HEADER VIRAL PROTEIN/IMMUNE SYSTEM 25-JUL-24 9CU5 TITLE LJF-085 FAB IN COMPLEX WITH HIV ENV JRFL NFL TD CC3+ TRIMER AND 35O22 TITLE 2 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: 35O22 HEAVY CHAIN FV; COMPND 3 CHAIN: D, F, J; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 35O22 LIGHT CHAIN FV; COMPND 7 CHAIN: E, G, K; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: LJF-085 HEAVY CHAIN FV; COMPND 11 CHAIN: H, I; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: LJF-085 LIGHT CHAIN FV; COMPND 15 CHAIN: L, M; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: HIV ENV JRFL NFL TD CC3+ GP140; COMPND 19 CHAIN: C, B, A; COMPND 20 FRAGMENT: UNP RESIDUES 30-655; COMPND 21 SYNONYM: ENV POLYPROTEIN; COMPND 22 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: MACACA MULATTA; SOURCE 17 ORGANISM_TAXID: 9544; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 21 MOL_ID: 4; SOURCE 22 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 23 ORGANISM_TAXID: 9544; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 27 MOL_ID: 5; SOURCE 28 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 29 ORGANISM_TAXID: 11676; SOURCE 30 GENE: ENV; SOURCE 31 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 32 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS NHP, RHESUS MACAQUE, GP120 INTERFACE, HIV, NFL, NEUTRALIZING KEYWDS 2 ANTIBODY, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR G.OZOROWSKI,A.B.WARD REVDAT 1 21-MAY-25 9CU5 0 JRNL AUTH F.A.SCHLEICH,S.BALE,J.GUENAGA,G.OZOROWSKI,M.ADORI,X.LIN, JRNL AUTH 2 X.CASTRO DOPICO,R.WILSON,M.CHERNYSHEV,A.T.COTGREAVE, JRNL AUTH 3 M.MANDOLESI,J.CLUFF,E.D.DOYLE,L.M.SEWALL,W.H.LEE,S.ZHANG, JRNL AUTH 4 S.O'DELL,B.S.HEALY,D.LIM,V.R.LEWIS,E.BEN-AKIVA,D.J.IRVINE, JRNL AUTH 5 N.A.DORIA-ROSE,M.CORCORAN,D.CARNATHAN,G.SILVESTRI, JRNL AUTH 6 I.A.WILSON,A.B.WARD,G.B.KARLSSON HEDESTAM,R.T.WYATT JRNL TITL VACCINATION OF NONHUMAN PRIMATES ELICITS A BROADLY JRNL TITL 2 NEUTRALIZING ANTIBODY LINEAGE TARGETING A QUATERNARY EPITOPE JRNL TITL 3 ON THE HIV-1 ENV TRIMER. JRNL REF IMMUNITY 2025 JRNL REFN ISSN 1074-7613 JRNL PMID 40339576 JRNL DOI 10.1016/J.IMMUNI.2025.04.010 REMARK 2 REMARK 2 RESOLUTION. 3.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : EPU, PHENIX, 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) : 3.400 REMARK 3 NUMBER OF PARTICLES : 64443 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 9CU5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1000286298. 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 : LJF-085 FAB IN COMPLEX WITH HIV REMARK 245 ENV JRFL NFL TD CC3+ TRIMER AND REMARK 245 35O22 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 5.80 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 : NULL 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 : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4500.00 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: TRIDECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, G, J, K, H, L, I, M, REMARK 350 AND CHAINS: C, B, A, N, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V, W 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 GLN D 1 REMARK 465 SER D 113 REMARK 465 GLN E 1 REMARK 465 LYS E 111 REMARK 465 GLN F 1 REMARK 465 SER F 112 REMARK 465 SER F 113 REMARK 465 GLN G 1 REMARK 465 LYS G 111 REMARK 465 GLN J 1 REMARK 465 SER J 113 REMARK 465 GLN K 1 REMARK 465 LYS K 111 REMARK 465 SER H 112 REMARK 465 SER H 113 REMARK 465 LYS L 107 REMARK 465 SER I 112 REMARK 465 SER I 113 REMARK 465 LYS M 107 REMARK 465 VAL C 31 REMARK 465 TYR C 61 REMARK 465 ASP C 62 REMARK 465 THR C 137 REMARK 465 ASN C 138 REMARK 465 THR C 139 REMARK 465 THR C 140 REMARK 465 ASN C 141 REMARK 465 ASP C 142 REMARK 465 SER C 143 REMARK 465 GLU C 144 REMARK 465 GLY C 145 REMARK 465 ASN C 401 REMARK 465 THR C 402 REMARK 465 GLU C 403 REMARK 465 GLY C 404 REMARK 465 SER C 405 REMARK 465 ASN C 406 REMARK 465 ASN C 407 REMARK 465 GLY C 458 REMARK 465 GLY C 459 REMARK 465 ILE C 460 REMARK 465 ASN C 461 REMARK 465 VAL C 505A REMARK 465 GLN C 505B REMARK 465 GLY C 505C REMARK 465 GLY C 505D REMARK 465 GLY C 505E REMARK 465 GLY C 505F REMARK 465 SER C 505G REMARK 465 GLY C 505H REMARK 465 GLY C 505I REMARK 465 GLY C 505J REMARK 465 GLY C 505K REMARK 465 SER C 505L REMARK 465 ALA C 505M REMARK 465 VAL C 505N REMARK 465 GLY C 505O REMARK 465 ILE C 505P REMARK 465 GLY C 505Q REMARK 465 ALA C 505R REMARK 465 GLY C 547 REMARK 465 ILE C 548 REMARK 465 VAL C 549 REMARK 465 GLN C 550 REMARK 465 PRO C 551 REMARK 465 GLN C 552 REMARK 465 SER C 553 REMARK 465 ASN C 554 REMARK 465 LEU C 555 REMARK 465 LEU C 556 REMARK 465 ARG C 557 REMARK 465 ALA C 558 REMARK 465 PRO C 559 REMARK 465 GLU C 560 REMARK 465 ALA C 561 REMARK 465 GLN C 562 REMARK 465 GLN C 563 REMARK 465 ARG C 564 REMARK 465 MET C 565 REMARK 465 LEU C 566 REMARK 465 GLN C 567 REMARK 465 ASP C 664 REMARK 465 GLY C 665 REMARK 465 GLY C 666 REMARK 465 GLY C 667 REMARK 465 GLY C 668 REMARK 465 SER C 669 REMARK 465 HIS C 670 REMARK 465 HIS C 671 REMARK 465 HIS C 672 REMARK 465 HIS C 673 REMARK 465 HIS C 674 REMARK 465 HIS C 675 REMARK 465 HIS C 676 REMARK 465 HIS C 677 REMARK 465 GLY C 678 REMARK 465 SER C 679 REMARK 465 GLY C 680 REMARK 465 CYS C 681 REMARK 465 VAL B 31 REMARK 465 ALA B 60 REMARK 465 TYR B 61 REMARK 465 ASP B 62 REMARK 465 THR B 63 REMARK 465 THR B 139 REMARK 465 ASN B 140 REMARK 465 THR B 141 REMARK 465 THR B 142 REMARK 465 ASN B 143 REMARK 465 ASP B 144 REMARK 465 SER B 145 REMARK 465 GLU B 146 REMARK 465 GLY B 147 REMARK 465 THR B 148 REMARK 465 MET B 149 REMARK 465 ASN B 401 REMARK 465 THR B 402 REMARK 465 GLU B 403 REMARK 465 GLY B 404 REMARK 465 SER B 405 REMARK 465 ASN B 406 REMARK 465 ASN B 407 REMARK 465 GLY B 458 REMARK 465 GLY B 459 REMARK 465 ILE B 460 REMARK 465 ASN B 461 REMARK 465 ARG B 503A REMARK 465 VAL B 503B REMARK 465 VAL B 503C REMARK 465 GLN B 503D REMARK 465 GLY B 503E REMARK 465 GLY B 503F REMARK 465 GLY B 503G REMARK 465 GLY B 503H REMARK 465 SER B 503I REMARK 465 GLY B 503J REMARK 465 GLY B 503K REMARK 465 GLY B 503L REMARK 465 GLY B 503M REMARK 465 SER B 503N REMARK 465 ALA B 503O REMARK 465 VAL B 503P REMARK 465 GLY B 503Q REMARK 465 ILE B 503R REMARK 465 GLY B 503S REMARK 465 ALA B 503T REMARK 465 VAL B 503U REMARK 465 ARG B 503V REMARK 465 GLY B 547 REMARK 465 ILE B 548 REMARK 465 VAL B 549 REMARK 465 GLN B 550 REMARK 465 PRO 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 ARG B 564 REMARK 465 MET B 565 REMARK 465 LEU B 566 REMARK 465 GLN B 567 REMARK 465 ASP B 664 REMARK 465 GLY B 665 REMARK 465 GLY B 666 REMARK 465 GLY B 667 REMARK 465 GLY B 668 REMARK 465 SER B 669 REMARK 465 HIS B 670 REMARK 465 HIS B 671 REMARK 465 HIS B 672 REMARK 465 HIS B 673 REMARK 465 HIS B 674 REMARK 465 HIS B 675 REMARK 465 HIS B 676 REMARK 465 HIS B 677 REMARK 465 GLY B 678 REMARK 465 SER B 679 REMARK 465 GLY B 680 REMARK 465 CYS B 681 REMARK 465 VAL A 31 REMARK 465 ALA A 58 REMARK 465 LYS A 59 REMARK 465 ALA A 60 REMARK 465 TYR A 61 REMARK 465 ASP A 62 REMARK 465 THR A 63 REMARK 465 GLU A 64 REMARK 465 LYS A 65 REMARK 465 ASN A 140 REMARK 465 THR A 141 REMARK 465 THR A 142 REMARK 465 ASN A 143 REMARK 465 ASP A 144 REMARK 465 SER A 145 REMARK 465 GLU A 146 REMARK 465 GLY A 147 REMARK 465 THR A 148 REMARK 465 MET A 149 REMARK 465 THR A 162 REMARK 465 THR A 163 REMARK 465 GLU A 164 REMARK 465 LEU A 165 REMARK 465 ARG A 166 REMARK 465 ASP A 167 REMARK 465 LYS A 168 REMARK 465 ASN A 401 REMARK 465 THR A 402 REMARK 465 GLU A 403 REMARK 465 GLY A 404 REMARK 465 SER A 405 REMARK 465 ASN A 406 REMARK 465 ASN A 407 REMARK 465 GLY A 458 REMARK 465 GLY A 459 REMARK 465 ILE A 460 REMARK 465 ASN A 461 REMARK 465 ARG A 503A REMARK 465 VAL A 503B REMARK 465 VAL A 503C REMARK 465 GLN A 503D REMARK 465 GLY A 503E REMARK 465 GLY A 503F REMARK 465 GLY A 503G REMARK 465 GLY A 503H REMARK 465 SER A 503I REMARK 465 GLY A 503J REMARK 465 GLY A 503K REMARK 465 GLY A 503L REMARK 465 GLY A 503M REMARK 465 SER A 503N REMARK 465 ALA A 503O REMARK 465 VAL A 503P REMARK 465 GLY A 503Q REMARK 465 ILE A 503R REMARK 465 GLY A 503S REMARK 465 GLY A 547 REMARK 465 ILE A 548 REMARK 465 VAL A 549 REMARK 465 GLN A 550 REMARK 465 PRO A 551 REMARK 465 GLN A 552 REMARK 465 SER A 553 REMARK 465 ASN A 554 REMARK 465 LEU A 555 REMARK 465 LEU A 556 REMARK 465 ARG A 557 REMARK 465 ALA A 558 REMARK 465 PRO A 559 REMARK 465 GLU A 560 REMARK 465 ALA A 561 REMARK 465 GLN A 562 REMARK 465 GLN A 563 REMARK 465 ARG A 564 REMARK 465 MET A 565 REMARK 465 LEU A 566 REMARK 465 GLN A 567 REMARK 465 ASP A 664 REMARK 465 GLY A 665 REMARK 465 GLY A 666 REMARK 465 GLY A 667 REMARK 465 GLY A 668 REMARK 465 SER A 669 REMARK 465 HIS A 670 REMARK 465 HIS A 671 REMARK 465 HIS A 672 REMARK 465 HIS A 673 REMARK 465 HIS A 674 REMARK 465 HIS A 675 REMARK 465 HIS A 676 REMARK 465 HIS A 677 REMARK 465 GLY A 678 REMARK 465 SER A 679 REMARK 465 GLY A 680 REMARK 465 CYS A 681 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 B 501 SG CYS A 662 1.53 REMARK 500 SG CYS G 23 SG CYS G 88 1.55 REMARK 500 NH2 ARG H 38 OE2 GLU H 46 1.90 REMARK 500 NE ARG F 43 OD1 ASP F 85 1.95 REMARK 500 NH2 ARG M 69 O GLY B 472 1.97 REMARK 500 NH2 ARG L 42 NE2 GLN L 45 2.12 REMARK 500 NH1 ARG C 503 OE2 GLU C 654 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS C 157 CA - CB - SG ANGL. DEV. = 7.5 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU D 11 57.81 -114.98 REMARK 500 LYS D 19 72.90 -100.45 REMARK 500 SER D 25 118.44 -164.15 REMARK 500 GLN D 39 58.58 -142.12 REMARK 500 ALA D 41 -129.69 38.77 REMARK 500 THR D 73E -167.44 -129.48 REMARK 500 ASN D 82B 70.98 55.65 REMARK 500 ILE E 47 -66.45 -91.05 REMARK 500 ASP F 65 -7.21 72.16 REMARK 500 ASP F 86 64.67 -102.99 REMARK 500 TYR F 101 -61.77 -109.31 REMARK 500 CYS G 27C -162.37 -124.91 REMARK 500 PRO G 44 -179.69 -67.05 REMARK 500 GLU G 50 -71.61 -74.34 REMARK 500 ASP G 51 -30.01 -149.27 REMARK 500 THR G 100 -168.48 -69.07 REMARK 500 ASN J 82B 81.77 68.18 REMARK 500 GLN K 6 -165.93 -128.30 REMARK 500 CYS K 27C 150.39 -45.07 REMARK 500 LYS K 31 -155.62 -93.26 REMARK 500 ASP K 51 -106.12 58.64 REMARK 500 PRO K 80 44.62 -79.30 REMARK 500 SER H 15 -5.31 76.63 REMARK 500 ASP H 30 -150.30 -96.10 REMARK 500 ALA L 51 -10.59 75.44 REMARK 500 ARG L 69 -30.32 -130.59 REMARK 500 SER I 15 -4.22 81.99 REMARK 500 ASN I 60 109.62 -51.67 REMARK 500 ALA M 51 -12.08 72.11 REMARK 500 SER M 52 -2.88 -143.79 REMARK 500 PHE M 98 -159.73 -93.86 REMARK 500 ARG C 166 -64.36 67.76 REMARK 500 ASN C 186 -116.61 60.34 REMARK 500 SER C 195 -6.24 77.44 REMARK 500 GLN C 258 -64.72 62.18 REMARK 500 ASN C 262 -169.71 61.14 REMARK 500 PHE C 277 -5.42 70.38 REMARK 500 GLU C 354 -177.15 61.24 REMARK 500 THR C 388 11.03 -141.23 REMARK 500 ASN C 396 -115.99 57.90 REMARK 500 SER C 615 110.90 -161.09 REMARK 500 PRO B 124 51.84 -90.19 REMARK 500 GLN B 258 -6.54 72.36 REMARK 500 ASN B 262 156.74 63.76 REMARK 500 PHE B 277 -7.46 73.28 REMARK 500 ASN B 280 170.50 71.64 REMARK 500 ARG B 327 -167.93 -102.66 REMARK 500 GLU B 354 165.94 65.21 REMARK 500 ASN B 392 43.40 -144.57 REMARK 500 ASN B 396 -135.95 54.85 REMARK 500 REMARK 500 THIS ENTRY HAS 82 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-45928 RELATED DB: EMDB REMARK 900 LJF-085 FAB IN COMPLEX WITH HIV ENV JRFL NFL TD CC3+ TRIMER AND REMARK 900 35O22 FAB DBREF 9CU5 D 1 113 PDB 9CU5 9CU5 1 113 DBREF 9CU5 E 1 111 PDB 9CU5 9CU5 1 111 DBREF 9CU5 F 1 113 PDB 9CU5 9CU5 1 113 DBREF 9CU5 G 1 111 PDB 9CU5 9CU5 1 111 DBREF 9CU5 J 1 113 PDB 9CU5 9CU5 1 113 DBREF 9CU5 K 1 111 PDB 9CU5 9CU5 1 111 DBREF 9CU5 H 1 113 PDB 9CU5 9CU5 1 113 DBREF 9CU5 L 1 107 PDB 9CU5 9CU5 1 107 DBREF 9CU5 I 1 113 PDB 9CU5 9CU5 1 113 DBREF 9CU5 M 1 107 PDB 9CU5 9CU5 1 107 DBREF 9CU5 C 31 664 UNP Q75760 Q75760_9HIV1 30 655 DBREF 9CU5 B 31 664 UNP Q75760 Q75760_9HIV1 30 655 DBREF 9CU5 A 31 664 UNP Q75760 Q75760_9HIV1 30 655 SEQADV 9CU5 ASP C 47 UNP Q75760 GLU 46 ENGINEERED MUTATION SEQADV 9CU5 GLU C 49 UNP Q75760 THR 48 ENGINEERED MUTATION SEQADV 9CU5 LYS C 65 UNP Q75760 VAL 64 ENGINEERED MUTATION SEQADV 9CU5 THR C 106 UNP Q75760 GLU 105 ENGINEERED MUTATION SEQADV 9CU5 GLU C 164 UNP Q75760 SER 161 ENGINEERED MUTATION SEQADV 9CU5 LEU C 165 UNP Q75760 ILE 162 ENGINEERED MUTATION SEQADV 9CU5 LYS C 168 UNP Q75760 GLU 165 ENGINEERED MUTATION SEQADV 9CU5 VAL C 172 UNP Q75760 GLU 169 ENGINEERED MUTATION SEQADV 9CU5 TYR C 302 UNP Q75760 ASN 299 ENGINEERED MUTATION SEQADV 9CU5 ARG C 308 UNP Q75760 HIS 305 ENGINEERED MUTATION SEQADV 9CU5 MET C 320 UNP Q75760 THR 315 ENGINEERED MUTATION SEQADV 9CU5 ARG C 429 UNP Q75760 GLU 420 ENGINEERED MUTATION SEQADV 9CU5 GLN C 432 UNP Q75760 LYS 423 ENGINEERED MUTATION SEQADV 9CU5 ARG C 500 UNP Q75760 LYS 491 ENGINEERED MUTATION SEQADV 9CU5 CYS C 501 UNP Q75760 ALA 492 ENGINEERED MUTATION SEQADV 9CU5 GLY C 505C UNP Q75760 INSERTION SEQADV 9CU5 GLY C 505D UNP Q75760 INSERTION SEQADV 9CU5 GLY C 505E UNP Q75760 INSERTION SEQADV 9CU5 GLY C 505F UNP Q75760 INSERTION SEQADV 9CU5 SER C 505G UNP Q75760 INSERTION SEQADV 9CU5 GLY C 505H UNP Q75760 INSERTION SEQADV 9CU5 GLY C 505I UNP Q75760 ARG 499 ENGINEERED MUTATION SEQADV 9CU5 GLY C 505J UNP Q75760 GLU 500 ENGINEERED MUTATION SEQADV 9CU5 GLY C 505K UNP Q75760 LYS 501 ENGINEERED MUTATION SEQADV 9CU5 SER C 505L UNP Q75760 ARG 502 ENGINEERED MUTATION SEQADV 9CU5 ARG C 519 UNP Q75760 PHE 510 ENGINEERED MUTATION SEQADV 9CU5 ARG C 520 UNP Q75760 LEU 511 ENGINEERED MUTATION SEQADV 9CU5 ASN C 543 UNP Q75760 LEU 534 ENGINEERED MUTATION SEQADV 9CU5 PRO C 551 UNP Q75760 GLN 542 ENGINEERED MUTATION SEQADV 9CU5 SER C 553 UNP Q75760 ASN 544 ENGINEERED MUTATION SEQADV 9CU5 PRO C 559 UNP Q75760 ILE 550 ENGINEERED MUTATION SEQADV 9CU5 GLY C 569 UNP Q75760 THR 560 ENGINEERED MUTATION SEQADV 9CU5 ARG C 588 UNP Q75760 GLY 579 ENGINEERED MUTATION SEQADV 9CU5 CYS C 662 UNP Q75760 GLU 653 ENGINEERED MUTATION SEQADV 9CU5 GLY C 665 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 GLY C 666 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 GLY C 667 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 GLY C 668 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 SER C 669 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS C 670 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS C 671 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS C 672 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS C 673 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS C 674 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS C 675 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS C 676 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS C 677 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 GLY C 678 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 SER C 679 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 GLY C 680 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 CYS C 681 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 ASP B 47 UNP Q75760 GLU 46 ENGINEERED MUTATION SEQADV 9CU5 GLU B 49 UNP Q75760 THR 48 ENGINEERED MUTATION SEQADV 9CU5 LYS B 65 UNP Q75760 VAL 64 ENGINEERED MUTATION SEQADV 9CU5 THR B 106 UNP Q75760 GLU 105 ENGINEERED MUTATION SEQADV 9CU5 GLU B 164 UNP Q75760 SER 161 ENGINEERED MUTATION SEQADV 9CU5 LEU B 165 UNP Q75760 ILE 162 ENGINEERED MUTATION SEQADV 9CU5 LYS B 168 UNP Q75760 GLU 165 ENGINEERED MUTATION SEQADV 9CU5 VAL B 172 UNP Q75760 GLU 169 ENGINEERED MUTATION SEQADV 9CU5 TYR B 302 UNP Q75760 ASN 299 ENGINEERED MUTATION SEQADV 9CU5 ARG B 308 UNP Q75760 HIS 305 ENGINEERED MUTATION SEQADV 9CU5 MET B 320 UNP Q75760 THR 315 ENGINEERED MUTATION SEQADV 9CU5 ARG B 429 UNP Q75760 GLU 420 ENGINEERED MUTATION SEQADV 9CU5 GLN B 432 UNP Q75760 LYS 423 ENGINEERED MUTATION SEQADV 9CU5 ARG B 500 UNP Q75760 LYS 491 ENGINEERED MUTATION SEQADV 9CU5 CYS B 501 UNP Q75760 ALA 492 ENGINEERED MUTATION SEQADV 9CU5 GLY B 503E UNP Q75760 INSERTION SEQADV 9CU5 GLY B 503F UNP Q75760 INSERTION SEQADV 9CU5 GLY B 503G UNP Q75760 INSERTION SEQADV 9CU5 GLY B 503H UNP Q75760 INSERTION SEQADV 9CU5 SER B 503I UNP Q75760 INSERTION SEQADV 9CU5 GLY B 503J UNP Q75760 INSERTION SEQADV 9CU5 GLY B 503K UNP Q75760 ARG 499 ENGINEERED MUTATION SEQADV 9CU5 GLY B 503L UNP Q75760 GLU 500 ENGINEERED MUTATION SEQADV 9CU5 GLY B 503M UNP Q75760 LYS 501 ENGINEERED MUTATION SEQADV 9CU5 SER B 503N UNP Q75760 ARG 502 ENGINEERED MUTATION SEQADV 9CU5 ARG B 503V UNP Q75760 PHE 510 ENGINEERED MUTATION SEQADV 9CU5 ARG B 520 UNP Q75760 LEU 511 ENGINEERED MUTATION SEQADV 9CU5 ASN B 543 UNP Q75760 LEU 534 ENGINEERED MUTATION SEQADV 9CU5 PRO B 551 UNP Q75760 GLN 542 ENGINEERED MUTATION SEQADV 9CU5 SER B 553 UNP Q75760 ASN 544 ENGINEERED MUTATION SEQADV 9CU5 PRO B 559 UNP Q75760 ILE 550 ENGINEERED MUTATION SEQADV 9CU5 GLY B 569 UNP Q75760 THR 560 ENGINEERED MUTATION SEQADV 9CU5 ARG B 588 UNP Q75760 GLY 579 ENGINEERED MUTATION SEQADV 9CU5 CYS B 662 UNP Q75760 GLU 653 ENGINEERED MUTATION SEQADV 9CU5 GLY B 665 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 GLY B 666 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 GLY B 667 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 GLY B 668 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 SER B 669 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS B 670 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS B 671 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS B 672 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS B 673 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS B 674 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS B 675 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS B 676 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS B 677 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 GLY B 678 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 SER B 679 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 GLY B 680 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 CYS B 681 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 ASP A 47 UNP Q75760 GLU 46 ENGINEERED MUTATION SEQADV 9CU5 GLU A 49 UNP Q75760 THR 48 ENGINEERED MUTATION SEQADV 9CU5 LYS A 65 UNP Q75760 VAL 64 ENGINEERED MUTATION SEQADV 9CU5 THR A 106 UNP Q75760 GLU 105 ENGINEERED MUTATION SEQADV 9CU5 GLU A 164 UNP Q75760 SER 161 ENGINEERED MUTATION SEQADV 9CU5 LEU A 165 UNP Q75760 ILE 162 ENGINEERED MUTATION SEQADV 9CU5 LYS A 168 UNP Q75760 GLU 165 ENGINEERED MUTATION SEQADV 9CU5 VAL A 172 UNP Q75760 GLU 169 ENGINEERED MUTATION SEQADV 9CU5 TYR A 302 UNP Q75760 ASN 299 ENGINEERED MUTATION SEQADV 9CU5 ARG A 308 UNP Q75760 HIS 305 ENGINEERED MUTATION SEQADV 9CU5 MET A 320 UNP Q75760 THR 315 ENGINEERED MUTATION SEQADV 9CU5 ARG A 429 UNP Q75760 GLU 420 ENGINEERED MUTATION SEQADV 9CU5 GLN A 432 UNP Q75760 LYS 423 ENGINEERED MUTATION SEQADV 9CU5 ARG A 500 UNP Q75760 LYS 491 ENGINEERED MUTATION SEQADV 9CU5 CYS A 501 UNP Q75760 ALA 492 ENGINEERED MUTATION SEQADV 9CU5 GLY A 503E UNP Q75760 INSERTION SEQADV 9CU5 GLY A 503F UNP Q75760 INSERTION SEQADV 9CU5 GLY A 503G UNP Q75760 INSERTION SEQADV 9CU5 GLY A 503H UNP Q75760 INSERTION SEQADV 9CU5 SER A 503I UNP Q75760 INSERTION SEQADV 9CU5 GLY A 503J UNP Q75760 INSERTION SEQADV 9CU5 GLY A 503K UNP Q75760 ARG 499 ENGINEERED MUTATION SEQADV 9CU5 GLY A 503L UNP Q75760 GLU 500 ENGINEERED MUTATION SEQADV 9CU5 GLY A 503M UNP Q75760 LYS 501 ENGINEERED MUTATION SEQADV 9CU5 SER A 503N UNP Q75760 ARG 502 ENGINEERED MUTATION SEQADV 9CU5 ARG A 519 UNP Q75760 PHE 510 ENGINEERED MUTATION SEQADV 9CU5 ARG A 520 UNP Q75760 LEU 511 ENGINEERED MUTATION SEQADV 9CU5 ASN A 543 UNP Q75760 LEU 534 ENGINEERED MUTATION SEQADV 9CU5 PRO A 551 UNP Q75760 GLN 542 ENGINEERED MUTATION SEQADV 9CU5 SER A 553 UNP Q75760 ASN 544 ENGINEERED MUTATION SEQADV 9CU5 PRO A 559 UNP Q75760 ILE 550 ENGINEERED MUTATION SEQADV 9CU5 GLY A 569 UNP Q75760 THR 560 ENGINEERED MUTATION SEQADV 9CU5 ARG A 588 UNP Q75760 GLY 579 ENGINEERED MUTATION SEQADV 9CU5 CYS A 662 UNP Q75760 GLU 653 ENGINEERED MUTATION SEQADV 9CU5 GLY A 665 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 GLY A 666 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 GLY A 667 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 GLY A 668 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 SER A 669 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS A 670 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS A 671 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS A 672 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS A 673 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS A 674 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS A 675 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS A 676 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 HIS A 677 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 GLY A 678 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 SER A 679 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 GLY A 680 UNP Q75760 EXPRESSION TAG SEQADV 9CU5 CYS A 681 UNP Q75760 EXPRESSION TAG SEQRES 1 D 131 GLN GLY GLN LEU VAL GLN SER GLY ALA GLU LEU LYS LYS SEQRES 2 D 131 PRO GLY ALA SER VAL LYS ILE SER CYS LYS THR SER GLY SEQRES 3 D 131 TYR ARG PHE ASN PHE TYR HIS ILE ASN TRP ILE ARG GLN SEQRES 4 D 131 THR ALA GLY ARG GLY PRO GLU TRP MET GLY TRP ILE SER SEQRES 5 D 131 PRO TYR SER GLY ASP LYS ASN LEU ALA PRO ALA PHE GLN SEQRES 6 D 131 ASP ARG VAL ILE MET THR THR ASP THR GLU VAL PRO VAL SEQRES 7 D 131 THR SER PHE THR SER THR GLY ALA ALA TYR MET GLU ILE SEQRES 8 D 131 ARG ASN LEU LYS PHE ASP ASP THR GLY THR TYR PHE CYS SEQRES 9 D 131 ALA LYS GLY LEU LEU ARG ASP GLY SER SER THR TRP LEU SEQRES 10 D 131 PRO TYR LEU TRP GLY GLN GLY THR LEU LEU THR VAL SER SEQRES 11 D 131 SER SEQRES 1 E 114 GLN SER VAL LEU THR GLN SER ALA SER VAL SER GLY SER SEQRES 2 E 114 LEU GLY GLN SER VAL THR ILE SER CYS THR GLY PRO ASN SEQRES 3 E 114 SER VAL CYS CYS SER HIS LYS SER ILE SER TRP TYR GLN SEQRES 4 E 114 TRP PRO PRO GLY ARG ALA PRO THR LEU ILE ILE TYR GLU SEQRES 5 E 114 ASP ASN GLU ARG ALA PRO GLY ILE SER PRO ARG PHE SER SEQRES 6 E 114 GLY TYR LYS SER TYR TRP SER ALA TYR LEU THR ILE SER SEQRES 7 E 114 ASP LEU ARG PRO GLU ASP GLU THR THR TYR TYR CYS CYS SEQRES 8 E 114 SER TYR THR HIS ASN SER GLY CYS VAL PHE GLY THR GLY SEQRES 9 E 114 THR LYS VAL SER VAL LEU GLY GLN SER LYS SEQRES 1 F 131 GLN GLY GLN LEU VAL GLN SER GLY ALA GLU LEU LYS LYS SEQRES 2 F 131 PRO GLY ALA SER VAL LYS ILE SER CYS LYS THR SER GLY SEQRES 3 F 131 TYR ARG PHE ASN PHE TYR HIS ILE ASN TRP ILE ARG GLN SEQRES 4 F 131 THR ALA GLY ARG GLY PRO GLU TRP MET GLY TRP ILE SER SEQRES 5 F 131 PRO TYR SER GLY ASP LYS ASN LEU ALA PRO ALA PHE GLN SEQRES 6 F 131 ASP ARG VAL ILE MET THR THR ASP THR GLU VAL PRO VAL SEQRES 7 F 131 THR SER PHE THR SER THR GLY ALA ALA TYR MET GLU ILE SEQRES 8 F 131 ARG ASN LEU LYS PHE ASP ASP THR GLY THR TYR PHE CYS SEQRES 9 F 131 ALA LYS GLY LEU LEU ARG ASP GLY SER SER THR TRP LEU SEQRES 10 F 131 PRO TYR LEU TRP GLY GLN GLY THR LEU LEU THR VAL SER SEQRES 11 F 131 SER SEQRES 1 G 114 GLN SER VAL LEU THR GLN SER ALA SER VAL SER GLY SER SEQRES 2 G 114 LEU GLY GLN SER VAL THR ILE SER CYS THR GLY PRO ASN SEQRES 3 G 114 SER VAL CYS CYS SER HIS LYS SER ILE SER TRP TYR GLN SEQRES 4 G 114 TRP PRO PRO GLY ARG ALA PRO THR LEU ILE ILE TYR GLU SEQRES 5 G 114 ASP ASN GLU ARG ALA PRO GLY ILE SER PRO ARG PHE SER SEQRES 6 G 114 GLY TYR LYS SER TYR TRP SER ALA TYR LEU THR ILE SER SEQRES 7 G 114 ASP LEU ARG PRO GLU ASP GLU THR THR TYR TYR CYS CYS SEQRES 8 G 114 SER TYR THR HIS ASN SER GLY CYS VAL PHE GLY THR GLY SEQRES 9 G 114 THR LYS VAL SER VAL LEU GLY GLN SER LYS SEQRES 1 J 131 GLN GLY GLN LEU VAL GLN SER GLY ALA GLU LEU LYS LYS SEQRES 2 J 131 PRO GLY ALA SER VAL LYS ILE SER CYS LYS THR SER GLY SEQRES 3 J 131 TYR ARG PHE ASN PHE TYR HIS ILE ASN TRP ILE ARG GLN SEQRES 4 J 131 THR ALA GLY ARG GLY PRO GLU TRP MET GLY TRP ILE SER SEQRES 5 J 131 PRO TYR SER GLY ASP LYS ASN LEU ALA PRO ALA PHE GLN SEQRES 6 J 131 ASP ARG VAL ILE MET THR THR ASP THR GLU VAL PRO VAL SEQRES 7 J 131 THR SER PHE THR SER THR GLY ALA ALA TYR MET GLU ILE SEQRES 8 J 131 ARG ASN LEU LYS PHE ASP ASP THR GLY THR TYR PHE CYS SEQRES 9 J 131 ALA LYS GLY LEU LEU ARG ASP GLY SER SER THR TRP LEU SEQRES 10 J 131 PRO TYR LEU TRP GLY GLN GLY THR LEU LEU THR VAL SER SEQRES 11 J 131 SER SEQRES 1 K 114 GLN SER VAL LEU THR GLN SER ALA SER VAL SER GLY SER SEQRES 2 K 114 LEU GLY GLN SER VAL THR ILE SER CYS THR GLY PRO ASN SEQRES 3 K 114 SER VAL CYS CYS SER HIS LYS SER ILE SER TRP TYR GLN SEQRES 4 K 114 TRP PRO PRO GLY ARG ALA PRO THR LEU ILE ILE TYR GLU SEQRES 5 K 114 ASP ASN GLU ARG ALA PRO GLY ILE SER PRO ARG PHE SER SEQRES 6 K 114 GLY TYR LYS SER TYR TRP SER ALA TYR LEU THR ILE SER SEQRES 7 K 114 ASP LEU ARG PRO GLU ASP GLU THR THR TYR TYR CYS CYS SEQRES 8 K 114 SER TYR THR HIS ASN SER GLY CYS VAL PHE GLY THR GLY SEQRES 9 K 114 THR LYS VAL SER VAL LEU GLY GLN SER LYS SEQRES 1 H 123 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 123 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 123 GLY SER ILE ASP ASP TYR PHE TRP ASN TRP VAL ARG GLN SEQRES 4 H 123 PRO PRO GLY LYS PRO LEU GLU CYS ILE GLY TYR ILE PHE SEQRES 5 H 123 GLY ARG GLY GLY GLY THR LYS TYR ASN PRO SER LEU ASP SEQRES 6 H 123 ASN ARG VAL THR ILE SER THR ASP THR PRO ASN GLN PHE SEQRES 7 H 123 SER LEU LYS LEU ARG SER VAL THR VAL ALA ASP THR ALA SEQRES 8 H 123 ILE TYR TYR CYS ALA ARG TRP ASN LEU TYR ASP ASP ASP SEQRES 9 H 123 PHE GLY TYR ASN SER PHE ALA VAL TRP GLY ARG GLY VAL SEQRES 10 H 123 LEU VAL THR VAL SER SER SEQRES 1 L 107 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 107 SER VAL GLY ASP THR VAL THR ILE THR CYS GLN ALA ARG SEQRES 3 L 107 HIS ALA VAL GLY LYS ASN LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 107 PRO GLY ARG GLY PRO GLN LEU LEU ILE TYR MET ALA SER SEQRES 5 L 107 SER ARG HIS SER GLY VAL PRO SER ARG PHE ARG GLY SER SEQRES 6 L 107 GLY SER GLY ARG GLU PHE THR LEU THR ILE ASN ASN LEU SEQRES 7 L 107 GLN PRO GLU ASP PHE ALA THR TYR SER CYS GLN GLN GLY SEQRES 8 L 107 TYR THR TYR PRO TRP THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 L 107 GLU MET LYS SEQRES 1 I 123 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 I 123 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 I 123 GLY SER ILE ASP ASP TYR PHE TRP ASN TRP VAL ARG GLN SEQRES 4 I 123 PRO PRO GLY LYS PRO LEU GLU CYS ILE GLY TYR ILE PHE SEQRES 5 I 123 GLY ARG GLY GLY GLY THR LYS TYR ASN PRO SER LEU ASP SEQRES 6 I 123 ASN ARG VAL THR ILE SER THR ASP THR PRO ASN GLN PHE SEQRES 7 I 123 SER LEU LYS LEU ARG SER VAL THR VAL ALA ASP THR ALA SEQRES 8 I 123 ILE TYR TYR CYS ALA ARG TRP ASN LEU TYR ASP ASP ASP SEQRES 9 I 123 PHE GLY TYR ASN SER PHE ALA VAL TRP GLY ARG GLY VAL SEQRES 10 I 123 LEU VAL THR VAL SER SER SEQRES 1 M 107 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 M 107 SER VAL GLY ASP THR VAL THR ILE THR CYS GLN ALA ARG SEQRES 3 M 107 HIS ALA VAL GLY LYS ASN LEU ASN TRP TYR GLN GLN LYS SEQRES 4 M 107 PRO GLY ARG GLY PRO GLN LEU LEU ILE TYR MET ALA SER SEQRES 5 M 107 SER ARG HIS SER GLY VAL PRO SER ARG PHE ARG GLY SER SEQRES 6 M 107 GLY SER GLY ARG GLU PHE THR LEU THR ILE ASN ASN LEU SEQRES 7 M 107 GLN PRO GLU ASP PHE ALA THR TYR SER CYS GLN GLN GLY SEQRES 8 M 107 TYR THR TYR PRO TRP THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 M 107 GLU MET LYS SEQRES 1 C 649 VAL GLU LYS LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 C 649 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 C 649 ASP ALA LYS ALA TYR ASP THR GLU LYS HIS ASN VAL TRP SEQRES 4 C 649 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 C 649 GLU VAL VAL LEU GLU ASN VAL THR GLU HIS PHE ASN MET SEQRES 6 C 649 TRP LYS ASN ASN MET VAL GLU GLN MET GLN THR ASP ILE SEQRES 7 C 649 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 C 649 LEU THR PRO LEU CYS VAL THR LEU ASN CYS LYS ASP VAL SEQRES 9 C 649 ASN ALA THR ASN THR THR ASN ASP SER GLU GLY THR MET SEQRES 10 C 649 GLU ARG GLY GLU ILE LYS ASN CYS SER PHE ASN ILE THR SEQRES 11 C 649 THR GLU LEU ARG ASP LYS VAL GLN LYS VAL TYR ALA LEU SEQRES 12 C 649 PHE TYR LYS LEU ASP VAL VAL PRO ILE ASP ASN ASN ASN SEQRES 13 C 649 THR SER TYR ARG LEU ILE SER CYS ASP THR SER VAL ILE SEQRES 14 C 649 THR GLN ALA CYS PRO LYS ILE SER PHE GLU PRO ILE PRO SEQRES 15 C 649 ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS SEQRES 16 C 649 CYS ASN ASP LYS THR PHE ASN GLY LYS GLY PRO CYS LYS SEQRES 17 C 649 ASN VAL SER THR VAL GLN CYS THR HIS GLY ILE ARG PRO SEQRES 18 C 649 VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA SEQRES 19 C 649 GLU GLU GLU VAL VAL ILE ARG SER ASP ASN PHE THR ASN SEQRES 20 C 649 ASN ALA LYS THR ILE ILE VAL GLN LEU LYS GLU SER VAL SEQRES 21 C 649 GLU ILE ASN CYS THR ARG PRO ASN ASN TYR THR ARG LYS SEQRES 22 C 649 SER ILE ARG ILE GLY PRO GLY ARG ALA PHE TYR THR MET SEQRES 23 C 649 GLY GLU ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN SEQRES 24 C 649 ILE SER ARG ALA LYS TRP ASN ASP THR LEU LYS GLN ILE SEQRES 25 C 649 VAL ILE LYS LEU ARG GLU GLN PHE GLU ASN LYS THR ILE SEQRES 26 C 649 VAL PHE ASN HIS SER SER GLY GLY ASP PRO GLU ILE VAL SEQRES 27 C 649 MET HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS SEQRES 28 C 649 ASN SER THR GLN LEU PHE ASN SER THR TRP ASN ASN ASN SEQRES 29 C 649 THR GLU GLY SER ASN ASN THR GLU GLY ASN THR ILE THR SEQRES 30 C 649 LEU PRO CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN SEQRES 31 C 649 ARG VAL GLY GLN ALA MET TYR ALA PRO PRO ILE ARG GLY SEQRES 32 C 649 GLN ILE ARG CYS SER SER ASN ILE THR GLY LEU LEU LEU SEQRES 33 C 649 THR ARG ASP GLY GLY ILE ASN GLU ASN GLY THR GLU ILE SEQRES 34 C 649 PHE ARG PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SEQRES 35 C 649 SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU PRO SEQRES 36 C 649 LEU GLY VAL ALA PRO THR ARG CYS LYS ARG ARG VAL VAL SEQRES 37 C 649 GLN GLY GLY GLY GLY SER GLY GLY GLY GLY SER ALA VAL SEQRES 38 C 649 GLY ILE GLY ALA VAL ARG ARG GLY PHE LEU GLY ALA ALA SEQRES 39 C 649 GLY SER THR MET GLY ALA ALA SER MET THR LEU THR VAL SEQRES 40 C 649 GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN PRO GLN SEQRES 41 C 649 SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN ARG MET SEQRES 42 C 649 LEU GLN LEU GLY VAL TRP GLY ILE LYS GLN LEU GLN ALA SEQRES 43 C 649 ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP GLN GLN SEQRES 44 C 649 LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU ILE CYS SEQRES 45 C 649 THR THR ALA VAL PRO TRP ASN ALA SER TRP SER ASN LYS SEQRES 46 C 649 SER LEU ASP ARG ILE TRP ASN ASN MET THR TRP MET GLU SEQRES 47 C 649 TRP GLU ARG GLU ILE ASP ASN TYR THR SER GLU ILE TYR SEQRES 48 C 649 THR LEU ILE GLU GLU SER GLN ASN GLN GLN GLU LYS ASN SEQRES 49 C 649 GLU GLN GLU LEU LEU CYS LEU ASP GLY GLY GLY GLY SER SEQRES 50 C 649 HIS HIS HIS HIS HIS HIS HIS HIS GLY SER GLY CYS SEQRES 1 B 649 VAL GLU LYS LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 B 649 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 B 649 ASP ALA LYS ALA TYR ASP THR GLU LYS HIS ASN VAL TRP SEQRES 4 B 649 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 B 649 GLU VAL VAL LEU GLU ASN VAL THR GLU HIS PHE ASN MET SEQRES 6 B 649 TRP LYS ASN ASN MET VAL GLU GLN MET GLN THR ASP ILE SEQRES 7 B 649 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 B 649 LEU THR PRO LEU CYS VAL THR LEU ASN CYS LYS ASP VAL SEQRES 9 B 649 ASN ALA THR ASN THR THR ASN ASP SER GLU GLY THR MET SEQRES 10 B 649 GLU ARG GLY GLU ILE LYS ASN CYS SER PHE ASN ILE THR SEQRES 11 B 649 THR GLU LEU ARG ASP LYS VAL GLN LYS VAL TYR ALA LEU SEQRES 12 B 649 PHE TYR LYS LEU ASP VAL VAL PRO ILE ASP ASN ASN ASN SEQRES 13 B 649 THR SER TYR ARG LEU ILE SER CYS ASP THR SER VAL ILE SEQRES 14 B 649 THR GLN ALA CYS PRO LYS ILE SER PHE GLU PRO ILE PRO SEQRES 15 B 649 ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS SEQRES 16 B 649 CYS ASN ASP LYS THR PHE ASN GLY LYS GLY PRO CYS LYS SEQRES 17 B 649 ASN VAL SER THR VAL GLN CYS THR HIS GLY ILE ARG PRO SEQRES 18 B 649 VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA SEQRES 19 B 649 GLU GLU GLU VAL VAL ILE ARG SER ASP ASN PHE THR ASN SEQRES 20 B 649 ASN ALA LYS THR ILE ILE VAL GLN LEU LYS GLU SER VAL SEQRES 21 B 649 GLU ILE ASN CYS THR ARG PRO ASN ASN TYR THR ARG LYS SEQRES 22 B 649 SER ILE ARG ILE GLY PRO GLY ARG ALA PHE TYR THR MET SEQRES 23 B 649 GLY GLU ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN SEQRES 24 B 649 ILE SER ARG ALA LYS TRP ASN ASP THR LEU LYS GLN ILE SEQRES 25 B 649 VAL ILE LYS LEU ARG GLU GLN PHE GLU ASN LYS THR ILE SEQRES 26 B 649 VAL PHE ASN HIS SER SER GLY GLY ASP PRO GLU ILE VAL SEQRES 27 B 649 MET HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS SEQRES 28 B 649 ASN SER THR GLN LEU PHE ASN SER THR TRP ASN ASN ASN SEQRES 29 B 649 THR GLU GLY SER ASN ASN THR GLU GLY ASN THR ILE THR SEQRES 30 B 649 LEU PRO CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN SEQRES 31 B 649 ARG VAL GLY GLN ALA MET TYR ALA PRO PRO ILE ARG GLY SEQRES 32 B 649 GLN ILE ARG CYS SER SER ASN ILE THR GLY LEU LEU LEU SEQRES 33 B 649 THR ARG ASP GLY GLY ILE ASN GLU ASN GLY THR GLU ILE SEQRES 34 B 649 PHE ARG PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SEQRES 35 B 649 SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU PRO SEQRES 36 B 649 LEU GLY VAL ALA PRO THR ARG CYS LYS ARG ARG VAL VAL SEQRES 37 B 649 GLN GLY GLY GLY GLY SER GLY GLY GLY GLY SER ALA VAL SEQRES 38 B 649 GLY ILE GLY ALA VAL ARG ARG GLY PHE LEU GLY ALA ALA SEQRES 39 B 649 GLY SER THR MET GLY ALA ALA SER MET THR LEU THR VAL SEQRES 40 B 649 GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN PRO GLN SEQRES 41 B 649 SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN ARG MET SEQRES 42 B 649 LEU GLN LEU GLY VAL TRP GLY ILE LYS GLN LEU GLN ALA SEQRES 43 B 649 ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP GLN GLN SEQRES 44 B 649 LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU ILE CYS SEQRES 45 B 649 THR THR ALA VAL PRO TRP ASN ALA SER TRP SER ASN LYS SEQRES 46 B 649 SER LEU ASP ARG ILE TRP ASN ASN MET THR TRP MET GLU SEQRES 47 B 649 TRP GLU ARG GLU ILE ASP ASN TYR THR SER GLU ILE TYR SEQRES 48 B 649 THR LEU ILE GLU GLU SER GLN ASN GLN GLN GLU LYS ASN SEQRES 49 B 649 GLU GLN GLU LEU LEU CYS LEU ASP GLY GLY GLY GLY SER SEQRES 50 B 649 HIS HIS HIS HIS HIS HIS HIS HIS GLY SER GLY CYS SEQRES 1 A 649 VAL GLU LYS LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 A 649 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 A 649 ASP ALA LYS ALA TYR ASP THR GLU LYS HIS ASN VAL TRP SEQRES 4 A 649 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 A 649 GLU VAL VAL LEU GLU ASN VAL THR GLU HIS PHE ASN MET SEQRES 6 A 649 TRP LYS ASN ASN MET VAL GLU GLN MET GLN THR ASP ILE SEQRES 7 A 649 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 A 649 LEU THR PRO LEU CYS VAL THR LEU ASN CYS LYS ASP VAL SEQRES 9 A 649 ASN ALA THR ASN THR THR ASN ASP SER GLU GLY THR MET SEQRES 10 A 649 GLU ARG GLY GLU ILE LYS ASN CYS SER PHE ASN ILE THR SEQRES 11 A 649 THR GLU LEU ARG ASP LYS VAL GLN LYS VAL TYR ALA LEU SEQRES 12 A 649 PHE TYR LYS LEU ASP VAL VAL PRO ILE ASP ASN ASN ASN SEQRES 13 A 649 THR SER TYR ARG LEU ILE SER CYS ASP THR SER VAL ILE SEQRES 14 A 649 THR GLN ALA CYS PRO LYS ILE SER PHE GLU PRO ILE PRO SEQRES 15 A 649 ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS SEQRES 16 A 649 CYS ASN ASP LYS THR PHE ASN GLY LYS GLY PRO CYS LYS SEQRES 17 A 649 ASN VAL SER THR VAL GLN CYS THR HIS GLY ILE ARG PRO SEQRES 18 A 649 VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA SEQRES 19 A 649 GLU GLU GLU VAL VAL ILE ARG SER ASP ASN PHE THR ASN SEQRES 20 A 649 ASN ALA LYS THR ILE ILE VAL GLN LEU LYS GLU SER VAL SEQRES 21 A 649 GLU ILE ASN CYS THR ARG PRO ASN ASN TYR THR ARG LYS SEQRES 22 A 649 SER ILE ARG ILE GLY PRO GLY ARG ALA PHE TYR THR MET SEQRES 23 A 649 GLY GLU ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN SEQRES 24 A 649 ILE SER ARG ALA LYS TRP ASN ASP THR LEU LYS GLN ILE SEQRES 25 A 649 VAL ILE LYS LEU ARG GLU GLN PHE GLU ASN LYS THR ILE SEQRES 26 A 649 VAL PHE ASN HIS SER SER GLY GLY ASP PRO GLU ILE VAL SEQRES 27 A 649 MET HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS SEQRES 28 A 649 ASN SER THR GLN LEU PHE ASN SER THR TRP ASN ASN ASN SEQRES 29 A 649 THR GLU GLY SER ASN ASN THR GLU GLY ASN THR ILE THR SEQRES 30 A 649 LEU PRO CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN SEQRES 31 A 649 ARG VAL GLY GLN ALA MET TYR ALA PRO PRO ILE ARG GLY SEQRES 32 A 649 GLN ILE ARG CYS SER SER ASN ILE THR GLY LEU LEU LEU SEQRES 33 A 649 THR ARG ASP GLY GLY ILE ASN GLU ASN GLY THR GLU ILE SEQRES 34 A 649 PHE ARG PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SEQRES 35 A 649 SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU PRO SEQRES 36 A 649 LEU GLY VAL ALA PRO THR ARG CYS LYS ARG ARG VAL VAL SEQRES 37 A 649 GLN GLY GLY GLY GLY SER GLY GLY GLY GLY SER ALA VAL SEQRES 38 A 649 GLY ILE GLY ALA VAL ARG ARG GLY PHE LEU GLY ALA ALA SEQRES 39 A 649 GLY SER THR MET GLY ALA ALA SER MET THR LEU THR VAL SEQRES 40 A 649 GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN PRO GLN SEQRES 41 A 649 SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN ARG MET SEQRES 42 A 649 LEU GLN LEU GLY VAL TRP GLY ILE LYS GLN LEU GLN ALA SEQRES 43 A 649 ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP GLN GLN SEQRES 44 A 649 LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU ILE CYS SEQRES 45 A 649 THR THR ALA VAL PRO TRP ASN ALA SER TRP SER ASN LYS SEQRES 46 A 649 SER LEU ASP ARG ILE TRP ASN ASN MET THR TRP MET GLU SEQRES 47 A 649 TRP GLU ARG GLU ILE ASP ASN TYR THR SER GLU ILE TYR SEQRES 48 A 649 THR LEU ILE GLU GLU SER GLN ASN GLN GLN GLU LYS ASN SEQRES 49 A 649 GLU GLN GLU LEU LEU CYS LEU ASP GLY GLY GLY GLY SER SEQRES 50 A 649 HIS HIS HIS HIS HIS HIS HIS HIS GLY SER GLY CYS HET NAG N 1 14 HET NAG N 2 14 HET BMA N 3 11 HET MAN N 4 11 HET MAN N 5 11 HET NAG O 1 14 HET NAG O 2 14 HET NAG P 1 14 HET NAG P 2 14 HET BMA P 3 11 HET MAN P 4 11 HET MAN P 5 11 HET NAG Q 1 14 HET NAG Q 2 14 HET BMA Q 3 11 HET MAN Q 4 11 HET MAN Q 5 11 HET NAG R 1 14 HET NAG R 2 14 HET NAG S 1 14 HET NAG S 2 14 HET NAG T 1 14 HET NAG T 2 14 HET BMA T 3 11 HET MAN T 4 11 HET MAN T 5 11 HET MAN T 6 11 HET MAN T 7 11 HET MAN T 8 11 HET MAN T 9 11 HET MAN T 10 11 HET NAG U 1 14 HET NAG U 2 14 HET BMA U 3 11 HET MAN U 4 11 HET MAN U 5 11 HET NAG V 1 14 HET NAG V 2 14 HET NAG W 1 14 HET NAG W 2 14 HET BMA W 3 11 HET MAN W 4 11 HET NAG C 701 14 HET NAG C 702 14 HET NAG C 703 14 HET NAG C 704 14 HET NAG C 705 14 HET NAG C 706 14 HET NAG C 707 14 HET NAG C 708 14 HET NAG C 709 14 HET NAG C 710 14 HET NAG C 711 14 HET NAG C 712 14 HET NAG B 701 14 HET NAG B 702 14 HET NAG B 703 14 HET NAG B 704 14 HET NAG B 705 14 HET NAG B 706 14 HET NAG B 707 14 HET NAG B 708 14 HET NAG B 709 14 HET NAG B 710 14 HET NAG B 711 14 HET NAG B 712 14 HET NAG A 701 14 HET NAG A 702 14 HET NAG A 703 14 HET NAG A 704 14 HET NAG A 705 14 HET NAG A 706 14 HET NAG A 707 14 HET NAG A 708 14 HET NAG A 709 14 HET NAG A 710 14 HET NAG A 711 14 HET NAG A 712 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 14 NAG 56(C8 H15 N O6) FORMUL 14 BMA 6(C6 H12 O6) FORMUL 14 MAN 16(C6 H12 O6) HELIX 1 AA1 ARG D 28 TYR D 32 5 5 HELIX 2 AA2 PRO D 61 GLN D 64 5 4 HELIX 3 AA3 LYS D 83 ASP D 86 5 4 HELIX 4 AA4 CYS E 27C LYS E 31 5 5 HELIX 5 AA5 ARG E 79 GLU E 83 5 5 HELIX 6 AA6 PRO F 61 GLN F 64 5 4 HELIX 7 AA7 ARG G 79 GLU G 83 5 5 HELIX 8 AA8 PRO J 61 GLN J 64 5 4 HELIX 9 AA9 LYS J 83 ASP J 86 5 4 HELIX 10 AB1 PRO K 26 CYS K 27C 5 5 HELIX 11 AB2 THR H 83 THR H 87 5 5 HELIX 12 AB3 GLN L 79 PHE L 83 5 5 HELIX 13 AB4 THR I 83 THR I 87 5 5 HELIX 14 AB5 GLN M 79 PHE M 83 5 5 HELIX 15 AB6 ALA C 70 CYS C 74 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 ARG C 335 PHE C 353 1 19 HELIX 19 AC1 ASP C 368 MET C 373 1 6 HELIX 20 AC2 ASN C 377 GLU C 381 5 5 HELIX 21 AC3 ASN C 425 ARG C 429 5 5 HELIX 22 AC4 MET C 475 SER C 481 1 7 HELIX 23 AC5 THR C 529 THR C 536 1 8 HELIX 24 AC6 THR C 536 ASN C 543 1 8 HELIX 25 AC7 GLY C 569 TRP C 596 1 28 HELIX 26 AC8 SER C 618 ASN C 624 1 7 HELIX 27 AC9 THR C 627 ILE C 635 1 9 HELIX 28 AD1 ILE C 635 SER C 649 1 15 HELIX 29 AD2 SER C 649 LEU C 661 1 13 HELIX 30 AD3 ASN B 98 LEU B 116 1 19 HELIX 31 AD4 LEU B 122 CYS B 126 5 5 HELIX 32 AD5 ARG B 335 GLU B 354 1 20 HELIX 33 AD6 ASP B 368 MET B 373 1 6 HELIX 34 AD7 ARG B 476 SER B 481 1 6 HELIX 35 AD8 THR B 536 LEU B 545 1 10 HELIX 36 AD9 GLY B 569 TRP B 596 1 28 HELIX 37 AE1 SER B 618 TRP B 623 1 6 HELIX 38 AE2 THR B 627 ILE B 635 1 9 HELIX 39 AE3 TYR B 638 SER B 649 1 12 HELIX 40 AE4 GLN B 650 LEU B 660 1 11 HELIX 41 AE5 ASN A 98 LYS A 117 1 20 HELIX 42 AE6 THR A 123 VAL A 127 5 5 HELIX 43 AE7 SER A 334 PHE A 353 1 20 HELIX 44 AE8 ASP A 368 MET A 373 1 6 HELIX 45 AE9 ASP A 474 SER A 481 1 8 HELIX 46 AF1 THR A 529 SER A 534 1 6 HELIX 47 AF2 GLY A 572 TRP A 596 1 25 HELIX 48 AF3 SER A 618 TRP A 623 1 6 HELIX 49 AF4 THR A 627 ASP A 636 1 10 HELIX 50 AF5 TYR A 638 ASN A 656 1 19 SHEET 1 AA1 4 GLN D 3 GLN D 6 0 SHEET 2 AA1 4 VAL D 18 SER D 25 -1 O SER D 25 N GLN D 3 SHEET 3 AA1 4 SER D 74 ILE D 82 -1 O ALA D 78 N CYS D 22 SHEET 4 AA1 4 VAL D 67 THR D 71 -1 N THR D 70 O TYR D 79 SHEET 1 AA2 4 GLN D 3 GLN D 6 0 SHEET 2 AA2 4 VAL D 18 SER D 25 -1 O SER D 25 N GLN D 3 SHEET 3 AA2 4 SER D 74 ILE D 82 -1 O ALA D 78 N CYS D 22 SHEET 4 AA2 4 VAL D 73B PRO D 73C-1 N VAL D 73B O THR D 75 SHEET 1 AA3 5 LYS D 57 LEU D 59 0 SHEET 2 AA3 5 GLU D 46 ILE D 51 -1 N TRP D 50 O ASN D 58 SHEET 3 AA3 5 ILE D 34 THR D 40 -1 N ARG D 38 O GLU D 46 SHEET 4 AA3 5 GLY D 88 LYS D 94 -1 O PHE D 91 N ILE D 37 SHEET 5 AA3 5 THR D 107 LEU D 109 -1 O LEU D 109 N GLY D 88 SHEET 1 AA4 4 THR E 5 GLN E 6 0 SHEET 2 AA4 4 VAL E 19 THR E 24 -1 O THR E 24 N THR E 5 SHEET 3 AA4 4 ALA E 71 ILE E 75 -1 O LEU E 73 N ILE E 21 SHEET 4 AA4 4 PHE E 62 LYS E 66 -1 N SER E 63 O THR E 74 SHEET 1 AA5 5 SER E 9 SER E 14 0 SHEET 2 AA5 5 THR E 102 LEU E 107 1 O LEU E 107 N GLY E 13 SHEET 3 AA5 5 THR E 85 TYR E 91 -1 N TYR E 86 O THR E 102 SHEET 4 AA5 5 SER E 32 GLN E 37 -1 N SER E 34 O CYS E 89 SHEET 5 AA5 5 THR E 45 LEU E 46 -1 O THR E 45 N GLN E 37 SHEET 1 AA6 4 SER E 9 SER E 14 0 SHEET 2 AA6 4 THR E 102 LEU E 107 1 O LEU E 107 N GLY E 13 SHEET 3 AA6 4 THR E 85 TYR E 91 -1 N TYR E 86 O THR E 102 SHEET 4 AA6 4 VAL E 97 PHE E 98 -1 O VAL E 97 N SER E 90 SHEET 1 AA7 4 VAL F 5 GLN F 6 0 SHEET 2 AA7 4 VAL F 18 LYS F 23 -1 O LYS F 23 N VAL F 5 SHEET 3 AA7 4 ALA F 77 ILE F 82 -1 O ALA F 78 N CYS F 22 SHEET 4 AA7 4 VAL F 67 THR F 71 -1 N THR F 70 O TYR F 79 SHEET 1 AA8 5 LYS F 57 LEU F 59 0 SHEET 2 AA8 5 GLY F 44 ILE F 51 -1 N TRP F 50 O ASN F 58 SHEET 3 AA8 5 ILE F 34 THR F 40 -1 N ILE F 34 O ILE F 51 SHEET 4 AA8 5 GLY F 88 GLY F 95 -1 O PHE F 91 N ILE F 37 SHEET 5 AA8 5 PRO F 100F TRP F 103 -1 O TYR F 101 N LYS F 94 SHEET 1 AA9 5 LYS F 57 LEU F 59 0 SHEET 2 AA9 5 GLY F 44 ILE F 51 -1 N TRP F 50 O ASN F 58 SHEET 3 AA9 5 ILE F 34 THR F 40 -1 N ILE F 34 O ILE F 51 SHEET 4 AA9 5 GLY F 88 GLY F 95 -1 O PHE F 91 N ILE F 37 SHEET 5 AA9 5 THR F 107 LEU F 108 -1 O THR F 107 N TYR F 90 SHEET 1 AB1 2 VAL F 73B THR F 73E 0 SHEET 2 AB1 2 THR F 73H THR F 75 -1 O THR F 75 N VAL F 73B SHEET 1 AB2 4 THR G 5 GLN G 6 0 SHEET 2 AB2 4 VAL G 19 THR G 24 -1 O THR G 24 N THR G 5 SHEET 3 AB2 4 SER G 70 ILE G 75 -1 O ALA G 71 N CYS G 23 SHEET 4 AB2 4 GLY G 64 LYS G 66 -1 N TYR G 65 O TYR G 72 SHEET 1 AB3 5 VAL G 11 SER G 14 0 SHEET 2 AB3 5 THR G 102 LEU G 107 1 O SER G 105 N GLY G 13 SHEET 3 AB3 5 THR G 85 TYR G 91 -1 N TYR G 86 O THR G 102 SHEET 4 AB3 5 SER G 32 GLN G 37 -1 N SER G 32 O TYR G 91 SHEET 5 AB3 5 THR G 45 ILE G 48 -1 O THR G 45 N GLN G 37 SHEET 1 AB4 4 VAL G 11 SER G 14 0 SHEET 2 AB4 4 THR G 102 LEU G 107 1 O SER G 105 N GLY G 13 SHEET 3 AB4 4 THR G 85 TYR G 91 -1 N TYR G 86 O THR G 102 SHEET 4 AB4 4 VAL G 97 PHE G 98 -1 O VAL G 97 N SER G 90 SHEET 1 AB5 4 GLN J 3 GLN J 6 0 SHEET 2 AB5 4 SER J 17 TYR J 27 -1 O SER J 25 N GLN J 3 SHEET 3 AB5 4 SER J 74 ARG J 82A-1 O GLY J 76 N THR J 24 SHEET 4 AB5 4 VAL J 67 THR J 71 -1 N THR J 70 O TYR J 79 SHEET 1 AB6 4 GLN J 3 GLN J 6 0 SHEET 2 AB6 4 SER J 17 TYR J 27 -1 O SER J 25 N GLN J 3 SHEET 3 AB6 4 SER J 74 ARG J 82A-1 O GLY J 76 N THR J 24 SHEET 4 AB6 4 VAL J 73B PRO J 73C-1 N VAL J 73B O THR J 75 SHEET 1 AB7 6 GLU J 10 LYS J 12 0 SHEET 2 AB7 6 THR J 107 VAL J 111 1 O THR J 110 N GLU J 10 SHEET 3 AB7 6 GLY J 88 GLY J 95 -1 N GLY J 88 O LEU J 109 SHEET 4 AB7 6 ILE J 34 THR J 40 -1 N GLN J 39 O THR J 89 SHEET 5 AB7 6 PRO J 45 SER J 52 -1 O ILE J 51 N ILE J 34 SHEET 6 AB7 6 ASP J 56 LEU J 59 -1 O ASP J 56 N SER J 52 SHEET 1 AB8 4 GLU J 10 LYS J 12 0 SHEET 2 AB8 4 THR J 107 VAL J 111 1 O THR J 110 N GLU J 10 SHEET 3 AB8 4 GLY J 88 GLY J 95 -1 N GLY J 88 O LEU J 109 SHEET 4 AB8 4 PRO J 100F TRP J 103 -1 O TYR J 101 N LYS J 94 SHEET 1 AB9 4 THR K 5 GLN K 6 0 SHEET 2 AB9 4 ILE K 21 THR K 24 -1 O THR K 24 N THR K 5 SHEET 3 AB9 4 ALA K 71 ILE K 75 -1 O ALA K 71 N CYS K 23 SHEET 4 AB9 4 PHE K 62 LYS K 66 -1 N SER K 63 O THR K 74 SHEET 1 AC1 5 SER K 9 GLY K 13 0 SHEET 2 AC1 5 THR K 102 VAL K 106 1 O SER K 105 N GLY K 13 SHEET 3 AC1 5 THR K 85 TYR K 91 -1 N TYR K 86 O THR K 102 SHEET 4 AC1 5 SER K 32 TRP K 38 -1 N SER K 34 O CYS K 89 SHEET 5 AC1 5 THR K 45 ILE K 48 -1 O THR K 45 N GLN K 37 SHEET 1 AC2 4 SER K 9 GLY K 13 0 SHEET 2 AC2 4 THR K 102 VAL K 106 1 O SER K 105 N GLY K 13 SHEET 3 AC2 4 THR K 85 TYR K 91 -1 N TYR K 86 O THR K 102 SHEET 4 AC2 4 CYS K 96 PHE K 98 -1 O VAL K 97 N SER K 90 SHEET 1 AC3 4 LEU H 4 SER H 7 0 SHEET 2 AC3 4 LEU H 18 VAL H 24 -1 O THR H 21 N SER H 7 SHEET 3 AC3 4 GLN H 77 LEU H 82 -1 O PHE H 78 N CYS H 22 SHEET 4 AC3 4 VAL H 67 SER H 70 -1 N SER H 70 O SER H 79 SHEET 1 AC4 5 THR H 57 TYR H 59 0 SHEET 2 AC4 5 GLU H 46 PHE H 52 -1 N TYR H 50 O LYS H 58 SHEET 3 AC4 5 PHE H 33 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 4 AC4 5 ALA H 88 TRP H 95 -1 O TRP H 95 N PHE H 33 SHEET 5 AC4 5 PHE H 100G TRP H 103 -1 O VAL H 102 N ARG H 94 SHEET 1 AC5 5 THR H 57 TYR H 59 0 SHEET 2 AC5 5 GLU H 46 PHE H 52 -1 N TYR H 50 O LYS H 58 SHEET 3 AC5 5 PHE H 33 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 4 AC5 5 ALA H 88 TRP H 95 -1 O TRP H 95 N PHE H 33 SHEET 5 AC5 5 VAL H 107 VAL H 109 -1 O VAL H 109 N ALA H 88 SHEET 1 AC6 4 MET L 4 SER L 7 0 SHEET 2 AC6 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AC6 4 GLU L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AC6 4 PHE L 62 SER L 67 -1 N ARG L 63 O THR L 74 SHEET 1 AC7 5 SER L 10 SER L 12 0 SHEET 2 AC7 5 THR L 102 GLU L 105 1 O GLU L 105 N LEU L 11 SHEET 3 AC7 5 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AC7 5 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AC7 5 GLN L 45 ILE L 48 -1 O LEU L 47 N TRP L 35 SHEET 1 AC8 4 GLN I 3 SER I 7 0 SHEET 2 AC8 4 LEU I 18 SER I 25 -1 O THR I 23 N GLN I 5 SHEET 3 AC8 4 GLN I 77 LEU I 82 -1 O LEU I 82 N LEU I 18 SHEET 4 AC8 4 VAL I 67 THR I 73 -1 N THR I 68 O LYS I 81 SHEET 1 AC9 5 THR I 57 TYR I 59 0 SHEET 2 AC9 5 GLU I 46 PHE I 52 -1 N TYR I 50 O LYS I 58 SHEET 3 AC9 5 PHE I 33 GLN I 39 -1 N ARG I 38 O GLU I 46 SHEET 4 AC9 5 ALA I 88 TRP I 95 -1 O TRP I 95 N PHE I 33 SHEET 5 AC9 5 PHE I 100G TRP I 103 -1 O VAL I 102 N ARG I 94 SHEET 1 AD1 5 THR I 57 TYR I 59 0 SHEET 2 AD1 5 GLU I 46 PHE I 52 -1 N TYR I 50 O LYS I 58 SHEET 3 AD1 5 PHE I 33 GLN I 39 -1 N ARG I 38 O GLU I 46 SHEET 4 AD1 5 ALA I 88 TRP I 95 -1 O TRP I 95 N PHE I 33 SHEET 5 AD1 5 VAL I 107 VAL I 109 -1 O VAL I 107 N TYR I 90 SHEET 1 AD2 4 MET M 4 SER M 7 0 SHEET 2 AD2 4 VAL M 19 ALA M 25 -1 O GLN M 24 N THR M 5 SHEET 3 AD2 4 GLU M 70 ILE M 75 -1 O PHE M 71 N CYS M 23 SHEET 4 AD2 4 PHE M 62 SER M 67 -1 N ARG M 63 O THR M 74 SHEET 1 AD3 6 SER M 10 SER M 12 0 SHEET 2 AD3 6 THR M 102 GLU M 105 1 O GLU M 105 N LEU M 11 SHEET 3 AD3 6 THR M 85 GLN M 90 -1 N TYR M 86 O THR M 102 SHEET 4 AD3 6 LEU M 33 GLN M 38 -1 N GLN M 38 O THR M 85 SHEET 5 AD3 6 GLN M 45 TYR M 49 -1 O GLN M 45 N GLN M 37 SHEET 6 AD3 6 SER M 53 ARG M 54 -1 O SER M 53 N TYR M 49 SHEET 1 AD4 3 LEU C 494 THR C 499 0 SHEET 2 AD4 3 TRP C 35 TYR C 40 -1 N TYR C 39 O GLY C 495 SHEET 3 AD4 3 ILE C 603 PRO C 609 -1 O CYS C 604 N VAL C 38 SHEET 1 AD5 5 TRP C 45 ASP C 47 0 SHEET 2 AD5 5 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AD5 5 PHE C 223 CYS C 228 -1 N LEU C 226 O LYS C 487 SHEET 4 AD5 5 VAL C 242 VAL C 245 -1 O VAL C 245 N ILE C 225 SHEET 5 AD5 5 GLU C 83 LEU C 86 -1 N VAL C 84 O THR C 244 SHEET 1 AD6 3 VAL C 75 PRO C 76 0 SHEET 2 AD6 3 PHE C 53 SER C 56 1 N SER C 56 O VAL C 75 SHEET 3 AD6 3 HIS C 216 CYS C 218 -1 O CYS C 218 N PHE C 53 SHEET 1 AD7 2 GLU C 91 ASN C 94 0 SHEET 2 AD7 2 LYS C 236 CYS C 239 -1 O GLY C 237 N PHE C 93 SHEET 1 AD8 5 VAL C 169 TYR C 177 0 SHEET 2 AD8 5 ILE C 154 THR C 162 -1 N ILE C 161 O GLN C 170 SHEET 3 AD8 5 LEU C 129 CYS C 131 -1 N ASN C 130 O SER C 158 SHEET 4 AD8 5 SER C 190 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AD8 5 VAL C 181 PRO C 183 -1 N VAL C 182 O ARG C 192 SHEET 1 AD9 3 VAL C 200 GLN C 203 0 SHEET 2 AD9 3 GLN C 432 TYR C 435 1 O TYR C 435 N THR C 202 SHEET 3 AD9 3 ILE C 423 ILE C 424 -1 N ILE C 424 O MET C 434 SHEET 1 AE1 7 LEU C 259 LEU C 261 0 SHEET 2 AE1 7 ILE C 443 ARG C 456 -1 O GLY C 451 N LEU C 260 SHEET 3 AE1 7 ILE C 284 ARG C 298 -1 N VAL C 292 O ILE C 449 SHEET 4 AE1 7 ALA C 329 SER C 334 -1 O ASN C 332 N ASN C 295 SHEET 5 AE1 7 THR C 413 LYS C 421 -1 O ILE C 414 N ILE C 333 SHEET 6 AE1 7 PHE C 382 CYS C 385 -1 N TYR C 384 O ARG C 419 SHEET 7 AE1 7 HIS C 374 PHE C 376 -1 N HIS C 374 O CYS C 385 SHEET 1 AE2 6 VAL C 271 ARG C 273 0 SHEET 2 AE2 6 ILE C 284 ARG C 298 -1 O ILE C 285 N ARG C 273 SHEET 3 AE2 6 ILE C 443 ARG C 456 -1 O ILE C 449 N VAL C 292 SHEET 4 AE2 6 THR C 465 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 5 AE2 6 THR C 357 PHE C 361 1 N VAL C 359 O PHE C 468 SHEET 6 AE2 6 SER C 393 THR C 394 -1 O SER C 393 N PHE C 361 SHEET 1 AE3 2 ASN C 301 GLY C 312 0 SHEET 2 AE3 2 ARG C 315 ILE C 323A-1 O THR C 319 N LYS C 305 SHEET 1 AE4 3 LEU B 494 THR B 499 0 SHEET 2 AE4 3 TRP B 35 TYR B 40 -1 N TRP B 35 O THR B 499 SHEET 3 AE4 3 ILE B 603 PRO B 609 -1 O CYS B 604 N VAL B 38 SHEET 1 AE5 5 TRP B 45 ASP B 47 0 SHEET 2 AE5 5 TYR B 486 ILE B 491 -1 O LYS B 490 N LYS B 46 SHEET 3 AE5 5 PHE B 223 CYS B 228 -1 N ALA B 224 O VAL B 489 SHEET 4 AE5 5 VAL B 242 VAL B 245 -1 O SER B 243 N LYS B 227 SHEET 5 AE5 5 GLU B 83 VAL B 84 -1 N VAL B 84 O THR B 244 SHEET 1 AE6 3 VAL B 75 PRO B 76 0 SHEET 2 AE6 3 PHE B 53 SER B 56 1 N SER B 56 O VAL B 75 SHEET 3 AE6 3 ILE B 215 CYS B 218 -1 O CYS B 218 N PHE B 53 SHEET 1 AE7 2 HIS B 92 ASN B 94 0 SHEET 2 AE7 2 LYS B 236 PRO B 238 -1 O GLY B 237 N PHE B 93 SHEET 1 AE8 5 GLN B 170 TYR B 177 0 SHEET 2 AE8 5 ILE B 154 ILE B 161 -1 N CYS B 157 O ALA B 174 SHEET 3 AE8 5 LEU B 129 ASP B 133 -1 N ASN B 130 O SER B 158 SHEET 4 AE8 5 SER B 190 LEU B 193 -1 O TYR B 191 N LEU B 129 SHEET 5 AE8 5 VAL B 181 PRO B 183 -1 N VAL B 182 O ARG B 192 SHEET 1 AE9 3 VAL B 200 GLN B 203 0 SHEET 2 AE9 3 GLN B 432 TYR B 435 1 O ALA B 433 N THR B 202 SHEET 3 AE9 3 ILE B 423 ILE B 424 -1 N ILE B 424 O MET B 434 SHEET 1 AF1 3 LEU B 259 LEU B 261 0 SHEET 2 AF1 3 ILE B 443 ARG B 456 -1 O GLY B 451 N LEU B 260 SHEET 3 AF1 3 GLU B 293 ARG B 298 -1 N CYS B 296 O CYS B 445 SHEET 1 AF2 6 VAL B 271 ARG B 273 0 SHEET 2 AF2 6 ILE B 284 GLN B 287 -1 O ILE B 285 N ARG B 273 SHEET 3 AF2 6 ILE B 443 ARG B 456 -1 O LEU B 454 N ILE B 284 SHEET 4 AF2 6 THR B 465 PRO B 470 -1 O ARG B 469 N THR B 455 SHEET 5 AF2 6 THR B 357 PHE B 361 1 N THR B 357 O GLU B 466 SHEET 6 AF2 6 SER B 393 THR B 394 -1 O SER B 393 N PHE B 361 SHEET 1 AF3 2 ASN B 301 GLY B 312 0 SHEET 2 AF3 2 ARG B 315 ILE B 323A-1 O GLY B 321 N THR B 303 SHEET 1 AF4 3 ALA B 329 SER B 334 0 SHEET 2 AF4 3 THR B 413 LYS B 421 -1 O ILE B 414 N ILE B 333 SHEET 3 AF4 3 PHE B 382 CYS B 385 -1 N TYR B 384 O ARG B 419 SHEET 1 AF5 3 LEU A 494 THR A 499 0 SHEET 2 AF5 3 TRP A 35 TYR A 40 -1 N TYR A 39 O GLY A 495 SHEET 3 AF5 3 ILE A 603 PRO A 609 -1 O CYS A 604 N VAL A 38 SHEET 1 AF6 5 TRP A 45 ASP A 47 0 SHEET 2 AF6 5 LYS A 487 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AF6 5 PHE A 223 CYS A 228 -1 N LEU A 226 O LYS A 487 SHEET 4 AF6 5 VAL A 242 VAL A 245 -1 O VAL A 245 N ILE A 225 SHEET 5 AF6 5 VAL A 84 VAL A 85 -1 N VAL A 84 O THR A 244 SHEET 1 AF7 2 GLU A 91 ASN A 94 0 SHEET 2 AF7 2 LYS A 236 CYS A 239 -1 O GLY A 237 N PHE A 93 SHEET 1 AF8 5 VAL A 172 TYR A 177 0 SHEET 2 AF8 5 ILE A 154 PHE A 159 -1 N CYS A 157 O ALA A 174 SHEET 3 AF8 5 LEU A 129 LYS A 132 -1 N ASN A 130 O SER A 158 SHEET 4 AF8 5 SER A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 5 AF8 5 VAL A 181 PRO A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AF9 3 VAL A 200 GLN A 203 0 SHEET 2 AF9 3 GLN A 432 TYR A 435 1 O ALA A 433 N THR A 202 SHEET 3 AF9 3 ILE A 423 ILE A 424 -1 N ILE A 424 O MET A 434 SHEET 1 AG1 6 LEU A 259 LEU A 261 0 SHEET 2 AG1 6 SER A 447 ARG A 456 -1 O GLY A 451 N LEU A 260 SHEET 3 AG1 6 ILE A 284 THR A 297 -1 N ILE A 294 O SER A 447 SHEET 4 AG1 6 THR A 465 PRO A 470 0 SHEET 5 AG1 6 THR A 357 PHE A 361 1 N THR A 357 O GLU A 466 SHEET 6 AG1 6 SER A 393 TRP A 395 -1 O TRP A 395 N ILE A 358 SHEET 1 AG2 5 VAL A 271 ARG A 273 0 SHEET 2 AG2 5 ILE A 284 THR A 297 -1 O GLN A 287 N VAL A 271 SHEET 3 AG2 5 SER A 447 ARG A 456 -1 O SER A 447 N ILE A 294 SHEET 4 AG2 5 ALA A 329 ASN A 332 0 SHEET 5 AG2 5 LEU A 416 CYS A 418 -1 O LEU A 416 N CYS A 331 SSBOND 1 CYS D 22 CYS D 92 1555 1555 2.04 SSBOND 2 CYS E 23 CYS E 88 1555 1555 1.81 SSBOND 3 CYS E 89 CYS E 96 1555 1555 2.03 SSBOND 4 CYS F 22 CYS F 92 1555 1555 2.04 SSBOND 5 CYS G 89 CYS G 96 1555 1555 2.03 SSBOND 6 CYS J 22 CYS J 92 1555 1555 2.02 SSBOND 7 CYS K 23 CYS K 88 1555 1555 2.03 SSBOND 8 CYS K 89 CYS K 96 1555 1555 2.04 SSBOND 9 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 10 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 11 CYS I 22 CYS I 92 1555 1555 2.04 SSBOND 12 CYS M 23 CYS M 88 1555 1555 2.04 SSBOND 13 CYS C 54 CYS C 74 1555 1555 2.03 SSBOND 14 CYS C 119 CYS C 205 1555 1555 2.03 SSBOND 15 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 16 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 17 CYS C 218 CYS C 247 1555 1555 2.03 SSBOND 18 CYS C 228 CYS C 239 1555 1555 1.95 SSBOND 19 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 20 CYS C 378 CYS C 445 1555 1555 1.80 SSBOND 21 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 22 CYS C 501 CYS B 662 1555 1555 2.03 SSBOND 23 CYS C 598 CYS C 604 1555 1555 2.03 SSBOND 24 CYS C 662 CYS A 501 1555 1555 2.04 SSBOND 25 CYS B 54 CYS B 74 1555 1555 2.04 SSBOND 26 CYS B 119 CYS B 205 1555 1555 2.03 SSBOND 27 CYS B 126 CYS B 196 1555 1555 1.91 SSBOND 28 CYS B 131 CYS B 157 1555 1555 2.03 SSBOND 29 CYS B 218 CYS B 247 1555 1555 2.03 SSBOND 30 CYS B 228 CYS B 239 1555 1555 2.03 SSBOND 31 CYS B 296 CYS B 331 1555 1555 2.01 SSBOND 32 CYS B 378 CYS B 445 1555 1555 2.03 SSBOND 33 CYS B 385 CYS B 418 1555 1555 2.03 SSBOND 34 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 35 CYS A 54 CYS A 74 1555 1555 2.03 SSBOND 36 CYS A 119 CYS A 205 1555 1555 2.03 SSBOND 37 CYS A 126 CYS A 196 1555 1555 2.03 SSBOND 38 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 39 CYS A 218 CYS A 247 1555 1555 2.03 SSBOND 40 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 41 CYS A 296 CYS A 331 1555 1555 2.02 SSBOND 42 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 43 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 44 CYS A 598 CYS A 604 1555 1555 2.02 LINK ND2 ASN C 88 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN C 156 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN C 160 C1 NAG C 701 1555 1555 1.45 LINK ND2 ASN C 241 C1 NAG C 702 1555 1555 1.44 LINK ND2 ASN C 262 C1 NAG P 1 1555 1555 1.46 LINK ND2 ASN C 276 C1 NAG C 703 1555 1555 1.44 LINK ND2 ASN C 295 C1 NAG C 704 1555 1555 1.43 LINK ND2 ASN C 301 C1 NAG C 705 1555 1555 1.44 LINK ND2 ASN C 332 C1 NAG C 706 1555 1555 1.44 LINK ND2 ASN C 339 C1 NAG C 711 1555 1555 1.44 LINK ND2 ASN C 362 C1 NAG C 707 1555 1555 1.46 LINK ND2 ASN C 386 C1 NAG C 708 1555 1555 1.45 LINK ND2 ASN C 392 C1 NAG C 709 1555 1555 1.44 LINK ND2 ASN C 448 C1 NAG C 710 1555 1555 1.44 LINK ND2 ASN C 625 C1 NAG C 712 1555 1555 1.45 LINK ND2 ASN B 88 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN B 156 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN B 160 C1 NAG B 701 1555 1555 1.44 LINK ND2 ASN B 241 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN B 262 C1 NAG T 1 1555 1555 1.45 LINK ND2 ASN B 276 C1 NAG B 702 1555 1555 1.44 LINK ND2 ASN B 295 C1 NAG B 703 1555 1555 1.44 LINK ND2 ASN B 301 C1 NAG B 704 1555 1555 1.44 LINK ND2 ASN B 332 C1 NAG B 705 1555 1555 1.43 LINK ND2 ASN B 339 C1 NAG B 710 1555 1555 1.44 LINK ND2 ASN B 362 C1 NAG B 706 1555 1555 1.44 LINK ND2 ASN B 386 C1 NAG B 707 1555 1555 1.44 LINK ND2 ASN B 392 C1 NAG B 708 1555 1555 1.44 LINK ND2 ASN B 448 C1 NAG B 709 1555 1555 1.44 LINK ND2 ASN B 625 C1 NAG B 711 1555 1555 1.44 LINK ND2 ASN B 637 C1 NAG B 712 1555 1555 1.44 LINK ND2 ASN A 88 C1 NAG U 1 1555 1555 1.43 LINK ND2 ASN A 156 C1 NAG V 1 1555 1555 1.45 LINK ND2 ASN A 160 C1 NAG A 701 1555 1555 1.44 LINK ND2 ASN A 241 C1 NAG A 702 1555 1555 1.44 LINK ND2 ASN A 262 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN A 276 C1 NAG A 703 1555 1555 1.44 LINK ND2 ASN A 295 C1 NAG A 704 1555 1555 1.44 LINK ND2 ASN A 301 C1 NAG A 705 1555 1555 1.44 LINK ND2 ASN A 332 C1 NAG A 706 1555 1555 1.44 LINK ND2 ASN A 339 C1 NAG A 711 1555 1555 1.45 LINK ND2 ASN A 362 C1 NAG A 707 1555 1555 1.44 LINK ND2 ASN A 386 C1 NAG A 708 1555 1555 1.45 LINK ND2 ASN A 392 C1 NAG A 709 1555 1555 1.44 LINK ND2 ASN A 448 C1 NAG A 710 1555 1555 1.44 LINK ND2 ASN A 625 C1 NAG A 712 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.44 LINK O3 BMA N 3 C1 MAN N 4 1555 1555 1.44 LINK O6 BMA N 3 C1 MAN N 5 1555 1555 1.45 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 P 2 C1 BMA P 3 1555 1555 1.45 LINK O3 BMA P 3 C1 MAN P 4 1555 1555 1.45 LINK O2 MAN P 4 C1 MAN P 5 1555 1555 1.44 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44 LINK O4 NAG Q 2 C1 BMA Q 3 1555 1555 1.46 LINK O3 BMA Q 3 C1 MAN Q 4 1555 1555 1.44 LINK O6 BMA Q 3 C1 MAN Q 5 1555 1555 1.44 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.44 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.44 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.45 LINK O4 NAG T 2 C1 BMA T 3 1555 1555 1.44 LINK O3 BMA T 3 C1 MAN T 4 1555 1555 1.44 LINK O6 BMA T 3 C1 MAN T 7 1555 1555 1.44 LINK O2 MAN T 4 C1 MAN T 5 1555 1555 1.44 LINK O2 MAN T 5 C1 MAN T 6 1555 1555 1.46 LINK O3 MAN T 7 C1 MAN T 8 1555 1555 1.45 LINK O6 MAN T 7 C1 MAN T 10 1555 1555 1.44 LINK O2 MAN T 8 C1 MAN T 9 1555 1555 1.45 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.43 LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.45 LINK O3 BMA U 3 C1 MAN U 4 1555 1555 1.44 LINK O6 BMA U 3 C1 MAN U 5 1555 1555 1.45 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.44 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.45 LINK O4 NAG W 2 C1 BMA W 3 1555 1555 1.44 LINK O3 BMA W 3 C1 MAN W 4 1555 1555 1.44 CISPEP 1 SER L 7 PRO L 8 0 -17.16 CISPEP 2 TYR L 94 PRO L 95 0 7.06 CISPEP 3 SER M 7 PRO M 8 0 -5.02 CISPEP 4 TYR M 94 PRO M 95 0 12.87 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