HEADER VIRAL PROTEIN 12-DEC-24 9MIH TITLE 273-4D01 FAB IN COMPLEX WITH HIV-1 BG505 SOSIP ENV TRIMER AND RM20A3 TITLE 2 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: 273-4D01 KAPPA CHAIN FV; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HIV-1 ENVELOPE GLYCOPROTEIN BG505 SOSIP.664 GP120; COMPND 7 CHAIN: A, C, E; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ENVELOPE GLYCOPROTEIN GP160; COMPND 11 CHAIN: B, D, F; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: RM20A3 HEAVY CHAIN FV; COMPND 15 CHAIN: G, J, M; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: RM20A3 LIGHT CHAIN FV; COMPND 19 CHAIN: I, K, N; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 6; COMPND 22 MOLECULE: 273-4D01 HEAVY CHAIN FV; COMPND 23 CHAIN: H; COMPND 24 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 8 ORGANISM_TAXID: 11676; SOURCE 9 GENE: ENV; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 14 ORGANISM_TAXID: 11676; SOURCE 15 GENE: ENV; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 20 ORGANISM_TAXID: 9544; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 23 MOL_ID: 5; SOURCE 24 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 25 ORGANISM_TAXID: 9544; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 28 MOL_ID: 6; SOURCE 29 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 30 ORGANISM_TAXID: 11676; SOURCE 31 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV-1, SOSIP, GERMLINE TARGETING, VRC01, CLINICAL TRIAL, PRECURSOR KEYWDS 2 ANTIBODY, VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR S.PHULERA,G.OZOROWSKI,A.B.WARD REVDAT 1 21-MAY-25 9MIH 0 JRNL AUTH T.G.CANIELS,M.PRABHAKARAN,G.OZOROWSKI,K.J.MACPHEE,W.WU, JRNL AUTH 2 K.VAN DER STRATEN,S.AGRAWAL,R.DERKING,E.I.M.M.REISS, JRNL AUTH 3 K.MILLARD,M.TURROJA,A.DESROSIERS,J.BETHONY,E.MALKIN, JRNL AUTH 4 M.H.LIESDEK,A.VAN DER VEEN,M.KLOUWENS,S.PHULERA,I.A.WILSON, JRNL AUTH 5 A.B.WARD JRNL TITL PRECISE TARGETING OF HIV BROADLY NEUTRALIZING ANTIBODY JRNL TITL 2 PRECURSORS IN HUMANS JRNL REF SCIENCE 2025 JRNL REFN ESSN 1095-9203 JRNL DOI 10.1126/SCIENCE.ADV5572 REMARK 2 REMARK 2 RESOLUTION. 3.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, UCSF CHIMERAX, PHENIX, REMARK 3 CRYOSPARC, CRYOSPARC, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.900 REMARK 3 NUMBER OF PARTICLES : 13058 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 9MIH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1000291041. 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 : 273-4D01 FAB IN COMPLEX WITH REMARK 245 HIV-1 BG505 SOSIP ENV TRIMER REMARK 245 AND RM20A3 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 3.40 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 7000 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS GLACIOS REMARK 245 DETECTOR TYPE : TFS FALCON 4I (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 700.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 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) : 4530.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 190000 REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 200 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 14-MERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 14-MERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, A, B, G, I, C, D, J, K, E, REMARK 350 AND CHAINS: F, M, N, H, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V 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 ASP L 1 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 ASP A 57 REMARK 465 ALA A 58 REMARK 465 LYS A 59 REMARK 465 ALA A 60 REMARK 465 TYR A 61 REMARK 465 GLU A 62 REMARK 465 THR A 63 REMARK 465 GLU A 64 REMARK 465 LYS A 65 REMARK 465 HIS A 66 REMARK 465 ASN A 67 REMARK 465 VAL A 68 REMARK 465 TRP A 69 REMARK 465 ALA A 70 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 ASN A 185K REMARK 465 ASN A 399 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 ASN A 411 REMARK 465 ARG A 504 REMARK 465 VAL A 505 REMARK 465 VAL A 506 REMARK 465 GLY A 507 REMARK 465 ARG A 508 REMARK 465 ARG A 509 REMARK 465 ARG A 510 REMARK 465 ARG A 511 REMARK 465 ARG A 512 REMARK 465 ARG A 513 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 SER B 546 REMARK 465 GLY B 547 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 LEU B 568 REMARK 465 SER G 113 REMARK 465 GLY I 108 REMARK 465 GLN I 109 REMARK 465 PRO I 110 REMARK 465 LYS I 111 REMARK 465 ALA I 112 REMARK 465 SER I 113 REMARK 465 PRO I 114 REMARK 465 THR I 115 REMARK 465 VAL I 116 REMARK 465 THR I 117 REMARK 465 LEU I 118 REMARK 465 PHE I 119 REMARK 465 PRO I 120 REMARK 465 PRO I 121 REMARK 465 SER I 122 REMARK 465 SER I 123 REMARK 465 GLU I 124 REMARK 465 GLU I 125 REMARK 465 LEU I 126 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 ASP C 57 REMARK 465 ALA C 58 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 LYS C 65 REMARK 465 HIS C 66 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 SER C 398 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 ASN C 411 REMARK 465 GLY C 458 REMARK 465 GLY C 459 REMARK 465 SER C 460 REMARK 465 THR C 461 REMARK 465 ASN C 462 REMARK 465 ARG C 504 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 D 512 REMARK 465 VAL D 513 REMARK 465 GLY D 514 REMARK 465 ILE D 515 REMARK 465 GLY D 516 REMARK 465 ALA D 517 REMARK 465 VAL D 518 REMARK 465 PHE D 519 REMARK 465 GLY D 547 REMARK 465 ILE D 548 REMARK 465 VAL D 549 REMARK 465 GLN D 550 REMARK 465 GLN D 551 REMARK 465 GLN D 552 REMARK 465 SER D 553 REMARK 465 ASN D 554 REMARK 465 LEU D 555 REMARK 465 LEU D 556 REMARK 465 ARG D 557 REMARK 465 ALA D 558 REMARK 465 PRO D 559 REMARK 465 GLU D 560 REMARK 465 ALA D 561 REMARK 465 GLN D 562 REMARK 465 GLN D 563 REMARK 465 HIS D 564 REMARK 465 LEU D 565 REMARK 465 LEU D 566 REMARK 465 LYS D 567 REMARK 465 LEU D 568 REMARK 465 SER J 113 REMARK 465 GLY K 108 REMARK 465 GLN K 109 REMARK 465 PRO K 110 REMARK 465 LYS K 111 REMARK 465 ALA K 112 REMARK 465 SER K 113 REMARK 465 PRO K 114 REMARK 465 THR K 115 REMARK 465 VAL K 116 REMARK 465 THR K 117 REMARK 465 LEU K 118 REMARK 465 PHE K 119 REMARK 465 PRO K 120 REMARK 465 PRO K 121 REMARK 465 SER K 122 REMARK 465 SER K 123 REMARK 465 GLU K 124 REMARK 465 GLU K 125 REMARK 465 LEU K 126 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 ASP E 57 REMARK 465 ALA E 58 REMARK 465 LYS E 59 REMARK 465 ALA E 60 REMARK 465 TYR E 61 REMARK 465 GLU E 62 REMARK 465 THR E 63 REMARK 465 GLU E 64 REMARK 465 LYS E 65 REMARK 465 HIS E 66 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 ASN E 185K REMARK 465 SER E 398 REMARK 465 ASN E 399 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 ASN E 411 REMARK 465 GLY E 459 REMARK 465 SER E 460 REMARK 465 THR E 461 REMARK 465 ASN E 462 REMARK 465 ARG E 504 REMARK 465 VAL E 505 REMARK 465 VAL E 506 REMARK 465 GLY E 507 REMARK 465 ARG E 508 REMARK 465 ARG E 509 REMARK 465 ARG E 510 REMARK 465 ARG E 511 REMARK 465 ARG E 512 REMARK 465 ARG E 513 REMARK 465 ALA F 512 REMARK 465 VAL F 513 REMARK 465 GLY F 514 REMARK 465 ILE F 515 REMARK 465 GLY F 516 REMARK 465 ALA F 517 REMARK 465 VAL F 518 REMARK 465 PHE F 519 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 LEU F 568 REMARK 465 SER M 113 REMARK 465 GLY N 108 REMARK 465 GLN N 109 REMARK 465 PRO N 110 REMARK 465 LYS N 111 REMARK 465 ALA N 112 REMARK 465 SER N 113 REMARK 465 PRO N 114 REMARK 465 THR N 115 REMARK 465 VAL N 116 REMARK 465 THR N 117 REMARK 465 LEU N 118 REMARK 465 PHE N 119 REMARK 465 PRO N 120 REMARK 465 PRO N 121 REMARK 465 SER N 122 REMARK 465 SER N 123 REMARK 465 GLU N 124 REMARK 465 GLU N 125 REMARK 465 LEU N 126 REMARK 465 SER H 112 REMARK 465 SER H 113 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 SG CYS E 378 SG CYS E 445 1.24 REMARK 500 O LEU F 663 OD1 ASP F 664 1.77 REMARK 500 NH2 ARG K 94 OD2 ASP F 664 1.80 REMARK 500 OD2 ASP E 107 OH TYR E 217 2.09 REMARK 500 OH TYR L 32 OE1 GLU H 99 2.11 REMARK 500 OE1 GLU L 96 ND2 ASN A 280 2.13 REMARK 500 O GLY M 96 OH TYR N 96 2.13 REMARK 500 O VAL A 36 OG1 THR B 606 2.14 REMARK 500 OE1 GLN K 6 OG1 THR K 102 2.15 REMARK 500 O ASN A 363 NH1 ARG A 469 2.16 REMARK 500 O3 NAG P 1 O5 NAG P 2 2.18 REMARK 500 N GLY J 96 O TYR J 100G 2.19 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 ASP I 27B CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES REMARK 500 ASP I 60 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES REMARK 500 ASP F 659 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES REMARK 500 ASP M 101 CB - CG - OD1 ANGL. DEV. = 7.0 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 GLN L 27 -166.12 -123.60 REMARK 500 SER L 30 -140.21 56.14 REMARK 500 TYR L 32 94.41 -68.74 REMARK 500 ALA L 51 -129.87 58.57 REMARK 500 ALA L 84 -178.57 -172.56 REMARK 500 TYR L 91 -134.98 52.32 REMARK 500 GLU L 96 45.78 -91.89 REMARK 500 PHE L 98 139.95 -33.74 REMARK 500 PRO A 118 46.12 -84.29 REMARK 500 THR A 163 -169.89 -115.79 REMARK 500 LEU A 175 52.51 -140.23 REMARK 500 HIS A 249 -165.63 -77.78 REMARK 500 GLN A 258 -7.56 71.91 REMARK 500 LEU A 259 108.73 -163.54 REMARK 500 ASN A 262 176.78 66.65 REMARK 500 ASN A 280 19.71 54.10 REMARK 500 ASN A 425 57.55 -91.06 REMARK 500 GLN A 428 42.62 37.78 REMARK 500 SER A 460 -60.90 68.72 REMARK 500 ASN A 462 -129.23 52.05 REMARK 500 LEU G 11 103.12 -161.83 REMARK 500 PRO G 41 78.04 -69.69 REMARK 500 VAL G 48 -61.75 -100.77 REMARK 500 SER G 82B -65.83 61.42 REMARK 500 LEU G 82C 165.62 79.96 REMARK 500 ALA G 88 168.22 179.54 REMARK 500 LYS G 100E -68.69 -109.91 REMARK 500 ASP I 50 -179.76 59.57 REMARK 500 ASP I 82 45.08 -89.58 REMARK 500 ASN C 80 81.81 -151.16 REMARK 500 THR C 135 37.38 -140.45 REMARK 500 SER C 241 61.38 63.44 REMARK 500 GLN C 258 -6.26 69.21 REMARK 500 LEU C 259 103.97 -161.24 REMARK 500 THR C 387 29.34 48.39 REMARK 500 TRP C 395 -0.74 74.02 REMARK 500 TRP C 427 -143.37 60.69 REMARK 500 LYS C 487 141.68 -171.49 REMARK 500 ALA D 525 52.63 -93.69 REMARK 500 SER J 82B -69.95 64.07 REMARK 500 ALA J 100 -6.02 77.42 REMARK 500 LYS J 100E -68.72 -92.86 REMARK 500 ASP K 50 179.78 71.22 REMARK 500 SER K 76 -146.57 58.26 REMARK 500 LEU E 122 53.04 -91.73 REMARK 500 ASP E 141 -7.73 78.39 REMARK 500 GLN E 258 -5.37 71.04 REMARK 500 LEU E 259 127.81 -170.20 REMARK 500 ILE E 309 -63.36 -121.03 REMARK 500 SER E 365 -165.10 -79.47 REMARK 500 REMARK 500 THIS ENTRY HAS 69 RAMACHANDRAN OUTLIERS. 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 C 602 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-48290 RELATED DB: EMDB REMARK 900 273-4D01 FAB IN COMPLEX WITH HIV-1 BG505 SOSIP ENV TRIMER AND REMARK 900 RM20A3 FAB DBREF 9MIH L 1 107 PDB 9MIH 9MIH 1 107 DBREF 9MIH A 31 508 UNP Q2N0S6 Q2N0S6_9HIV1 30 505 DBREF 9MIH B 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 9MIH G 1 113 PDB 9MIH 9MIH 1 113 DBREF 9MIH I 3 126 PDB 9MIH 9MIH 3 126 DBREF 9MIH C 31 508 UNP Q2N0S6 Q2N0S6_9HIV1 30 505 DBREF 9MIH D 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 9MIH J 1 113 PDB 9MIH 9MIH 1 113 DBREF 9MIH K 3 126 PDB 9MIH 9MIH 3 126 DBREF 9MIH E 31 508 UNP Q2N0S6 Q2N0S6_9HIV1 30 505 DBREF 9MIH F 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 9MIH M 1 113 PDB 9MIH 9MIH 1 113 DBREF 9MIH N 3 126 PDB 9MIH 9MIH 3 126 DBREF 9MIH H 1 113 PDB 9MIH 9MIH 1 113 SEQADV 9MIH MET A -4 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ASP A -3 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ALA A -2 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH MET A -1 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH LYS A 0 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG A 1 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH GLY A 2 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH LEU A 3 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH CYS A 4 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH CYS A 5 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH VAL A 6 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH LEU A 7 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH LEU A 8 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH LEU A 9 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH CYS A 10 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH GLY A 11 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ALA A 12 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH VAL A 13 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH PHE A 14 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH VAL A 15 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH SER A 16 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH PRO A 17 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH SER A 18 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH GLN A 19 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH GLU A 20 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ILE A 21 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH HIS A 22 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ALA A 23 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG A 24 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH PHE A 25 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG A 26 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG A 27 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH GLY A 28 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ALA A 29 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG A 30 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ASN A 332 UNP Q2N0S6 THR 330 ENGINEERED MUTATION SEQADV 9MIH CYS A 501 UNP Q2N0S6 ALA 498 ENGINEERED MUTATION SEQADV 9MIH ARG A 509 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG A 510 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG A 511 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG A 512 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG A 513 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH PRO B 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 9MIH CYS B 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 9MIH MET C -4 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ASP C -3 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ALA C -2 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH MET C -1 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH LYS C 0 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG C 1 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH GLY C 2 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH LEU C 3 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH CYS C 4 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH CYS C 5 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH VAL C 6 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH LEU C 7 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH LEU C 8 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH LEU C 9 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH CYS C 10 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH GLY C 11 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ALA C 12 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH VAL C 13 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH PHE C 14 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH VAL C 15 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH SER C 16 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH PRO C 17 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH SER C 18 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH GLN C 19 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH GLU C 20 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ILE C 21 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH HIS C 22 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ALA C 23 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG C 24 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH PHE C 25 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG C 26 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG C 27 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH GLY C 28 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ALA C 29 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG C 30 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ASN C 332 UNP Q2N0S6 THR 330 ENGINEERED MUTATION SEQADV 9MIH CYS C 501 UNP Q2N0S6 ALA 498 ENGINEERED MUTATION SEQADV 9MIH ARG C 509 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG C 510 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG C 511 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG C 512 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG C 513 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH PRO D 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 9MIH CYS D 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 9MIH MET E -4 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ASP E -3 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ALA E -2 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH MET E -1 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH LYS E 0 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG E 1 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH GLY E 2 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH LEU E 3 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH CYS E 4 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH CYS E 5 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH VAL E 6 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH LEU E 7 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH LEU E 8 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH LEU E 9 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH CYS E 10 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH GLY E 11 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ALA E 12 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH VAL E 13 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH PHE E 14 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH VAL E 15 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH SER E 16 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH PRO E 17 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH SER E 18 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH GLN E 19 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH GLU E 20 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ILE E 21 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH HIS E 22 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ALA E 23 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG E 24 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH PHE E 25 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG E 26 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG E 27 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH GLY E 28 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ALA E 29 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG E 30 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ASN E 332 UNP Q2N0S6 THR 330 ENGINEERED MUTATION SEQADV 9MIH CYS E 501 UNP Q2N0S6 ALA 498 ENGINEERED MUTATION SEQADV 9MIH ARG E 509 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG E 510 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG E 511 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG E 512 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH ARG E 513 UNP Q2N0S6 EXPRESSION TAG SEQADV 9MIH PRO F 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 9MIH CYS F 605 UNP Q2N0S6 THR 602 CONFLICT SEQRES 1 L 103 ASP ILE GLN VAL THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 103 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 103 GLN GLY ILE SER ASN TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 103 PRO GLY LYS VAL PRO LYS LEU LEU ILE TYR GLY ALA SER SEQRES 5 L 103 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 103 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 103 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN ILE TYR SEQRES 8 L 103 GLU THR PHE GLY GLN GLY THR LYS VAL ASP ILE LYS SEQRES 1 A 516 MET ASP ALA MET LYS ARG GLY LEU CYS CYS VAL LEU LEU SEQRES 2 A 516 LEU CYS GLY ALA VAL PHE VAL SER PRO SER GLN GLU ILE SEQRES 3 A 516 HIS ALA ARG PHE ARG ARG GLY ALA ARG ALA GLU ASN LEU SEQRES 4 A 516 TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP LYS ASP SEQRES 5 A 516 ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA LYS ALA SEQRES 6 A 516 TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR HIS ALA SEQRES 7 A 516 CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE HIS LEU SEQRES 8 A 516 GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS ASN ASN SEQRES 9 A 516 MET VAL GLU GLN MET HIS THR ASP ILE ILE SER LEU TRP SEQRES 10 A 516 ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR PRO LEU SEQRES 11 A 516 CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN ASN ILE SEQRES 12 A 516 THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SER PHE SEQRES 13 A 516 ASN MET THR THR GLU LEU ARG ASP LYS LYS GLN LYS VAL SEQRES 14 A 516 TYR SER LEU PHE TYR ARG LEU ASP VAL VAL GLN ILE ASN SEQRES 15 A 516 GLU ASN GLN GLY ASN ARG SER ASN ASN SER ASN LYS GLU SEQRES 16 A 516 TYR ARG LEU ILE ASN CYS ASN THR SER ALA ILE THR GLN SEQRES 17 A 516 ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE HIS SEQRES 18 A 516 TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS SEQRES 19 A 516 ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SER VAL SEQRES 20 A 516 SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SEQRES 21 A 516 SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU GLU SEQRES 22 A 516 GLU VAL MET ILE ARG SER GLU ASN ILE THR ASN ASN ALA SEQRES 23 A 516 LYS ASN ILE LEU VAL GLN PHE ASN THR PRO VAL GLN ILE SEQRES 24 A 516 ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SER ILE SEQRES 25 A 516 ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA THR GLY ASP SEQRES 26 A 516 ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN VAL SER SEQRES 27 A 516 LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL VAL LYS SEQRES 28 A 516 GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE ILE ARG SEQRES 29 A 516 PHE ALA ASN SER SER GLY GLY ASP LEU GLU VAL THR THR SEQRES 30 A 516 HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN SEQRES 31 A 516 THR SER GLY LEU PHE ASN SER THR TRP ILE SER ASN THR SEQRES 32 A 516 SER VAL GLN GLY SER ASN SER THR GLY SER ASN ASP SER SEQRES 33 A 516 ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE ASN MET SEQRES 34 A 516 TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO PRO ILE SEQRES 35 A 516 GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR GLY LEU SEQRES 36 A 516 ILE LEU THR ARG ASP GLY GLY SER THR ASN SER THR THR SEQRES 37 A 516 GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG ASP ASN SEQRES 38 A 516 TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE SEQRES 39 A 516 GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS ARG ARG SEQRES 40 A 516 VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 B 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 B 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 B 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 B 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 B 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 B 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 B 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 B 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 B 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 B 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 B 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 B 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 G 125 GLU VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 G 125 PRO GLY GLY SER LEU LYS LEU SER CYS ARG ALA SER GLY SEQRES 3 G 125 TYR THR PHE SER SER PHE ALA MET SER TRP VAL ARG GLN SEQRES 4 G 125 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER LEU ILE ASN SEQRES 5 G 125 ASP ARG GLY GLY LEU THR PHE TYR VAL ASP SER VAL LYS SEQRES 6 G 125 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 G 125 LEU SER LEU GLN MET HIS SER LEU ARG ASP GLY ASP THR SEQRES 8 G 125 ALA VAL TYR TYR CYS ALA THR GLY GLY MET SER SER ALA SEQRES 9 G 125 LEU GLN SER SER LYS TYR TYR PHE ASP PHE TRP GLY GLN SEQRES 10 G 125 GLY ALA LEU VAL THR VAL SER SER SEQRES 1 I 128 ALA LEU THR GLN PRO PRO SER VAL SER GLY SER PRO GLY SEQRES 2 I 128 GLN SER VAL THR ILE SER CYS THR GLY THR SER SER ASP SEQRES 3 I 128 ILE GLY SER TYR ASN TYR VAL SER TRP TYR GLN GLN HIS SEQRES 4 I 128 PRO GLY LYS ALA PRO LYS LEU MET ILE TYR ASP VAL THR SEQRES 5 I 128 GLN ARG PRO SER GLY VAL SER ASP ARG PHE SER GLY SER SEQRES 6 I 128 LYS SER GLY ASN THR ALA SER LEU THR ILE SER GLY LEU SEQRES 7 I 128 GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS SER ALA TYR SEQRES 8 I 128 ALA GLY ARG GLN THR PHE TYR ILE PHE GLY GLY GLY THR SEQRES 9 I 128 ARG LEU THR VAL LEU GLY GLN PRO LYS ALA SER PRO THR SEQRES 10 I 128 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU 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 D 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 D 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 D 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 D 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 D 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 D 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 D 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 D 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 D 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 D 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 D 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 D 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 J 125 GLU VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 J 125 PRO GLY GLY SER LEU LYS LEU SER CYS ARG ALA SER GLY SEQRES 3 J 125 TYR THR PHE SER SER PHE ALA MET SER TRP VAL ARG GLN SEQRES 4 J 125 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER LEU ILE ASN SEQRES 5 J 125 ASP ARG GLY GLY LEU THR PHE TYR VAL ASP SER VAL LYS SEQRES 6 J 125 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 J 125 LEU SER LEU GLN MET HIS SER LEU ARG ASP GLY ASP THR SEQRES 8 J 125 ALA VAL TYR TYR CYS ALA THR GLY GLY MET SER SER ALA SEQRES 9 J 125 LEU GLN SER SER LYS TYR TYR PHE ASP PHE TRP GLY GLN SEQRES 10 J 125 GLY ALA LEU VAL THR VAL SER SER SEQRES 1 K 128 ALA LEU THR GLN PRO PRO SER VAL SER GLY SER PRO GLY SEQRES 2 K 128 GLN SER VAL THR ILE SER CYS THR GLY THR SER SER ASP SEQRES 3 K 128 ILE GLY SER TYR ASN TYR VAL SER TRP TYR GLN GLN HIS SEQRES 4 K 128 PRO GLY LYS ALA PRO LYS LEU MET ILE TYR ASP VAL THR SEQRES 5 K 128 GLN ARG PRO SER GLY VAL SER ASP ARG PHE SER GLY SER SEQRES 6 K 128 LYS SER GLY ASN THR ALA SER LEU THR ILE SER GLY LEU SEQRES 7 K 128 GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS SER ALA TYR SEQRES 8 K 128 ALA GLY ARG GLN THR PHE TYR ILE PHE GLY GLY GLY THR SEQRES 9 K 128 ARG LEU THR VAL LEU GLY GLN PRO LYS ALA SER PRO THR SEQRES 10 K 128 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 1 E 516 MET ASP ALA MET LYS ARG GLY LEU CYS CYS VAL LEU LEU SEQRES 2 E 516 LEU CYS GLY ALA VAL PHE VAL SER PRO SER GLN GLU ILE SEQRES 3 E 516 HIS ALA ARG PHE ARG ARG GLY ALA ARG ALA GLU ASN LEU SEQRES 4 E 516 TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP LYS ASP SEQRES 5 E 516 ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA LYS ALA SEQRES 6 E 516 TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR HIS ALA SEQRES 7 E 516 CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE HIS LEU SEQRES 8 E 516 GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS ASN ASN SEQRES 9 E 516 MET VAL GLU GLN MET HIS THR ASP ILE ILE SER LEU TRP SEQRES 10 E 516 ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR PRO LEU SEQRES 11 E 516 CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN ASN ILE SEQRES 12 E 516 THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SER PHE SEQRES 13 E 516 ASN MET THR THR GLU LEU ARG ASP LYS LYS GLN LYS VAL SEQRES 14 E 516 TYR SER LEU PHE TYR ARG LEU ASP VAL VAL GLN ILE ASN SEQRES 15 E 516 GLU ASN GLN GLY ASN ARG SER ASN ASN SER ASN LYS GLU SEQRES 16 E 516 TYR ARG LEU ILE ASN CYS ASN THR SER ALA ILE THR GLN SEQRES 17 E 516 ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE HIS SEQRES 18 E 516 TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS SEQRES 19 E 516 ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SER VAL SEQRES 20 E 516 SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SEQRES 21 E 516 SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU GLU SEQRES 22 E 516 GLU VAL MET ILE ARG SER GLU ASN ILE THR ASN ASN ALA SEQRES 23 E 516 LYS ASN ILE LEU VAL GLN PHE ASN THR PRO VAL GLN ILE SEQRES 24 E 516 ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SER ILE SEQRES 25 E 516 ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA THR GLY ASP SEQRES 26 E 516 ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN VAL SER SEQRES 27 E 516 LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL VAL LYS SEQRES 28 E 516 GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE ILE ARG SEQRES 29 E 516 PHE ALA ASN SER SER GLY GLY ASP LEU GLU VAL THR THR SEQRES 30 E 516 HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN SEQRES 31 E 516 THR SER GLY LEU PHE ASN SER THR TRP ILE SER ASN THR SEQRES 32 E 516 SER VAL GLN GLY SER ASN SER THR GLY SER ASN ASP SER SEQRES 33 E 516 ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE ASN MET SEQRES 34 E 516 TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO PRO ILE SEQRES 35 E 516 GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR GLY LEU SEQRES 36 E 516 ILE LEU THR ARG ASP GLY GLY SER THR ASN SER THR THR SEQRES 37 E 516 GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG ASP ASN SEQRES 38 E 516 TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE SEQRES 39 E 516 GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS ARG ARG SEQRES 40 E 516 VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 F 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 F 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 F 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 F 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 F 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 F 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 F 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 F 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 F 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 F 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 F 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 F 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 M 125 GLU VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 M 125 PRO GLY GLY SER LEU LYS LEU SER CYS ARG ALA SER GLY SEQRES 3 M 125 TYR THR PHE SER SER PHE ALA MET SER TRP VAL ARG GLN SEQRES 4 M 125 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER LEU ILE ASN SEQRES 5 M 125 ASP ARG GLY GLY LEU THR PHE TYR VAL ASP SER VAL LYS SEQRES 6 M 125 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 M 125 LEU SER LEU GLN MET HIS SER LEU ARG ASP GLY ASP THR SEQRES 8 M 125 ALA VAL TYR TYR CYS ALA THR GLY GLY MET SER SER ALA SEQRES 9 M 125 LEU GLN SER SER LYS TYR TYR PHE ASP PHE TRP GLY GLN SEQRES 10 M 125 GLY ALA LEU VAL THR VAL SER SER SEQRES 1 N 128 ALA LEU THR GLN PRO PRO SER VAL SER GLY SER PRO GLY SEQRES 2 N 128 GLN SER VAL THR ILE SER CYS THR GLY THR SER SER ASP SEQRES 3 N 128 ILE GLY SER TYR ASN TYR VAL SER TRP TYR GLN GLN HIS SEQRES 4 N 128 PRO GLY LYS ALA PRO LYS LEU MET ILE TYR ASP VAL THR SEQRES 5 N 128 GLN ARG PRO SER GLY VAL SER ASP ARG PHE SER GLY SER SEQRES 6 N 128 LYS SER GLY ASN THR ALA SER LEU THR ILE SER GLY LEU SEQRES 7 N 128 GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS SER ALA TYR SEQRES 8 N 128 ALA GLY ARG GLN THR PHE TYR ILE PHE GLY GLY GLY THR SEQRES 9 N 128 ARG LEU THR VAL LEU GLY GLN PRO LYS ALA SER PRO THR SEQRES 10 N 128 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 1 H 120 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 120 PRO GLY ALA SER VAL LYS VAL SER CYS LYS THR SER GLY SEQRES 3 H 120 TYR THR PHE THR ASP PHE TYR MET HIS TRP MET ARG GLN SEQRES 4 H 120 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 H 120 PRO THR GLY GLY GLY VAL ASN TYR ALA HIS LYS PHE GLN SEQRES 6 H 120 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 H 120 ALA TYR MET GLU LEU SER ARG LEU THR SER ASP ASP THR SEQRES 8 H 120 GLY VAL TYR TYR CYS ALA ARG SER PRO ALA ARG GLU LEU SEQRES 9 H 120 LEU PRO LEU ASP TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 H 120 VAL SER SER HET NAG O 1 14 HET NAG O 2 14 HET NAG P 1 14 HET NAG P 2 14 HET NAG Q 1 14 HET NAG Q 2 14 HET NAG R 1 14 HET NAG R 2 14 HET BMA R 3 11 HET NAG S 1 14 HET NAG S 2 14 HET NAG T 1 14 HET NAG T 2 14 HET NAG U 1 14 HET NAG U 2 14 HET BMA U 3 11 HET MAN U 4 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 NAG A 601 14 HET NAG A 602 14 HET NAG A 603 14 HET NAG A 604 14 HET NAG A 605 14 HET NAG A 606 14 HET NAG A 607 14 HET NAG A 608 14 HET NAG A 609 14 HET NAG A 610 14 HET NAG A 611 14 HET NAG B 701 14 HET NAG C 601 14 HET NAG C 602 14 HET NAG C 603 14 HET NAG C 604 14 HET NAG C 605 14 HET NAG C 606 14 HET NAG C 607 14 HET NAG C 608 14 HET NAG C 609 14 HET NAG C 610 14 HET NAG C 611 14 HET NAG C 612 14 HET NAG C 613 14 HET NAG C 614 14 HET NAG C 615 14 HET NAG D 701 14 HET NAG D 702 14 HET NAG E 601 14 HET NAG E 602 14 HET NAG E 603 14 HET NAG E 604 14 HET NAG E 605 14 HET NAG E 606 14 HET NAG E 607 14 HET NAG E 608 14 HET NAG E 609 14 HET NAG E 610 14 HET NAG E 611 14 HET NAG E 612 14 HET NAG F 701 14 HET NAG F 702 14 HET NAG F 703 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 15 NAG 60(C8 H15 N O6) FORMUL 18 BMA 3(C6 H12 O6) FORMUL 21 MAN 3(C6 H12 O6) HELIX 1 AA1 ASN A 99 LYS A 117 1 19 HELIX 2 AA2 TYR A 177 LEU A 179 5 3 HELIX 3 AA3 ASN A 195 ASN A 197 5 3 HELIX 4 AA4 LYS A 335 GLY A 354 1 20 HELIX 5 AA5 ASP A 368 THR A 373 1 6 HELIX 6 AA6 THR A 387 LEU A 390 5 4 HELIX 7 AA7 ASN A 425 ARG A 429 5 5 HELIX 8 AA8 ASP A 474 SER A 481 1 8 HELIX 9 AA9 THR B 529 MET B 535 1 7 HELIX 10 AB1 THR B 536 ASN B 543 1 8 HELIX 11 AB2 TRP B 571 ILE B 595 1 25 HELIX 12 AB3 ASN B 618 ASN B 625 1 8 HELIX 13 AB4 THR B 627 ILE B 635 1 9 HELIX 14 AB5 TYR B 638 LEU B 663 1 26 HELIX 15 AB6 ARG G 83 THR G 87 5 5 HELIX 16 AB7 ASN C 98 LYS C 117 1 20 HELIX 17 AB8 LEU C 122 CYS C 126 5 5 HELIX 18 AB9 ASN C 195 THR C 198 5 4 HELIX 19 AC1 LYS C 335 ARG C 350 1 16 HELIX 20 AC2 ASP C 368 THR C 373 1 6 HELIX 21 AC3 SER C 388 ASN C 392 5 5 HELIX 22 AC4 ASP C 474 LEU C 483 1 10 HELIX 23 AC5 THR D 529 THR D 536 1 8 HELIX 24 AC6 THR D 536 LEU D 544 1 9 HELIX 25 AC7 VAL D 570 ILE D 595 1 26 HELIX 26 AC8 ASN D 618 ASN D 625 1 8 HELIX 27 AC9 THR D 627 ILE D 635 1 9 HELIX 28 AD1 TYR D 638 LEU D 663 1 26 HELIX 29 AD2 THR J 28 PHE J 32 5 5 HELIX 30 AD3 ASP J 61 LYS J 64 5 4 HELIX 31 AD4 ASN E 94 LYS E 97 5 4 HELIX 32 AD5 ASN E 98 LYS E 117 1 20 HELIX 33 AD6 LEU E 122 CYS E 126 5 5 HELIX 34 AD7 ASN E 195 THR E 198 5 4 HELIX 35 AD8 LYS E 335 PHE E 353 1 19 HELIX 36 AD9 ASP E 368 THR E 373 1 6 HELIX 37 AE1 MET E 475 LEU E 483 1 9 HELIX 38 AE2 THR F 529 SER F 534 1 6 HELIX 39 AE3 THR F 536 ASN F 543 1 8 HELIX 40 AE4 VAL F 570 ILE F 595 1 26 HELIX 41 AE5 ASN F 618 ASN F 625 1 8 HELIX 42 AE6 THR F 627 ILE F 635 1 9 HELIX 43 AE7 TYR F 638 ALA F 662 1 25 HELIX 44 AE8 THR M 28 PHE M 32 5 5 HELIX 45 AE9 ASP M 61 LYS M 64 5 4 HELIX 46 AF1 ARG M 83 THR M 87 5 5 HELIX 47 AF2 THR H 28 THR H 30 5 3 HELIX 48 AF3 HIS H 61 GLN H 64 5 4 HELIX 49 AF4 THR H 83 THR H 87 5 5 SHEET 1 AA1 4 THR L 5 SER L 7 0 SHEET 2 AA1 4 VAL L 19 ARG L 24 -1 O ARG L 24 N THR L 5 SHEET 3 AA1 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA1 4 SER L 63 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA2 5 SER L 10 SER L 12 0 SHEET 2 AA2 5 THR L 102 ASP L 105 1 O LYS L 103 N LEU L 11 SHEET 3 AA2 5 THR L 85 GLN L 89 -1 N TYR L 86 O THR L 102 SHEET 4 AA2 5 ALA L 34 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AA2 5 LYS L 45 ILE L 48 -1 O LYS L 45 N GLN L 37 SHEET 1 AA3 2 TRP A 35 TYR A 40 0 SHEET 2 AA3 2 LEU A 494 THR A 499 -1 O THR A 499 N TRP A 35 SHEET 1 AA4 4 TRP A 45 ASP A 47 0 SHEET 2 AA4 4 LYS A 487 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AA4 4 PHE A 223 LEU A 226 -1 N ALA A 224 O VAL A 489 SHEET 4 AA4 4 THR A 244 VAL A 245 -1 O VAL A 245 N ILE A 225 SHEET 1 AA5 2 PHE A 53 ALA A 55 0 SHEET 2 AA5 2 HIS A 216 CYS A 218 -1 O CYS A 218 N PHE A 53 SHEET 1 AA6 2 GLU A 91 ASN A 94 0 SHEET 2 AA6 2 THR A 236 CYS A 239 -1 O CYS A 239 N GLU A 91 SHEET 1 AA7 5 LYS A 169 VAL A 172 0 SHEET 2 AA7 5 LYS A 155 THR A 162 -1 N PHE A 159 O VAL A 172 SHEET 3 AA7 5 LEU A 129 ASN A 133 -1 N GLN A 130 O SER A 158 SHEET 4 AA7 5 GLU A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 5 AA7 5 VAL A 181 GLN A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AA8 3 ILE A 201 GLN A 203 0 SHEET 2 AA8 3 ALA A 433 TYR A 435 1 O TYR A 435 N THR A 202 SHEET 3 AA8 3 ILE A 423 ILE A 424 -1 N ILE A 424 O MET A 434 SHEET 1 AA9 8 SER A 256 THR A 257 0 SHEET 2 AA9 8 HIS A 374 CYS A 378 -1 O SER A 375 N THR A 257 SHEET 3 AA9 8 GLU A 381 CYS A 385 -1 O GLU A 381 N CYS A 378 SHEET 4 AA9 8 SER A 413 LYS A 421 -1 O ARG A 419 N TYR A 384 SHEET 5 AA9 8 HIS A 330 SER A 334 -1 N CYS A 331 O LEU A 416 SHEET 6 AA9 8 ILE A 284 ARG A 298 -1 N THR A 297 O HIS A 330 SHEET 7 AA9 8 ILE A 443 ARG A 456 -1 O THR A 450 N PHE A 288 SHEET 8 AA9 8 MET A 271 ARG A 273 0 SHEET 1 AB1 6 LEU A 260 LEU A 261 0 SHEET 2 AB1 6 ILE A 443 ARG A 456 -1 O GLY A 451 N LEU A 260 SHEET 3 AB1 6 ILE A 284 ARG A 298 -1 N PHE A 288 O THR A 450 SHEET 4 AB1 6 GLU A 466 PRO A 470 0 SHEET 5 AB1 6 ILE A 359 PHE A 361 1 N ARG A 360 O PHE A 468 SHEET 6 AB1 6 SER A 393 TRP A 395 -1 O SER A 393 N PHE A 361 SHEET 1 AB2 2 LYS A 305 ARG A 308 0 SHEET 2 AB2 2 ALA A 316 ALA A 319 -1 O PHE A 317 N ILE A 307 SHEET 1 AB3 4 GLN G 3 GLU G 6 0 SHEET 2 AB3 4 LYS G 19 SER G 25 -1 O SER G 25 N GLN G 3 SHEET 3 AB3 4 THR G 77 GLN G 81 -1 O LEU G 80 N LEU G 20 SHEET 4 AB3 4 THR G 68 ASP G 72 -1 N ASP G 72 O THR G 77 SHEET 1 AB4 5 THR G 57 TYR G 59 0 SHEET 2 AB4 5 LEU G 45 ILE G 51 -1 N LEU G 50 O PHE G 58 SHEET 3 AB4 5 MET G 34 GLN G 39 -1 N TRP G 36 O VAL G 48 SHEET 4 AB4 5 ALA G 88 GLY G 95 -1 O TYR G 91 N VAL G 37 SHEET 5 AB4 5 PHE G 100H TRP G 103 -1 O ASP G 101 N THR G 94 SHEET 1 AB5 5 THR G 57 TYR G 59 0 SHEET 2 AB5 5 LEU G 45 ILE G 51 -1 N LEU G 50 O PHE G 58 SHEET 3 AB5 5 MET G 34 GLN G 39 -1 N TRP G 36 O VAL G 48 SHEET 4 AB5 5 ALA G 88 GLY G 95 -1 O TYR G 91 N VAL G 37 SHEET 5 AB5 5 ALA G 107 VAL G 109 -1 O ALA G 107 N TYR G 90 SHEET 1 AB6 2 SER I 9 GLY I 13 0 SHEET 2 AB6 2 ARG I 103 VAL I 106 1 O THR I 105 N VAL I 11 SHEET 1 AB7 3 VAL I 19 THR I 24 0 SHEET 2 AB7 3 THR I 70 ILE I 75 -1 O ILE I 75 N VAL I 19 SHEET 3 AB7 3 SER I 63 SER I 67 -1 N SER I 67 O THR I 70 SHEET 1 AB8 4 LYS I 45 ILE I 48 0 SHEET 2 AB8 4 VAL I 33 GLN I 38 -1 N GLN I 37 O LYS I 45 SHEET 3 AB8 4 ASP I 85 TYR I 91 -1 O TYR I 87 N TYR I 36 SHEET 4 AB8 4 TYR I 96 PHE I 98 -1 O ILE I 97 N ALA I 90 SHEET 1 AB9 3 GLY C 495 THR C 499 0 SHEET 2 AB9 3 TRP C 35 TYR C 39 -1 N TYR C 39 O GLY C 495 SHEET 3 AB9 3 ILE D 603 PRO D 609 -1 O VAL D 608 N VAL C 36 SHEET 1 AC1 5 TRP C 45 ASP C 47 0 SHEET 2 AC1 5 VAL C 488 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AC1 5 PHE C 223 CYS C 228 -1 N ALA C 224 O VAL C 489 SHEET 4 AC1 5 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 AC1 5 GLU C 83 HIS C 85 -1 N ILE C 84 O THR C 244 SHEET 1 AC2 2 PHE C 53 ALA C 55 0 SHEET 2 AC2 2 HIS C 216 CYS C 218 -1 O HIS C 216 N ALA C 55 SHEET 1 AC3 2 THR C 90 ASN C 94 0 SHEET 2 AC3 2 THR C 236 PRO C 240 -1 O GLY C 237 N PHE C 93 SHEET 1 AC4 5 GLN C 170 TYR C 177 0 SHEET 2 AC4 5 LEU C 154 MET C 161 -1 N LYS C 155 O PHE C 176 SHEET 3 AC4 5 LEU C 129 THR C 132 -1 N GLN C 130 O SER C 158 SHEET 4 AC4 5 GLU C 190 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AC4 5 VAL C 181 GLN C 183 -1 N VAL C 182 O ARG C 192 SHEET 1 AC5 3 THR C 202 GLN C 203 0 SHEET 2 AC5 3 MET C 434 TYR C 435 1 O TYR C 435 N THR C 202 SHEET 3 AC5 3 ILE C 423 ILE C 424 -1 N ILE C 424 O MET C 434 SHEET 1 AC6 7 LEU C 259 LEU C 261 0 SHEET 2 AC6 7 ILE C 443 ARG C 456 -1 O GLY C 451 N LEU C 260 SHEET 3 AC6 7 ILE C 284 ARG C 298 -1 N PHE C 288 O THR C 450 SHEET 4 AC6 7 ALA C 329 SER C 334 -1 O HIS C 330 N THR C 297 SHEET 5 AC6 7 SER C 413 ARG C 419 -1 O ILE C 414 N VAL C 333 SHEET 6 AC6 7 GLU C 381 CYS C 385 -1 N TYR C 384 O ARG C 419 SHEET 7 AC6 7 HIS C 374 CYS C 378 -1 N CYS C 378 O GLU C 381 SHEET 1 AC7 6 MET C 271 ARG C 273 0 SHEET 2 AC7 6 ILE C 284 ARG C 298 -1 O LEU C 285 N ARG C 273 SHEET 3 AC7 6 ILE C 443 ARG C 456 -1 O THR C 450 N PHE C 288 SHEET 4 AC7 6 THR C 465 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 5 AC7 6 ILE C 358 PHE C 361 1 N ARG C 360 O GLU C 466 SHEET 6 AC7 6 SER C 393 THR C 394 -1 O SER C 393 N PHE C 361 SHEET 1 AC8 2 ARG C 304 ARG C 308 0 SHEET 2 AC8 2 ALA C 316 THR C 320 -1 O ALA C 319 N LYS C 305 SHEET 1 AC9 4 GLN J 3 THR J 7 0 SHEET 2 AC9 4 GLY J 15 SER J 25 -1 O SER J 21 N THR J 7 SHEET 3 AC9 4 THR J 77 SER J 82B-1 O SER J 82B N GLY J 15 SHEET 4 AC9 4 PHE J 67 ASP J 72 -1 N THR J 68 O GLN J 81 SHEET 1 AD1 6 GLY J 10 LEU J 11 0 SHEET 2 AD1 6 ALA J 107 THR J 110 1 O THR J 110 N GLY J 10 SHEET 3 AD1 6 ALA J 88 GLY J 95 -1 N TYR J 90 O ALA J 107 SHEET 4 AD1 6 MET J 34 GLN J 39 -1 N GLN J 39 O VAL J 89 SHEET 5 AD1 6 LEU J 45 ILE J 51 -1 O ILE J 51 N MET J 34 SHEET 6 AD1 6 THR J 57 TYR J 59 -1 O PHE J 58 N LEU J 50 SHEET 1 AD2 4 GLY J 10 LEU J 11 0 SHEET 2 AD2 4 ALA J 107 THR J 110 1 O THR J 110 N GLY J 10 SHEET 3 AD2 4 ALA J 88 GLY J 95 -1 N TYR J 90 O ALA J 107 SHEET 4 AD2 4 PHE J 100H ASP J 101 -1 O ASP J 101 N THR J 94 SHEET 1 AD3 2 SER K 9 SER K 12 0 SHEET 2 AD3 2 ARG K 103 THR K 105 1 O THR K 105 N VAL K 11 SHEET 1 AD4 3 SER K 18 THR K 24 0 SHEET 2 AD4 3 THR K 70 GLY K 77 -1 O ALA K 71 N CYS K 23 SHEET 3 AD4 3 SER K 63 SER K 67 -1 N SER K 63 O THR K 74 SHEET 1 AD5 4 LEU K 46 TYR K 49 0 SHEET 2 AD5 4 VAL K 33 GLN K 38 -1 N TRP K 35 O ILE K 48 SHEET 3 AD5 4 ASP K 85 TYR K 91 -1 O SER K 89 N SER K 34 SHEET 4 AD5 4 TYR K 96 PHE K 98 -1 N ILE K 97 O ALA K 90 SHEET 1 AD6 3 LEU E 494 THR E 499 0 SHEET 2 AD6 3 TRP E 35 TYR E 40 -1 N TRP E 35 O THR E 499 SHEET 3 AD6 3 ILE F 603 PRO F 609 -1 O VAL F 608 N VAL E 36 SHEET 1 AD7 5 TRP E 45 ASP E 47 0 SHEET 2 AD7 5 TYR E 486 ILE E 491 -1 O LYS E 490 N LYS E 46 SHEET 3 AD7 5 PHE E 223 CYS E 228 -1 N ALA E 224 O VAL E 489 SHEET 4 AD7 5 VAL E 242 VAL E 245 -1 O SER E 243 N LYS E 227 SHEET 5 AD7 5 GLU E 83 HIS E 85 -1 N ILE E 84 O THR E 244 SHEET 1 AD8 2 PHE E 53 ALA E 55 0 SHEET 2 AD8 2 HIS E 216 CYS E 218 -1 O CYS E 218 N PHE E 53 SHEET 1 AD9 2 THR E 90 GLU E 92 0 SHEET 2 AD9 2 PRO E 238 PRO E 240 -1 O CYS E 239 N GLU E 91 SHEET 1 AE1 5 LYS E 169 TYR E 177 0 SHEET 2 AE1 5 LEU E 154 THR E 162 -1 N CYS E 157 O SER E 174 SHEET 3 AE1 5 LEU E 129 THR E 132 -1 N GLN E 130 O SER E 158 SHEET 4 AE1 5 GLU E 190 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 5 AE1 5 VAL E 181 GLN E 183 -1 N VAL E 182 O ARG E 192 SHEET 1 AE2 7 LEU E 259 LEU E 261 0 SHEET 2 AE2 7 ILE E 443 ARG E 456 -1 O GLY E 451 N LEU E 260 SHEET 3 AE2 7 ILE E 284 ARG E 298 -1 N VAL E 292 O ILE E 449 SHEET 4 AE2 7 HIS E 330 SER E 334 -1 O ASN E 332 N ASN E 295 SHEET 5 AE2 7 SER E 413 ILE E 420 -1 O ILE E 414 N VAL E 333 SHEET 6 AE2 7 GLU E 381 CYS E 385 -1 N TYR E 384 O ARG E 419 SHEET 7 AE2 7 HIS E 374 CYS E 378 -1 N HIS E 374 O CYS E 385 SHEET 1 AE3 6 MET E 271 ARG E 273 0 SHEET 2 AE3 6 ILE E 284 ARG E 298 -1 O LEU E 285 N ARG E 273 SHEET 3 AE3 6 ILE E 443 ARG E 456 -1 O ILE E 449 N VAL E 292 SHEET 4 AE3 6 THR E 465 PRO E 470 -1 O ARG E 469 N THR E 455 SHEET 5 AE3 6 ILE E 358 PHE E 361 1 N ILE E 358 O GLU E 466 SHEET 6 AE3 6 SER E 393 TRP E 395 -1 O TRP E 395 N ILE E 359 SHEET 1 AE4 2 ARG E 304 ARG E 308 0 SHEET 2 AE4 2 ALA E 316 THR E 320 -1 O ALA E 319 N LYS E 305 SHEET 1 AE5 2 ILE E 423 ILE E 424 0 SHEET 2 AE5 2 MET E 434 TYR E 435 -1 O MET E 434 N ILE E 424 SHEET 1 AE6 4 GLN M 3 THR M 7 0 SHEET 2 AE6 4 SER M 17 SER M 25 -1 O SER M 21 N THR M 7 SHEET 3 AE6 4 THR M 77 HIS M 82A-1 O LEU M 78 N CYS M 22 SHEET 4 AE6 4 PHE M 67 ASP M 72 -1 N SER M 70 O SER M 79 SHEET 1 AE7 6 LEU M 11 VAL M 12 0 SHEET 2 AE7 6 ALA M 107 VAL M 111 1 O THR M 110 N VAL M 12 SHEET 3 AE7 6 ALA M 88 THR M 94 -1 N TYR M 90 O ALA M 107 SHEET 4 AE7 6 MET M 34 GLN M 39 -1 N GLN M 39 O VAL M 89 SHEET 5 AE7 6 LEU M 45 ILE M 51 -1 O GLU M 46 N ARG M 38 SHEET 6 AE7 6 PHE M 58 TYR M 59 -1 O PHE M 58 N LEU M 50 SHEET 1 AE8 5 SER N 9 GLY N 13 0 SHEET 2 AE8 5 THR N 102 VAL N 106 1 O THR N 105 N VAL N 11 SHEET 3 AE8 5 ASP N 85 ALA N 90 -1 N TYR N 86 O THR N 102 SHEET 4 AE8 5 VAL N 33 GLN N 38 -1 N GLN N 38 O ASP N 85 SHEET 5 AE8 5 PRO N 44 ILE N 48 -1 O LYS N 45 N GLN N 37 SHEET 1 AE9 4 SER N 9 GLY N 13 0 SHEET 2 AE9 4 THR N 102 VAL N 106 1 O THR N 105 N VAL N 11 SHEET 3 AE9 4 ASP N 85 ALA N 90 -1 N TYR N 86 O THR N 102 SHEET 4 AE9 4 ILE N 97 PHE N 98 -1 O ILE N 97 N ALA N 90 SHEET 1 AF1 3 VAL N 19 THR N 24 0 SHEET 2 AF1 3 THR N 70 ILE N 75 -1 O ILE N 75 N VAL N 19 SHEET 3 AF1 3 PHE N 62 SER N 67 -1 N SER N 67 O THR N 70 SHEET 1 AF2 4 GLN H 3 GLN H 6 0 SHEET 2 AF2 4 SER H 17 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AF2 4 THR H 77 SER H 82A-1 O MET H 80 N VAL H 20 SHEET 4 AF2 4 VAL H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AF3 6 GLU H 10 VAL H 11 0 SHEET 2 AF3 6 THR H 107 THR H 110 1 O LEU H 108 N GLU H 10 SHEET 3 AF3 6 GLY H 88 PRO H 96 -1 N TYR H 90 O THR H 107 SHEET 4 AF3 6 PHE H 32 GLN H 39 -1 N HIS H 35 O ALA H 93 SHEET 5 AF3 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AF3 6 VAL H 57 TYR H 59 -1 O ASN H 58 N TRP H 50 SHEET 1 AF4 4 GLU H 10 VAL H 11 0 SHEET 2 AF4 4 THR H 107 THR H 110 1 O LEU H 108 N GLU H 10 SHEET 3 AF4 4 GLY H 88 PRO H 96 -1 N TYR H 90 O THR H 107 SHEET 4 AF4 4 ASP H 101 TRP H 103 -1 O ASP H 101 N ARG H 94 SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.11 SSBOND 2 CYS A 54 CYS A 74 1555 1555 2.04 SSBOND 3 CYS A 119 CYS A 205 1555 1555 2.03 SSBOND 4 CYS A 126 CYS A 196 1555 1555 2.03 SSBOND 5 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 6 CYS A 218 CYS A 247 1555 1555 2.03 SSBOND 7 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 8 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 9 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 10 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 11 CYS A 501 CYS B 605 1555 1555 2.03 SSBOND 12 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 13 CYS G 22 CYS G 92 1555 1555 2.11 SSBOND 14 CYS I 23 CYS I 88 1555 1555 2.04 SSBOND 15 CYS C 54 CYS C 74 1555 1555 2.03 SSBOND 16 CYS C 119 CYS C 205 1555 1555 2.04 SSBOND 17 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 18 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 19 CYS C 218 CYS C 247 1555 1555 2.03 SSBOND 20 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 21 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 22 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 23 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 24 CYS C 501 CYS D 605 1555 1555 2.03 SSBOND 25 CYS D 598 CYS D 604 1555 1555 2.03 SSBOND 26 CYS J 22 CYS J 92 1555 1555 2.33 SSBOND 27 CYS K 23 CYS K 88 1555 1555 2.03 SSBOND 28 CYS E 54 CYS E 74 1555 1555 2.03 SSBOND 29 CYS E 119 CYS E 205 1555 1555 2.32 SSBOND 30 CYS E 126 CYS E 196 1555 1555 2.03 SSBOND 31 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 32 CYS E 218 CYS E 247 1555 1555 2.03 SSBOND 33 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 34 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 35 CYS E 385 CYS E 418 1555 1555 2.03 SSBOND 36 CYS E 501 CYS F 605 1555 1555 2.03 SSBOND 37 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 38 CYS M 22 CYS M 92 1555 1555 2.03 SSBOND 39 CYS N 23 CYS N 88 1555 1555 2.03 SSBOND 40 CYS H 22 CYS H 92 1555 1555 2.04 LINK ND2 ASN A 88 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 133 C1 NAG A 602 1555 1555 1.44 LINK ND2 ASN A 156 C1 NAG A 608 1555 1555 1.44 LINK ND2 ASN A 160 C1 NAG A 603 1555 1555 1.44 LINK ND2 ASN A 197 C1 NAG A 609 1555 1555 1.44 LINK ND2 ASN A 234 C1 NAG A 604 1555 1555 1.44 LINK ND2 ASN A 262 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN A 276 C1 NAG A 610 1555 1555 1.44 LINK ND2 ASN A 295 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN A 301 C1 NAG A 605 1555 1555 1.44 LINK ND2 ASN A 332 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN A 339 C1 NAG A 606 1555 1555 1.44 LINK ND2 ASN A 363 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN A 386 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN A 392 C1 NAG A 607 1555 1555 1.44 LINK ND2 ASN A 448 C1 NAG A 611 1555 1555 1.44 LINK ND2 ASN B 637 C1 NAG B 701 1555 1555 1.44 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 603 1555 1555 1.45 LINK ND2 ASN C 197 C1 NAG C 613 1555 1555 1.45 LINK ND2 ASN C 234 C1 NAG C 604 1555 1555 1.44 LINK ND2 ASN C 262 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN C 276 C1 NAG C 605 1555 1555 1.44 LINK ND2 ASN C 295 C1 NAG C 606 1555 1555 1.44 LINK ND2 ASN C 301 C1 NAG C 607 1555 1555 1.44 LINK ND2 ASN C 332 C1 NAG C 608 1555 1555 1.44 LINK ND2 ASN C 339 C1 NAG C 609 1555 1555 1.44 LINK ND2 ASN C 355 C1 NAG C 610 1555 1555 1.45 LINK ND2 ASN C 363 C1 NAG C 611 1555 1555 1.44 LINK ND2 ASN C 386 C1 NAG C 615 1555 1555 1.44 LINK ND2 ASN C 392 C1 NAG C 612 1555 1555 1.44 LINK ND2 ASN C 448 C1 NAG C 614 1555 1555 1.44 LINK ND2 ASN D 611 C1 NAG D 701 1555 1555 1.44 LINK ND2 ASN D 618 C1 NAG D 702 1555 1555 1.44 LINK ND2 ASN E 88 C1 NAG E 601 1555 1555 1.44 LINK ND2 ASN E 156 C1 NAG E 609 1555 1555 1.44 LINK ND2 ASN E 160 C1 NAG E 602 1555 1555 1.44 LINK ND2 ASN E 197 C1 NAG E 610 1555 1555 1.44 LINK ND2 ASN E 234 C1 NAG E 603 1555 1555 1.44 LINK ND2 ASN E 262 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN E 276 C1 NAG E 604 1555 1555 1.44 LINK ND2 ASN E 295 C1 NAG E 605 1555 1555 1.44 LINK ND2 ASN E 301 C1 NAG E 606 1555 1555 1.45 LINK ND2 ASN E 332 C1 NAG E 607 1555 1555 1.44 LINK ND2 ASN E 363 C1 NAG E 608 1555 1555 1.44 LINK ND2 ASN E 386 C1 NAG E 611 1555 1555 1.44 LINK ND2 ASN E 448 C1 NAG E 612 1555 1555 1.45 LINK ND2 ASN F 611 C1 NAG F 701 1555 1555 1.43 LINK ND2 ASN F 618 C1 NAG F 703 1555 1555 1.44 LINK ND2 ASN F 637 C1 NAG F 702 1555 1555 1.43 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.44 LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.44 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 U 2 C1 BMA U 3 1555 1555 1.44 LINK O3 BMA U 3 C1 MAN U 4 1555 1555 1.44 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.44 LINK O4 NAG V 2 C1 BMA V 3 1555 1555 1.44 LINK O3 BMA V 3 C1 MAN V 4 1555 1555 1.45 LINK O6 BMA V 3 C1 MAN V 5 1555 1555 1.45 CISPEP 1 SER L 7 PRO L 8 0 -6.51 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