HEADER VIRAL PROTEIN/IMMUNE SYSTEM 11-AUG-22 8E1P TITLE CRYSTAL STRUCTURE OF BG505 SOSIP.V4.1-GT1.2 TRIMER IN COMPLEX WITH GL- TITLE 2 PGV20 AND PGT124 FABS COMPND MOL_ID: 1; COMPND 2 MOLECULE: GERMLINE PGV20 HEAVY CHAIN; COMPND 3 CHAIN: F, H, N; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: GERMLINE PGV20 LIGHT CHAIN; COMPND 7 CHAIN: I; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: GERMLINE PGV20 LIGHT CHAIN; COMPND 11 CHAIN: L, O; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: PGT124 FAB LIGHT CHAIN; COMPND 15 CHAIN: A, C, J; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: BG505-SOSIP.V4.1-GT1.2GP120; COMPND 19 CHAIN: E, G, M; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 6; COMPND 22 MOLECULE: PGT124 FAB HEAVY CHAIN; COMPND 23 CHAIN: B, D, K; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 7; COMPND 26 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 27 CHAIN: Y, X, Z; COMPND 28 FRAGMENT: UNP RESIDUES 509-661; COMPND 29 SYNONYM: ENV POLYPROTEIN; COMPND 30 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 31 ORGANISM_COMMON: HIV-1; SOURCE 32 ORGANISM_TAXID: 11676; SOURCE 33 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 34 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 35 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 36 MOL_ID: 6; SOURCE 37 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 38 ORGANISM_COMMON: HUMAN; SOURCE 39 ORGANISM_TAXID: 9606; SOURCE 40 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 41 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 42 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 43 MOL_ID: 7; SOURCE 44 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 45 ORGANISM_TAXID: 11676; SOURCE 46 GENE: ENV; SOURCE 47 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 48 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 49 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV ENVELOPE GLYCOPROTEIN, ANTIBODY, CD4 ANTIBODY, VIRAL PROTEIN- KEYWDS 2 IMMUNE SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR A.SARKAR,S.KUMAR,I.A.WILSON JRNL AUTH T.G.CANIELS,M.MEDINA-RAMIREZ,J.ZHANG,A.SARKAR,S.KUMAR, JRNL AUTH 2 A.LABRANCHE,R.DERKING,J.D.ALLEN,J.L.SNITSELAAR, JRNL AUTH 3 J.CAPELLA-PUJOL,I.D.M.SANCHEZ,A.YASMEEN,M.DIAZ,Y.ALDON, JRNL AUTH 4 T.P.L.BIJL,S.VENKATAYOGI,J.S.MARTIN BEEM,A.NEWMAN,C.JIANG, JRNL AUTH 5 W.H.LEE,M.PATER,J.A.BURGER,M.J.VAN BREEMEN,S.W.DE TAEYE, JRNL AUTH 6 K.RANTALAINEN,C.LABRANCHE,K.O.SAUNDERS,D.MONTEFIORI, JRNL AUTH 7 G.OZOROWSKI,A.B.WARD,M.CRISPIN,J.P.MOORE,P.J.KLASSE, JRNL AUTH 8 B.F.HAYNES,I.A.WILSON,K.WIEHE,L.VERKOCZY,R.W.SANDERS JRNL TITL GERMLINE-TARGETING HIV-1 ENV VACCINATION INDUCES VRC01-CLASS JRNL TITL 2 ANTIBODIES WITH RARE INSERTIONS. JRNL REF CELL REP MED V. 4 01003 2023 JRNL REFN ISSN 2666-3791 JRNL PMID 37044090 JRNL DOI 10.1016/J.XCRM.2023.101003 REMARK 2 REMARK 2 RESOLUTION. 3.82 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2_4158 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.82 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.76 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.310 REMARK 3 COMPLETENESS FOR RANGE (%) : 94.3 REMARK 3 NUMBER OF REFLECTIONS : 63928 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.272 REMARK 3 R VALUE (WORKING SET) : 0.271 REMARK 3 FREE R VALUE : 0.301 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970 REMARK 3 FREE R VALUE TEST SET COUNT : 3180 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 49.7600 - 10.8400 0.92 2648 148 0.2710 0.3002 REMARK 3 2 10.8400 - 8.6200 0.94 2651 133 0.2144 0.2139 REMARK 3 3 8.6200 - 7.5300 0.95 2686 133 0.2422 0.2702 REMARK 3 4 7.5300 - 6.8500 0.94 2641 138 0.2650 0.2831 REMARK 3 5 6.8500 - 6.3600 0.95 2665 136 0.2666 0.3058 REMARK 3 6 6.3600 - 5.9800 0.96 2704 138 0.2606 0.2888 REMARK 3 7 5.9800 - 5.6800 0.96 2677 141 0.2666 0.3354 REMARK 3 8 5.6800 - 5.4400 0.96 2684 139 0.2663 0.2674 REMARK 3 9 5.4400 - 5.2300 0.96 2680 142 0.2556 0.2904 REMARK 3 10 5.2300 - 5.0500 0.96 2677 137 0.2549 0.2911 REMARK 3 11 5.0500 - 4.8900 0.96 2682 145 0.2542 0.3032 REMARK 3 12 4.8900 - 4.7500 0.95 2637 140 0.2543 0.2822 REMARK 3 13 4.7500 - 4.6300 0.96 2699 138 0.2644 0.2871 REMARK 3 14 4.6300 - 4.5100 0.96 2674 139 0.2632 0.3029 REMARK 3 15 4.5100 - 4.4100 0.96 2675 140 0.2698 0.3148 REMARK 3 16 4.4100 - 4.3200 0.96 2676 155 0.2886 0.3412 REMARK 3 17 4.3200 - 4.2300 0.96 2701 139 0.2953 0.3343 REMARK 3 18 4.2300 - 4.1500 0.96 2662 140 0.3181 0.3588 REMARK 3 19 4.1500 - 4.0800 0.96 2694 144 0.3219 0.3254 REMARK 3 20 4.0800 - 4.0100 0.96 2706 142 0.3414 0.3658 REMARK 3 21 4.0100 - 3.9400 0.95 2614 126 0.3395 0.3547 REMARK 3 22 3.9400 - 3.8800 0.96 2704 146 0.3405 0.3938 REMARK 3 23 3.8800 - 3.8200 0.69 1911 101 0.3362 0.3747 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.614 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.544 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 104.9 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 122.3 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.003 35188 REMARK 3 ANGLE : 0.531 47888 REMARK 3 CHIRALITY : 0.044 5646 REMARK 3 PLANARITY : 0.004 5976 REMARK 3 DIHEDRAL : 10.188 12824 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8E1P 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_1000267681. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-DEC-17 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 21-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63948 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.800 REMARK 200 RESOLUTION RANGE LOW (A) : 49.760 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7 REMARK 200 DATA REDUNDANCY : 2.900 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.82 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.88 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: PDB ENTRY 5W6D REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 65.63 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.58 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M TRIS, PH REMARK 280 8.5, 12% W/V PEG8000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 277.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 78.83300 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL 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: OCTADECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, H, I, L, N, O, A, C, E, G, REMARK 350 AND CHAINS: J, M, B, D, K, Y, X, Z, P, REMARK 350 AND CHAINS: Q, R, S, T, U, V, W, a, b, c, REMARK 350 AND CHAINS: d, e, f, g, h, i 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 LYS F 138 REMARK 465 SER F 139 REMARK 465 THR F 140 REMARK 465 LYS H 138 REMARK 465 SER H 139 REMARK 465 THR H 140 REMARK 465 GLU I 1 REMARK 465 VAL I 29A REMARK 465 GLY I 29B REMARK 465 GLY I 29C REMARK 465 TYR I 29D REMARK 465 SER L 27A REMARK 465 ASP L 27B REMARK 465 VAL L 27C REMARK 465 GLY L 27D REMARK 465 GLY L 27E REMARK 465 TYR L 27F REMARK 465 LYS N 138 REMARK 465 SER N 139 REMARK 465 THR N 140 REMARK 465 GLU O 1 REMARK 465 VAL O 29A REMARK 465 GLY O 29B REMARK 465 GLY O 29C REMARK 465 TYR O 29D REMARK 465 SER A 4 REMARK 465 GLU A 210 REMARK 465 CYS A 211 REMARK 465 SER A 212 REMARK 465 SER C 4 REMARK 465 GLU C 210 REMARK 465 CYS C 211 REMARK 465 SER C 212 REMARK 465 ALA E 31 REMARK 465 GLU E 62 REMARK 465 THR E 63 REMARK 465 THR E 135 REMARK 465 ASN E 136 REMARK 465 ASP E 149 REMARK 465 MET E 150 REMARK 465 ARG E 151 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 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 G 31 REMARK 465 GLU G 62 REMARK 465 THR G 63 REMARK 465 ASP G 149 REMARK 465 MET G 150 REMARK 465 ARG G 151 REMARK 465 ASN G 399 REMARK 465 THR G 400 REMARK 465 SER G 401 REMARK 465 VAL G 402 REMARK 465 GLN G 403 REMARK 465 GLY G 404 REMARK 465 SER G 405 REMARK 465 ASN G 406 REMARK 465 SER G 407 REMARK 465 THR G 408 REMARK 465 GLY G 409 REMARK 465 SER G 410 REMARK 465 GLY G 507 REMARK 465 ARG G 508 REMARK 465 ARG G 509 REMARK 465 ARG G 510 REMARK 465 ARG G 511 REMARK 465 ARG G 512 REMARK 465 ARG G 513 REMARK 465 SER J 4 REMARK 465 GLU J 210 REMARK 465 CYS J 211 REMARK 465 SER J 212 REMARK 465 ALA M 31 REMARK 465 GLU M 62 REMARK 465 THR M 63 REMARK 465 ASP M 149 REMARK 465 MET M 150 REMARK 465 ARG M 151 REMARK 465 ASN M 399 REMARK 465 THR M 400 REMARK 465 SER M 401 REMARK 465 VAL M 402 REMARK 465 GLN M 403 REMARK 465 GLY M 404 REMARK 465 SER M 405 REMARK 465 ASN M 406 REMARK 465 SER M 407 REMARK 465 THR M 408 REMARK 465 GLY M 409 REMARK 465 SER M 410 REMARK 465 GLY M 507 REMARK 465 ARG M 508 REMARK 465 ARG M 509 REMARK 465 ARG M 510 REMARK 465 ARG M 511 REMARK 465 ARG M 512 REMARK 465 ARG M 513 REMARK 465 GLN B 1 REMARK 465 SER B 127 REMARK 465 SER B 128 REMARK 465 LYS B 129 REMARK 465 SER B 130 REMARK 465 THR B 131 REMARK 465 LYS B 214 REMARK 465 SER B 215 REMARK 465 CYS B 216 REMARK 465 ASP B 217 REMARK 465 GLN D 1 REMARK 465 SER D 127 REMARK 465 SER D 128 REMARK 465 LYS D 129 REMARK 465 SER D 130 REMARK 465 THR D 131 REMARK 465 LYS D 214 REMARK 465 SER D 215 REMARK 465 CYS D 216 REMARK 465 ASP D 217 REMARK 465 GLN K 1 REMARK 465 SER K 127 REMARK 465 SER K 128 REMARK 465 LYS K 129 REMARK 465 SER K 130 REMARK 465 THR K 131 REMARK 465 LYS K 214 REMARK 465 SER K 215 REMARK 465 CYS K 216 REMARK 465 ASP K 217 REMARK 465 ALA Y 512 REMARK 465 VAL Y 513 REMARK 465 GLY Y 514 REMARK 465 ILE Y 515 REMARK 465 GLY Y 516 REMARK 465 ALA Y 517 REMARK 465 GLY Y 547 REMARK 465 ILE Y 548 REMARK 465 VAL Y 549 REMARK 465 GLN Y 550 REMARK 465 GLN Y 551 REMARK 465 GLN Y 552 REMARK 465 SER Y 553 REMARK 465 ASN Y 554 REMARK 465 LEU Y 555 REMARK 465 LEU Y 556 REMARK 465 ARG Y 557 REMARK 465 ALA Y 558 REMARK 465 PRO Y 559 REMARK 465 GLU Y 560 REMARK 465 ALA Y 561 REMARK 465 GLN Y 562 REMARK 465 GLN Y 563 REMARK 465 HIS Y 564 REMARK 465 ALA X 512 REMARK 465 VAL X 513 REMARK 465 GLY X 514 REMARK 465 ILE X 515 REMARK 465 GLY X 516 REMARK 465 ALA X 517 REMARK 465 GLY X 547 REMARK 465 ILE X 548 REMARK 465 VAL X 549 REMARK 465 GLN X 550 REMARK 465 GLN X 551 REMARK 465 GLN X 552 REMARK 465 SER X 553 REMARK 465 ASN X 554 REMARK 465 LEU X 555 REMARK 465 LEU X 556 REMARK 465 ARG X 557 REMARK 465 ALA X 558 REMARK 465 PRO X 559 REMARK 465 GLU X 560 REMARK 465 ALA X 561 REMARK 465 GLN X 562 REMARK 465 GLN X 563 REMARK 465 HIS X 564 REMARK 465 ALA Z 512 REMARK 465 VAL Z 513 REMARK 465 GLY Z 514 REMARK 465 ILE Z 515 REMARK 465 GLY Z 516 REMARK 465 ALA Z 517 REMARK 465 GLY Z 547 REMARK 465 ILE Z 548 REMARK 465 VAL Z 549 REMARK 465 GLN Z 550 REMARK 465 GLN Z 551 REMARK 465 GLN Z 552 REMARK 465 SER Z 553 REMARK 465 ASN Z 554 REMARK 465 LEU Z 555 REMARK 465 LEU Z 556 REMARK 465 ARG Z 557 REMARK 465 ALA Z 558 REMARK 465 PRO Z 559 REMARK 465 GLU Z 560 REMARK 465 ALA Z 561 REMARK 465 GLN Z 562 REMARK 465 GLN Z 563 REMARK 465 HIS Z 564 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 NE2 HIS M 330 O7 NAG g 1 1.30 REMARK 500 CD2 HIS M 330 O7 NAG g 1 1.97 REMARK 500 OG SER M 447 O7 NAG e 1 2.18 REMARK 500 ND2 ASN Z 611 O5 NAG Z 701 2.19 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 CYS F 22 96.02 -161.33 REMARK 500 GLN F 43 -159.67 -120.16 REMARK 500 ASN F 59 77.87 -157.41 REMARK 500 ARG F 85 75.82 54.85 REMARK 500 GLN F 103 83.66 54.25 REMARK 500 ASP F 104 -131.71 46.16 REMARK 500 GLU F 106 -33.77 101.10 REMARK 500 THR F 144 87.12 -173.50 REMARK 500 ASP F 153 81.40 54.47 REMARK 500 GLN H 43 -164.36 -122.96 REMARK 500 ASN H 59 76.88 -158.09 REMARK 500 ARG H 85 75.22 54.80 REMARK 500 GLU H 106 -153.57 -82.40 REMARK 500 THR H 144 165.13 101.24 REMARK 500 ASP H 153 81.16 57.03 REMARK 500 SER I 27 162.28 64.28 REMARK 500 ASP I 29 35.53 -174.37 REMARK 500 VAL I 51 -60.41 63.53 REMARK 500 ASP I 82 37.12 -80.34 REMARK 500 TYR I 91 -113.91 51.62 REMARK 500 VAL I 106 -123.69 37.77 REMARK 500 PRO I 110 101.02 -26.95 REMARK 500 ASN I 129 55.17 -90.89 REMARK 500 ASP I 139 69.37 23.57 REMARK 500 SER I 176 114.78 -160.09 REMARK 500 SER I 188 -74.72 -89.41 REMARK 500 ALA L 3 -82.16 57.78 REMARK 500 VAL L 51 -62.38 64.09 REMARK 500 TYR L 91 -119.76 57.07 REMARK 500 VAL L 106 -129.27 30.91 REMARK 500 PRO L 110 -128.40 -3.55 REMARK 500 LYS L 111 -133.15 42.36 REMARK 500 ALA L 112 77.93 69.00 REMARK 500 ASP L 139 57.33 20.52 REMARK 500 SER L 188 -75.49 -89.71 REMARK 500 CYS N 22 92.21 -161.83 REMARK 500 GLN N 43 -164.33 -120.98 REMARK 500 ASN N 54 -71.52 -58.12 REMARK 500 ASN N 59 76.71 -155.12 REMARK 500 ARG N 85 74.16 55.44 REMARK 500 GLN N 103 -3.84 71.75 REMARK 500 SER N 122 -124.14 66.44 REMARK 500 ASP N 153 81.98 57.05 REMARK 500 SER O 27 -116.52 51.52 REMARK 500 VAL O 51 -63.61 65.03 REMARK 500 ASN O 69 30.15 -94.34 REMARK 500 TYR O 91 -120.80 55.28 REMARK 500 ALA O 112 124.38 162.77 REMARK 500 ALA O 131 119.27 -162.52 REMARK 500 ASP O 139 65.12 25.13 REMARK 500 REMARK 500 THIS ENTRY HAS 167 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 MAN h 1 DBREF 8E1P F 1 225 PDB 8E1P 8E1P 1 225 DBREF 8E1P H 1 225 PDB 8E1P 8E1P 1 225 DBREF 8E1P I 1 212 PDB 8E1P 8E1P 1 212 DBREF 8E1P L 1 212 PDB 8E1P 8E1P 1 212 DBREF 8E1P N 1 225 PDB 8E1P 8E1P 1 225 DBREF 8E1P O 1 212 PDB 8E1P 8E1P 1 212 DBREF 8E1P A 4 212 PDB 8E1P 8E1P 4 212 DBREF 8E1P C 4 212 PDB 8E1P 8E1P 4 212 DBREF 8E1P E 31 513 PDB 8E1P 8E1P 31 513 DBREF 8E1P G 31 513 PDB 8E1P 8E1P 31 513 DBREF 8E1P J 4 212 PDB 8E1P 8E1P 4 212 DBREF 8E1P M 31 513 PDB 8E1P 8E1P 31 513 DBREF 8E1P B 1 217 PDB 8E1P 8E1P 1 217 DBREF 8E1P D 1 217 PDB 8E1P 8E1P 1 217 DBREF 8E1P K 1 217 PDB 8E1P 8E1P 1 217 DBREF 8E1P Y 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 8E1P X 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 8E1P Z 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 SEQADV 8E1P PRO Y 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 8E1P CYS Y 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 8E1P PRO X 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 8E1P CYS X 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 8E1P PRO Z 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 8E1P CYS Z 605 UNP Q2N0S6 THR 602 CONFLICT SEQRES 1 F 225 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 F 225 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 F 225 TYR THR PHE THR GLY TYR TYR MET HIS TRP VAL ARG GLN SEQRES 4 F 225 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 F 225 PRO ASN SER GLY GLY THR ASN TYR ALA GLN LYS PHE GLN SEQRES 6 F 225 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 F 225 ALA TYR MET GLU LEU SER ARG LEU ARG SER ASP ASP THR SEQRES 8 F 225 ALA VAL TYR TYR CYS ALA ARG ARG MET ARG SER GLN ASP SEQRES 9 F 225 ARG GLU TRP ASP PHE GLN HIS TRP GLY GLN GLY THR LEU SEQRES 10 F 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 F 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 F 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 F 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 F 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 F 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 F 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 F 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 F 225 PRO LYS SER CYS SEQRES 1 H 225 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 225 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 225 TYR THR PHE THR GLY TYR TYR MET HIS TRP VAL ARG GLN SEQRES 4 H 225 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 H 225 PRO ASN SER GLY GLY THR ASN TYR ALA GLN LYS PHE GLN SEQRES 6 H 225 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 H 225 ALA TYR MET GLU LEU SER ARG LEU ARG SER ASP ASP THR SEQRES 8 H 225 ALA VAL TYR TYR CYS ALA ARG ARG MET ARG SER GLN ASP SEQRES 9 H 225 ARG GLU TRP ASP PHE GLN HIS TRP GLY GLN GLY THR LEU SEQRES 10 H 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 H 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 H 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 H 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 H 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 H 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 H 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 H 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 H 225 PRO LYS SER CYS SEQRES 1 I 210 GLU SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER SEQRES 2 I 210 PRO GLY GLN SER ILE THR ILE SER CYS THR GLY THR SER SEQRES 3 I 210 SER ASP VAL GLY GLY TYR ASN TYR VAL SER TRP TYR GLN SEQRES 4 I 210 GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE TYR GLU SEQRES 5 I 210 VAL SER ASN ARG PRO SER GLY VAL SER ASN ARG PHE SER SEQRES 6 I 210 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 I 210 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS SER SEQRES 8 I 210 SER TYR GLU PHE PHE GLY GLY GLY THR LYS VAL PHE VAL SEQRES 9 I 210 LEU GLY GLN PRO LYS ALA ALA PRO SER VAL THR LEU PHE SEQRES 10 I 210 PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA THR SEQRES 11 I 210 LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA VAL SEQRES 12 I 210 THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL LYS ALA SEQRES 13 I 210 GLY VAL GLU THR THR THR PRO SER LYS GLN SER ASN ASN SEQRES 14 I 210 LYS TYR ALA ALA SER SER TYR LEU SER LEU THR PRO GLU SEQRES 15 I 210 GLN TRP LYS SER HIS LYS SER TYR SER CYS GLN VAL THR SEQRES 16 I 210 HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO THR SEQRES 17 I 210 GLU CYS SEQRES 1 L 210 GLU SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER SEQRES 2 L 210 PRO GLY GLN SER ILE THR ILE SER CYS THR GLY THR SER SEQRES 3 L 210 SER ASP VAL GLY GLY TYR ASN TYR VAL SER TRP TYR GLN SEQRES 4 L 210 GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE TYR GLU SEQRES 5 L 210 VAL SER ASN ARG PRO SER GLY VAL SER ASN ARG PHE SER SEQRES 6 L 210 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 L 210 GLY LEU GLN ALA GLU GLU ASP ALA ASP TYR TYR CYS SER SEQRES 8 L 210 SER TYR GLU PHE PHE GLY GLY GLY THR LYS VAL PHE VAL SEQRES 9 L 210 LEU GLY GLN PRO LYS ALA ALA PRO SER VAL THR LEU PHE SEQRES 10 L 210 PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA THR SEQRES 11 L 210 LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA VAL SEQRES 12 L 210 THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL LYS ALA SEQRES 13 L 210 GLY VAL GLU THR THR THR PRO SER LYS GLN SER ASN ASN SEQRES 14 L 210 LYS TYR ALA ALA SER SER TYR LEU SER LEU THR PRO GLU SEQRES 15 L 210 GLN TRP LYS SER HIS LYS SER TYR SER CYS GLN VAL THR SEQRES 16 L 210 HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO THR SEQRES 17 L 210 GLU CYS SEQRES 1 N 225 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 N 225 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 N 225 TYR THR PHE THR GLY TYR TYR MET HIS TRP VAL ARG GLN SEQRES 4 N 225 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 N 225 PRO ASN SER GLY GLY THR ASN TYR ALA GLN LYS PHE GLN SEQRES 6 N 225 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 N 225 ALA TYR MET GLU LEU SER ARG LEU ARG SER ASP ASP THR SEQRES 8 N 225 ALA VAL TYR TYR CYS ALA ARG ARG MET ARG SER GLN ASP SEQRES 9 N 225 ARG GLU TRP ASP PHE GLN HIS TRP GLY GLN GLY THR LEU SEQRES 10 N 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 N 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 N 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 N 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 N 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 N 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 N 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 N 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 N 225 PRO LYS SER CYS SEQRES 1 O 210 GLU SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER SEQRES 2 O 210 PRO GLY GLN SER ILE THR ILE SER CYS THR GLY THR SER SEQRES 3 O 210 SER ASP VAL GLY GLY TYR ASN TYR VAL SER TRP TYR GLN SEQRES 4 O 210 GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE TYR GLU SEQRES 5 O 210 VAL SER ASN ARG PRO SER GLY VAL SER ASN ARG PHE SER SEQRES 6 O 210 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 O 210 GLY LEU GLN ALA GLU GLU ASP ALA ASP TYR TYR CYS SER SEQRES 8 O 210 SER TYR GLU PHE PHE GLY GLY GLY THR LYS VAL PHE VAL SEQRES 9 O 210 LEU GLY GLN PRO LYS ALA ALA PRO SER VAL THR LEU PHE SEQRES 10 O 210 PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA THR SEQRES 11 O 210 LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA VAL SEQRES 12 O 210 THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL LYS ALA SEQRES 13 O 210 GLY VAL GLU THR THR THR PRO SER LYS GLN SER ASN ASN SEQRES 14 O 210 LYS TYR ALA ALA SER SER TYR LEU SER LEU THR PRO GLU SEQRES 15 O 210 GLN TRP LYS SER HIS LYS SER TYR SER CYS GLN VAL THR SEQRES 16 O 210 HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO THR SEQRES 17 O 210 GLU CYS SEQRES 1 A 214 SER TYR VAL SER PRO LEU SER VAL ALA LEU GLY GLU THR SEQRES 2 A 214 ALA ARG ILE SER CYS GLY ARG GLN ALA LEU GLY SER ARG SEQRES 3 A 214 ALA VAL GLN TRP TYR GLN HIS LYS PRO GLY GLN ALA PRO SEQRES 4 A 214 ILE LEU LEU ILE TYR ASN ASN GLN ASP ARG PRO SER GLY SEQRES 5 A 214 ILE PRO GLU ARG PHE SER GLY THR PRO ASP ILE ASN PHE SEQRES 6 A 214 GLY THR THR ALA THR LEU THR ILE SER GLY VAL GLU VAL SEQRES 7 A 214 GLY ASP GLU ALA ASP TYR TYR CYS HIS MET TRP ASP SER SEQRES 8 A 214 ARG SER GLY PHE SER TRP SER PHE GLY GLY ALA THR ARG SEQRES 9 A 214 LEU THR VAL LEU SER GLN PRO LYS ALA ALA PRO SER VAL SEQRES 10 A 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN SEQRES 11 A 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO SEQRES 12 A 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO SEQRES 13 A 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SEQRES 14 A 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU SEQRES 15 A 214 THR PRO GLU GLN TRP LYS SER HIS LYS SER TYR SER CYS SEQRES 16 A 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL SEQRES 17 A 214 ALA PRO THR GLU CYS SER SEQRES 1 C 214 SER TYR VAL SER PRO LEU SER VAL ALA LEU GLY GLU THR SEQRES 2 C 214 ALA ARG ILE SER CYS GLY ARG GLN ALA LEU GLY SER ARG SEQRES 3 C 214 ALA VAL GLN TRP TYR GLN HIS LYS PRO GLY GLN ALA PRO SEQRES 4 C 214 ILE LEU LEU ILE TYR ASN ASN GLN ASP ARG PRO SER GLY SEQRES 5 C 214 ILE PRO GLU ARG PHE SER GLY THR PRO ASP ILE ASN PHE SEQRES 6 C 214 GLY THR THR ALA THR LEU THR ILE SER GLY VAL GLU VAL SEQRES 7 C 214 GLY ASP GLU ALA ASP TYR TYR CYS HIS MET TRP ASP SER SEQRES 8 C 214 ARG SER GLY PHE SER TRP SER PHE GLY GLY ALA THR ARG SEQRES 9 C 214 LEU THR VAL LEU SER GLN PRO LYS ALA ALA PRO SER VAL SEQRES 10 C 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN SEQRES 11 C 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO SEQRES 12 C 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO SEQRES 13 C 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SEQRES 14 C 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU SEQRES 15 C 214 THR PRO GLU GLN TRP LYS SER HIS LYS SER TYR SER CYS SEQRES 16 C 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL SEQRES 17 C 214 ALA PRO THR GLU CYS SER SEQRES 1 E 474 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 E 474 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 E 474 ASP ALA LYS ALA TYR GLU THR LYS LYS HIS ASN VAL TRP SEQRES 4 E 474 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 E 474 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 E 474 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 E 474 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 E 474 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 E 474 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 E 474 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 E 474 ARG GLN LYS VAL HIS ALA LEU PHE TYR LYS LEU ASP ILE SEQRES 12 E 474 VAL PRO ILE ASN GLU ASN GLN ASN THR SER TYR ARG LEU SEQRES 13 E 474 ILE ASN CYS ASN THR ALA ALA ILE THR GLN ALA CYS PRO SEQRES 14 E 474 LYS VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA SEQRES 15 E 474 PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS ASP LYS LYS SEQRES 16 E 474 PHE ASN GLY THR GLY PRO CYS PRO SER VAL SER THR VAL SEQRES 17 E 474 GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN SEQRES 18 E 474 LEU LEU LEU ASN GLY SER LEU ALA GLU GLU GLU VAL MET SEQRES 19 E 474 ILE ARG SER GLU ASP ILE ARG ASP ASN ALA LYS ASN ILE SEQRES 20 E 474 LEU VAL GLN PHE ASN THR PRO VAL GLN ILE ASN CYS THR SEQRES 21 E 474 ARG PRO ASN ASN ASN THR ARG LYS SER ILE ARG ILE GLY SEQRES 22 E 474 PRO GLY GLN TRP PHE TYR ALA THR GLY ASP ILE ILE GLY SEQRES 23 E 474 ASP ILE ARG GLN ALA HIS CYS ASN VAL SER LYS ALA THR SEQRES 24 E 474 TRP ASN GLU THR LEU GLY LYS VAL VAL LYS GLN LEU ARG SEQRES 25 E 474 LYS HIS PHE GLY ASN ASN THR ILE ILE ARG PHE ALA ASN SEQRES 26 E 474 SER SER GLY GLY ASP LEU GLU VAL THR THR HIS SER PHE SEQRES 27 E 474 ASN CYS GLY GLY GLU PHE PHE TYR CYS ASP THR SER GLY SEQRES 28 E 474 LEU PHE ASN SER THR TRP ILE SER ASN THR SER VAL GLN SEQRES 29 E 474 GLY SER ASN SER THR GLY SER ASN ASP SER ILE THR LEU SEQRES 30 E 474 PRO CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG SEQRES 31 E 474 ILE GLY GLN ALA MET TYR ALA PRO PRO ILE GLN GLY VAL SEQRES 32 E 474 ILE ARG CYS VAL SER ASN ILE THR GLY LEU ILE LEU THR SEQRES 33 E 474 ARG ASP GLY GLY SER THR ASP SER THR THR GLU THR PHE SEQRES 34 E 474 ARG PRO SER GLY GLY ASP MET ARG ASP ASN TRP ARG SER SEQRES 35 E 474 GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU PRO LEU SEQRES 36 E 474 GLY VAL ALA PRO THR ARG CYS LYS ARG ARG VAL VAL GLY SEQRES 37 E 474 ARG ARG ARG ARG ARG ARG SEQRES 1 G 474 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 G 474 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 G 474 ASP ALA LYS ALA TYR GLU THR LYS LYS HIS ASN VAL TRP SEQRES 4 G 474 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 G 474 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 G 474 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 G 474 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 G 474 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 G 474 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 G 474 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 G 474 ARG GLN LYS VAL HIS ALA LEU PHE TYR LYS LEU ASP ILE SEQRES 12 G 474 VAL PRO ILE ASN GLU ASN GLN ASN THR SER TYR ARG LEU SEQRES 13 G 474 ILE ASN CYS ASN THR ALA ALA ILE THR GLN ALA CYS PRO SEQRES 14 G 474 LYS VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA SEQRES 15 G 474 PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS ASP LYS LYS SEQRES 16 G 474 PHE ASN GLY THR GLY PRO CYS PRO SER VAL SER THR VAL SEQRES 17 G 474 GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN SEQRES 18 G 474 LEU LEU LEU ASN GLY SER LEU ALA GLU GLU GLU VAL MET SEQRES 19 G 474 ILE ARG SER GLU ASP ILE ARG ASP ASN ALA LYS ASN ILE SEQRES 20 G 474 LEU VAL GLN PHE ASN THR PRO VAL GLN ILE ASN CYS THR SEQRES 21 G 474 ARG PRO ASN ASN ASN THR ARG LYS SER ILE ARG ILE GLY SEQRES 22 G 474 PRO GLY GLN TRP PHE TYR ALA THR GLY ASP ILE ILE GLY SEQRES 23 G 474 ASP ILE ARG GLN ALA HIS CYS ASN VAL SER LYS ALA THR SEQRES 24 G 474 TRP ASN GLU THR LEU GLY LYS VAL VAL LYS GLN LEU ARG SEQRES 25 G 474 LYS HIS PHE GLY ASN ASN THR ILE ILE ARG PHE ALA ASN SEQRES 26 G 474 SER SER GLY GLY ASP LEU GLU VAL THR THR HIS SER PHE SEQRES 27 G 474 ASN CYS GLY GLY GLU PHE PHE TYR CYS ASP THR SER GLY SEQRES 28 G 474 LEU PHE ASN SER THR TRP ILE SER ASN THR SER VAL GLN SEQRES 29 G 474 GLY SER ASN SER THR GLY SER ASN ASP SER ILE THR LEU SEQRES 30 G 474 PRO CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG SEQRES 31 G 474 ILE GLY GLN ALA MET TYR ALA PRO PRO ILE GLN GLY VAL SEQRES 32 G 474 ILE ARG CYS VAL SER ASN ILE THR GLY LEU ILE LEU THR SEQRES 33 G 474 ARG ASP GLY GLY SER THR ASP SER THR THR GLU THR PHE SEQRES 34 G 474 ARG PRO SER GLY GLY ASP MET ARG ASP ASN TRP ARG SER SEQRES 35 G 474 GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU PRO LEU SEQRES 36 G 474 GLY VAL ALA PRO THR ARG CYS LYS ARG ARG VAL VAL GLY SEQRES 37 G 474 ARG ARG ARG ARG ARG ARG SEQRES 1 J 214 SER TYR VAL SER PRO LEU SER VAL ALA LEU GLY GLU THR SEQRES 2 J 214 ALA ARG ILE SER CYS GLY ARG GLN ALA LEU GLY SER ARG SEQRES 3 J 214 ALA VAL GLN TRP TYR GLN HIS LYS PRO GLY GLN ALA PRO SEQRES 4 J 214 ILE LEU LEU ILE TYR ASN ASN GLN ASP ARG PRO SER GLY SEQRES 5 J 214 ILE PRO GLU ARG PHE SER GLY THR PRO ASP ILE ASN PHE SEQRES 6 J 214 GLY THR THR ALA THR LEU THR ILE SER GLY VAL GLU VAL SEQRES 7 J 214 GLY ASP GLU ALA ASP TYR TYR CYS HIS MET TRP ASP SER SEQRES 8 J 214 ARG SER GLY PHE SER TRP SER PHE GLY GLY ALA THR ARG SEQRES 9 J 214 LEU THR VAL LEU SER GLN PRO LYS ALA ALA PRO SER VAL SEQRES 10 J 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN SEQRES 11 J 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO SEQRES 12 J 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO SEQRES 13 J 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SEQRES 14 J 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU SEQRES 15 J 214 THR PRO GLU GLN TRP LYS SER HIS LYS SER TYR SER CYS SEQRES 16 J 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL SEQRES 17 J 214 ALA PRO THR GLU CYS SER SEQRES 1 M 474 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 M 474 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 M 474 ASP ALA LYS ALA TYR GLU THR LYS LYS HIS ASN VAL TRP SEQRES 4 M 474 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 M 474 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 M 474 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 M 474 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 M 474 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 M 474 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 M 474 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 M 474 ARG GLN LYS VAL HIS ALA LEU PHE TYR LYS LEU ASP ILE SEQRES 12 M 474 VAL PRO ILE ASN GLU ASN GLN ASN THR SER TYR ARG LEU SEQRES 13 M 474 ILE ASN CYS ASN THR ALA ALA ILE THR GLN ALA CYS PRO SEQRES 14 M 474 LYS VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA SEQRES 15 M 474 PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS ASP LYS LYS SEQRES 16 M 474 PHE ASN GLY THR GLY PRO CYS PRO SER VAL SER THR VAL SEQRES 17 M 474 GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN SEQRES 18 M 474 LEU LEU LEU ASN GLY SER LEU ALA GLU GLU GLU VAL MET SEQRES 19 M 474 ILE ARG SER GLU ASP ILE ARG ASP ASN ALA LYS ASN ILE SEQRES 20 M 474 LEU VAL GLN PHE ASN THR PRO VAL GLN ILE ASN CYS THR SEQRES 21 M 474 ARG PRO ASN ASN ASN THR ARG LYS SER ILE ARG ILE GLY SEQRES 22 M 474 PRO GLY GLN TRP PHE TYR ALA THR GLY ASP ILE ILE GLY SEQRES 23 M 474 ASP ILE ARG GLN ALA HIS CYS ASN VAL SER LYS ALA THR SEQRES 24 M 474 TRP ASN GLU THR LEU GLY LYS VAL VAL LYS GLN LEU ARG SEQRES 25 M 474 LYS HIS PHE GLY ASN ASN THR ILE ILE ARG PHE ALA ASN SEQRES 26 M 474 SER SER GLY GLY ASP LEU GLU VAL THR THR HIS SER PHE SEQRES 27 M 474 ASN CYS GLY GLY GLU PHE PHE TYR CYS ASP THR SER GLY SEQRES 28 M 474 LEU PHE ASN SER THR TRP ILE SER ASN THR SER VAL GLN SEQRES 29 M 474 GLY SER ASN SER THR GLY SER ASN ASP SER ILE THR LEU SEQRES 30 M 474 PRO CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG SEQRES 31 M 474 ILE GLY GLN ALA MET TYR ALA PRO PRO ILE GLN GLY VAL SEQRES 32 M 474 ILE ARG CYS VAL SER ASN ILE THR GLY LEU ILE LEU THR SEQRES 33 M 474 ARG ASP GLY GLY SER THR ASP SER THR THR GLU THR PHE SEQRES 34 M 474 ARG PRO SER GLY GLY ASP MET ARG ASP ASN TRP ARG SER SEQRES 35 M 474 GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU PRO LEU SEQRES 36 M 474 GLY VAL ALA PRO THR ARG CYS LYS ARG ARG VAL VAL GLY SEQRES 37 M 474 ARG ARG ARG ARG ARG ARG SEQRES 1 B 236 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL ARG SEQRES 2 B 236 PRO SER GLU THR LEU SER VAL THR CYS ILE VAL SER GLY SEQRES 3 B 236 GLY SER ILE SER ASN TYR TYR TRP THR TRP ILE ARG GLN SEQRES 4 B 236 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SER SEQRES 5 B 236 ASP ARG GLU THR THR THR TYR ASN PRO SER LEU ASN SER SEQRES 6 B 236 ARG ALA VAL ILE SER ARG ASP THR SER LYS ASN GLN LEU SEQRES 7 B 236 SER LEU GLN LEU ARG SER VAL THR THR ALA ASP THR ALA SEQRES 8 B 236 ILE TYR PHE CYS ALA THR ALA ARG ARG GLY GLN ARG ILE SEQRES 9 B 236 TYR GLY VAL VAL SER PHE GLY GLU PHE PHE TYR TYR TYR SEQRES 10 B 236 TYR MET ASP VAL TRP GLY LYS GLY THR ALA VAL THR VAL SEQRES 11 B 236 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 12 B 236 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 13 B 236 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 14 B 236 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 15 B 236 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 16 B 236 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 17 B 236 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 18 B 236 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 19 B 236 CYS ASP SEQRES 1 D 236 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL ARG SEQRES 2 D 236 PRO SER GLU THR LEU SER VAL THR CYS ILE VAL SER GLY SEQRES 3 D 236 GLY SER ILE SER ASN TYR TYR TRP THR TRP ILE ARG GLN SEQRES 4 D 236 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SER SEQRES 5 D 236 ASP ARG GLU THR THR THR TYR ASN PRO SER LEU ASN SER SEQRES 6 D 236 ARG ALA VAL ILE SER ARG ASP THR SER LYS ASN GLN LEU SEQRES 7 D 236 SER LEU GLN LEU ARG SER VAL THR THR ALA ASP THR ALA SEQRES 8 D 236 ILE TYR PHE CYS ALA THR ALA ARG ARG GLY GLN ARG ILE SEQRES 9 D 236 TYR GLY VAL VAL SER PHE GLY GLU PHE PHE TYR TYR TYR SEQRES 10 D 236 TYR MET ASP VAL TRP GLY LYS GLY THR ALA VAL THR VAL SEQRES 11 D 236 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 12 D 236 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 13 D 236 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 14 D 236 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 15 D 236 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 16 D 236 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 17 D 236 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 18 D 236 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 19 D 236 CYS ASP SEQRES 1 K 236 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL ARG SEQRES 2 K 236 PRO SER GLU THR LEU SER VAL THR CYS ILE VAL SER GLY SEQRES 3 K 236 GLY SER ILE SER ASN TYR TYR TRP THR TRP ILE ARG GLN SEQRES 4 K 236 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SER SEQRES 5 K 236 ASP ARG GLU THR THR THR TYR ASN PRO SER LEU ASN SER SEQRES 6 K 236 ARG ALA VAL ILE SER ARG ASP THR SER LYS ASN GLN LEU SEQRES 7 K 236 SER LEU GLN LEU ARG SER VAL THR THR ALA ASP THR ALA SEQRES 8 K 236 ILE TYR PHE CYS ALA THR ALA ARG ARG GLY GLN ARG ILE SEQRES 9 K 236 TYR GLY VAL VAL SER PHE GLY GLU PHE PHE TYR TYR TYR SEQRES 10 K 236 TYR MET ASP VAL TRP GLY LYS GLY THR ALA VAL THR VAL SEQRES 11 K 236 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 12 K 236 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 13 K 236 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 14 K 236 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 15 K 236 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 16 K 236 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 17 K 236 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 18 K 236 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 19 K 236 CYS ASP SEQRES 1 Y 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 Y 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 Y 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 Y 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 Y 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 Y 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 Y 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 Y 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 Y 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 Y 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 Y 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 Y 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 X 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 X 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 X 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 X 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 X 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 X 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 X 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 X 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 X 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 X 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 X 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 X 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 Z 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 Z 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 Z 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 Z 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 Z 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 Z 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 Z 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 Z 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 Z 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 Z 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 Z 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 Z 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP 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 G 601 14 HET NAG G 602 14 HET NAG G 603 14 HET NAG G 604 14 HET NAG G 605 14 HET NAG G 606 14 HET NAG G 607 14 HET NAG M 601 14 HET NAG M 602 14 HET NAG M 603 14 HET NAG M 604 14 HET NAG M 605 14 HET NAG M 606 14 HET NAG M 607 14 HET NAG M 608 14 HET NAG Y 701 14 HET NAG Y 702 14 HET NAG Y 703 14 HET NAG X 701 14 HET NAG X 702 14 HET NAG Z 701 14 HET NAG Z 702 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 NAG R 1 14 HET NAG R 2 14 HET BMA R 3 11 HET MAN R 4 11 HET MAN R 5 11 HET MAN R 6 11 HET MAN R 7 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 NAG V 1 14 HET NAG V 2 14 HET NAG W 1 14 HET NAG W 2 14 HET NAG a 1 14 HET NAG a 2 14 HET NAG a 3 14 HET MAN a 4 11 HET MAN a 5 11 HET MAN a 6 11 HET MAN a 7 11 HET MAN a 8 11 HET MAN a 9 11 HET NAG b 1 14 HET NAG b 2 14 HET NAG c 1 14 HET NAG c 2 14 HET BMA c 3 11 HET NAG d 1 14 HET NAG d 2 14 HET NAG e 1 14 HET NAG e 2 14 HET BMA e 3 11 HET NAG f 1 14 HET NAG f 2 14 HET NAG g 1 14 HET NAG g 2 14 HET BMA g 3 11 HET MAN g 4 11 HET MAN g 5 11 HET MAN g 6 11 HET MAN h 1 11 HET MAN h 2 11 HET MAN h 3 11 HET NAG i 1 14 HET NAG i 2 14 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 19 NAG 63(C8 H15 N O6) FORMUL 49 BMA 6(C6 H12 O6) FORMUL 51 MAN 16(C6 H12 O6) HELIX 1 AA1 THR F 28 TYR F 32 5 5 HELIX 2 AA2 ARG F 87 THR F 91 5 5 HELIX 3 AA3 SER F 165 ALA F 167 5 3 HELIX 4 AA4 PRO F 194 LEU F 198 5 5 HELIX 5 AA5 THR H 28 TYR H 32 5 5 HELIX 6 AA6 ARG H 87 THR H 91 5 5 HELIX 7 AA7 SER H 165 ALA H 167 5 3 HELIX 8 AA8 PRO H 194 LEU H 198 5 5 HELIX 9 AA9 PRO H 211 ASN H 213 5 3 HELIX 10 AB1 SER I 122 ALA I 128 1 7 HELIX 11 AB2 THR I 182 LYS I 187 1 6 HELIX 12 AB3 SER L 122 ALA L 128 1 7 HELIX 13 AB4 THR L 182 LYS L 187 1 6 HELIX 14 AB5 THR N 28 TYR N 32 5 5 HELIX 15 AB6 GLN N 62 GLN N 65 5 4 HELIX 16 AB7 ARG N 87 THR N 91 5 5 HELIX 17 AB8 SER N 165 ALA N 167 5 3 HELIX 18 AB9 SER N 196 LEU N 198 5 3 HELIX 19 AC1 LYS N 210 ASN N 213 5 4 HELIX 20 AC2 SER O 122 ALA O 128 1 7 HELIX 21 AC3 THR O 182 LYS O 187 1 6 HELIX 22 AC4 GLU A 79 GLU A 83 5 5 HELIX 23 AC5 SER A 121 GLN A 126 1 6 HELIX 24 AC6 THR A 181 LYS A 186 1 6 HELIX 25 AC7 GLU C 79 GLU C 83 5 5 HELIX 26 AC8 SER C 121 GLN C 126 1 6 HELIX 27 AC9 THR C 181 LYS C 186 1 6 HELIX 28 AD1 ASN E 98 SER E 115 1 18 HELIX 29 AD2 LEU E 122 CYS E 126 5 5 HELIX 30 AD3 LYS E 335 ARG E 350 1 16 HELIX 31 AD4 MET E 475 TYR E 484 1 10 HELIX 32 AD5 ASN G 98 SER G 115 1 18 HELIX 33 AD6 LEU G 122 CYS G 126 5 5 HELIX 34 AD7 ASN G 195 THR G 198 5 4 HELIX 35 AD8 SER G 334 ARG G 350 1 17 HELIX 36 AD9 LYS G 351 PHE G 353 5 3 HELIX 37 AE1 ASN G 425 ARG G 429 5 5 HELIX 38 AE2 MET G 475 TYR G 484 1 10 HELIX 39 AE3 SER J 121 GLN J 126 1 6 HELIX 40 AE4 THR J 181 LYS J 186 1 6 HELIX 41 AE5 ASN M 98 SER M 115 1 18 HELIX 42 AE6 LEU M 122 CYS M 126 5 5 HELIX 43 AE7 SER M 334 ARG M 350 1 17 HELIX 44 AE8 MET M 475 TYR M 484 1 10 HELIX 45 AE9 SER B 28 TYR B 32 5 5 HELIX 46 AF1 PRO B 61 ASN B 64 5 4 HELIX 47 AF2 THR B 83 THR B 87 5 5 HELIX 48 AF3 PRO D 61 ASN D 64 5 4 HELIX 49 AF4 THR D 83 THR D 87 5 5 HELIX 50 AF5 SER K 28 TYR K 32 5 5 HELIX 51 AF6 PRO K 61 ASN K 64 5 4 HELIX 52 AF7 THR K 83 THR K 87 5 5 HELIX 53 AF8 THR Y 529 SER Y 534 1 6 HELIX 54 AF9 THR Y 536 ASN Y 543 1 8 HELIX 55 AG1 THR Y 569 TRP Y 596 1 28 HELIX 56 AG2 ASN Y 618 ASP Y 624 1 7 HELIX 57 AG3 THR Y 627 SER Y 636 1 10 HELIX 58 AG4 TYR Y 638 SER Y 649 1 12 HELIX 59 AG5 GLN Y 650 ALA Y 662 1 13 HELIX 60 AG6 THR X 529 SER X 534 1 6 HELIX 61 AG7 THR X 536 ASN X 543 1 8 HELIX 62 AG8 THR X 569 TRP X 596 1 28 HELIX 63 AG9 ASN X 618 ASP X 624 1 7 HELIX 64 AH1 THR X 627 ILE X 635 1 9 HELIX 65 AH2 TYR X 638 SER X 649 1 12 HELIX 66 AH3 GLN X 650 ALA X 662 1 13 HELIX 67 AH4 THR Z 529 SER Z 534 1 6 HELIX 68 AH5 THR Z 536 ASN Z 543 1 8 HELIX 69 AH6 THR Z 569 TRP Z 596 1 28 HELIX 70 AH7 ASN Z 618 ASP Z 624 1 7 HELIX 71 AH8 THR Z 627 ILE Z 635 1 9 HELIX 72 AH9 TYR Z 638 SER Z 649 1 12 HELIX 73 AI1 GLN Z 650 ALA Z 662 1 13 SHEET 1 AA1 4 GLN F 3 GLN F 6 0 SHEET 2 AA1 4 VAL F 18 SER F 25 -1 O LYS F 23 N VAL F 5 SHEET 3 AA1 4 THR F 78 LEU F 83 -1 O MET F 81 N VAL F 20 SHEET 4 AA1 4 VAL F 68 ASP F 73 -1 N THR F 71 O TYR F 80 SHEET 1 AA2 7 GLU F 10 LYS F 12 0 SHEET 2 AA2 7 MET F 34 GLN F 39 0 SHEET 3 AA2 7 LEU F 45 ILE F 51 -1 O MET F 48 N TRP F 36 SHEET 4 AA2 7 THR F 58 TYR F 60 -1 O ASN F 59 N TRP F 50 SHEET 5 AA2 7 ALA F 92 ARG F 99 -1 O TYR F 95 N VAL F 37 SHEET 6 AA2 7 PHE F 109 TRP F 112 -1 O HIS F 111 N ARG F 98 SHEET 7 AA2 7 THR F 116 VAL F 120 -1 O THR F 116 N TYR F 94 SHEET 1 AA3 5 SER F 129 LEU F 133 0 SHEET 2 AA3 5 ALA F 145 TYR F 154 -1 O LEU F 150 N PHE F 131 SHEET 3 AA3 5 VAL F 172 THR F 174 0 SHEET 4 AA3 5 VAL F 178 LEU F 179 0 SHEET 5 AA3 5 TYR F 185 VAL F 193 -1 O SER F 186 N VAL F 178 SHEET 1 AA4 3 THR F 160 TRP F 163 0 SHEET 2 AA4 3 ILE F 204 HIS F 209 -1 O ASN F 206 N SER F 162 SHEET 3 AA4 3 THR F 214 LYS F 219 -1 O VAL F 216 N VAL F 207 SHEET 1 AA5 4 GLN H 3 GLN H 6 0 SHEET 2 AA5 4 VAL H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AA5 4 THR H 78 LEU H 83 -1 O ALA H 79 N CYS H 22 SHEET 4 AA5 4 VAL H 68 ASP H 73 -1 N THR H 71 O TYR H 80 SHEET 1 AA6 7 GLU H 10 LYS H 12 0 SHEET 2 AA6 7 MET H 34 GLN H 39 0 SHEET 3 AA6 7 LEU H 45 ILE H 51 -1 O MET H 48 N TRP H 36 SHEET 4 AA6 7 THR H 58 TYR H 60 -1 O ASN H 59 N TRP H 50 SHEET 5 AA6 7 ALA H 92 ARG H 98 -1 O TYR H 95 N VAL H 37 SHEET 6 AA6 7 HIS H 111 TRP H 112 -1 O HIS H 111 N ARG H 98 SHEET 7 AA6 7 THR H 116 VAL H 120 -1 O THR H 116 N TYR H 94 SHEET 1 AA7 5 SER H 129 LEU H 133 0 SHEET 2 AA7 5 ALA H 145 TYR H 154 -1 O LYS H 152 N SER H 129 SHEET 3 AA7 5 VAL H 172 THR H 174 0 SHEET 4 AA7 5 VAL H 178 LEU H 179 0 SHEET 5 AA7 5 TYR H 185 VAL H 193 -1 O SER H 186 N VAL H 178 SHEET 1 AA8 3 VAL H 159 TRP H 163 0 SHEET 2 AA8 3 ILE H 204 HIS H 209 -1 O ASN H 206 N SER H 162 SHEET 3 AA8 3 THR H 214 LYS H 219 -1 O VAL H 216 N VAL H 207 SHEET 1 AA9 4 LEU I 4 THR I 5 0 SHEET 2 AA9 4 ILE I 19 GLY I 25 -1 O THR I 24 N THR I 5 SHEET 3 AA9 4 THR I 70 ILE I 75 -1 O ALA I 71 N CYS I 23 SHEET 4 AA9 4 PHE I 62 SER I 67 -1 N SER I 63 O THR I 74 SHEET 1 AB1 6 SER I 9 VAL I 11 0 SHEET 2 AB1 6 SER I 34 GLN I 38 0 SHEET 3 AB1 6 LYS I 45 ILE I 48 -1 O MET I 47 N TRP I 35 SHEET 4 AB1 6 ASP I 85 SER I 90 -1 O ASP I 85 N GLN I 38 SHEET 5 AB1 6 PHE I 97 PHE I 98 -1 O PHE I 97 N SER I 90 SHEET 6 AB1 6 THR I 102 VAL I 104 -1 O THR I 102 N TYR I 86 SHEET 1 AB2 5 SER I 115 PHE I 119 0 SHEET 2 AB2 5 ALA I 131 PHE I 140 -1 O LEU I 136 N THR I 117 SHEET 3 AB2 5 VAL I 160 GLU I 161 0 SHEET 4 AB2 5 SER I 166 LYS I 167 0 SHEET 5 AB2 5 TYR I 173 LEU I 181 -1 O ALA I 174 N SER I 166 SHEET 1 AB3 5 VAL I 145 LYS I 150 0 SHEET 2 AB3 5 PRO I 155 VAL I 156 -1 O VAL I 156 N TRP I 149 SHEET 3 AB3 5 TYR I 192 HIS I 198 -1 O GLN I 195 N ALA I 148 SHEET 4 AB3 5 SER I 201 VAL I 203 -1 O SER I 201 N HIS I 198 SHEET 5 AB3 5 THR I 206 VAL I 207 -1 O VAL I 207 N TYR I 192 SHEET 1 AB4 4 LEU L 4 THR L 5 0 SHEET 2 AB4 4 ILE L 19 GLY L 25 -1 O THR L 24 N THR L 5 SHEET 3 AB4 4 THR L 70 ILE L 75 -1 O ALA L 71 N CYS L 23 SHEET 4 AB4 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB5 6 SER L 9 VAL L 11 0 SHEET 2 AB5 6 SER L 34 GLN L 38 0 SHEET 3 AB5 6 LYS L 45 ILE L 48 -1 O ILE L 48 N TRP L 35 SHEET 4 AB5 6 ASP L 85 SER L 90 -1 O SER L 89 N SER L 34 SHEET 5 AB5 6 PHE L 97 PHE L 98 -1 O PHE L 97 N SER L 90 SHEET 6 AB5 6 THR L 102 VAL L 104 -1 O THR L 102 N TYR L 86 SHEET 1 AB6 5 SER L 115 PHE L 119 0 SHEET 2 AB6 5 ALA L 131 PHE L 140 -1 O LEU L 136 N THR L 117 SHEET 3 AB6 5 VAL L 160 THR L 162 0 SHEET 4 AB6 5 SER L 166 LYS L 167 0 SHEET 5 AB6 5 TYR L 173 LEU L 181 -1 O ALA L 174 N SER L 166 SHEET 1 AB7 5 THR L 146 LYS L 150 0 SHEET 2 AB7 5 PRO L 155 VAL L 156 -1 O VAL L 156 N TRP L 149 SHEET 3 AB7 5 TYR L 192 HIS L 198 -1 O GLN L 195 N ALA L 148 SHEET 4 AB7 5 SER L 201 VAL L 203 -1 O SER L 201 N HIS L 198 SHEET 5 AB7 5 THR L 206 VAL L 207 -1 O VAL L 207 N TYR L 192 SHEET 1 AB8 4 GLN N 3 GLN N 6 0 SHEET 2 AB8 4 SER N 17 SER N 25 -1 O LYS N 23 N VAL N 5 SHEET 3 AB8 4 THR N 78 SER N 84 -1 O MET N 81 N VAL N 20 SHEET 4 AB8 4 VAL N 68 ASP N 73 -1 N THR N 71 O TYR N 80 SHEET 1 AB9 7 GLU N 10 LYS N 12 0 SHEET 2 AB9 7 MET N 34 GLN N 39 0 SHEET 3 AB9 7 GLU N 46 ILE N 51 -1 O MET N 48 N TRP N 36 SHEET 4 AB9 7 THR N 58 TYR N 60 -1 O ASN N 59 N TRP N 50 SHEET 5 AB9 7 VAL N 93 ARG N 98 -1 O TYR N 95 N VAL N 37 SHEET 6 AB9 7 HIS N 111 TRP N 112 -1 O HIS N 111 N ARG N 98 SHEET 7 AB9 7 THR N 116 VAL N 120 -1 O THR N 116 N TYR N 94 SHEET 1 AC1 5 SER N 129 LEU N 133 0 SHEET 2 AC1 5 THR N 144 TYR N 154 -1 O LEU N 150 N PHE N 131 SHEET 3 AC1 5 VAL N 172 THR N 174 0 SHEET 4 AC1 5 VAL N 178 LEU N 179 0 SHEET 5 AC1 5 TYR N 185 PRO N 194 -1 O SER N 186 N VAL N 178 SHEET 1 AC2 3 THR N 160 TRP N 163 0 SHEET 2 AC2 3 ILE N 204 HIS N 209 -1 O ASN N 206 N SER N 162 SHEET 3 AC2 3 THR N 214 LYS N 219 -1 O VAL N 216 N VAL N 207 SHEET 1 AC3 4 LEU O 4 THR O 5 0 SHEET 2 AC3 4 ILE O 19 GLY O 25 -1 O THR O 24 N THR O 5 SHEET 3 AC3 4 THR O 70 ILE O 75 -1 O ALA O 71 N CYS O 23 SHEET 4 AC3 4 PHE O 62 SER O 67 -1 N SER O 65 O SER O 72 SHEET 1 AC4 6 SER O 9 SER O 12 0 SHEET 2 AC4 6 SER O 34 GLN O 38 0 SHEET 3 AC4 6 LYS O 45 TYR O 49 -1 O ILE O 48 N TRP O 35 SHEET 4 AC4 6 ASP O 85 SER O 90 -1 O SER O 89 N SER O 34 SHEET 5 AC4 6 PHE O 97 PHE O 98 -1 O PHE O 97 N SER O 90 SHEET 6 AC4 6 THR O 102 PHE O 105 -1 O THR O 102 N TYR O 86 SHEET 1 AC5 5 SER O 115 PHE O 119 0 SHEET 2 AC5 5 ALA O 131 PHE O 140 -1 O LEU O 136 N THR O 117 SHEET 3 AC5 5 VAL O 160 GLU O 161 0 SHEET 4 AC5 5 SER O 166 LYS O 167 0 SHEET 5 AC5 5 TYR O 173 LEU O 181 -1 O ALA O 174 N SER O 166 SHEET 1 AC6 5 VAL O 145 LYS O 150 0 SHEET 2 AC6 5 PRO O 155 VAL O 156 -1 O VAL O 156 N TRP O 149 SHEET 3 AC6 5 TYR O 192 HIS O 198 -1 O GLN O 195 N ALA O 148 SHEET 4 AC6 5 SER O 201 VAL O 203 -1 O SER O 201 N HIS O 198 SHEET 5 AC6 5 THR O 206 VAL O 207 -1 O VAL O 207 N TYR O 192 SHEET 1 AC7 2 VAL A 6 VAL A 13 0 SHEET 2 AC7 2 ALA A 101 VAL A 106 1 O THR A 105 N VAL A 13 SHEET 1 AC8 3 ARG A 20 SER A 22 0 SHEET 2 AC8 3 THR A 72 ILE A 75 -1 O LEU A 73 N ILE A 21 SHEET 3 AC8 3 PHE A 62 SER A 63 -1 N SER A 63 O THR A 74 SHEET 1 AC9 3 ILE A 45 ILE A 48 0 SHEET 2 AC9 3 GLN A 34 HIS A 38 -1 N GLN A 37 O ILE A 45 SHEET 3 AC9 3 ASP A 85 HIS A 89 -1 O ASP A 85 N HIS A 38 SHEET 1 AD1 5 SER A 114 PHE A 118 0 SHEET 2 AD1 5 ALA A 130 PHE A 139 -1 O LEU A 135 N THR A 116 SHEET 3 AD1 5 VAL A 159 THR A 161 0 SHEET 4 AD1 5 SER A 165 LYS A 166 0 SHEET 5 AD1 5 TYR A 172 LEU A 180 -1 O ALA A 173 N SER A 165 SHEET 1 AD2 4 SER A 153 VAL A 155 0 SHEET 2 AD2 4 THR A 145 ALA A 150 -1 N ALA A 150 O SER A 153 SHEET 3 AD2 4 TYR A 191 HIS A 197 -1 O GLN A 194 N ALA A 147 SHEET 4 AD2 4 SER A 200 VAL A 206 -1 O SER A 200 N HIS A 197 SHEET 1 AD3 5 VAL C 6 VAL C 13 0 SHEET 2 AD3 5 ALA C 101 VAL C 106 1 O THR C 105 N VAL C 13 SHEET 3 AD3 5 ASP C 85 HIS C 89 -1 N TYR C 86 O THR C 102 SHEET 4 AD3 5 GLN C 34 HIS C 38 -1 N HIS C 38 O ASP C 85 SHEET 5 AD3 5 ILE C 45 ILE C 48 -1 O ILE C 48 N TRP C 35 SHEET 1 AD4 3 ALA C 19 SER C 22 0 SHEET 2 AD4 3 THR C 72 ILE C 75 -1 O LEU C 73 N ILE C 21 SHEET 3 AD4 3 PHE C 62 SER C 63 -1 N SER C 63 O THR C 74 SHEET 1 AD5 5 SER C 114 PHE C 118 0 SHEET 2 AD5 5 ALA C 130 PHE C 139 -1 O LEU C 135 N THR C 116 SHEET 3 AD5 5 VAL C 159 THR C 161 0 SHEET 4 AD5 5 SER C 165 LYS C 166 0 SHEET 5 AD5 5 TYR C 172 LEU C 180 -1 O ALA C 173 N SER C 165 SHEET 1 AD6 4 SER C 153 VAL C 155 0 SHEET 2 AD6 4 THR C 145 ALA C 150 -1 N ALA C 150 O SER C 153 SHEET 3 AD6 4 TYR C 191 HIS C 197 -1 O GLN C 194 N ALA C 147 SHEET 4 AD6 4 SER C 200 VAL C 206 -1 O SER C 200 N HIS C 197 SHEET 1 AD7 3 LEU E 494 THR E 499 0 SHEET 2 AD7 3 TRP E 35 TYR E 40 -1 N TRP E 35 O THR E 499 SHEET 3 AD7 3 ILE X 603 PRO X 609 -1 O CYS X 604 N VAL E 38 SHEET 1 AD8 5 TRP E 45 ASP E 47 0 SHEET 2 AD8 5 VAL E 488 ILE E 491 -1 O LYS E 490 N LYS E 46 SHEET 3 AD8 5 PHE E 223 CYS E 228 -1 N ALA E 224 O VAL E 489 SHEET 4 AD8 5 VAL E 242 VAL E 245 -1 O VAL E 245 N ILE E 225 SHEET 5 AD8 5 ILE E 84 LEU E 86 -1 N ILE E 84 O THR E 244 SHEET 1 AD9 2 GLU E 91 ASN E 94 0 SHEET 2 AD9 2 THR E 236 CYS E 239 -1 O CYS E 239 N GLU E 91 SHEET 1 AE1 5 ARG E 169 TYR E 177 0 SHEET 2 AE1 5 LEU E 154 THR E 162 -1 N MET E 161 O GLN E 170 SHEET 3 AE1 5 LEU E 129 ASN E 133 -1 N GLN E 130 O SER E 158 SHEET 4 AE1 5 SER E 190 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 5 AE1 5 ILE E 181 PRO E 183 -1 N VAL E 182 O ARG E 192 SHEET 1 AE2 3 ALA E 200 GLN E 203 0 SHEET 2 AE2 3 GLN E 432 TYR E 435 1 O ALA E 433 N THR E 202 SHEET 3 AE2 3 ILE E 423 ILE E 424 -1 N ILE E 424 O MET E 434 SHEET 1 AE312 LEU E 259 LEU E 261 0 SHEET 2 AE312 MET E 271 ARG E 273 0 SHEET 3 AE312 ILE E 284 GLY E 312 -1 O LEU E 285 N ARG E 273 SHEET 4 AE312 GLN E 315 GLY E 321 -1 O GLY E 321 N THR E 303 SHEET 5 AE312 HIS E 330 SER E 334 -1 O ASN E 332 N ASN E 295 SHEET 6 AE312 ILE E 358 PHE E 361 0 SHEET 7 AE312 THR E 373 CYS E 378 0 SHEET 8 AE312 GLU E 381 ASP E 386 -1 O CYS E 385 N HIS E 374 SHEET 9 AE312 SER E 393 TRP E 395 -1 O TRP E 395 N ILE E 359 SHEET 10 AE312 SER E 413 LYS E 421 -1 O PRO E 417 N ASP E 386 SHEET 11 AE312 GLY E 441 ARG E 456 -1 O THR E 450 N PHE E 288 SHEET 12 AE312 THR E 465 PRO E 470 -1 O ARG E 469 N THR E 455 SHEET 1 AE4 3 LEU G 494 THR G 499 0 SHEET 2 AE4 3 TRP G 35 TYR G 40 -1 N TRP G 35 O THR G 499 SHEET 3 AE4 3 ILE Y 603 PRO Y 609 -1 O VAL Y 608 N VAL G 36 SHEET 1 AE5 5 TRP G 45 ASP G 47 0 SHEET 2 AE5 5 VAL G 488 ILE G 491 -1 O LYS G 490 N LYS G 46 SHEET 3 AE5 5 PHE G 223 CYS G 228 -1 N ALA G 224 O VAL G 489 SHEET 4 AE5 5 VAL G 242 VAL G 245 -1 O VAL G 245 N ILE G 225 SHEET 5 AE5 5 ILE G 84 LEU G 86 -1 N ILE G 84 O THR G 244 SHEET 1 AE6 2 GLU G 91 ASN G 94 0 SHEET 2 AE6 2 THR G 236 CYS G 239 -1 O CYS G 239 N GLU G 91 SHEET 1 AE7 3 GLN G 130 ASN G 133 0 SHEET 2 AE7 3 LEU G 154 THR G 162 -1 O SER G 158 N GLN G 130 SHEET 3 AE7 3 ARG G 169 TYR G 177 -1 O GLN G 170 N MET G 161 SHEET 1 AE8 2 ILE G 181 PRO G 183 0 SHEET 2 AE8 2 TYR G 191 LEU G 193 -1 O ARG G 192 N VAL G 182 SHEET 1 AE9 3 ALA G 200 GLN G 203 0 SHEET 2 AE9 3 GLN G 432 TYR G 435 1 O TYR G 435 N THR G 202 SHEET 3 AE9 3 ILE G 423 ILE G 424 -1 N ILE G 424 O MET G 434 SHEET 1 AF1 7 LEU G 259 LEU G 260 0 SHEET 2 AF1 7 MET G 271 SER G 274 0 SHEET 3 AF1 7 ILE G 284 GLN G 287 -1 O LEU G 285 N ARG G 273 SHEET 4 AF1 7 ILE G 358 PHE G 361 0 SHEET 5 AF1 7 SER G 393 TRP G 395 -1 O TRP G 395 N ILE G 359 SHEET 6 AF1 7 GLY G 451 ARG G 456 -1 O LEU G 452 N VAL G 286 SHEET 7 AF1 7 THR G 465 PRO G 470 -1 O ARG G 469 N THR G 455 SHEET 1 AF2 6 HIS G 374 CYS G 378 0 SHEET 2 AF2 6 GLU G 381 CYS G 385 -1 O CYS G 385 N HIS G 374 SHEET 3 AF2 6 LEU G 416 LYS G 421 -1 O ARG G 419 N TYR G 384 SHEET 4 AF2 6 HIS G 330 CYS G 331 -1 N CYS G 331 O LEU G 416 SHEET 5 AF2 6 ILE G 294 ASN G 302 -1 N THR G 297 O HIS G 330 SHEET 6 AF2 6 GLY G 441 SER G 447 -1 O SER G 447 N ILE G 294 SHEET 1 AF3 2 ARG G 304 ARG G 308 0 SHEET 2 AF3 2 TRP G 316 THR G 320 -1 O ALA G 319 N LYS G 305 SHEET 1 AF4 5 VAL J 6 VAL J 13 0 SHEET 2 AF4 5 ALA J 101 VAL J 106 1 O ALA J 101 N SER J 7 SHEET 3 AF4 5 ASP J 85 HIS J 89 -1 N TYR J 86 O THR J 102 SHEET 4 AF4 5 GLN J 34 HIS J 38 -1 N GLN J 34 O HIS J 89 SHEET 5 AF4 5 ILE J 45 ILE J 48 -1 O ILE J 45 N GLN J 37 SHEET 1 AF5 3 THR J 18 SER J 22 0 SHEET 2 AF5 3 THR J 72 SER J 76 -1 O LEU J 73 N ILE J 21 SHEET 3 AF5 3 PHE J 62 SER J 63 -1 N SER J 63 O THR J 74 SHEET 1 AF6 5 SER J 114 PHE J 118 0 SHEET 2 AF6 5 ALA J 130 PHE J 139 -1 O SER J 137 N SER J 114 SHEET 3 AF6 5 VAL J 159 THR J 161 0 SHEET 4 AF6 5 SER J 165 LYS J 166 0 SHEET 5 AF6 5 TYR J 172 LEU J 180 -1 O ALA J 173 N SER J 165 SHEET 1 AF7 4 SER J 153 VAL J 155 0 SHEET 2 AF7 4 VAL J 144 ALA J 150 -1 N ALA J 150 O SER J 153 SHEET 3 AF7 4 TYR J 191 HIS J 197 -1 O GLN J 194 N ALA J 147 SHEET 4 AF7 4 SER J 200 VAL J 206 -1 O SER J 200 N HIS J 197 SHEET 1 AF8 3 LEU M 494 THR M 499 0 SHEET 2 AF8 3 TRP M 35 TYR M 40 -1 N TRP M 35 O THR M 499 SHEET 3 AF8 3 ILE Z 603 PRO Z 609 -1 O CYS Z 604 N VAL M 38 SHEET 1 AF9 5 TRP M 45 ASP M 47 0 SHEET 2 AF9 5 VAL M 488 ILE M 491 -1 O LYS M 490 N LYS M 46 SHEET 3 AF9 5 PHE M 223 CYS M 228 -1 N ALA M 224 O VAL M 489 SHEET 4 AF9 5 VAL M 242 VAL M 245 -1 O SER M 243 N LYS M 227 SHEET 5 AF9 5 ILE M 84 LEU M 86 -1 N ILE M 84 O THR M 244 SHEET 1 AG1 2 GLU M 91 ASN M 94 0 SHEET 2 AG1 2 THR M 236 CYS M 239 -1 O CYS M 239 N GLU M 91 SHEET 1 AG2 3 LEU M 129 GLN M 130 0 SHEET 2 AG2 3 SER M 190 LEU M 193 -1 O TYR M 191 N LEU M 129 SHEET 3 AG2 3 ILE M 181 PRO M 183 -1 N VAL M 182 O ARG M 192 SHEET 1 AG3 2 LEU M 154 LYS M 155 0 SHEET 2 AG3 2 PHE M 176 TYR M 177 -1 O PHE M 176 N LYS M 155 SHEET 1 AG4 2 SER M 158 THR M 162 0 SHEET 2 AG4 2 ARG M 169 HIS M 173 -1 O GLN M 170 N MET M 161 SHEET 1 AG5 3 ALA M 200 GLN M 203 0 SHEET 2 AG5 3 GLN M 432 TYR M 435 1 O TYR M 435 N THR M 202 SHEET 3 AG5 3 ILE M 423 ILE M 424 -1 N ILE M 424 O MET M 434 SHEET 1 AG611 LEU M 259 LEU M 261 0 SHEET 2 AG611 MET M 271 SER M 274 0 SHEET 3 AG611 ILE M 284 ASN M 302 -1 O LEU M 285 N ARG M 273 SHEET 4 AG611 HIS M 330 VAL M 333 -1 O ASN M 332 N ASN M 295 SHEET 5 AG611 ILE M 358 PHE M 361 0 SHEET 6 AG611 HIS M 374 CYS M 378 0 SHEET 7 AG611 GLU M 381 CYS M 385 -1 O CYS M 385 N HIS M 374 SHEET 8 AG611 SER M 393 TRP M 395 -1 O TRP M 395 N ILE M 359 SHEET 9 AG611 ILE M 414 LYS M 421 -1 O ARG M 419 N TYR M 384 SHEET 10 AG611 GLY M 441 ARG M 456 -1 O SER M 447 N ILE M 294 SHEET 11 AG611 THR M 465 PRO M 470 -1 O ARG M 469 N THR M 455 SHEET 1 AG7 2 ARG M 304 GLY M 312 0 SHEET 2 AG7 2 GLN M 315 THR M 320 -1 O ALA M 319 N LYS M 305 SHEET 1 AG8 4 GLN B 3 SER B 7 0 SHEET 2 AG8 4 THR B 17 SER B 25 -1 O SER B 25 N GLN B 3 SHEET 3 AG8 4 GLN B 77 ARG B 82A-1 O LEU B 82 N LEU B 18 SHEET 4 AG8 4 ALA B 67 ASP B 72 -1 N SER B 70 O SER B 79 SHEET 1 AG9 7 LEU B 11 VAL B 12 0 SHEET 2 AG9 7 TYR B 33 GLN B 39 0 SHEET 3 AG9 7 LEU B 45 ILE B 51 -1 O ILE B 51 N TRP B 34 SHEET 4 AG9 7 THR B 57 TYR B 59 -1 O THR B 58 N TYR B 50 SHEET 5 AG9 7 ALA B 88 ILE B 100A-1 O PHE B 91 N ILE B 37 SHEET 6 AG9 7 PHE B 100J TRP B 103 -1 O TYR B 100M N GLY B 98 SHEET 7 AG9 7 THR B 107 VAL B 111 -1 O VAL B 109 N ALA B 88 SHEET 1 AH1 5 SER B 120 LEU B 124 0 SHEET 2 AH1 5 THR B 135 TYR B 145 -1 O LEU B 141 N PHE B 122 SHEET 3 AH1 5 VAL B 163 THR B 165 0 SHEET 4 AH1 5 VAL B 169 LEU B 170 0 SHEET 5 AH1 5 TYR B 176 PRO B 185 -1 O SER B 177 N VAL B 169 SHEET 1 AH2 3 THR B 151 TRP B 154 0 SHEET 2 AH2 3 ILE B 195 HIS B 200 -1 O ASN B 197 N SER B 153 SHEET 3 AH2 3 THR B 205 LYS B 210 -1 O LYS B 209 N CYS B 196 SHEET 1 AH3 4 GLN D 3 SER D 7 0 SHEET 2 AH3 4 THR D 17 SER D 25 -1 O ILE D 23 N GLN D 5 SHEET 3 AH3 4 GLN D 77 ARG D 82A-1 O LEU D 82 N LEU D 18 SHEET 4 AH3 4 ALA D 67 ASP D 72 -1 N VAL D 68 O GLN D 81 SHEET 1 AH4 7 LEU D 11 VAL D 12 0 SHEET 2 AH4 7 TYR D 33 GLN D 39 0 SHEET 3 AH4 7 LEU D 45 ILE D 51 -1 O ILE D 51 N TRP D 34 SHEET 4 AH4 7 THR D 57 TYR D 59 -1 O THR D 58 N TYR D 50 SHEET 5 AH4 7 ALA D 88 ILE D 100A-1 O PHE D 91 N ILE D 37 SHEET 6 AH4 7 PHE D 100J TRP D 103 -1 O TYR D 100M N GLY D 98 SHEET 7 AH4 7 THR D 107 VAL D 111 -1 O VAL D 109 N ALA D 88 SHEET 1 AH5 5 PHE D 122 LEU D 124 0 SHEET 2 AH5 5 THR D 135 TYR D 145 -1 O LEU D 141 N PHE D 122 SHEET 3 AH5 5 VAL D 163 THR D 165 0 SHEET 4 AH5 5 VAL D 169 LEU D 170 0 SHEET 5 AH5 5 TYR D 176 PRO D 185 -1 O SER D 177 N VAL D 169 SHEET 1 AH6 2 THR D 151 TRP D 154 0 SHEET 2 AH6 2 CYS D 196 ASN D 199 -1 O ASN D 197 N SER D 153 SHEET 1 AH7 4 GLN K 3 SER K 7 0 SHEET 2 AH7 4 VAL K 20 SER K 25 -1 O SER K 25 N GLN K 3 SHEET 3 AH7 4 GLN K 77 GLN K 81 -1 O LEU K 78 N CYS K 22 SHEET 4 AH7 4 VAL K 68 ASP K 72 -1 N ASP K 72 O GLN K 77 SHEET 1 AH8 2 LEU K 11 VAL K 12 0 SHEET 2 AH8 2 THR K 110 VAL K 111 1 O THR K 110 N VAL K 12 SHEET 1 AH9 6 TYR K 33 GLN K 39 0 SHEET 2 AH9 6 LEU K 45 ILE K 51 -1 O ILE K 51 N TRP K 34 SHEET 3 AH9 6 THR K 57 TYR K 59 -1 O THR K 58 N TYR K 50 SHEET 4 AH9 6 ILE K 89 ILE K 100A-1 O PHE K 91 N ILE K 37 SHEET 5 AH9 6 PHE K 100J TRP K 103 -1 O TYR K 100M N GLY K 98 SHEET 6 AH9 6 THR K 107 ALA K 108 -1 O THR K 107 N TYR K 90 SHEET 1 AI1 5 PHE K 122 LEU K 124 0 SHEET 2 AI1 5 THR K 135 TYR K 145 -1 O LEU K 141 N PHE K 122 SHEET 3 AI1 5 VAL K 163 THR K 165 0 SHEET 4 AI1 5 VAL K 169 LEU K 170 0 SHEET 5 AI1 5 TYR K 176 PRO K 185 -1 O SER K 177 N VAL K 169 SHEET 1 AI2 2 THR K 151 TRP K 154 0 SHEET 2 AI2 2 CYS K 196 ASN K 199 -1 O ASN K 197 N SER K 153 SSBOND 1 CYS F 22 CYS F 96 1555 1555 2.04 SSBOND 2 CYS F 149 CYS F 205 1555 1555 2.03 SSBOND 3 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 4 CYS H 149 CYS H 205 1555 1555 2.03 SSBOND 5 CYS I 23 CYS I 88 1555 1555 2.04 SSBOND 6 CYS I 135 CYS I 194 1555 1555 2.03 SSBOND 7 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 8 CYS L 135 CYS L 194 1555 1555 2.04 SSBOND 9 CYS N 22 CYS N 96 1555 1555 2.04 SSBOND 10 CYS N 149 CYS N 205 1555 1555 2.03 SSBOND 11 CYS O 23 CYS O 88 1555 1555 2.03 SSBOND 12 CYS O 135 CYS O 194 1555 1555 2.03 SSBOND 13 CYS A 23 CYS A 88 1555 1555 2.04 SSBOND 14 CYS A 134 CYS A 193 1555 1555 2.03 SSBOND 15 CYS C 23 CYS C 88 1555 1555 2.04 SSBOND 16 CYS C 134 CYS C 193 1555 1555 2.03 SSBOND 17 CYS E 54 CYS E 74 1555 1555 2.04 SSBOND 18 CYS E 119 CYS E 205 1555 1555 2.04 SSBOND 19 CYS E 126 CYS E 196 1555 1555 2.04 SSBOND 20 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 21 CYS E 218 CYS E 247 1555 1555 2.03 SSBOND 22 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 23 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 24 CYS E 378 CYS E 445 1555 1555 2.03 SSBOND 25 CYS E 385 CYS E 418 1555 1555 2.03 SSBOND 26 CYS E 501 CYS X 605 1555 1555 2.03 SSBOND 27 CYS G 54 CYS G 74 1555 1555 2.04 SSBOND 28 CYS G 119 CYS G 205 1555 1555 2.04 SSBOND 29 CYS G 126 CYS G 196 1555 1555 2.04 SSBOND 30 CYS G 131 CYS G 157 1555 1555 2.03 SSBOND 31 CYS G 218 CYS G 247 1555 1555 2.03 SSBOND 32 CYS G 228 CYS G 239 1555 1555 2.04 SSBOND 33 CYS G 296 CYS G 331 1555 1555 2.03 SSBOND 34 CYS G 378 CYS G 445 1555 1555 2.03 SSBOND 35 CYS G 385 CYS G 418 1555 1555 2.03 SSBOND 36 CYS G 501 CYS Y 605 1555 1555 2.03 SSBOND 37 CYS J 23 CYS J 88 1555 1555 2.04 SSBOND 38 CYS J 134 CYS J 193 1555 1555 2.03 SSBOND 39 CYS M 54 CYS M 74 1555 1555 2.03 SSBOND 40 CYS M 119 CYS M 205 1555 1555 2.04 SSBOND 41 CYS M 126 CYS M 196 1555 1555 2.03 SSBOND 42 CYS M 131 CYS M 157 1555 1555 2.03 SSBOND 43 CYS M 218 CYS M 247 1555 1555 2.03 SSBOND 44 CYS M 228 CYS M 239 1555 1555 2.03 SSBOND 45 CYS M 296 CYS M 331 1555 1555 2.03 SSBOND 46 CYS M 378 CYS M 445 1555 1555 2.03 SSBOND 47 CYS M 385 CYS M 418 1555 1555 2.03 SSBOND 48 CYS M 501 CYS Z 605 1555 1555 2.03 SSBOND 49 CYS B 22 CYS B 92 1555 1555 2.03 SSBOND 50 CYS B 140 CYS B 196 1555 1555 2.03 SSBOND 51 CYS D 22 CYS D 92 1555 1555 2.03 SSBOND 52 CYS D 140 CYS D 196 1555 1555 2.03 SSBOND 53 CYS K 22 CYS K 92 1555 1555 2.03 SSBOND 54 CYS K 140 CYS K 196 1555 1555 2.03 SSBOND 55 CYS Y 598 CYS Y 604 1555 1555 2.03 SSBOND 56 CYS X 598 CYS X 604 1555 1555 2.03 SSBOND 57 CYS Z 598 CYS Z 604 1555 1555 2.03 LINK ND2 ASN E 133 C1 NAG E 601 1555 1555 1.45 LINK ND2 ASN E 156 C1 NAG E 602 1555 1555 1.45 LINK ND2 ASN E 160 C1 NAG E 603 1555 1555 1.44 LINK ND2 ASN E 234 C1 NAG E 604 1555 1555 1.45 LINK ND2 ASN E 262 C1 NAG P 1 1555 1555 1.45 LINK ND2 ASN E 295 C1 NAG E 605 1555 1555 1.44 LINK ND2 ASN E 301 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN E 332 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN E 339 C1 NAG E 606 1555 1555 1.44 LINK ND2 ASN E 355 C1 NAG E 607 1555 1555 1.44 LINK ND2 ASN E 363 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN E 392 C1 NAG E 608 1555 1555 1.44 LINK ND2 ASN E 448 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN G 88 C1 NAG G 601 1555 1555 1.44 LINK ND2 ASN G 156 C1 NAG G 602 1555 1555 1.45 LINK ND2 ASN G 160 C1 NAG G 603 1555 1555 1.45 LINK ND2 ASN G 234 C1 NAG G 604 1555 1555 1.46 LINK ND2 ASN G 262 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN G 295 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN G 301 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN G 332 C1 NAG a 1 1555 1555 1.45 LINK ND2 ASN G 339 C1 NAG G 605 1555 1555 1.44 LINK ND2 ASN G 355 C1 NAG G 606 1555 1555 1.44 LINK ND2 ASN G 363 C1 NAG b 1 1555 1555 1.45 LINK ND2 ASN G 392 C1 NAG G 607 1555 1555 1.44 LINK ND2 ASN G 448 C1 NAG c 1 1555 1555 1.44 LINK ND2 ASN M 88 C1 NAG M 601 1555 1555 1.45 LINK ND2 ASN M 133 C1 NAG M 602 1555 1555 1.45 LINK ND2 ASN M 156 C1 NAG d 1 1555 1555 1.43 LINK ND2 ASN M 160 C1 NAG M 603 1555 1555 1.44 LINK ND2 ASN M 234 C1 NAG M 604 1555 1555 1.44 LINK ND2 ASN M 262 C1 NAG e 1 1555 1555 1.44 LINK ND2 ASN M 295 C1 NAG M 605 1555 1555 1.44 LINK ND2 ASN M 301 C1 NAG f 1 1555 1555 1.44 LINK ND2 ASN M 332 C1 NAG g 1 1555 1555 1.43 LINK ND2 ASN M 339 C1 NAG M 606 1555 1555 1.44 LINK ND2 ASN M 363 C1 NAG i 1 1555 1555 1.44 LINK ND2 ASN M 392 C1 NAG M 607 1555 1555 1.44 LINK ND2 ASN M 448 C1 NAG M 608 1555 1555 1.44 LINK ND2 ASN Y 611 C1 NAG Y 701 1555 1555 1.44 LINK ND2 ASN Y 618 C1 NAG Y 702 1555 1555 1.44 LINK ND2 ASN Y 637 C1 NAG Y 703 1555 1555 1.44 LINK ND2 ASN X 611 C1 NAG X 701 1555 1555 1.44 LINK ND2 ASN X 637 C1 NAG X 702 1555 1555 1.44 LINK ND2 ASN Z 611 C1 NAG Z 701 1555 1555 1.43 LINK ND2 ASN Z 618 C1 NAG Z 702 1555 1555 1.44 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.46 LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.45 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.45 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 O3 BMA R 3 C1 MAN R 4 1555 1555 1.44 LINK O6 BMA R 3 C1 MAN R 7 1555 1555 1.45 LINK O2 MAN R 4 C1 MAN R 5 1555 1555 1.44 LINK O2 MAN R 5 C1 MAN R 6 1555 1555 1.44 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.45 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.44 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.45 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 a 1 C1 NAG a 2 1555 1555 1.45 LINK O4 NAG a 2 C1 NAG a 3 1555 1555 1.44 LINK O3 NAG a 3 C1 MAN a 4 1555 1555 1.46 LINK O6 NAG a 3 C1 MAN a 7 1555 1555 1.44 LINK O2 MAN a 4 C1 MAN a 5 1555 1555 1.44 LINK O2 MAN a 5 C1 MAN a 6 1555 1555 1.45 LINK O3 MAN a 7 C1 MAN a 8 1555 1555 1.44 LINK O6 MAN a 7 C1 MAN a 9 1555 1555 1.45 LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.44 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.44 LINK O4 NAG c 2 C1 BMA c 3 1555 1555 1.45 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.44 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.45 LINK O4 NAG e 2 C1 BMA e 3 1555 1555 1.45 LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.44 LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.44 LINK O4 NAG g 2 C1 BMA g 3 1555 1555 1.44 LINK O6 BMA g 3 C1 MAN g 4 1555 1555 1.44 LINK O3 MAN g 4 C1 MAN g 5 1555 1555 1.45 LINK O6 MAN g 4 C1 MAN g 6 1555 1555 1.45 LINK O2 MAN h 1 C1 MAN h 2 1555 1555 1.45 LINK O2 MAN h 2 C1 MAN h 3 1555 1555 1.44 LINK O4 NAG i 1 C1 NAG i 2 1555 1555 1.45 CISPEP 1 GLY F 142 GLY F 143 0 -8.81 CISPEP 2 PHE F 155 PRO F 156 0 -5.98 CISPEP 3 GLU F 157 PRO F 158 0 -0.41 CISPEP 4 SER F 170 GLY F 171 0 -1.48 CISPEP 5 GLY H 142 GLY H 143 0 0.60 CISPEP 6 PHE H 155 PRO H 156 0 -6.76 CISPEP 7 GLU H 157 PRO H 158 0 -4.47 CISPEP 8 SER I 56 GLY I 57 0 -2.51 CISPEP 9 GLY I 108 GLN I 109 0 -3.80 CISPEP 10 TYR I 141 PRO I 142 0 0.97 CISPEP 11 ALA I 151 ASP I 152 0 -9.68 CISPEP 12 SER L 56 GLY L 57 0 -2.35 CISPEP 13 TYR L 141 PRO L 142 0 -1.97 CISPEP 14 ALA L 151 ASP L 152 0 -7.36 CISPEP 15 SER N 121 SER N 122 0 11.45 CISPEP 16 GLY N 142 GLY N 143 0 0.91 CISPEP 17 PHE N 155 PRO N 156 0 -4.87 CISPEP 18 GLU N 157 PRO N 158 0 -3.68 CISPEP 19 SER N 170 GLY N 171 0 -1.08 CISPEP 20 SER O 56 GLY O 57 0 0.38 CISPEP 21 GLY O 108 GLN O 109 0 4.37 CISPEP 22 TYR O 141 PRO O 142 0 4.04 CISPEP 23 ALA O 151 ASP O 152 0 -5.13 CISPEP 24 TYR A 140 PRO A 141 0 -0.26 CISPEP 25 TYR C 140 PRO C 141 0 -0.05 CISPEP 26 ASN E 186A GLN E 187 0 0.86 CISPEP 27 ASN G 186A GLN G 187 0 -0.48 CISPEP 28 TYR J 140 PRO J 141 0 -2.02 CISPEP 29 ASN M 186A GLN M 187 0 -2.34 CISPEP 30 PHE B 146 PRO B 147 0 -3.54 CISPEP 31 GLU B 148 PRO B 149 0 -2.91 CISPEP 32 SER B 161 GLY B 162 0 -0.44 CISPEP 33 SER B 203 ASN B 204 0 -3.51 CISPEP 34 PHE D 146 PRO D 147 0 -4.91 CISPEP 35 GLU D 148 PRO D 149 0 -2.39 CISPEP 36 SER D 161 GLY D 162 0 0.45 CISPEP 37 SER D 203 ASN D 204 0 -3.82 CISPEP 38 PHE K 146 PRO K 147 0 -2.73 CISPEP 39 GLU K 148 PRO K 149 0 -3.59 CISPEP 40 SER K 161 GLY K 162 0 -0.19 CISPEP 41 SER K 203 ASN K 204 0 -3.93 CRYST1 146.057 157.666 158.558 90.00 102.97 90.00 P 1 21 1 6 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 0.006847 0.000000 0.001577 0.00000 SCALE2 0.000000 0.006343 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006472 0.00000