G 260 SHEET 3 AB7 7 ILE G 284 ASN G 302 -1 N VAL G 292 O ILE G 449 SHEET 4 AB7 7 HIS G 330 SER G 334 -1 O HIS G 330 N THR G 297 SHEET 5 AB7 7 SER G 413 LYS G 421 -1 O ILE G 414 N VAL G 333 SHEET 6 AB7 7 GLU G 381 CYS G 385 -1 N TYR G 384 O ARG G 419 SHEET 7 AB7 7 HIS G 374 CYS G 378 -1 N HIS G 374 O CYS G 385 SHEET 1 AB8 6 MET G 271 ARG G 273 0 SHEET 2 AB8 6 ILE G 284 ASN G 302 -1 O GLN G 287 N MET G 271 SHEET 3 AB8 6 GLY G 441 ARG G 456 -1 O ILE G 449 N VAL G 292 SHEET 4 AB8 6 THR G 465 PRO G 470 -1 O ARG G 469 N THR G 455 SHEET 5 AB8 6 ILE G 358 PHE G 361 1 N ILE G 358 O GLU G 466 SHEET 6 AB8 6 SER G 393 TRP G 395 -1 O SER G 393 N PHE G 361 SHEET 1 AB9 2 ARG G 304 GLY G 312 0 SHEET 2 AB9 2 GLN G 315 THR G 320 -1 O ALA G 319 N LYS G 305 SHEET 1 AC1 5 TRP I 45 ASP I 47 0 SHEET 2 AC1 5 TYR I 486 ILE I 491 -1 O LYS I 490 N LYS I 46 SHEET 3 AC1 5 PHE I 223 CYS I 228 -1 N ALA I 224 O VAL I 489 SHEET 4 AC1 5 VAL I 242 VAL I 245 -1 O SER I 243 N LYS I 227 SHEET 5 AC1 5 ILE I 84 LEU I 86 -1 N LEU I 86 O VAL I 242 SHEET 1 AC2 3 VAL I 75 PRO I 76 0 SHEET 2 AC2 3 PHE I 53 SER I 56 1 N SER I 56 O VAL I 75 SHEET 3 AC2 3 HIS I 216 CYS I 218 -1 O CYS I 218 N PHE I 53 SHEET 1 AC3 2 GLU I 91 ASN I 94 0 SHEET 2 AC3 2 THR I 236 CYS I 239 -1 O GLY I 237 N PHE I 93 SHEET 1 AC4 4 VAL I 120 LYS I 121 0 SHEET 2 AC4 4 ALA I 200 GLN I 203 -1 O GLN I 203 N VAL I 120 SHEET 3 AC4 4 GLN I 432 TYR I 435 1 O TYR I 435 N THR I 202 SHEET 4 AC4 4 ILE I 423 ILE I 424 -1 N ILE I 424 O MET I 434 SHEET 1 AC5 5 LYS I 169 TYR I 177 0 SHEET 2 AC5 5 LEU I 154 THR I 162 -1 N CYS I 157 O SER I 174 SHEET 3 AC5 5 LEU I 129 ASN I 133 -1 N GLN I 130 O SER I 158 SHEET 4 AC5 5 LYS I 189 LEU I 193 -1 O TYR I 191 N LEU I 129 SHEET 5 AC5 5 VAL I 181 ILE I 184 -1 N ILE I 184 O GLU I 190 SHEET 1 AC6 7 LEU I 259 LEU I 261 0 SHEET 2 AC6 7 ILE I 443 ARG I 456 -1 O THR I 450 N LEU I 260 SHEET 3 AC6 7 ILE I 284 ARG I 298 -1 N VAL I 292 O ILE I 449 SHEET 4 AC6 7 ALA I 329 SER I 334 -1 O HIS I 330 N THR I 297 SHEET 5 AC6 7 SER I 413 ILE I 420 -1 O LEU I 416 N CYS I 331 SHEET 6 AC6 7 GLU I 381 CYS I 385 -1 N TYR I 384 O ARG I 419 SHEET 7 AC6 7 HIS I 374 CYS I 378 -1 N HIS I 374 O CYS I 385 SHEET 1 AC7 6 MET I 271 ARG I 273 0 SHEET 2 AC7 6 ILE I 284 ARG I 298 -1 O LEU I 285 N ARG I 273 SHEET 3 AC7 6 ILE I 443 ARG I 456 -1 O ILE I 449 N VAL I 292 SHEET 4 AC7 6 THR I 465 PRO I 470 -1 O ARG I 469 N THR I 455 SHEET 5 AC7 6 ILE I 358 PHE I 361 1 N ARG I 360 O GLU I 466 SHEET 6 AC7 6 SER I 393 TRP I 395 -1 O SER I 393 N PHE I 361 SHEET 1 AC8 2 ARG I 304 GLY I 312 0 SHEET 2 AC8 2 GLN I 315 THR I 320 -1 O ALA I 319 N LYS I 305 SHEET 1 AC9 4 GLN H 3 GLN H 6 0 SHEET 2 AC9 4 SER H 17 TYR H 25 -1 O GLN H 23 N VAL H 5 SHEET 3 AC9 4 THR H 77 ARG H 82A-1 O LEU H 82 N VAL H 18 SHEET 4 AC9 4 LEU H 67 ASP H 72 -1 N THR H 68 O GLU H 81 SHEET 1 AD1 6 GLU H 10 LYS H 12 0 SHEET 2 AD1 6 SER H 107 VAL H 111 1 O THR H 108 N GLU H 10 SHEET 3 AD1 6 ALA H 88 GLY H 95 -1 N ALA H 88 O VAL H 109 SHEET 4 AD1 6 SER H 33 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AD1 6 LEU H 45 PHE H 51 -1 O PHE H 51 N PHE H 34 SHEET 6 AD1 6 ASN H 58 TYR H 59 -1 O ASN H 58 N GLY H 50 SHEET 1 AD2 4 GLU H 10 LYS H 12 0 SHEET 2 AD2 4 SER H 107 VAL H 111 1 O THR H 108 N GLU H 10 SHEET 3 AD2 4 ALA H 88 GLY H 95 -1 N ALA H 88 O VAL H 109 SHEET 4 AD2 4 VAL H 102 TRP H 103 -1 O VAL H 102 N GLY H 94 SHEET 1 AD3 2 ALA H 97 SER H 99 0 SHEET 2 AD3 2 PHE H 100E TYR H 100G-1 O HIS H 100F N TYR H 98 SHEET 1 AD4 4 SER H 120 LEU H 124 0 SHEET 2 AD4 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AD4 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AD4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AD5 4 THR H 131 SER H 132 0 SHEET 2 AD5 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 SHEET 3 AD5 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AD5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AD6 3 THR H 151 TRP H 154 0 SHEET 2 AD6 3 TYR H 194 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AD6 3 THR H 205 VAL H 211 -1 O VAL H 207 N VAL H 198 SHEET 1 AD7 4 LEU L 4 SER L 7 0 SHEET 2 AD7 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AD7 4 HIS L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AD7 4 PHE L 62 SER L 67 -1 N ARG L 63 O THR L 74 SHEET 1 AD8 6 THR L 10 ALA L 13 0 SHEET 2 AD8 6 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AD8 6 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AD8 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AD8 6 LYS L 45 THR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AD8 6 SER L 53 LEU L 54 -1 O SER L 53 N THR L 49 SHEET 1 AD9 4 THR L 10 ALA L 13 0 SHEET 2 AD9 4 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AD9 4 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AD9 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AE1 4 SER L 114 PHE L 118 0 SHEET 2 AE1 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AE1 4 TYR L 173 SER L 182 -1 O LEU L 181 N ALA L 130 SHEET 4 AE1 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AE2 4 ALA L 153 LEU L 154 0 SHEET 2 AE2 4 ALA L 144 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AE2 4 VAL L 191 HIS L 198 -1 O ALA L 193 N LYS L 149 SHEET 4 AE2 4 VAL L 205 ASN L 210 -1 O PHE L 209 N TYR L 192 SSBOND 1 CYS A 598 CYS A 604 1555 1555 2.03 SSBOND 2 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 3 CYS C 54 CYS C 74 1555 1555 2.03 SSBOND 4 CYS C 119 CYS C 205 1555 1555 2.04 SSBOND 5 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 6 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 7 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 8 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 9 CYS C 378 CYS C 445 1555 1555 2.04 SSBOND 10 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 11 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 12 CYS G 54 CYS G 74 1555 1555 2.03 SSBOND 13 CYS G 119 CYS G 205 1555 1555 2.03 SSBOND 14 CYS G 126 CYS G 196 1555 1555 2.03 SSBOND 15 CYS G 131 CYS G 157 1555 1555 2.03 SSBOND 16 CYS G 228 CYS G 239 1555 1555 2.03 SSBOND 17 CYS G 296 CYS G 331 1555 1555 2.03 SSBOND 18 CYS G 378 CYS G 445 1555 1555 2.03 SSBOND 19 CYS G 385 CYS G 418 1555 1555 2.03 SSBOND 20 CYS I 54 CYS I 74 1555 1555 2.03 SSBOND 21 CYS I 119 CYS I 205 1555 1555 2.04 SSBOND 22 CYS I 126 CYS I 196 1555 1555 2.03 SSBOND 23 CYS I 131 CYS I 157 1555 1555 2.03 SSBOND 24 CYS I 228 CYS I 239 1555 1555 2.03 SSBOND 25 CYS I 296 CYS I 331 1555 1555 2.03 SSBOND 26 CYS I 378 CYS I 445 1555 1555 2.03 SSBOND 27 CYS I 385 CYS I 418 1555 1555 2.03 SSBOND 28 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 29 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 30 CYS H 216 CYS L 214 1555 1555 2.03 SSBOND 31 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 32 CYS L 134 CYS L 194 1555 1555 2.03 LINK ND2 ASN C 88 C1 NAG C 601 1555 1555 1.44 LINK ND2 ASN C 156 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN C 160 C1 NAG C 609 1555 1555 1.44 LINK ND2 ASN C 197 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN C 234 C1 NAG C 602 1555 1555 1.45 LINK ND2 ASN C 262 C1 NAG j 1 1555 1555 1.44 LINK ND2 ASN C 295 C1 NAG C 604 1555 1555 1.44 LINK ND2 ASN C 301 C1 NAG C 605 1555 1555 1.44 LINK ND2 ASN C 332 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN C 339 C1 NAG C 608 1555 1555 1.44 LINK ND2 ASN C 355 C1 NAG C 603 1555 1555 1.46 LINK ND2 ASN C 363 C1 NAG C 607 1555 1555 1.44 LINK ND2 ASN C 386 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN C 392 C1 NAG C 606 1555 1555 1.44 LINK ND2 ASN C 448 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN F 637 C1 NAG F 701 1555 1555 1.44 LINK ND2 ASN G 133 C1 NAG G 602 1555 1555 1.45 LINK ND2 ASN G 156 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN G 160 C1 NAG G 601 1555 1555 1.44 LINK ND2 ASN G 197 C1 NAG G 609 1555 1555 1.44 LINK ND2 ASN G 234 C1 NAG G 610 1555 1555 1.44 LINK ND2 ASN G 262 C1 NAG k 1 1555 1555 1.44 LINK ND2 ASN G 276 C1 NAG G 608 1555 1555 1.44 LINK ND2 ASN G 295 C1 NAG G 605 1555 1555 1.44 LINK ND2 ASN G 301 C1 NAG G 603 1555 1555 1.44 LINK ND2 ASN G 332 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN G 363 C1 NAG G 607 1555 1555 1.44 LINK ND2 ASN G 386 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN G 392 C1 NAG G 606 1555 1555 1.44 LINK ND2 ASN G 448 C1 NAG G 604 1555 1555 1.44 LINK ND2 ASN I 88 C1 NAG q 1 1555 1555 1.44 LINK ND2 ASN I 156 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN I 160 C1 NAG I 607 1555 1555 1.44 LINK ND2 ASN I 197 C1 NAG I 606 1555 1555 1.44 LINK ND2 ASN I 234 C1 NAG I 601 1555 1555 1.44 LINK ND2 ASN I 262 C1 NAG e 1 1555 1555 1.44 LINK ND2 ASN I 276 C1 NAG u 1 1555 1555 1.44 LINK ND2 ASN I 295 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN I 301 C1 NAG I 603 1555 1555 1.44 LINK ND2 ASN I 332 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN I 339 C1 NAG I 605 1555 1555 1.44 LINK ND2 ASN I 355 C1 NAG I 604 1555 1555 1.45 LINK ND2 ASN I 363 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN I 386 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN I 392 C1 NAG I 602 1555 1555 1.44 LINK ND2 ASN I 448 C1 NAG M 1 1555 1555 1.44 LINK O4 NAG q 1 C1 NAG q 2 1555 1555 1.44 LINK O4 NAG q 2 C1 BMA q 3 1555 1555 1.45 LINK O4 NAG u 1 C1 NAG u 2 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 J 1 C1 NAG J 2 1555 1555 1.46 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 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 S 1 C1 NAG S 2 1555 1555 1.44 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 1.45 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.44 LINK O4 NAG e 2 C1 BMA e 3 1555 1555 1.45 LINK O3 BMA e 3 C1 MAN e 4 1555 1555 1.45 LINK O2 MAN e 4 C1 MAN e 5 1555 1555 1.45 LINK O4 NAG j 1 C1 NAG j 2 1555 1555 1.44 LINK O4 NAG j 2 C1 BMA j 3 1555 1555 1.45 LINK O3 BMA j 3 C1 MAN j 4 1555 1555 1.45 LINK O4 NAG k 1 C1 NAG k 2 1555 1555 1.44 LINK O4 NAG k 2 C1 BMA k 3 1555 1555 1.45 LINK O3 BMA k 3 C1 MAN k 4 1555 1555 1.45 CISPEP 1 PHE H 146 PRO H 147 0 -1.33 CISPEP 2 GLU H 148 PRO H 149 0 -1.41 CISPEP 3 SER L 7 PRO L 8 0 -5.06 CISPEP 4 PHE L 94 PRO L 95 0 -3.59 CISPEP 5 TYR L 140 PRO L 141 0 4.86 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