HEADER VIRAL PROTEIN/IMMUNE SYSTEM 07-JUN-21 7N65 TITLE COMPLEX STRUCTURE OF HIV SUPERINFECTION FAB QA013.2 AND TITLE 2 BG505.SOSIP.664 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 3 CHAIN: A, E, I; COMPND 4 SYNONYM: ENV POLYPROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 9 CHAIN: B, F, J; COMPND 10 SYNONYM: ENV POLYPROTEIN; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: FAB QA013.2 HEAVY CHAIN, VARIABLE REGION; COMPND 14 CHAIN: C, G, K; COMPND 15 ENGINEERED: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: FAB QA013.2 LIGHT CHAIN, , VARIABLE REGION; COMPND 18 CHAIN: D, H, L; COMPND 19 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 STRAIN: BG505; SOURCE 5 GENE: ENV; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 12 ORGANISM_TAXID: 11676; SOURCE 13 STRAIN: BG505; SOURCE 14 GENE: ENV; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: EXPI 293F; SOURCE 19 MOL_ID: 3; SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 21 ORGANISM_COMMON: HUMAN; SOURCE 22 ORGANISM_TAXID: 9606; SOURCE 23 CELL_LINE: PERIPHERAL BLOOD MONONUCLEAR CELL; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 27 EXPRESSION_SYSTEM_CELL_LINE: HEK 293F; SOURCE 28 MOL_ID: 4; SOURCE 29 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 30 ORGANISM_COMMON: HUMAN; SOURCE 31 ORGANISM_TAXID: 9606; SOURCE 32 CELL_LINE: PERIPHERAL BLOOD MONONUCLEAR CELL; SOURCE 33 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 34 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 35 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 36 EXPRESSION_SYSTEM_CELL_LINE: HEK 293F KEYWDS HIV-1 ENVELOPE, SUPERINFECTION ANTIBODY QA013.2, VIRAL PROTEIN, VIRAL KEYWDS 2 PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR V.MANGALA PRASAD,M.M.SHIPLEY,J.M.OVERBAUGH,K.K.LEE JRNL AUTH M.M.SHIPLEY,V.MANGALA PRASAD,L.E.DOEPKER,A.S.DINGENS, JRNL AUTH 2 D.K.RALPH,E.HARKINS,A.DHAR,D.ARENZ,V.CHOHAN,H.WEIGHT, JRNL AUTH 3 K.MANDALIYA,J.D.BLOOM,F.MATSEN IV,K.K.LEE,J.M.OVERBAUGH JRNL TITL FUNCTIONAL DEVELOPMENT OF A V3/GLYCAN-SPECIFIC BROADLY JRNL TITL 2 NEUTRALIZING ANTIBODY ISOLATED FROM A CASE OF HIV JRNL TITL 3 SUPERINFECTION. JRNL REF ELIFE V. 10 2021 JRNL REFN ESSN 2050-084X JRNL PMID 34263727 JRNL DOI 10.7554/ELIFE.68110 REMARK 2 REMARK 2 RESOLUTION. 4.15 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CTFFIND, UCSF CHIMERA, RELION, RELION, REMARK 3 RELION, PHENIX REMARK 3 RECONSTRUCTION SCHEMA : FOURIER SPACE REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 5ACO 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 : RIGID BODY FITTING IN CHIMERA, FOLLOWED BY REMARK 3 REAL SPACE REFINEMENT IN PHENIX USING REFERENCE MODEL RESTRAINTS 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) : 4.150 REMARK 3 NUMBER OF PARTICLES : 113470 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 7N65 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000255470. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : COMPLEX OF HIV-1 ENVELOPE REMARK 245 PROTEIN WITH SUPER-INFECTION REMARK 245 FAB QA013.2 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.05 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : 3UL SAMPLE VOLUME, BLOTTED FOR REMARK 245 3-4 SECONDS REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 6475 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1700.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 3500.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 44.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 110000 REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : PRELIMINARY GRID SCREENING REMARK 245 WAS PERFORMED MANUALLY 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: DODECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J, REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, a, b, c, REMARK 350 AND CHAINS: d, e, f, g, h, i, j, k, l, REMARK 350 AND CHAINS: m, n, o, p, q, r, s, t, u, v, REMARK 350 AND CHAINS: w, x, y, z, 0, 1, 2, 3, 4, REMARK 350 AND CHAINS: 5, 6, 7, 8, 9, AA REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A -4 REMARK 465 ASP A -3 REMARK 465 ALA A -2 REMARK 465 MET A -1 REMARK 465 LYS A 0 REMARK 465 ARG A 1 REMARK 465 GLY A 2 REMARK 465 LEU A 3 REMARK 465 CYS A 4 REMARK 465 CYS A 5 REMARK 465 VAL A 6 REMARK 465 LEU A 7 REMARK 465 LEU A 8 REMARK 465 LEU A 9 REMARK 465 CYS A 10 REMARK 465 GLY A 11 REMARK 465 ALA A 12 REMARK 465 VAL A 13 REMARK 465 PHE A 14 REMARK 465 VAL A 15 REMARK 465 SER A 16 REMARK 465 PRO A 17 REMARK 465 SER A 18 REMARK 465 GLN A 19 REMARK 465 GLU A 20 REMARK 465 ILE A 21 REMARK 465 HIS A 22 REMARK 465 ALA A 23 REMARK 465 ARG A 24 REMARK 465 PHE A 25 REMARK 465 ARG A 26 REMARK 465 ARG A 27 REMARK 465 GLY A 28 REMARK 465 ALA A 29 REMARK 465 ARG A 30 REMARK 465 ALA A 31 REMARK 465 GLU A 32 REMARK 465 GLU A 185A REMARK 465 ASN A 185B REMARK 465 GLN A 185C REMARK 465 GLY A 185D REMARK 465 ASN A 185E REMARK 465 ARG A 185F REMARK 465 SER A 185G REMARK 465 ASN A 185H REMARK 465 ASN A 185I REMARK 465 SER A 185J REMARK 465 THR A 400 REMARK 465 SER A 401 REMARK 465 VAL A 402 REMARK 465 GLN A 403 REMARK 465 GLY A 404 REMARK 465 SER A 405 REMARK 465 ASN A 406 REMARK 465 SER A 407 REMARK 465 THR A 408 REMARK 465 GLY A 409 REMARK 465 SER A 410 REMARK 465 VAL B 504 REMARK 465 GLY B 505 REMARK 465 ARG B 506 REMARK 465 ARG B 507 REMARK 465 ARG B 508 REMARK 465 ARG B 509 REMARK 465 ARG B 510 REMARK 465 ARG B 511 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 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 GLN D 1 REMARK 465 MET E -4 REMARK 465 ASP E -3 REMARK 465 ALA E -2 REMARK 465 MET E -1 REMARK 465 LYS E 0 REMARK 465 ARG E 1 REMARK 465 GLY E 2 REMARK 465 LEU E 3 REMARK 465 CYS E 4 REMARK 465 CYS E 5 REMARK 465 VAL E 6 REMARK 465 LEU E 7 REMARK 465 LEU E 8 REMARK 465 LEU E 9 REMARK 465 CYS E 10 REMARK 465 GLY E 11 REMARK 465 ALA E 12 REMARK 465 VAL E 13 REMARK 465 PHE E 14 REMARK 465 VAL E 15 REMARK 465 SER E 16 REMARK 465 PRO E 17 REMARK 465 SER E 18 REMARK 465 GLN E 19 REMARK 465 GLU E 20 REMARK 465 ILE E 21 REMARK 465 HIS E 22 REMARK 465 ALA E 23 REMARK 465 ARG E 24 REMARK 465 PHE E 25 REMARK 465 ARG E 26 REMARK 465 ARG E 27 REMARK 465 GLY E 28 REMARK 465 ALA E 29 REMARK 465 ARG E 30 REMARK 465 ALA E 31 REMARK 465 GLU E 32 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 SER E 185J 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 VAL F 504 REMARK 465 GLY F 505 REMARK 465 ARG F 506 REMARK 465 ARG F 507 REMARK 465 ARG F 508 REMARK 465 ARG F 509 REMARK 465 ARG F 510 REMARK 465 ARG F 511 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 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 GLN H 1 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 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 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 J 504 REMARK 465 GLY J 505 REMARK 465 ARG J 506 REMARK 465 ARG J 507 REMARK 465 ARG J 508 REMARK 465 ARG J 509 REMARK 465 ARG J 510 REMARK 465 ARG J 511 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 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 ALA J 561 REMARK 465 GLN J 562 REMARK 465 GLN J 563 REMARK 465 HIS J 564 REMARK 465 LEU J 565 REMARK 465 GLN 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 GLU A 62 CG CD OE1 OE2 REMARK 470 THR A 63 OG1 CG2 REMARK 470 GLU A 64 CG CD OE1 OE2 REMARK 470 LYS A 65 CG CD CE NZ REMARK 470 HIS A 66 CG ND1 CD2 CE1 NE2 REMARK 470 ASN A 67 CG OD1 ND2 REMARK 470 SER A 460 OG REMARK 470 GLN B 551 CG CD OE1 NE2 REMARK 470 GLU E 62 CG CD OE1 OE2 REMARK 470 THR E 63 OG1 CG2 REMARK 470 GLU E 64 CG CD OE1 OE2 REMARK 470 LYS E 65 CG CD CE NZ REMARK 470 HIS E 66 CG ND1 CD2 CE1 NE2 REMARK 470 ASN E 67 CG OD1 ND2 REMARK 470 SER E 460 OG REMARK 470 GLN F 551 CG CD OE1 NE2 REMARK 470 GLU I 62 CG CD OE1 OE2 REMARK 470 THR I 63 OG1 CG2 REMARK 470 GLU I 64 CG CD OE1 OE2 REMARK 470 LYS I 65 CG CD CE NZ REMARK 470 HIS I 66 CG ND1 CD2 CE1 NE2 REMARK 470 ASN I 67 CG OD1 ND2 REMARK 470 SER I 460 OG REMARK 470 GLN J 551 CG CD OE1 NE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 N ARG C 30 O6 MAN V 7 1.20 REMARK 500 N GLY C 28 O2 BMA V 3 1.20 REMARK 500 NE ARG C 31 O6 NAG V 2 1.25 REMARK 500 CZ3 TRP G 33 O3 MAN n 5 1.27 REMARK 500 CB PHE C 29 O4 MAN V 7 1.27 REMARK 500 NE ARG G 31 O6 NAG m 2 1.32 REMARK 500 NE ARG K 31 O6 NAG 3 2 1.33 REMARK 500 N ARG G 30 O6 MAN m 7 1.33 REMARK 500 N GLY G 28 O2 BMA m 3 1.34 REMARK 500 N GLY K 28 O2 BMA 3 3 1.36 REMARK 500 CB PHE G 29 O4 MAN m 7 1.38 REMARK 500 N ARG K 30 O6 MAN 3 7 1.38 REMARK 500 CZ3 TRP K 33 O3 MAN 4 5 1.40 REMARK 500 NZ LYS C 59 C6 MAN C 201 1.43 REMARK 500 NZ LYS G 59 C6 MAN G 201 1.43 REMARK 500 NZ LYS K 59 C6 MAN K 201 1.43 REMARK 500 CZ3 TRP C 33 O3 MAN W 5 1.46 REMARK 500 CB PHE K 29 O4 MAN 3 7 1.49 REMARK 500 CA GLY C 28 O2 BMA V 3 1.54 REMARK 500 C LEU C 27 O2 BMA V 3 1.62 REMARK 500 CA GLY G 28 O2 BMA m 3 1.65 REMARK 500 C LEU G 27 O2 BMA m 3 1.68 REMARK 500 CZ3 TRP G 33 C3 MAN n 5 1.69 REMARK 500 CA GLY K 28 O2 BMA 3 3 1.72 REMARK 500 C LEU K 27 O2 BMA 3 3 1.75 REMARK 500 CZ3 TRP K 33 C3 MAN 4 5 1.82 REMARK 500 CE3 TRP G 33 O3 MAN n 5 1.87 REMARK 500 CE3 TRP K 33 O3 MAN 4 5 1.88 REMARK 500 CZ3 TRP C 33 C3 MAN W 5 1.88 REMARK 500 OE2 GLU B 647 NH1 ARG F 542 1.94 REMARK 500 NZ LYS K 59 O6 MAN K 201 1.94 REMARK 500 NZ LYS G 59 O6 MAN G 201 1.95 REMARK 500 CD ARG G 31 O6 NAG m 2 1.97 REMARK 500 CD ARG C 31 O6 NAG V 2 1.97 REMARK 500 O LEU C 27 O2 BMA V 3 2.00 REMARK 500 O LEU G 27 O2 BMA m 3 2.00 REMARK 500 CE3 TRP C 33 O3 MAN W 5 2.02 REMARK 500 NZ LYS C 59 O6 MAN C 201 2.06 REMARK 500 CD ARG K 31 O6 NAG 3 2 2.08 REMARK 500 OG SER I 274 O ASN I 283 2.09 REMARK 500 OG SER A 274 O ASN A 283 2.09 REMARK 500 OG SER E 274 O ASN E 283 2.09 REMARK 500 CA PHE C 29 O4 MAN V 7 2.09 REMARK 500 N GLU E 64 O VAL E 208 2.11 REMARK 500 N GLU I 64 O VAL I 208 2.11 REMARK 500 N GLU A 64 O VAL A 208 2.11 REMARK 500 O LEU A 175 OG1 THR A 320 2.11 REMARK 500 O LEU I 175 OG1 THR I 320 2.11 REMARK 500 O LEU E 175 OG1 THR E 320 2.11 REMARK 500 CE LYS G 59 C6 MAN G 201 2.12 REMARK 500 REMARK 500 THIS ENTRY HAS 99 CLOSE CONTACTS REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 CYS A 218 C ALA A 219 N -0.146 REMARK 500 CYS E 218 C ALA E 219 N -0.145 REMARK 500 CYS I 218 C ALA I 219 N -0.146 REMARK 500 REMARK 500 REMARK: NULL 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 A 247 CA - CB - SG ANGL. DEV. = 11.7 DEGREES REMARK 500 CYS A 445 CA - CB - SG ANGL. DEV. = 12.0 DEGREES REMARK 500 TYR D 93 CG - CD2 - CE2 ANGL. DEV. = -4.8 DEGREES REMARK 500 CYS E 247 CA - CB - SG ANGL. DEV. = 11.7 DEGREES REMARK 500 CYS E 445 CA - CB - SG ANGL. DEV. = 11.9 DEGREES REMARK 500 TYR H 93 CG - CD2 - CE2 ANGL. DEV. = -4.8 DEGREES REMARK 500 CYS I 247 CA - CB - SG ANGL. DEV. = 11.6 DEGREES REMARK 500 CYS I 445 CA - CB - SG ANGL. DEV. = 11.9 DEGREES REMARK 500 TYR L 93 CG - CD2 - CE2 ANGL. DEV. = -4.8 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 LYS A 59 43.54 -142.43 REMARK 500 THR A 63 42.89 -143.78 REMARK 500 LYS A 65 -17.94 83.87 REMARK 500 HIS A 66 -34.08 -155.34 REMARK 500 ASN A 67 -151.30 -177.15 REMARK 500 VAL A 68 -72.82 -80.15 REMARK 500 TRP A 69 -62.43 -122.21 REMARK 500 ALA A 70 -20.61 -143.45 REMARK 500 PRO A 81 83.90 -67.17 REMARK 500 ASN A 88 -1.60 73.56 REMARK 500 MET A 95 -7.90 -59.98 REMARK 500 LEU A 122 40.51 -89.52 REMARK 500 PRO A 124 2.41 -65.47 REMARK 500 CYS A 126 75.51 -67.74 REMARK 500 THR A 135 92.02 -67.79 REMARK 500 ASP A 140 113.25 -162.34 REMARK 500 THR A 163 -163.72 -128.99 REMARK 500 ARG A 166 68.75 -69.07 REMARK 500 ASP A 167 -159.52 -156.98 REMARK 500 LYS A 168 127.80 -35.49 REMARK 500 ARG A 178 -6.21 -54.32 REMARK 500 THR A 198 -30.26 -136.41 REMARK 500 PRO A 206 55.14 -93.47 REMARK 500 SER A 209 -169.70 -112.02 REMARK 500 GLN A 258 -9.70 73.57 REMARK 500 ASN A 262 6.29 55.44 REMARK 500 GLU A 268 -6.10 66.28 REMARK 500 SER A 274 143.63 -171.72 REMARK 500 LYS A 282 -168.79 -100.60 REMARK 500 CYS A 378 116.82 -162.11 REMARK 500 ASN A 392 44.99 -144.57 REMARK 500 GLN A 428 3.66 58.14 REMARK 500 SER A 463 -59.38 -120.03 REMARK 500 THR A 464 -35.10 -130.73 REMARK 500 PRO A 493 4.31 -63.38 REMARK 500 ARG A 500 47.14 -84.03 REMARK 500 ARG A 503 155.97 -47.49 REMARK 500 ARG A 504 -162.52 -121.14 REMARK 500 SER B 534 5.51 -62.68 REMARK 500 ILE B 548 -7.78 -52.60 REMARK 500 GLN B 550 -0.04 62.26 REMARK 500 LYS B 567 -158.26 -81.89 REMARK 500 THR B 569 73.86 53.99 REMARK 500 TRP B 571 -11.90 78.70 REMARK 500 TRP B 596 81.80 -65.46 REMARK 500 CYS B 598 -63.10 -121.64 REMARK 500 SER B 599 -15.51 63.43 REMARK 500 LYS B 601 -168.12 -73.69 REMARK 500 LEU B 602 -18.32 72.99 REMARK 500 THR B 606 -166.77 -126.37 REMARK 500 REMARK 500 THIS ENTRY HAS 185 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 HIS A 66 ASN A 67 -142.26 REMARK 500 CYS A 501 LYS A 502 -131.55 REMARK 500 HIS E 66 ASN E 67 -142.28 REMARK 500 CYS E 501 LYS E 502 -131.54 REMARK 500 HIS I 66 ASN I 67 -142.33 REMARK 500 CYS I 501 LYS I 502 -131.55 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 MAN C 201 REMARK 610 MAN G 201 REMARK 610 MAN K 201 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-24195 RELATED DB: EMDB REMARK 900 COMPLEX STRUCTURE OF HIV SUPERINFECTION FAB QA013.2 AND REMARK 900 BG505.SOSIP.664 DBREF1 7N65 A 31 505 UNP A0A6H1VCM1_9PLVG DBREF2 7N65 A A0A6H1VCM1 30 502 DBREF 7N65 B 511 664 UNP Q2N0S7 Q2N0S7_9HIV1 508 661 DBREF 7N65 C 1 128 PDB 7N65 7N65 1 128 DBREF 7N65 D 1 108 PDB 7N65 7N65 1 108 DBREF1 7N65 E 31 505 UNP A0A6H1VCM1_9PLVG DBREF2 7N65 E A0A6H1VCM1 30 502 DBREF 7N65 F 511 664 UNP Q2N0S7 Q2N0S7_9HIV1 508 661 DBREF 7N65 G 1 128 PDB 7N65 7N65 1 128 DBREF 7N65 H 1 108 PDB 7N65 7N65 1 108 DBREF1 7N65 I 31 505 UNP A0A6H1VCM1_9PLVG DBREF2 7N65 I A0A6H1VCM1 30 502 DBREF 7N65 J 511 664 UNP Q2N0S7 Q2N0S7_9HIV1 508 661 DBREF 7N65 K 1 128 PDB 7N65 7N65 1 128 DBREF 7N65 L 1 108 PDB 7N65 7N65 1 108 SEQADV 7N65 MET A -4 UNP A0A6H1VCM INITIATING METHIONINE SEQADV 7N65 ASP A -3 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ALA A -2 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 MET A -1 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 LYS A 0 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ARG A 1 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 GLY A 2 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 LEU A 3 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 CYS A 4 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 CYS A 5 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 VAL A 6 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 LEU A 7 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 LEU A 8 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 LEU A 9 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 CYS A 10 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 GLY A 11 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ALA A 12 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 VAL A 13 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 PHE A 14 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 VAL A 15 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 SER A 16 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 PRO A 17 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 SER A 18 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 GLN A 19 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 GLU A 20 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ILE A 21 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 HIS A 22 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ALA A 23 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ARG A 24 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 PHE A 25 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ARG A 26 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ARG A 27 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 GLY A 28 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ALA A 29 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ARG A 30 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 SER A 375 UNP A0A6H1VCM TYR 373 CONFLICT SEQADV 7N65 CYS A 501 UNP A0A6H1VCM ALA 498 CONFLICT SEQADV 7N65 VAL B 504 UNP Q2N0S7 EXPRESSION TAG SEQADV 7N65 GLY B 505 UNP Q2N0S7 EXPRESSION TAG SEQADV 7N65 ARG B 506 UNP Q2N0S7 EXPRESSION TAG SEQADV 7N65 ARG B 507 UNP Q2N0S7 EXPRESSION TAG SEQADV 7N65 ARG B 508 UNP Q2N0S7 EXPRESSION TAG SEQADV 7N65 ARG B 509 UNP Q2N0S7 EXPRESSION TAG SEQADV 7N65 ARG B 510 UNP Q2N0S7 EXPRESSION TAG SEQADV 7N65 PRO B 559 UNP Q2N0S7 ILE 556 CONFLICT SEQADV 7N65 CYS B 605 UNP Q2N0S7 THR 602 CONFLICT SEQADV 7N65 MET E -4 UNP A0A6H1VCM INITIATING METHIONINE SEQADV 7N65 ASP E -3 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ALA E -2 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 MET E -1 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 LYS E 0 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ARG E 1 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 GLY E 2 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 LEU E 3 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 CYS E 4 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 CYS E 5 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 VAL E 6 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 LEU E 7 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 LEU E 8 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 LEU E 9 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 CYS E 10 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 GLY E 11 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ALA E 12 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 VAL E 13 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 PHE E 14 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 VAL E 15 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 SER E 16 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 PRO E 17 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 SER E 18 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 GLN E 19 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 GLU E 20 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ILE E 21 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 HIS E 22 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ALA E 23 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ARG E 24 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 PHE E 25 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ARG E 26 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ARG E 27 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 GLY E 28 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ALA E 29 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ARG E 30 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 SER E 375 UNP A0A6H1VCM TYR 373 CONFLICT SEQADV 7N65 CYS E 501 UNP A0A6H1VCM ALA 498 CONFLICT SEQADV 7N65 VAL F 504 UNP Q2N0S7 EXPRESSION TAG SEQADV 7N65 GLY F 505 UNP Q2N0S7 EXPRESSION TAG SEQADV 7N65 ARG F 506 UNP Q2N0S7 EXPRESSION TAG SEQADV 7N65 ARG F 507 UNP Q2N0S7 EXPRESSION TAG SEQADV 7N65 ARG F 508 UNP Q2N0S7 EXPRESSION TAG SEQADV 7N65 ARG F 509 UNP Q2N0S7 EXPRESSION TAG SEQADV 7N65 ARG F 510 UNP Q2N0S7 EXPRESSION TAG SEQADV 7N65 PRO F 559 UNP Q2N0S7 ILE 556 CONFLICT SEQADV 7N65 CYS F 605 UNP Q2N0S7 THR 602 CONFLICT SEQADV 7N65 MET I -4 UNP A0A6H1VCM INITIATING METHIONINE SEQADV 7N65 ASP I -3 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ALA I -2 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 MET I -1 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 LYS I 0 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ARG I 1 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 GLY I 2 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 LEU I 3 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 CYS I 4 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 CYS I 5 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 VAL I 6 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 LEU I 7 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 LEU I 8 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 LEU I 9 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 CYS I 10 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 GLY I 11 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ALA I 12 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 VAL I 13 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 PHE I 14 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 VAL I 15 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 SER I 16 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 PRO I 17 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 SER I 18 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 GLN I 19 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 GLU I 20 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ILE I 21 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 HIS I 22 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ALA I 23 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ARG I 24 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 PHE I 25 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ARG I 26 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ARG I 27 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 GLY I 28 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ALA I 29 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 ARG I 30 UNP A0A6H1VCM EXPRESSION TAG SEQADV 7N65 SER I 375 UNP A0A6H1VCM TYR 373 CONFLICT SEQADV 7N65 CYS I 501 UNP A0A6H1VCM ALA 498 CONFLICT SEQADV 7N65 VAL J 504 UNP Q2N0S7 EXPRESSION TAG SEQADV 7N65 GLY J 505 UNP Q2N0S7 EXPRESSION TAG SEQADV 7N65 ARG J 506 UNP Q2N0S7 EXPRESSION TAG SEQADV 7N65 ARG J 507 UNP Q2N0S7 EXPRESSION TAG SEQADV 7N65 ARG J 508 UNP Q2N0S7 EXPRESSION TAG SEQADV 7N65 ARG J 509 UNP Q2N0S7 EXPRESSION TAG SEQADV 7N65 ARG J 510 UNP Q2N0S7 EXPRESSION TAG SEQADV 7N65 PRO J 559 UNP Q2N0S7 ILE 556 CONFLICT SEQADV 7N65 CYS J 605 UNP Q2N0S7 THR 602 CONFLICT SEQRES 1 A 508 MET ASP ALA MET LYS ARG GLY LEU CYS CYS VAL LEU LEU SEQRES 2 A 508 LEU CYS GLY ALA VAL PHE VAL SER PRO SER GLN GLU ILE SEQRES 3 A 508 HIS ALA ARG PHE ARG ARG GLY ALA ARG ALA GLU ASN LEU SEQRES 4 A 508 TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP LYS ASP SEQRES 5 A 508 ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA LYS ALA SEQRES 6 A 508 TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR HIS ALA SEQRES 7 A 508 CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE HIS LEU SEQRES 8 A 508 GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS ASN ASN SEQRES 9 A 508 MET VAL GLU GLN MET HIS THR ASP ILE ILE SER LEU TRP SEQRES 10 A 508 ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR PRO LEU SEQRES 11 A 508 CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN ASN ILE SEQRES 12 A 508 THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SER PHE SEQRES 13 A 508 ASN MET THR THR GLU LEU ARG ASP LYS LYS GLN LYS VAL SEQRES 14 A 508 TYR SER LEU PHE TYR ARG LEU ASP VAL VAL GLN ILE ASN SEQRES 15 A 508 GLU ASN GLN GLY ASN ARG SER ASN ASN SER ASN LYS GLU SEQRES 16 A 508 TYR ARG LEU ILE ASN CYS ASN THR SER ALA ILE THR GLN SEQRES 17 A 508 ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE HIS SEQRES 18 A 508 TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS SEQRES 19 A 508 ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SER VAL SEQRES 20 A 508 SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SEQRES 21 A 508 SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU GLU SEQRES 22 A 508 GLU VAL MET ILE ARG SER GLU ASN ILE THR ASN ASN ALA SEQRES 23 A 508 LYS ASN ILE LEU VAL GLN PHE ASN THR PRO VAL GLN ILE SEQRES 24 A 508 ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SER ILE SEQRES 25 A 508 ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA THR GLY ASP SEQRES 26 A 508 ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN VAL SER SEQRES 27 A 508 LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL VAL LYS SEQRES 28 A 508 GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE ILE ARG SEQRES 29 A 508 PHE ALA ASN SER SER GLY GLY ASP LEU GLU VAL THR THR SEQRES 30 A 508 HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN SEQRES 31 A 508 THR SER GLY LEU PHE ASN SER THR TRP ILE SER ASN THR SEQRES 32 A 508 SER VAL GLN GLY SER ASN SER THR GLY SER ASN ASP SER SEQRES 33 A 508 ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE ASN MET SEQRES 34 A 508 TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO PRO ILE SEQRES 35 A 508 GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR GLY LEU SEQRES 36 A 508 ILE LEU THR ARG ASP GLY GLY SER THR ASN SER THR THR SEQRES 37 A 508 GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG ASP ASN SEQRES 38 A 508 TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE SEQRES 39 A 508 GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS ARG ARG SEQRES 40 A 508 VAL SEQRES 1 B 161 VAL GLY ARG ARG ARG ARG ARG ARG ALA VAL GLY ILE GLY SEQRES 2 B 161 ALA VAL PHE LEU GLY PHE LEU GLY ALA ALA GLY SER THR SEQRES 3 B 161 MET GLY ALA ALA SER MET THR LEU THR VAL GLN ALA ARG SEQRES 4 B 161 ASN LEU LEU SER GLY ILE VAL GLN GLN GLN SER ASN LEU SEQRES 5 B 161 LEU ARG ALA PRO GLU ALA GLN GLN HIS LEU LEU LYS LEU SEQRES 6 B 161 THR VAL TRP GLY ILE LYS GLN LEU GLN ALA ARG VAL LEU SEQRES 7 B 161 ALA VAL GLU ARG TYR LEU ARG ASP GLN GLN LEU LEU GLY SEQRES 8 B 161 ILE TRP GLY CYS SER GLY LYS LEU ILE CYS CYS THR ASN SEQRES 9 B 161 VAL PRO TRP ASN SER SER TRP SER ASN ARG ASN LEU SER SEQRES 10 B 161 GLU ILE TRP ASP ASN MET THR TRP LEU GLN TRP ASP LYS SEQRES 11 B 161 GLU ILE SER ASN TYR THR GLN ILE ILE TYR GLY LEU LEU SEQRES 12 B 161 GLU GLU SER GLN ASN GLN GLN GLU LYS ASN GLU GLN ASP SEQRES 13 B 161 LEU LEU ALA LEU ASP SEQRES 1 C 128 ASP ILE ARG ILE ALA GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 128 PRO GLY GLU SER LEU ARG LEU ALA CYS GLU ILE ILE GLU SEQRES 3 C 128 LEU GLY PHE ARG ARG ALA TRP THR THR TRP VAL ARG GLN SEQRES 4 C 128 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ASP ILE ASN SEQRES 5 C 128 GLU ASP GLY SER GLU LYS LYS TYR GLY PRO SER VAL THR SEQRES 6 C 128 GLY ARG PHE THR ILE SER ARG ASP ASN GLY LYS ASN LEU SEQRES 7 C 128 VAL PHE LEU GLN MET ASN SER LEU ARG VAL GLU ASP THR SEQRES 8 C 128 ALA THR TYR TYR CYS ALA ARG GLU ALA TYR HIS LEU VAL SEQRES 9 C 128 TYR ASP ASP ARG ILE PRO ARG GLY ASN TRP PHE ASP PRO SEQRES 10 C 128 TRP GLY PRO GLY THR LEU VAL THR VAL SER SER SEQRES 1 D 108 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 D 108 PRO GLY GLN ARG VAL VAL ILE SER CYS THR GLY SER ARG SEQRES 3 D 108 SER ASN ILE GLY ALA GLY TYR ASP VAL HIS TRP TYR GLN SEQRES 4 D 108 GLN SER PRO GLY LYS VAL PRO ARG ILE ILE ILE TYR GLY SEQRES 5 D 108 SER ASN SER ARG SER SER GLY VAL PRO ALA ARG PHE SER SEQRES 6 D 108 GLY SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR SEQRES 7 D 108 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 D 108 SER TYR ASP THR THR LEU THR ALA SER VAL PHE GLY GLY SEQRES 9 D 108 GLY THR LYS VAL SEQRES 1 E 508 MET ASP ALA MET LYS ARG GLY LEU CYS CYS VAL LEU LEU SEQRES 2 E 508 LEU CYS GLY ALA VAL PHE VAL SER PRO SER GLN GLU ILE SEQRES 3 E 508 HIS ALA ARG PHE ARG ARG GLY ALA ARG ALA GLU ASN LEU SEQRES 4 E 508 TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP LYS ASP SEQRES 5 E 508 ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA LYS ALA SEQRES 6 E 508 TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR HIS ALA SEQRES 7 E 508 CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE HIS LEU SEQRES 8 E 508 GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS ASN ASN SEQRES 9 E 508 MET VAL GLU GLN MET HIS THR ASP ILE ILE SER LEU TRP SEQRES 10 E 508 ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR PRO LEU SEQRES 11 E 508 CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN ASN ILE SEQRES 12 E 508 THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SER PHE SEQRES 13 E 508 ASN MET THR THR GLU LEU ARG ASP LYS LYS GLN LYS VAL SEQRES 14 E 508 TYR SER LEU PHE TYR ARG LEU ASP VAL VAL GLN ILE ASN SEQRES 15 E 508 GLU ASN GLN GLY ASN ARG SER ASN ASN SER ASN LYS GLU SEQRES 16 E 508 TYR ARG LEU ILE ASN CYS ASN THR SER ALA ILE THR GLN SEQRES 17 E 508 ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE HIS SEQRES 18 E 508 TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS SEQRES 19 E 508 ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SER VAL SEQRES 20 E 508 SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SEQRES 21 E 508 SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU GLU SEQRES 22 E 508 GLU VAL MET ILE ARG SER GLU ASN ILE THR ASN ASN ALA SEQRES 23 E 508 LYS ASN ILE LEU VAL GLN PHE ASN THR PRO VAL GLN ILE SEQRES 24 E 508 ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SER ILE SEQRES 25 E 508 ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA THR GLY ASP SEQRES 26 E 508 ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN VAL SER SEQRES 27 E 508 LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL VAL LYS SEQRES 28 E 508 GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE ILE ARG SEQRES 29 E 508 PHE ALA ASN SER SER GLY GLY ASP LEU GLU VAL THR THR SEQRES 30 E 508 HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN SEQRES 31 E 508 THR SER GLY LEU PHE ASN SER THR TRP ILE SER ASN THR SEQRES 32 E 508 SER VAL GLN GLY SER ASN SER THR GLY SER ASN ASP SER SEQRES 33 E 508 ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE ASN MET SEQRES 34 E 508 TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO PRO ILE SEQRES 35 E 508 GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR GLY LEU SEQRES 36 E 508 ILE LEU THR ARG ASP GLY GLY SER THR ASN SER THR THR SEQRES 37 E 508 GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG ASP ASN SEQRES 38 E 508 TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE SEQRES 39 E 508 GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS ARG ARG SEQRES 40 E 508 VAL SEQRES 1 F 161 VAL GLY ARG ARG ARG ARG ARG ARG ALA VAL GLY ILE GLY SEQRES 2 F 161 ALA VAL PHE LEU GLY PHE LEU GLY ALA ALA GLY SER THR SEQRES 3 F 161 MET GLY ALA ALA SER MET THR LEU THR VAL GLN ALA ARG SEQRES 4 F 161 ASN LEU LEU SER GLY ILE VAL GLN GLN GLN SER ASN LEU SEQRES 5 F 161 LEU ARG ALA PRO GLU ALA GLN GLN HIS LEU LEU LYS LEU SEQRES 6 F 161 THR VAL TRP GLY ILE LYS GLN LEU GLN ALA ARG VAL LEU SEQRES 7 F 161 ALA VAL GLU ARG TYR LEU ARG ASP GLN GLN LEU LEU GLY SEQRES 8 F 161 ILE TRP GLY CYS SER GLY LYS LEU ILE CYS CYS THR ASN SEQRES 9 F 161 VAL PRO TRP ASN SER SER TRP SER ASN ARG ASN LEU SER SEQRES 10 F 161 GLU ILE TRP ASP ASN MET THR TRP LEU GLN TRP ASP LYS SEQRES 11 F 161 GLU ILE SER ASN TYR THR GLN ILE ILE TYR GLY LEU LEU SEQRES 12 F 161 GLU GLU SER GLN ASN GLN GLN GLU LYS ASN GLU GLN ASP SEQRES 13 F 161 LEU LEU ALA LEU ASP SEQRES 1 G 128 ASP ILE ARG ILE ALA GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 G 128 PRO GLY GLU SER LEU ARG LEU ALA CYS GLU ILE ILE GLU SEQRES 3 G 128 LEU GLY PHE ARG ARG ALA TRP THR THR TRP VAL ARG GLN SEQRES 4 G 128 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ASP ILE ASN SEQRES 5 G 128 GLU ASP GLY SER GLU LYS LYS TYR GLY PRO SER VAL THR SEQRES 6 G 128 GLY ARG PHE THR ILE SER ARG ASP ASN GLY LYS ASN LEU SEQRES 7 G 128 VAL PHE LEU GLN MET ASN SER LEU ARG VAL GLU ASP THR SEQRES 8 G 128 ALA THR TYR TYR CYS ALA ARG GLU ALA TYR HIS LEU VAL SEQRES 9 G 128 TYR ASP ASP ARG ILE PRO ARG GLY ASN TRP PHE ASP PRO SEQRES 10 G 128 TRP GLY PRO GLY THR LEU VAL THR VAL SER SER SEQRES 1 H 108 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 H 108 PRO GLY GLN ARG VAL VAL ILE SER CYS THR GLY SER ARG SEQRES 3 H 108 SER ASN ILE GLY ALA GLY TYR ASP VAL HIS TRP TYR GLN SEQRES 4 H 108 GLN SER PRO GLY LYS VAL PRO ARG ILE ILE ILE TYR GLY SEQRES 5 H 108 SER ASN SER ARG SER SER GLY VAL PRO ALA ARG PHE SER SEQRES 6 H 108 GLY SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR SEQRES 7 H 108 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 H 108 SER TYR ASP THR THR LEU THR ALA SER VAL PHE GLY GLY SEQRES 9 H 108 GLY THR LYS VAL SEQRES 1 I 508 MET ASP ALA MET LYS ARG GLY LEU CYS CYS VAL LEU LEU SEQRES 2 I 508 LEU CYS GLY ALA VAL PHE VAL SER PRO SER GLN GLU ILE SEQRES 3 I 508 HIS ALA ARG PHE ARG ARG GLY ALA ARG ALA GLU ASN LEU SEQRES 4 I 508 TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP LYS ASP SEQRES 5 I 508 ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA LYS ALA SEQRES 6 I 508 TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR HIS ALA SEQRES 7 I 508 CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE HIS LEU SEQRES 8 I 508 GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS ASN ASN SEQRES 9 I 508 MET VAL GLU GLN MET HIS THR ASP ILE ILE SER LEU TRP SEQRES 10 I 508 ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR PRO LEU SEQRES 11 I 508 CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN ASN ILE SEQRES 12 I 508 THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SER PHE SEQRES 13 I 508 ASN MET THR THR GLU LEU ARG ASP LYS LYS GLN LYS VAL SEQRES 14 I 508 TYR SER LEU PHE TYR ARG LEU ASP VAL VAL GLN ILE ASN SEQRES 15 I 508 GLU ASN GLN GLY ASN ARG SER ASN ASN SER ASN LYS GLU SEQRES 16 I 508 TYR ARG LEU ILE ASN CYS ASN THR SER ALA ILE THR GLN SEQRES 17 I 508 ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE HIS SEQRES 18 I 508 TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS SEQRES 19 I 508 ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SER VAL SEQRES 20 I 508 SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SEQRES 21 I 508 SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU GLU SEQRES 22 I 508 GLU VAL MET ILE ARG SER GLU ASN ILE THR ASN ASN ALA SEQRES 23 I 508 LYS ASN ILE LEU VAL GLN PHE ASN THR PRO VAL GLN ILE SEQRES 24 I 508 ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SER ILE SEQRES 25 I 508 ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA THR GLY ASP SEQRES 26 I 508 ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN VAL SER SEQRES 27 I 508 LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL VAL LYS SEQRES 28 I 508 GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE ILE ARG SEQRES 29 I 508 PHE ALA ASN SER SER GLY GLY ASP LEU GLU VAL THR THR SEQRES 30 I 508 HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN SEQRES 31 I 508 THR SER GLY LEU PHE ASN SER THR TRP ILE SER ASN THR SEQRES 32 I 508 SER VAL GLN GLY SER ASN SER THR GLY SER ASN ASP SER SEQRES 33 I 508 ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE ASN MET SEQRES 34 I 508 TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO PRO ILE SEQRES 35 I 508 GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR GLY LEU SEQRES 36 I 508 ILE LEU THR ARG ASP GLY GLY SER THR ASN SER THR THR SEQRES 37 I 508 GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG ASP ASN SEQRES 38 I 508 TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE SEQRES 39 I 508 GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS ARG ARG SEQRES 40 I 508 VAL SEQRES 1 J 161 VAL GLY ARG ARG ARG ARG ARG ARG ALA VAL GLY ILE GLY SEQRES 2 J 161 ALA VAL PHE LEU GLY PHE LEU GLY ALA ALA GLY SER THR SEQRES 3 J 161 MET GLY ALA ALA SER MET THR LEU THR VAL GLN ALA ARG SEQRES 4 J 161 ASN LEU LEU SER GLY ILE VAL GLN GLN GLN SER ASN LEU SEQRES 5 J 161 LEU ARG ALA PRO GLU ALA GLN GLN HIS LEU LEU LYS LEU SEQRES 6 J 161 THR VAL TRP GLY ILE LYS GLN LEU GLN ALA ARG VAL LEU SEQRES 7 J 161 ALA VAL GLU ARG TYR LEU ARG ASP GLN GLN LEU LEU GLY SEQRES 8 J 161 ILE TRP GLY CYS SER GLY LYS LEU ILE CYS CYS THR ASN SEQRES 9 J 161 VAL PRO TRP ASN SER SER TRP SER ASN ARG ASN LEU SER SEQRES 10 J 161 GLU ILE TRP ASP ASN MET THR TRP LEU GLN TRP ASP LYS SEQRES 11 J 161 GLU ILE SER ASN TYR THR GLN ILE ILE TYR GLY LEU LEU SEQRES 12 J 161 GLU GLU SER GLN ASN GLN GLN GLU LYS ASN GLU GLN ASP SEQRES 13 J 161 LEU LEU ALA LEU ASP SEQRES 1 K 128 ASP ILE ARG ILE ALA GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 K 128 PRO GLY GLU SER LEU ARG LEU ALA CYS GLU ILE ILE GLU SEQRES 3 K 128 LEU GLY PHE ARG ARG ALA TRP THR THR TRP VAL ARG GLN SEQRES 4 K 128 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ASP ILE ASN SEQRES 5 K 128 GLU ASP GLY SER GLU LYS LYS TYR GLY PRO SER VAL THR SEQRES 6 K 128 GLY ARG PHE THR ILE SER ARG ASP ASN GLY LYS ASN LEU SEQRES 7 K 128 VAL PHE LEU GLN MET ASN SER LEU ARG VAL GLU ASP THR SEQRES 8 K 128 ALA THR TYR TYR CYS ALA ARG GLU ALA TYR HIS LEU VAL SEQRES 9 K 128 TYR ASP ASP ARG ILE PRO ARG GLY ASN TRP PHE ASP PRO SEQRES 10 K 128 TRP GLY PRO GLY THR LEU VAL THR VAL SER SER SEQRES 1 L 108 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 L 108 PRO GLY GLN ARG VAL VAL ILE SER CYS THR GLY SER ARG SEQRES 3 L 108 SER ASN ILE GLY ALA GLY TYR ASP VAL HIS TRP TYR GLN SEQRES 4 L 108 GLN SER PRO GLY LYS VAL PRO ARG ILE ILE ILE TYR GLY SEQRES 5 L 108 SER ASN SER ARG SER SER GLY VAL PRO ALA ARG PHE SER SEQRES 6 L 108 GLY SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR SEQRES 7 L 108 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 L 108 SER TYR ASP THR THR LEU THR ALA SER VAL PHE GLY GLY SEQRES 9 L 108 GLY THR LYS VAL HET NAG A 601 14 HET NAG B 701 14 HET NAG B 702 14 HET MAN C 201 11 HET NAG E 601 14 HET NAG F 701 14 HET NAG F 702 14 HET MAN G 201 11 HET NAG I 601 14 HET NAG J 701 14 HET NAG J 702 14 HET MAN K 201 11 HET NAG M 1 14 HET NAG M 2 14 HET BMA M 3 11 HET NAG N 1 14 HET NAG N 2 14 HET NAG O 1 14 HET NAG O 2 14 HET BMA O 3 11 HET NAG P 1 14 HET NAG P 2 14 HET BMA P 3 11 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 BMA S 3 11 HET MAN S 4 11 HET MAN S 5 11 HET MAN S 6 11 HET MAN S 7 11 HET NAG T 1 14 HET NAG T 2 14 HET BMA T 3 11 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 NAG V 1 14 HET NAG V 2 14 HET BMA V 3 11 HET MAN V 4 11 HET MAN V 5 11 HET MAN V 6 11 HET MAN V 7 11 HET NAG W 1 14 HET NAG W 2 14 HET BMA W 3 11 HET MAN W 4 11 HET MAN W 5 11 HET MAN W 6 11 HET MAN W 7 11 HET MAN W 8 11 HET NAG X 1 14 HET NAG X 2 14 HET NAG Y 1 14 HET NAG Y 2 14 HET BMA Y 3 11 HET NAG Z 1 14 HET NAG Z 2 14 HET BMA Z 3 11 HET NAG a 1 14 HET NAG a 2 14 HET NAG b 1 14 HET NAG b 2 14 HET NAG c 1 14 HET NAG c 2 14 HET NAG d 1 14 HET NAG d 2 14 HET BMA d 3 11 HET NAG e 1 14 HET NAG e 2 14 HET NAG f 1 14 HET NAG f 2 14 HET BMA f 3 11 HET NAG g 1 14 HET NAG g 2 14 HET BMA g 3 11 HET NAG h 1 14 HET NAG h 2 14 HET NAG i 1 14 HET NAG i 2 14 HET NAG j 1 14 HET NAG j 2 14 HET BMA j 3 11 HET MAN j 4 11 HET MAN j 5 11 HET MAN j 6 11 HET MAN j 7 11 HET NAG k 1 14 HET NAG k 2 14 HET BMA k 3 11 HET NAG l 1 14 HET NAG l 2 14 HET BMA l 3 11 HET MAN l 4 11 HET MAN l 5 11 HET NAG m 1 14 HET NAG m 2 14 HET BMA m 3 11 HET MAN m 4 11 HET MAN m 5 11 HET MAN m 6 11 HET MAN m 7 11 HET NAG n 1 14 HET NAG n 2 14 HET BMA n 3 11 HET MAN n 4 11 HET MAN n 5 11 HET MAN n 6 11 HET MAN n 7 11 HET MAN n 8 11 HET NAG o 1 14 HET NAG o 2 14 HET NAG p 1 14 HET NAG p 2 14 HET BMA p 3 11 HET NAG q 1 14 HET NAG q 2 14 HET BMA q 3 11 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 BMA u 3 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 BMA x 3 11 HET NAG y 1 14 HET NAG y 2 14 HET NAG z 1 14 HET NAG z 2 14 HET NAG 0 1 14 HET NAG 0 2 14 HET BMA 0 3 11 HET MAN 0 4 11 HET MAN 0 5 11 HET MAN 0 6 11 HET MAN 0 7 11 HET NAG 1 1 14 HET NAG 1 2 14 HET BMA 1 3 11 HET NAG 2 1 14 HET NAG 2 2 14 HET BMA 2 3 11 HET MAN 2 4 11 HET MAN 2 5 11 HET NAG 3 1 14 HET NAG 3 2 14 HET BMA 3 3 11 HET MAN 3 4 11 HET MAN 3 5 11 HET MAN 3 6 11 HET MAN 3 7 11 HET NAG 4 1 14 HET NAG 4 2 14 HET BMA 4 3 11 HET MAN 4 4 11 HET MAN 4 5 11 HET MAN 4 6 11 HET MAN 4 7 11 HET MAN 4 8 11 HET NAG 5 1 14 HET NAG 5 2 14 HET NAG 6 1 14 HET NAG 6 2 14 HET BMA 6 3 11 HET NAG 7 1 14 HET NAG 7 2 14 HET BMA 7 3 11 HET NAG 8 1 14 HET NAG 8 2 14 HET NAG 9 1 14 HET NAG 9 2 14 HET NAG AA 1 14 HET NAG AA 2 14 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM MAN ALPHA-D-MANNOSE HETNAM BMA BETA-D-MANNOSE FORMUL 13 NAG 111(C8 H15 N O6) FORMUL 16 MAN 48(C6 H12 O6) FORMUL 25 BMA 30(C6 H12 O6) HELIX 1 AA1 ASN A 99 LYS A 117 1 19 HELIX 2 AA2 LEU A 122 CYS A 126 5 5 HELIX 3 AA3 TYR A 177 LEU A 179 5 3 HELIX 4 AA4 ASN A 195 THR A 198 5 4 HELIX 5 AA5 LYS A 335 LYS A 351 1 17 HELIX 6 AA6 ASP A 368 THR A 373 1 6 HELIX 7 AA7 THR A 387 PHE A 391 5 5 HELIX 8 AA8 ASN A 425 ARG A 429 5 5 HELIX 9 AA9 ASP A 474 TYR A 484 1 11 HELIX 10 AB1 THR B 529 SER B 534 1 6 HELIX 11 AB2 LEU B 537 ASN B 543 1 7 HELIX 12 AB3 TRP B 571 TRP B 596 1 26 HELIX 13 AB4 LEU B 619 ASP B 624 1 6 HELIX 14 AB5 THR B 627 SER B 636 1 10 HELIX 15 AB6 TYR B 638 LYS B 655 1 18 HELIX 16 AB7 ASN B 656 ALA B 662 1 7 HELIX 17 AB8 GLY C 28 ALA C 32 5 5 HELIX 18 AB9 ARG C 87 THR C 91 5 5 HELIX 19 AC1 ALA C 100 VAL C 104 5 5 HELIX 20 AC2 ASN E 99 LYS E 117 1 19 HELIX 21 AC3 LEU E 122 CYS E 126 5 5 HELIX 22 AC4 TYR E 177 LEU E 179 5 3 HELIX 23 AC5 ASN E 195 THR E 198 5 4 HELIX 24 AC6 LYS E 335 LYS E 351 1 17 HELIX 25 AC7 ASP E 368 THR E 373 1 6 HELIX 26 AC8 THR E 387 PHE E 391 5 5 HELIX 27 AC9 ASN E 425 ARG E 429 5 5 HELIX 28 AD1 ASP E 474 TYR E 484 1 11 HELIX 29 AD2 THR F 529 SER F 534 1 6 HELIX 30 AD3 LEU F 537 ASN F 543 1 7 HELIX 31 AD4 TRP F 571 TRP F 596 1 26 HELIX 32 AD5 LEU F 619 ASP F 624 1 6 HELIX 33 AD6 THR F 627 SER F 636 1 10 HELIX 34 AD7 TYR F 638 LYS F 655 1 18 HELIX 35 AD8 ASN F 656 ALA F 662 1 7 HELIX 36 AD9 GLY G 28 ALA G 32 5 5 HELIX 37 AE1 ARG G 87 THR G 91 5 5 HELIX 38 AE2 ALA G 100 VAL G 104 5 5 HELIX 39 AE3 ASN I 99 LYS I 117 1 19 HELIX 40 AE4 LEU I 122 CYS I 126 5 5 HELIX 41 AE5 TYR I 177 LEU I 179 5 3 HELIX 42 AE6 ASN I 195 THR I 198 5 4 HELIX 43 AE7 LYS I 335 LYS I 351 1 17 HELIX 44 AE8 ASP I 368 THR I 373 1 6 HELIX 45 AE9 THR I 387 PHE I 391 5 5 HELIX 46 AF1 ASN I 425 ARG I 429 5 5 HELIX 47 AF2 ASP I 474 TYR I 484 1 11 HELIX 48 AF3 THR J 529 SER J 534 1 6 HELIX 49 AF4 LEU J 537 ASN J 543 1 7 HELIX 50 AF5 TRP J 571 TRP J 596 1 26 HELIX 51 AF6 LEU J 619 ASP J 624 1 6 HELIX 52 AF7 THR J 627 SER J 636 1 10 HELIX 53 AF8 TYR J 638 LYS J 655 1 18 HELIX 54 AF9 ASN J 656 ALA J 662 1 7 HELIX 55 AG1 GLY K 28 ALA K 32 5 5 HELIX 56 AG2 ARG K 87 THR K 91 5 5 HELIX 57 AG3 ALA K 100 VAL K 104 5 5 SHEET 1 AA1 2 TRP A 35 TYR A 40 0 SHEET 2 AA1 2 LEU A 494 THR A 499 -1 O GLY A 495 N TYR A 39 SHEET 1 AA2 5 TRP A 45 ASP A 47 0 SHEET 2 AA2 5 TYR A 486 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AA2 5 PHE A 223 CYS A 228 -1 N LEU A 226 O LYS A 487 SHEET 4 AA2 5 VAL A 242 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 5 AA2 5 GLU A 83 LEU A 86 -1 N LEU A 86 O VAL A 242 SHEET 1 AA3 2 ALA A 55 SER A 56 0 SHEET 2 AA3 2 VAL A 75 PRO A 76 1 O VAL A 75 N SER A 56 SHEET 1 AA4 2 GLU A 91 ASN A 94 0 SHEET 2 AA4 2 THR A 236 CYS A 239 -1 O GLY A 237 N PHE A 93 SHEET 1 AA5 5 GLN A 170 PHE A 176 0 SHEET 2 AA5 5 LYS A 155 MET A 161 -1 N CYS A 157 O SER A 174 SHEET 3 AA5 5 LEU A 129 ASN A 133 -1 N GLN A 130 O SER A 158 SHEET 4 AA5 5 LYS A 189 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 5 AA5 5 VAL A 181 VAL A 182 -1 N VAL A 182 O ARG A 192 SHEET 1 AA6 3 THR A 202 GLN A 203 0 SHEET 2 AA6 3 MET A 434 TYR A 435 1 O TYR A 435 N THR A 202 SHEET 3 AA6 3 ILE A 423 ILE A 424 -1 N ILE A 424 O MET A 434 SHEET 1 AA712 LEU A 259 LEU A 261 0 SHEET 2 AA712 ILE A 272 ARG A 273 0 SHEET 3 AA712 ILE A 284 ILE A 309 -1 O LEU A 285 N ARG A 273 SHEET 4 AA712 GLN A 315 ILE A 323 -1 O ILE A 323 N ASN A 301 SHEET 5 AA712 HIS A 330 SER A 334 -1 O ASN A 332 N ASN A 295 SHEET 6 AA712 ILE A 358 PHE A 361 0 SHEET 7 AA712 HIS A 374 CYS A 378 0 SHEET 8 AA712 GLU A 381 CYS A 385 -1 O CYS A 385 N HIS A 374 SHEET 9 AA712 SER A 393 TRP A 395 -1 O SER A 393 N PHE A 361 SHEET 10 AA712 SER A 413 ILE A 420 -1 O ARG A 419 N TYR A 384 SHEET 11 AA712 GLY A 441 ARG A 456 -1 O THR A 450 N PHE A 288 SHEET 12 AA712 THR A 465 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 1 AA8 5 GLY C 10 VAL C 12 0 SHEET 2 AA8 5 THR C 122 VAL C 126 1 O THR C 125 N GLY C 10 SHEET 3 AA8 5 ALA C 92 ARG C 98 -1 N TYR C 94 O THR C 122 SHEET 4 AA8 5 THR C 34 GLN C 39 -1 N VAL C 37 O TYR C 95 SHEET 5 AA8 5 GLU C 46 ASP C 50 -1 O VAL C 48 N TRP C 36 SHEET 1 AA9 3 SER C 17 LEU C 20 0 SHEET 2 AA9 3 LEU C 78 ASN C 84 -1 O MET C 83 N LEU C 18 SHEET 3 AA9 3 PHE C 68 ASP C 73 -1 N SER C 71 O PHE C 80 SHEET 1 AB1 3 VAL D 3 LEU D 4 0 SHEET 2 AB1 3 SER D 100 GLY D 103 1 O PHE D 102 N LEU D 4 SHEET 3 AB1 3 GLN D 91 TYR D 93 -1 N SER D 92 O VAL D 101 SHEET 1 AB2 3 VAL D 18 SER D 21 0 SHEET 2 AB2 3 SER D 72 ILE D 77 -1 O ILE D 77 N VAL D 18 SHEET 3 AB2 3 SER D 65 SER D 69 -1 N SER D 69 O SER D 72 SHEET 1 AB3 3 ARG D 47 ILE D 48 0 SHEET 2 AB3 3 TYR D 38 GLN D 40 -1 N GLN D 39 O ARG D 47 SHEET 3 AB3 3 ASP D 87 TYR D 89 -1 O ASP D 87 N GLN D 40 SHEET 1 AB4 2 ILE D 50 TYR D 51 0 SHEET 2 AB4 2 SER D 55 ARG D 56 -1 O SER D 55 N TYR D 51 SHEET 1 AB5 2 TRP E 35 TYR E 40 0 SHEET 2 AB5 2 LEU E 494 THR E 499 -1 O GLY E 495 N TYR E 39 SHEET 1 AB6 5 TRP E 45 ASP E 47 0 SHEET 2 AB6 5 TYR E 486 ILE E 491 -1 O LYS E 490 N LYS E 46 SHEET 3 AB6 5 PHE E 223 CYS E 228 -1 N LEU E 226 O LYS E 487 SHEET 4 AB6 5 VAL E 242 VAL E 245 -1 O SER E 243 N LYS E 227 SHEET 5 AB6 5 GLU E 83 LEU E 86 -1 N LEU E 86 O VAL E 242 SHEET 1 AB7 2 ALA E 55 SER E 56 0 SHEET 2 AB7 2 VAL E 75 PRO E 76 1 O VAL E 75 N SER E 56 SHEET 1 AB8 2 GLU E 91 ASN E 94 0 SHEET 2 AB8 2 THR E 236 CYS E 239 -1 O GLY E 237 N PHE E 93 SHEET 1 AB9 5 GLN E 170 PHE E 176 0 SHEET 2 AB9 5 LYS E 155 MET E 161 -1 N CYS E 157 O SER E 174 SHEET 3 AB9 5 LEU E 129 ASN E 133 -1 N GLN E 130 O SER E 158 SHEET 4 AB9 5 LYS E 189 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 5 AB9 5 VAL E 181 VAL E 182 -1 N VAL E 182 O ARG E 192 SHEET 1 AC1 3 THR E 202 GLN E 203 0 SHEET 2 AC1 3 MET E 434 TYR E 435 1 O TYR E 435 N THR E 202 SHEET 3 AC1 3 ILE E 423 ILE E 424 -1 N ILE E 424 O MET E 434 SHEET 1 AC212 LEU E 259 LEU E 261 0 SHEET 2 AC212 ILE E 272 ARG E 273 0 SHEET 3 AC212 ILE E 284 ILE E 309 -1 O LEU E 285 N ARG E 273 SHEET 4 AC212 GLN E 315 ILE E 323 -1 O ILE E 323 N ASN E 301 SHEET 5 AC212 HIS E 330 SER E 334 -1 O ASN E 332 N ASN E 295 SHEET 6 AC212 ILE E 358 PHE E 361 0 SHEET 7 AC212 HIS E 374 CYS E 378 0 SHEET 8 AC212 GLU E 381 CYS E 385 -1 O CYS E 385 N HIS E 374 SHEET 9 AC212 SER E 393 TRP E 395 -1 O SER E 393 N PHE E 361 SHEET 10 AC212 SER E 413 ILE E 420 -1 O ARG E 419 N TYR E 384 SHEET 11 AC212 GLY E 441 ARG E 456 -1 O THR E 450 N PHE E 288 SHEET 12 AC212 THR E 465 PRO E 470 -1 O ARG E 469 N THR E 455 SHEET 1 AC3 5 GLY G 10 VAL G 12 0 SHEET 2 AC3 5 THR G 122 VAL G 126 1 O THR G 125 N GLY G 10 SHEET 3 AC3 5 ALA G 92 ARG G 98 -1 N TYR G 94 O THR G 122 SHEET 4 AC3 5 THR G 34 GLN G 39 -1 N VAL G 37 O TYR G 95 SHEET 5 AC3 5 GLU G 46 ASP G 50 -1 O VAL G 48 N TRP G 36 SHEET 1 AC4 3 SER G 17 LEU G 20 0 SHEET 2 AC4 3 LEU G 78 ASN G 84 -1 O MET G 83 N LEU G 18 SHEET 3 AC4 3 PHE G 68 ASP G 73 -1 N SER G 71 O PHE G 80 SHEET 1 AC5 3 VAL H 3 LEU H 4 0 SHEET 2 AC5 3 SER H 100 GLY H 103 1 O PHE H 102 N LEU H 4 SHEET 3 AC5 3 GLN H 91 TYR H 93 -1 N SER H 92 O VAL H 101 SHEET 1 AC6 3 VAL H 18 SER H 21 0 SHEET 2 AC6 3 SER H 72 ILE H 77 -1 O ILE H 77 N VAL H 18 SHEET 3 AC6 3 SER H 65 SER H 69 -1 N SER H 69 O SER H 72 SHEET 1 AC7 3 ARG H 47 ILE H 48 0 SHEET 2 AC7 3 TYR H 38 GLN H 40 -1 N GLN H 39 O ARG H 47 SHEET 3 AC7 3 ASP H 87 TYR H 89 -1 O ASP H 87 N GLN H 40 SHEET 1 AC8 2 ILE H 50 TYR H 51 0 SHEET 2 AC8 2 SER H 55 ARG H 56 -1 O SER H 55 N TYR H 51 SHEET 1 AC9 2 TRP I 35 TYR I 40 0 SHEET 2 AC9 2 LEU I 494 THR I 499 -1 O GLY I 495 N TYR I 39 SHEET 1 AD1 5 TRP I 45 ASP I 47 0 SHEET 2 AD1 5 TYR I 486 ILE I 491 -1 O LYS I 490 N LYS I 46 SHEET 3 AD1 5 PHE I 223 CYS I 228 -1 N LEU I 226 O LYS I 487 SHEET 4 AD1 5 VAL I 242 VAL I 245 -1 O SER I 243 N LYS I 227 SHEET 5 AD1 5 GLU I 83 LEU I 86 -1 N LEU I 86 O VAL I 242 SHEET 1 AD2 2 ALA I 55 SER I 56 0 SHEET 2 AD2 2 VAL I 75 PRO I 76 1 O VAL I 75 N SER I 56 SHEET 1 AD3 2 GLU I 91 ASN I 94 0 SHEET 2 AD3 2 THR I 236 CYS I 239 -1 O GLY I 237 N PHE I 93 SHEET 1 AD4 5 GLN I 170 PHE I 176 0 SHEET 2 AD4 5 LYS I 155 MET I 161 -1 N CYS I 157 O SER I 174 SHEET 3 AD4 5 LEU I 129 ASN I 133 -1 N GLN I 130 O SER I 158 SHEET 4 AD4 5 LYS I 189 LEU I 193 -1 O TYR I 191 N LEU I 129 SHEET 5 AD4 5 VAL I 181 VAL I 182 -1 N VAL I 182 O ARG I 192 SHEET 1 AD5 3 THR I 202 GLN I 203 0 SHEET 2 AD5 3 MET I 434 TYR I 435 1 O TYR I 435 N THR I 202 SHEET 3 AD5 3 ILE I 423 ILE I 424 -1 N ILE I 424 O MET I 434 SHEET 1 AD612 LEU I 259 LEU I 261 0 SHEET 2 AD612 ILE I 272 ARG I 273 0 SHEET 3 AD612 ILE I 284 ILE I 309 -1 O LEU I 285 N ARG I 273 SHEET 4 AD612 GLN I 315 ILE I 323 -1 O ILE I 323 N ASN I 301 SHEET 5 AD612 HIS I 330 SER I 334 -1 O ASN I 332 N ASN I 295 SHEET 6 AD612 ILE I 358 PHE I 361 0 SHEET 7 AD612 HIS I 374 CYS I 378 0 SHEET 8 AD612 GLU I 381 CYS I 385 -1 O CYS I 385 N HIS I 374 SHEET 9 AD612 SER I 393 TRP I 395 -1 O SER I 393 N PHE I 361 SHEET 10 AD612 SER I 413 ILE I 420 -1 O ARG I 419 N TYR I 384 SHEET 11 AD612 GLY I 441 ARG I 456 -1 O THR I 450 N PHE I 288 SHEET 12 AD612 THR I 465 PRO I 470 -1 O ARG I 469 N THR I 455 SHEET 1 AD7 5 GLY K 10 VAL K 12 0 SHEET 2 AD7 5 THR K 122 VAL K 126 1 O THR K 125 N GLY K 10 SHEET 3 AD7 5 ALA K 92 ARG K 98 -1 N TYR K 94 O THR K 122 SHEET 4 AD7 5 THR K 34 GLN K 39 -1 N VAL K 37 O TYR K 95 SHEET 5 AD7 5 GLU K 46 ASP K 50 -1 O VAL K 48 N TRP K 36 SHEET 1 AD8 3 SER K 17 LEU K 20 0 SHEET 2 AD8 3 LEU K 78 ASN K 84 -1 O MET K 83 N LEU K 18 SHEET 3 AD8 3 PHE K 68 ASP K 73 -1 N SER K 71 O PHE K 80 SHEET 1 AD9 3 VAL L 3 LEU L 4 0 SHEET 2 AD9 3 SER L 100 GLY L 103 1 O PHE L 102 N LEU L 4 SHEET 3 AD9 3 GLN L 91 TYR L 93 -1 N SER L 92 O VAL L 101 SHEET 1 AE1 3 VAL L 18 SER L 21 0 SHEET 2 AE1 3 SER L 72 ILE L 77 -1 O ILE L 77 N VAL L 18 SHEET 3 AE1 3 SER L 65 SER L 69 -1 N SER L 69 O SER L 72 SHEET 1 AE2 3 ARG L 47 ILE L 48 0 SHEET 2 AE2 3 TYR L 38 GLN L 40 -1 N GLN L 39 O ARG L 47 SHEET 3 AE2 3 ASP L 87 TYR L 89 -1 O ASP L 87 N GLN L 40 SHEET 1 AE3 2 ILE L 50 TYR L 51 0 SHEET 2 AE3 2 SER L 55 ARG L 56 -1 O SER L 55 N TYR L 51 SSBOND 1 CYS A 54 CYS A 74 1555 1555 2.03 SSBOND 2 CYS A 119 CYS A 205 1555 1555 2.03 SSBOND 3 CYS A 126 CYS A 196 1555 1555 2.02 SSBOND 4 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 5 CYS A 218 CYS A 247 1555 1555 2.04 SSBOND 6 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 7 CYS A 296 CYS A 331 1555 1555 2.02 SSBOND 8 CYS A 378 CYS A 445 1555 1555 2.04 SSBOND 9 CYS A 385 CYS A 418 1555 1555 2.02 SSBOND 10 CYS A 501 CYS B 605 1555 1555 2.03 SSBOND 11 CYS B 598 CYS B 604 1555 1555 2.02 SSBOND 12 CYS C 22 CYS C 96 1555 1555 2.04 SSBOND 13 CYS D 22 CYS D 90 1555 1555 2.03 SSBOND 14 CYS E 54 CYS E 74 1555 1555 2.03 SSBOND 15 CYS E 119 CYS E 205 1555 1555 2.04 SSBOND 16 CYS E 126 CYS E 196 1555 1555 2.02 SSBOND 17 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 18 CYS E 218 CYS E 247 1555 1555 2.04 SSBOND 19 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 20 CYS E 296 CYS E 331 1555 1555 2.02 SSBOND 21 CYS E 378 CYS E 445 1555 1555 2.04 SSBOND 22 CYS E 385 CYS E 418 1555 1555 2.02 SSBOND 23 CYS E 501 CYS F 605 1555 1555 2.23 SSBOND 24 CYS F 598 CYS F 604 1555 1555 2.02 SSBOND 25 CYS G 22 CYS G 96 1555 1555 2.03 SSBOND 26 CYS H 22 CYS H 90 1555 1555 2.03 SSBOND 27 CYS I 54 CYS I 74 1555 1555 2.03 SSBOND 28 CYS I 119 CYS I 205 1555 1555 2.03 SSBOND 29 CYS I 126 CYS I 196 1555 1555 2.02 SSBOND 30 CYS I 131 CYS I 157 1555 1555 2.03 SSBOND 31 CYS I 218 CYS I 247 1555 1555 2.04 SSBOND 32 CYS I 228 CYS I 239 1555 1555 2.03 SSBOND 33 CYS I 296 CYS I 331 1555 1555 2.02 SSBOND 34 CYS I 378 CYS I 445 1555 1555 2.04 SSBOND 35 CYS I 385 CYS I 418 1555 1555 2.02 SSBOND 36 CYS I 501 CYS J 605 1555 1555 1.80 SSBOND 37 CYS J 598 CYS J 604 1555 1555 2.02 SSBOND 38 CYS K 22 CYS K 96 1555 1555 2.03 SSBOND 39 CYS L 22 CYS L 90 1555 1555 2.03 LINK ND2 ASN A 88 C1 NAG M 1 1555 1555 1.43 LINK ND2 ASN A 133 C1 NAG N 1 1555 1555 1.43 LINK ND2 ASN A 156 C1 NAG O 1 1555 1555 1.43 LINK ND2 ASN A 160 C1 NAG P 1 1555 1555 1.42 LINK ND2 ASN A 197 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN A 234 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN A 262 C1 NAG S 1 1555 1555 1.41 LINK ND2 ASN A 276 C1 NAG T 1 1555 1555 1.43 LINK ND2 ASN A 295 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN A 301 C1 NAG V 1 1555 1555 1.45 LINK ND2 ASN A 332 C1 NAG W 1 1555 1555 1.43 LINK ND2 ASN A 339 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 355 C1 NAG X 1 1555 1555 1.44 LINK ND2 ASN A 363 C1 NAG Y 1 1555 1555 1.43 LINK ND2 ASN A 386 C1 NAG Z 1 1555 1555 1.43 LINK ND2 ASN A 392 C1 NAG a 1 1555 1555 1.44 LINK ND2 ASN A 448 C1 NAG b 1 1555 1555 1.45 LINK ND2 ASN B 611 C1 NAG c 1 1555 1555 1.44 LINK ND2 ASN B 618 C1 NAG B 701 1555 1555 1.43 LINK ND2 ASN B 637 C1 NAG B 702 1555 1555 1.43 LINK ND2 ASN E 88 C1 NAG d 1 1555 1555 1.43 LINK ND2 ASN E 133 C1 NAG e 1 1555 1555 1.43 LINK ND2 ASN E 156 C1 NAG f 1 1555 1555 1.43 LINK ND2 ASN E 160 C1 NAG g 1 1555 1555 1.42 LINK ND2 ASN E 197 C1 NAG h 1 1555 1555 1.44 LINK ND2 ASN E 234 C1 NAG i 1 1555 1555 1.44 LINK ND2 ASN E 262 C1 NAG j 1 1555 1555 1.41 LINK ND2 ASN E 276 C1 NAG k 1 1555 1555 1.43 LINK ND2 ASN E 295 C1 NAG l 1 1555 1555 1.44 LINK ND2 ASN E 301 C1 NAG m 1 1555 1555 1.45 LINK ND2 ASN E 332 C1 NAG n 1 1555 1555 1.43 LINK ND2 ASN E 339 C1 NAG E 601 1555 1555 1.44 LINK ND2 ASN E 355 C1 NAG o 1 1555 1555 1.44 LINK ND2 ASN E 363 C1 NAG p 1 1555 1555 1.43 LINK ND2 ASN E 386 C1 NAG q 1 1555 1555 1.43 LINK ND2 ASN E 392 C1 NAG r 1 1555 1555 1.44 LINK ND2 ASN E 448 C1 NAG s 1 1555 1555 1.45 LINK ND2 ASN F 611 C1 NAG t 1 1555 1555 1.44 LINK ND2 ASN F 618 C1 NAG F 701 1555 1555 1.43 LINK ND2 ASN F 637 C1 NAG F 702 1555 1555 1.43 LINK ND2 ASN I 88 C1 NAG u 1 1555 1555 1.43 LINK ND2 ASN I 133 C1 NAG v 1 1555 1555 1.43 LINK ND2 ASN I 156 C1 NAG w 1 1555 1555 1.43 LINK ND2 ASN I 160 C1 NAG x 1 1555 1555 1.42 LINK ND2 ASN I 197 C1 NAG y 1 1555 1555 1.44 LINK ND2 ASN I 234 C1 NAG z 1 1555 1555 1.44 LINK ND2 ASN I 262 C1 NAG 0 1 1555 1555 1.41 LINK ND2 ASN I 276 C1 NAG 1 1 1555 1555 1.43 LINK ND2 ASN I 295 C1 NAG 2 1 1555 1555 1.44 LINK ND2 ASN I 301 C1 NAG 3 1 1555 1555 1.45 LINK ND2 ASN I 332 C1 NAG 4 1 1555 1555 1.43 LINK ND2 ASN I 339 C1 NAG I 601 1555 1555 1.44 LINK ND2 ASN I 355 C1 NAG 5 1 1555 1555 1.44 LINK ND2 ASN I 363 C1 NAG 6 1 1555 1555 1.43 LINK ND2 ASN I 386 C1 NAG 7 1 1555 1555 1.43 LINK ND2 ASN I 392 C1 NAG 8 1 1555 1555 1.44 LINK ND2 ASN I 448 C1 NAG 9 1 1555 1555 1.45 LINK ND2 ASN J 611 C1 NAGAA 1 1555 1555 1.44 LINK ND2 ASN J 618 C1 NAG J 701 1555 1555 1.43 LINK ND2 ASN J 637 C1 NAG J 702 1555 1555 1.43 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.45 LINK O4 NAG M 2 C1 BMA M 3 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.45 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.44 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44 LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.44 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.45 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.46 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.43 LINK O4 NAG S 2 C1 BMA S 3 1555 1555 1.44 LINK O3 BMA S 3 C1 MAN S 4 1555 1555 1.45 LINK O6 BMA S 3 C1 MAN S 6 1555 1555 1.44 LINK O2 MAN S 4 C1 MAN S 5 1555 1555 1.45 LINK O3 MAN S 6 C1 MAN S 7 1555 1555 1.44 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.44 LINK O4 NAG T 2 C1 BMA T 3 1555 1555 1.45 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.44 LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.44 LINK O3 BMA U 3 C1 MAN U 4 1555 1555 1.44 LINK O6 BMA U 3 C1 MAN U 5 1555 1555 1.44 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.47 LINK O4 NAG V 2 C1 BMA V 3 1555 1555 1.46 LINK O6 BMA V 3 C1 MAN V 4 1555 1555 1.42 LINK O3 BMA V 3 C1 MAN V 7 1555 1555 1.43 LINK O3 MAN V 4 C1 MAN V 5 1555 1555 1.45 LINK O6 MAN V 4 C1 MAN V 6 1555 1555 1.44 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.43 LINK O4 NAG W 2 C1 BMA W 3 1555 1555 1.44 LINK O3 BMA W 3 C1 MAN W 4 1555 1555 1.42 LINK O6 BMA W 3 C1 MAN W 6 1555 1555 1.45 LINK O2 MAN W 4 C1 MAN W 5 1555 1555 1.44 LINK O3 MAN W 6 C1 MAN W 7 1555 1555 1.43 LINK O6 MAN W 6 C1 MAN W 8 1555 1555 1.46 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.45 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.43 LINK O4 NAG Y 2 C1 BMA Y 3 1555 1555 1.45 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.44 LINK O4 NAG Z 2 C1 BMA Z 3 1555 1555 1.45 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.44 LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.43 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.45 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.45 LINK O4 NAG d 2 C1 BMA d 3 1555 1555 1.44 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.45 LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.44 LINK O4 NAG f 2 C1 BMA f 3 1555 1555 1.44 LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.44 LINK O4 NAG g 2 C1 BMA g 3 1555 1555 1.44 LINK O4 NAG h 1 C1 NAG h 2 1555 1555 1.45 LINK O4 NAG i 1 C1 NAG i 2 1555 1555 1.46 LINK O4 NAG j 1 C1 NAG j 2 1555 1555 1.43 LINK O4 NAG j 2 C1 BMA j 3 1555 1555 1.44 LINK O3 BMA j 3 C1 MAN j 4 1555 1555 1.45 LINK O6 BMA j 3 C1 MAN j 6 1555 1555 1.44 LINK O2 MAN j 4 C1 MAN j 5 1555 1555 1.44 LINK O3 MAN j 6 C1 MAN j 7 1555 1555 1.44 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 O4 NAG l 1 C1 NAG l 2 1555 1555 1.44 LINK O4 NAG l 2 C1 BMA l 3 1555 1555 1.44 LINK O3 BMA l 3 C1 MAN l 4 1555 1555 1.44 LINK O6 BMA l 3 C1 MAN l 5 1555 1555 1.44 LINK O4 NAG m 1 C1 NAG m 2 1555 1555 1.47 LINK O4 NAG m 2 C1 BMA m 3 1555 1555 1.46 LINK O6 BMA m 3 C1 MAN m 4 1555 1555 1.42 LINK O3 BMA m 3 C1 MAN m 7 1555 1555 1.43 LINK O3 MAN m 4 C1 MAN m 5 1555 1555 1.45 LINK O6 MAN m 4 C1 MAN m 6 1555 1555 1.44 LINK O4 NAG n 1 C1 NAG n 2 1555 1555 1.43 LINK O4 NAG n 2 C1 BMA n 3 1555 1555 1.44 LINK O3 BMA n 3 C1 MAN n 4 1555 1555 1.42 LINK O6 BMA n 3 C1 MAN n 6 1555 1555 1.45 LINK O2 MAN n 4 C1 MAN n 5 1555 1555 1.44 LINK O3 MAN n 6 C1 MAN n 7 1555 1555 1.43 LINK O6 MAN n 6 C1 MAN n 8 1555 1555 1.46 LINK O4 NAG o 1 C1 NAG o 2 1555 1555 1.45 LINK O4 NAG p 1 C1 NAG p 2 1555 1555 1.43 LINK O4 NAG p 2 C1 BMA p 3 1555 1555 1.45 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 r 1 C1 NAG r 2 1555 1555 1.44 LINK O4 NAG s 1 C1 NAG s 2 1555 1555 1.43 LINK O4 NAG t 1 C1 NAG t 2 1555 1555 1.45 LINK O4 NAG u 1 C1 NAG u 2 1555 1555 1.45 LINK O4 NAG u 2 C1 BMA u 3 1555 1555 1.44 LINK O4 NAG v 1 C1 NAG v 2 1555 1555 1.45 LINK O4 NAG w 1 C1 NAG w 2 1555 1555 1.44 LINK O4 NAG w 2 C1 BMA w 3 1555 1555 1.44 LINK O4 NAG x 1 C1 NAG x 2 1555 1555 1.44 LINK O4 NAG x 2 C1 BMA x 3 1555 1555 1.44 LINK O4 NAG y 1 C1 NAG y 2 1555 1555 1.45 LINK O4 NAG z 1 C1 NAG z 2 1555 1555 1.46 LINK O4 NAG 0 1 C1 NAG 0 2 1555 1555 1.43 LINK O4 NAG 0 2 C1 BMA 0 3 1555 1555 1.44 LINK O3 BMA 0 3 C1 MAN 0 4 1555 1555 1.45 LINK O6 BMA 0 3 C1 MAN 0 6 1555 1555 1.44 LINK O2 MAN 0 4 C1 MAN 0 5 1555 1555 1.44 LINK O3 MAN 0 6 C1 MAN 0 7 1555 1555 1.44 LINK O4 NAG 1 1 C1 NAG 1 2 1555 1555 1.44 LINK O4 NAG 1 2 C1 BMA 1 3 1555 1555 1.45 LINK O4 NAG 2 1 C1 NAG 2 2 1555 1555 1.44 LINK O4 NAG 2 2 C1 BMA 2 3 1555 1555 1.44 LINK O3 BMA 2 3 C1 MAN 2 4 1555 1555 1.44 LINK O6 BMA 2 3 C1 MAN 2 5 1555 1555 1.44 LINK O4 NAG 3 1 C1 NAG 3 2 1555 1555 1.47 LINK O4 NAG 3 2 C1 BMA 3 3 1555 1555 1.46 LINK O6 BMA 3 3 C1 MAN 3 4 1555 1555 1.43 LINK O3 BMA 3 3 C1 MAN 3 7 1555 1555 1.43 LINK O3 MAN 3 4 C1 MAN 3 5 1555 1555 1.45 LINK O6 MAN 3 4 C1 MAN 3 6 1555 1555 1.44 LINK O4 NAG 4 1 C1 NAG 4 2 1555 1555 1.43 LINK O4 NAG 4 2 C1 BMA 4 3 1555 1555 1.44 LINK O3 BMA 4 3 C1 MAN 4 4 1555 1555 1.42 LINK O6 BMA 4 3 C1 MAN 4 6 1555 1555 1.45 LINK O2 MAN 4 4 C1 MAN 4 5 1555 1555 1.43 LINK O3 MAN 4 6 C1 MAN 4 7 1555 1555 1.43 LINK O6 MAN 4 6 C1 MAN 4 8 1555 1555 1.46 LINK O4 NAG 5 1 C1 NAG 5 2 1555 1555 1.45 LINK O4 NAG 6 1 C1 NAG 6 2 1555 1555 1.43 LINK O4 NAG 6 2 C1 BMA 6 3 1555 1555 1.45 LINK O4 NAG 7 1 C1 NAG 7 2 1555 1555 1.44 LINK O4 NAG 7 2 C1 BMA 7 3 1555 1555 1.45 LINK O4 NAG 8 1 C1 NAG 8 2 1555 1555 1.44 LINK O4 NAG 9 1 C1 NAG 9 2 1555 1555 1.43 LINK O4 NAGAA 1 C1 NAGAA 2 1555 1555 1.45 CISPEP 1 ILE A 138 THR A 139 0 1.35 CISPEP 2 GLY A 312 PRO A 313 0 -3.15 CISPEP 3 ASN A 411 ASP A 412 0 -4.58 CISPEP 4 ILE E 138 THR E 139 0 1.42 CISPEP 5 GLY E 312 PRO E 313 0 -3.14 CISPEP 6 ASN E 411 ASP E 412 0 -4.53 CISPEP 7 ILE I 138 THR I 139 0 1.39 CISPEP 8 GLY I 312 PRO I 313 0 -3.21 CISPEP 9 ASN I 411 ASP I 412 0 -4.57 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