HEADER IMMUNE SYSTEM 11-AUG-14 4R2G TITLE CRYSTAL STRUCTURE OF PGT124 FAB BOUND TO HIV-1 JRCSF GP120 CORE AND TO TITLE 2 CD4 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SURFACE PROTEIN GP160; COMPND 3 CHAIN: E, O, A, K; COMPND 4 SYNONYM: GLYCOPROTEIN 120, GP120; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: T-CELL SURFACE GLYCOPROTEIN CD4; COMPND 8 CHAIN: F, B, H, L; COMPND 9 SYNONYM: T-CELL SURFACE ANTIGEN T4/LEU-3; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: PGT124 LIGHT CHAIN; COMPND 13 CHAIN: P, C, I, M; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: PGT124 HEAVY CHAIN; COMPND 17 CHAIN: Q, D, J, N; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 (JRCSF SOURCE 3 ISOLATE); SOURCE 4 ORGANISM_COMMON: HIV-1; SOURCE 5 ORGANISM_TAXID: 11688; SOURCE 6 GENE: ENV; SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 8 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM_CELL_LINE: 293 FREESTYLE; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 GENE: CD4; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 18 MOL_ID: 3; SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 20 ORGANISM_COMMON: HUMAN; SOURCE 21 ORGANISM_TAXID: 9606; SOURCE 22 GENE: IGL@; SOURCE 23 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 24 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM_CELL_LINE: 293 FREESTYLE; SOURCE 27 MOL_ID: 4; SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 29 ORGANISM_COMMON: HUMAN; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 GENE: IGH@; SOURCE 32 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 33 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 34 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 35 EXPRESSION_SYSTEM_CELL_LINE: 293 FREESTYLE KEYWDS PROTEIN-PROTEIN COMPLEX, IGG, ANTI-HIV ANTIBODIES, GP120, IMMUNE KEYWDS 2 SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR F.GARCES,I.A.WILSON REVDAT 2 15-OCT-14 4R2G 1 REMARK REVDAT 1 08-OCT-14 4R2G 0 JRNL AUTH F.GARCES,D.SOK,L.KONG,R.MCBRIDE,H.J.KIM,K.F.SAYE-FRANCISCO, JRNL AUTH 2 J.P.JULIEN,Y.HUA,A.CUPO,J.P.MOORE,J.C.PAULSON,A.B.WARD, JRNL AUTH 3 D.R.BURTON,I.A.WILSON JRNL TITL STRUCTURAL EVOLUTION OF GLYCAN RECOGNITION BY A FAMILY OF JRNL TITL 2 POTENT HIV ANTIBODIES. JRNL REF CELL(CAMBRIDGE,MASS.) V. 159 69 2014 JRNL REFN ISSN 0092-8674 JRNL PMID 25259921 JRNL DOI 10.1016/J.CELL.2014.09.009 REMARK 2 REMARK 2 RESOLUTION. 3.28 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.28 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.65 REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4 REMARK 3 NUMBER OF REFLECTIONS : 94587 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.210 REMARK 3 R VALUE (WORKING SET) : 0.207 REMARK 3 FREE R VALUE : 0.263 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 4720 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 39.6496 - 10.1457 0.95 3103 148 0.2446 0.2878 REMARK 3 2 10.1457 - 8.0753 0.97 3057 167 0.1800 0.2140 REMARK 3 3 8.0753 - 7.0610 0.97 3001 160 0.2032 0.2479 REMARK 3 4 7.0610 - 6.4184 0.99 3055 160 0.2076 0.2524 REMARK 3 5 6.4184 - 5.9600 0.99 3052 166 0.2083 0.2699 REMARK 3 6 5.9600 - 5.6096 1.00 3047 175 0.2065 0.2813 REMARK 3 7 5.6096 - 5.3294 0.94 2866 157 0.1934 0.2503 REMARK 3 8 5.3294 - 5.0979 0.99 3020 163 0.1730 0.2092 REMARK 3 9 5.0979 - 4.9020 0.99 3035 144 0.1669 0.2152 REMARK 3 10 4.9020 - 4.7331 1.00 3027 154 0.1650 0.2288 REMARK 3 11 4.7331 - 4.5854 1.00 3024 167 0.1596 0.2176 REMARK 3 12 4.5854 - 4.4545 0.99 3005 162 0.1620 0.2170 REMARK 3 13 4.4545 - 4.3374 1.00 2988 157 0.1679 0.2290 REMARK 3 14 4.3374 - 4.2317 1.00 3026 153 0.1693 0.2590 REMARK 3 15 4.2317 - 4.1356 0.98 2980 159 0.1838 0.2423 REMARK 3 16 4.1356 - 4.0476 0.95 2880 143 0.1988 0.2634 REMARK 3 17 4.0476 - 3.9667 1.00 3013 171 0.2115 0.2668 REMARK 3 18 3.9667 - 3.8920 0.99 2987 151 0.2427 0.3444 REMARK 3 19 3.8920 - 3.8225 0.99 2982 154 0.2388 0.2977 REMARK 3 20 3.8225 - 3.7578 1.00 3005 164 0.2211 0.2465 REMARK 3 21 3.7578 - 3.6972 1.00 3047 151 0.2261 0.2939 REMARK 3 22 3.6972 - 3.6403 0.99 2973 150 0.2624 0.3073 REMARK 3 23 3.6403 - 3.5868 1.00 2971 160 0.2482 0.3135 REMARK 3 24 3.5868 - 3.5364 1.00 3027 141 0.2422 0.3001 REMARK 3 25 3.5364 - 3.4886 1.00 3006 152 0.2521 0.2974 REMARK 3 26 3.4886 - 3.4433 1.00 2980 155 0.2877 0.3595 REMARK 3 27 3.4433 - 3.4003 0.99 3029 166 0.3104 0.3740 REMARK 3 28 3.4003 - 3.3593 0.99 2979 145 0.2826 0.3653 REMARK 3 29 3.3593 - 3.3203 0.93 2781 152 0.2794 0.3524 REMARK 3 30 3.3203 - 3.2830 0.98 2921 173 0.2883 0.3267 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) : 0.450 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.260 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 : 0.011 29813 REMARK 3 ANGLE : 1.373 40397 REMARK 3 CHIRALITY : 0.078 4717 REMARK 3 PLANARITY : 0.005 5058 REMARK 3 DIHEDRAL : 16.066 11109 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 4R2G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-AUG-14. REMARK 100 THE RCSB ID CODE IS RCSB086814. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-JUN-13 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL12-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 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 : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 94587 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.283 REMARK 200 RESOLUTION RANGE LOW (A) : 39.647 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3 REMARK 200 DATA REDUNDANCY : 6.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.28 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.40 REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9 REMARK 200 DATA REDUNDANCY IN SHELL : 6.30 REMARK 200 R MERGE FOR SHELL (I) : 0.87000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 67.34 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.77 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4M AMMONIUM SULPHATE, 0.1M TRIS, 13% REMARK 280 GLYCEROL, PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-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 82.20300 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 114.85600 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 82.71900 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 114.85600 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 82.20300 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 82.71900 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, P, Q 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D, O 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 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, I, J, K REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, M, N, A 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 THR E 317 REMARK 465 ARG E 318 REMARK 465 PRO E 319 REMARK 465 GLY E 320 REMARK 465 GLU E 321 REMARK 465 GLU E 492 REMARK 465 MET F 0 REMARK 465 VAL F 176 REMARK 465 LEU F 177 REMARK 465 ALA F 178 REMARK 465 PHE F 179 REMARK 465 GLN F 180 REMARK 465 LYS F 181 REMARK 465 ALA F 182 REMARK 465 SER F 183 REMARK 465 SER P 4 REMARK 465 GLU P 211 REMARK 465 CYS P 212 REMARK 465 SER P 213 REMARK 465 GLN Q 1 REMARK 465 LYS Q 147 REMARK 465 SER Q 148 REMARK 465 THR Q 149 REMARK 465 LYS Q 232 REMARK 465 SER Q 233 REMARK 465 CYS Q 234 REMARK 465 ASP Q 235 REMARK 465 MET B 0 REMARK 465 VAL B 176 REMARK 465 LEU B 177 REMARK 465 ALA B 178 REMARK 465 PHE B 179 REMARK 465 GLN B 180 REMARK 465 LYS B 181 REMARK 465 ALA B 182 REMARK 465 SER B 183 REMARK 465 SER C 4 REMARK 465 GLU C 211 REMARK 465 CYS C 212 REMARK 465 SER C 213 REMARK 465 GLN D 1 REMARK 465 SER D 146 REMARK 465 LYS D 147 REMARK 465 SER D 148 REMARK 465 THR D 149 REMARK 465 SER D 150 REMARK 465 GLY D 151 REMARK 465 LYS D 232 REMARK 465 SER D 233 REMARK 465 CYS D 234 REMARK 465 ASP D 235 REMARK 465 MET H 0 REMARK 465 LEU H 177 REMARK 465 ALA H 178 REMARK 465 PHE H 179 REMARK 465 GLN H 180 REMARK 465 LYS H 181 REMARK 465 ALA H 182 REMARK 465 SER H 183 REMARK 465 SER I 4 REMARK 465 GLU I 211 REMARK 465 CYS I 212 REMARK 465 SER I 213 REMARK 465 GLN J 1 REMARK 465 SER J 146 REMARK 465 LYS J 147 REMARK 465 SER J 148 REMARK 465 THR J 149 REMARK 465 SER J 150 REMARK 465 LYS J 232 REMARK 465 SER J 233 REMARK 465 CYS J 234 REMARK 465 ASP J 235 REMARK 465 MET L 0 REMARK 465 LYS L 1 REMARK 465 LYS L 2 REMARK 465 VAL L 176 REMARK 465 LEU L 177 REMARK 465 ALA L 178 REMARK 465 PHE L 179 REMARK 465 GLN L 180 REMARK 465 LYS L 181 REMARK 465 ALA L 182 REMARK 465 SER L 183 REMARK 465 SER M 4 REMARK 465 GLU M 211 REMARK 465 CYS M 212 REMARK 465 SER M 213 REMARK 465 LYS N 147 REMARK 465 SER N 148 REMARK 465 THR N 149 REMARK 465 SER N 150 REMARK 465 LYS N 232 REMARK 465 SER N 233 REMARK 465 CYS N 234 REMARK 465 ASP N 235 REMARK 465 THR O 317 REMARK 465 ARG O 318 REMARK 465 PRO O 319 REMARK 465 GLY O 320 REMARK 465 GLU O 321 REMARK 465 GLU O 492 REMARK 465 THR A 317 REMARK 465 ARG A 318 REMARK 465 PRO A 319 REMARK 465 GLY A 320 REMARK 465 GLU A 321 REMARK 465 ILE A 322 REMARK 465 GLU A 492 REMARK 465 THR K 317 REMARK 465 ARG K 318 REMARK 465 PRO K 319 REMARK 465 GLY K 320 REMARK 465 GLU K 321 REMARK 465 GLU K 492 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 VAL H 176 CG1 CG2 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 ND2 ASN A 356 O5 NAG A 517 1.50 REMARK 500 CB LYS P 150 OG SER P 193 1.64 REMARK 500 ND2 ASN A 276 O5 NAG A 516 1.70 REMARK 500 ND2 ASN E 332 O5 NAG E 501 1.75 REMARK 500 CG LYS P 150 OG SER P 193 1.80 REMARK 500 ND2 ASN O 332 O5 NAG O 501 1.83 REMARK 500 ND2 ASN O 392 O5 NAG O 516 1.86 REMARK 500 ND2 ASN E 276 O5 NAG E 512 1.90 REMARK 500 N LYS P 150 O SER P 193 1.92 REMARK 500 O2 MAN O 508 O5 MAN O 509 1.94 REMARK 500 O2 MAN K 508 O5 MAN K 509 1.94 REMARK 500 OG SER C 93 OD1 ASP O 325 1.95 REMARK 500 NH2 ARG B 54 OD2 ASP B 78 1.96 REMARK 500 OG SER M 30 OD2 ASP A 325 1.96 REMARK 500 ND2 ASN A 262 O5 NAG A 515 1.98 REMARK 500 ND2 ASN E 411 O5 NAG E 517 2.00 REMARK 500 O4 NAG E 502 O5 BMA E 503 2.02 REMARK 500 O4 NAG K 502 O5 BMA K 503 2.02 REMARK 500 O4 NAG O 502 O5 BMA O 503 2.02 REMARK 500 O4 NAG A 502 O5 BMA A 503 2.02 REMARK 500 ND2 ASN A 339 C2 NAG A 513 2.06 REMARK 500 O3 BMA K 503 C2 MAN K 508 2.06 REMARK 500 O3 BMA O 503 C2 MAN O 508 2.06 REMARK 500 ND2 ASN K 332 C8 NAG K 501 2.11 REMARK 500 O3 NAG A 501 O5 NAG A 502 2.17 REMARK 500 O3 NAG E 501 O5 NAG E 502 2.17 REMARK 500 O3 NAG K 501 O5 NAG K 502 2.17 REMARK 500 O3 NAG O 501 O5 NAG O 502 2.17 REMARK 500 O3 MAN O 504 O5 MAN O 507 2.18 REMARK 500 O3 MAN E 504 O5 MAN E 507 2.18 REMARK 500 O3 MAN A 504 O5 MAN A 507 2.18 REMARK 500 O3 MAN K 504 O5 MAN K 507 2.18 REMARK 500 ND2 ASN E 339 C2 NAG E 514 2.19 REMARK 500 O ILE A 215 O GLY A 250 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 PRO P 40 CD PRO P 40 N 0.163 REMARK 500 ARG N 100 CA ARG N 100 C -0.230 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 PRO P 8 C - N - CD ANGL. DEV. = 13.0 DEGREES REMARK 500 PRO P 40 CA - N - CD ANGL. DEV. = -9.2 DEGREES REMARK 500 SER P 107 N - CA - C ANGL. DEV. = -18.2 DEGREES REMARK 500 PRO Q 14 N - CA - C ANGL. DEV. = 21.0 DEGREES REMARK 500 PRO Q 165 C - N - CD ANGL. DEV. = 18.6 DEGREES REMARK 500 SER D 74 N - CA - CB ANGL. DEV. = 9.7 DEGREES REMARK 500 ILE N 100A C - N - CA ANGL. DEV. = -16.4 DEGREES REMARK 500 PRO A 206 C - N - CD ANGL. DEV. = 16.5 DEGREES REMARK 500 PRO A 253 C - N - CD ANGL. DEV. = 12.7 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 ASN E 94 85.89 -168.89 REMARK 500 GLN E 114 -60.34 74.06 REMARK 500 THR E 123 -68.94 -138.96 REMARK 500 ASN E 230 104.14 -57.82 REMARK 500 GLU E 268 -129.71 58.06 REMARK 500 ASN E 356 8.59 80.56 REMARK 500 HIS E 374 96.95 -69.88 REMARK 500 GLU E 399 -167.43 -111.71 REMARK 500 GLN E 422 -34.39 -138.38 REMARK 500 GLU E 462 -131.57 57.14 REMARK 500 SER E 463 -0.87 83.70 REMARK 500 LYS E 485 49.65 -100.73 REMARK 500 PRO F 48 39.55 -90.30 REMARK 500 SER F 49 -168.78 -78.72 REMARK 500 ASN F 73 77.37 46.63 REMARK 500 ASN F 103 53.37 39.17 REMARK 500 THR F 106 -4.55 77.69 REMARK 500 THR F 115 9.30 89.89 REMARK 500 GLN F 165 13.40 53.71 REMARK 500 PRO P 40 134.15 -31.49 REMARK 500 ASN P 50 -130.85 47.08 REMARK 500 ALA P 128 33.23 -85.36 REMARK 500 SER P 153 2.21 86.37 REMARK 500 SER P 169 -9.94 -56.83 REMARK 500 GLU P 199 39.91 71.83 REMARK 500 GLU Q 16 -173.50 -66.70 REMARK 500 ARG Q 54 33.52 -89.64 REMARK 500 GLU Q 55 12.09 51.06 REMARK 500 SER Q 174 -115.87 49.54 REMARK 500 ASP B 10 -163.14 -78.26 REMARK 500 LYS B 21 66.32 -105.63 REMARK 500 ASN B 30 -160.41 -102.32 REMARK 500 PRO B 48 43.00 -88.16 REMARK 500 THR B 106 30.97 87.20 REMARK 500 SER B 125 56.72 -110.94 REMARK 500 ASN C 51 -116.00 66.84 REMARK 500 PRO C 59 -178.85 -68.53 REMARK 500 PRO C 66 -169.86 -78.19 REMARK 500 ASP C 92 -157.15 -115.48 REMARK 500 ASP C 152 -127.93 57.80 REMARK 500 PRO C 165 123.66 -34.83 REMARK 500 SER C 188 -7.86 -56.78 REMARK 500 SER D 28 -166.93 -114.45 REMARK 500 SER D 82B 69.35 31.67 REMARK 500 PHE D 100J 144.49 -12.29 REMARK 500 ALA D 132 -166.09 -74.73 REMARK 500 PRO D 137 -171.06 -67.79 REMARK 500 SER D 138 83.86 -158.36 REMARK 500 ASP D 162 76.08 48.21 REMARK 500 PHE D 164 134.18 -176.40 REMARK 500 REMARK 500 THIS ENTRY HAS 119 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 LEU P 106A SER P 107 -32.04 REMARK 500 LEU M 106A SER M 107 -30.38 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 SER P 95 -12.29 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 SER J 221 23.8 L L OUTSIDE RANGE REMARK 500 PHE N 100G 22.0 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA E 503 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN E 504 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN E 505 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN E 506 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN E 507 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN E 508 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN E 509 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN E 510 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 511 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 512 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 513 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 514 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 515 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 516 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 517 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 518 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 519 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL Q 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL J 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL N 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG O 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG O 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA O 503 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN O 504 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN O 505 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN O 506 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN O 507 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN O 508 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN O 509 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN O 510 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG O 511 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG O 512 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG O 513 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG O 514 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG O 515 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG O 516 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG O 517 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL O 518 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 503 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 504 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 505 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 506 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 507 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 508 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 509 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 510 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 511 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 512 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 513 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 514 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 515 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 516 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 517 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 518 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 519 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 520 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 521 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG K 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG K 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA K 503 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN K 504 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN K 505 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN K 506 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN K 507 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN K 508 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN K 509 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN K 510 REMARK 800 REMARK 800 SITE_IDENTIFIER: IC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG K 511 REMARK 800 REMARK 800 SITE_IDENTIFIER: IC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG K 512 REMARK 800 REMARK 800 SITE_IDENTIFIER: IC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG K 513 REMARK 800 REMARK 800 SITE_IDENTIFIER: IC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG K 514 REMARK 800 REMARK 800 SITE_IDENTIFIER: IC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG K 515 REMARK 800 REMARK 800 SITE_IDENTIFIER: IC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL K 516 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4R26 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF PGT124 UNBOUND DBREF 4R2G E 199 302 UNP P20871 ENV_HV1JR 197 300 DBREF 4R2G E 320 492 UNP P20871 ENV_HV1JR 317 484 DBREF 4R2G F 1 183 UNP P01730 CD4_HUMAN 26 208 DBREF 4R2G P 108 213 UNP Q6GMW3 Q6GMW3_HUMAN 130 234 DBREF 4R2G Q 109 235 UNP Q6N096 Q6N096_HUMAN 132 240 DBREF 4R2G B 1 183 UNP P01730 CD4_HUMAN 26 208 DBREF 4R2G C 108 213 UNP Q6GMW3 Q6GMW3_HUMAN 130 234 DBREF 4R2G D 109 235 UNP Q6N096 Q6N096_HUMAN 132 240 DBREF 4R2G H 1 183 UNP P01730 CD4_HUMAN 26 208 DBREF 4R2G I 108 213 UNP Q6GMW3 Q6GMW3_HUMAN 130 234 DBREF 4R2G J 109 235 UNP Q6N096 Q6N096_HUMAN 132 240 DBREF 4R2G L 1 183 UNP P01730 CD4_HUMAN 26 208 DBREF 4R2G M 108 213 UNP Q6GMW3 Q6GMW3_HUMAN 130 234 DBREF 4R2G N 109 235 UNP Q6N096 Q6N096_HUMAN 132 240 DBREF 4R2G O 199 302 UNP P20871 ENV_HV1JR 197 300 DBREF 4R2G O 320 492 UNP P20871 ENV_HV1JR 317 484 DBREF 4R2G A 199 302 UNP P20871 ENV_HV1JR 197 300 DBREF 4R2G A 320 492 UNP P20871 ENV_HV1JR 317 484 DBREF 4R2G K 199 302 UNP P20871 ENV_HV1JR 197 300 DBREF 4R2G K 320 492 UNP P20871 ENV_HV1JR 317 484 DBREF 4R2G E 92 492 PDB 4R2G 4R2G 92 492 DBREF 4R2G O 92 492 PDB 4R2G 4R2G 92 492 DBREF 4R2G A 92 492 PDB 4R2G 4R2G 92 492 DBREF 4R2G K 92 492 PDB 4R2G 4R2G 92 492 DBREF 4R2G P 4 213 PDB 4R2G 4R2G 4 213 DBREF 4R2G C 4 213 PDB 4R2G 4R2G 4 213 DBREF 4R2G I 4 213 PDB 4R2G 4R2G 4 213 DBREF 4R2G M 4 213 PDB 4R2G 4R2G 4 213 DBREF 4R2G Q 1 235 PDB 4R2G 4R2G 1 235 DBREF 4R2G D 1 235 PDB 4R2G 4R2G 1 235 DBREF 4R2G J 1 235 PDB 4R2G 4R2G 1 235 DBREF 4R2G N 1 235 PDB 4R2G 4R2G 1 235 SEQADV 4R2G THR E 317 UNP P20871 LINKER SEQADV 4R2G ARG E 318 UNP P20871 LINKER SEQADV 4R2G PRO E 319 UNP P20871 LINKER SEQADV 4R2G MET F 0 UNP P01730 EXPRESSION TAG SEQADV 4R2G MET B 0 UNP P01730 EXPRESSION TAG SEQADV 4R2G MET H 0 UNP P01730 EXPRESSION TAG SEQADV 4R2G MET L 0 UNP P01730 EXPRESSION TAG SEQADV 4R2G THR O 317 UNP P20871 LINKER SEQADV 4R2G ARG O 318 UNP P20871 LINKER SEQADV 4R2G PRO O 319 UNP P20871 LINKER SEQADV 4R2G THR A 317 UNP P20871 LINKER SEQADV 4R2G ARG A 318 UNP P20871 LINKER SEQADV 4R2G PRO A 319 UNP P20871 LINKER SEQADV 4R2G THR K 317 UNP P20871 LINKER SEQADV 4R2G ARG K 318 UNP P20871 LINKER SEQADV 4R2G PRO K 319 UNP P20871 LINKER SEQRES 1 E 309 ASP PHE ASN MET TRP LYS ASN ASN MET VAL GLU GLN MET SEQRES 2 E 309 GLN GLU ASP VAL ILE ASN LEU TRP ASP GLN SER LEU LYS SEQRES 3 E 309 PRO CYS VAL LYS LEU THR GLY GLY SER VAL ILE THR GLN SEQRES 4 E 309 ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE HIS SEQRES 5 E 309 TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS ASN SEQRES 6 E 309 ASN LYS THR PHE ASN GLY LYS GLY GLN CYS LYS ASN VAL SEQRES 7 E 309 SER THR VAL GLN CYS THR HIS GLY ILE ARG PRO VAL VAL SEQRES 8 E 309 SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU GLU SEQRES 9 E 309 LYS VAL VAL ILE ARG SER ASP ASN PHE THR ASP ASN ALA SEQRES 10 E 309 LYS THR ILE ILE VAL GLN LEU ASN GLU SER VAL LYS ILE SEQRES 11 E 309 ASN CYS THR ARG PRO SER ASN ASN THR ARG PRO GLY GLU SEQRES 12 E 309 ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN ILE SER SEQRES 13 E 309 ARG ALA GLN TRP ASN ASN THR LEU LYS GLN ILE VAL GLU SEQRES 14 E 309 LYS LEU ARG GLU GLN PHE ASN ASN LYS THR ILE VAL PHE SEQRES 15 E 309 THR HIS SER SER GLY GLY ASP PRO GLU ILE VAL MET HIS SEQRES 16 E 309 SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN SER SEQRES 17 E 309 THR GLN LEU PHE ASN SER THR TRP ASN ASP THR GLU LYS SEQRES 18 E 309 SER SER GLY THR GLU GLY ASN ASP THR ILE ILE LEU PRO SEQRES 19 E 309 CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN GLU VAL SEQRES 20 E 309 GLY LYS ALA MET TYR ALA PRO PRO ILE LYS GLY GLN ILE SEQRES 21 E 309 ARG CYS SER SER ASN ILE THR GLY LEU LEU LEU THR ARG SEQRES 22 E 309 ASP GLY GLY LYS ASN GLU SER GLU ILE GLU ILE PHE ARG SEQRES 23 E 309 PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU SEQRES 24 E 309 LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU SEQRES 1 F 184 MET LYS LYS VAL VAL LEU GLY LYS LYS GLY ASP THR VAL SEQRES 2 F 184 GLU LEU THR CYS THR ALA SER GLN LYS LYS SER ILE GLN SEQRES 3 F 184 PHE HIS TRP LYS ASN SER ASN GLN ILE LYS ILE LEU GLY SEQRES 4 F 184 ASN GLN GLY SER PHE LEU THR LYS GLY PRO SER LYS LEU SEQRES 5 F 184 ASN ASP ARG ALA ASP SER ARG ARG SER LEU TRP ASP GLN SEQRES 6 F 184 GLY ASN PHE PRO LEU ILE ILE LYS ASN LEU LYS ILE GLU SEQRES 7 F 184 ASP SER ASP THR TYR ILE CYS GLU VAL GLU ASP GLN LYS SEQRES 8 F 184 GLU GLU VAL GLN LEU LEU VAL PHE GLY LEU THR ALA ASN SEQRES 9 F 184 SER ASP THR HIS LEU LEU GLN GLY GLN SER LEU THR LEU SEQRES 10 F 184 THR LEU GLU SER PRO PRO GLY SER SER PRO SER VAL GLN SEQRES 11 F 184 CYS ARG SER PRO ARG GLY LYS ASN ILE GLN GLY GLY LYS SEQRES 12 F 184 THR LEU SER VAL SER GLN LEU GLU LEU GLN ASP SER GLY SEQRES 13 F 184 THR TRP THR CYS THR VAL LEU GLN ASN GLN LYS LYS VAL SEQRES 14 F 184 GLU PHE LYS ILE ASP ILE VAL VAL LEU ALA PHE GLN LYS SEQRES 15 F 184 ALA SER SEQRES 1 P 214 SER TYR VAL SER PRO LEU SER VAL ALA LEU GLY GLU THR SEQRES 2 P 214 ALA ARG ILE SER CYS GLY ARG GLN ALA LEU GLY SER ARG SEQRES 3 P 214 ALA VAL GLN TRP TYR GLN HIS LYS PRO GLY GLN ALA PRO SEQRES 4 P 214 ILE LEU LEU ILE TYR ASN ASN GLN ASP ARG PRO SER GLY SEQRES 5 P 214 ILE PRO GLU ARG PHE SER GLY THR PRO ASP ILE ASN PHE SEQRES 6 P 214 GLY THR THR ALA THR LEU THR ILE SER GLY VAL GLU VAL SEQRES 7 P 214 GLY ASP GLU ALA ASP TYR TYR CYS HIS MET TRP ASP SER SEQRES 8 P 214 ARG SER GLY PHE SER TRP SER PHE GLY GLY ALA THR ARG SEQRES 9 P 214 LEU THR VAL LEU SER GLN PRO LYS ALA ALA PRO SER VAL SEQRES 10 P 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN SEQRES 11 P 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO SEQRES 12 P 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO SEQRES 13 P 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SEQRES 14 P 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU SEQRES 15 P 214 THR PRO GLU GLN TRP LYS SER HIS LYS SER TYR SER CYS SEQRES 16 P 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL SEQRES 17 P 214 ALA PRO THR GLU CYS SER SEQRES 1 Q 236 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL ARG SEQRES 2 Q 236 PRO SER GLU THR LEU SER VAL THR CYS ILE VAL SER GLY SEQRES 3 Q 236 GLY SER ILE SER ASN TYR TYR TRP THR TRP ILE ARG GLN SEQRES 4 Q 236 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SER SEQRES 5 Q 236 ASP ARG GLU THR THR THR TYR ASN PRO SER LEU ASN SER SEQRES 6 Q 236 ARG ALA VAL ILE SER ARG ASP THR SER LYS ASN GLN LEU SEQRES 7 Q 236 SER LEU GLN LEU ARG SER VAL THR THR ALA ASP THR ALA SEQRES 8 Q 236 ILE TYR PHE CYS ALA THR ALA ARG ARG GLY GLN ARG ILE SEQRES 9 Q 236 TYR GLY VAL VAL SER PHE GLY GLU PHE PHE TYR TYR TYR SEQRES 10 Q 236 TYR MET ASP VAL TRP GLY LYS GLY THR ALA VAL THR VAL SEQRES 11 Q 236 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 12 Q 236 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 13 Q 236 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 14 Q 236 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 15 Q 236 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 16 Q 236 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 17 Q 236 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 18 Q 236 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 19 Q 236 CYS ASP SEQRES 1 B 184 MET LYS LYS VAL VAL LEU GLY LYS LYS GLY ASP THR VAL SEQRES 2 B 184 GLU LEU THR CYS THR ALA SER GLN LYS LYS SER ILE GLN SEQRES 3 B 184 PHE HIS TRP LYS ASN SER ASN GLN ILE LYS ILE LEU GLY SEQRES 4 B 184 ASN GLN GLY SER PHE LEU THR LYS GLY PRO SER LYS LEU SEQRES 5 B 184 ASN ASP ARG ALA ASP SER ARG ARG SER LEU TRP ASP GLN SEQRES 6 B 184 GLY ASN PHE PRO LEU ILE ILE LYS ASN LEU LYS ILE GLU SEQRES 7 B 184 ASP SER ASP THR TYR ILE CYS GLU VAL GLU ASP GLN LYS SEQRES 8 B 184 GLU GLU VAL GLN LEU LEU VAL PHE GLY LEU THR ALA ASN SEQRES 9 B 184 SER ASP THR HIS LEU LEU GLN GLY GLN SER LEU THR LEU SEQRES 10 B 184 THR LEU GLU SER PRO PRO GLY SER SER PRO SER VAL GLN SEQRES 11 B 184 CYS ARG SER PRO ARG GLY LYS ASN ILE GLN GLY GLY LYS SEQRES 12 B 184 THR LEU SER VAL SER GLN LEU GLU LEU GLN ASP SER GLY SEQRES 13 B 184 THR TRP THR CYS THR VAL LEU GLN ASN GLN LYS LYS VAL SEQRES 14 B 184 GLU PHE LYS ILE ASP ILE VAL VAL LEU ALA PHE GLN LYS SEQRES 15 B 184 ALA 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 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 H 184 MET LYS LYS VAL VAL LEU GLY LYS LYS GLY ASP THR VAL SEQRES 2 H 184 GLU LEU THR CYS THR ALA SER GLN LYS LYS SER ILE GLN SEQRES 3 H 184 PHE HIS TRP LYS ASN SER ASN GLN ILE LYS ILE LEU GLY SEQRES 4 H 184 ASN GLN GLY SER PHE LEU THR LYS GLY PRO SER LYS LEU SEQRES 5 H 184 ASN ASP ARG ALA ASP SER ARG ARG SER LEU TRP ASP GLN SEQRES 6 H 184 GLY ASN PHE PRO LEU ILE ILE LYS ASN LEU LYS ILE GLU SEQRES 7 H 184 ASP SER ASP THR TYR ILE CYS GLU VAL GLU ASP GLN LYS SEQRES 8 H 184 GLU GLU VAL GLN LEU LEU VAL PHE GLY LEU THR ALA ASN SEQRES 9 H 184 SER ASP THR HIS LEU LEU GLN GLY GLN SER LEU THR LEU SEQRES 10 H 184 THR LEU GLU SER PRO PRO GLY SER SER PRO SER VAL GLN SEQRES 11 H 184 CYS ARG SER PRO ARG GLY LYS ASN ILE GLN GLY GLY LYS SEQRES 12 H 184 THR LEU SER VAL SER GLN LEU GLU LEU GLN ASP SER GLY SEQRES 13 H 184 THR TRP THR CYS THR VAL LEU GLN ASN GLN LYS LYS VAL SEQRES 14 H 184 GLU PHE LYS ILE ASP ILE VAL VAL LEU ALA PHE GLN LYS SEQRES 15 H 184 ALA SER SEQRES 1 I 214 SER TYR VAL SER PRO LEU SER VAL ALA LEU GLY GLU THR SEQRES 2 I 214 ALA ARG ILE SER CYS GLY ARG GLN ALA LEU GLY SER ARG SEQRES 3 I 214 ALA VAL GLN TRP TYR GLN HIS LYS PRO GLY GLN ALA PRO SEQRES 4 I 214 ILE LEU LEU ILE TYR ASN ASN GLN ASP ARG PRO SER GLY SEQRES 5 I 214 ILE PRO GLU ARG PHE SER GLY THR PRO ASP ILE ASN PHE SEQRES 6 I 214 GLY THR THR ALA THR LEU THR ILE SER GLY VAL GLU VAL SEQRES 7 I 214 GLY ASP GLU ALA ASP TYR TYR CYS HIS MET TRP ASP SER SEQRES 8 I 214 ARG SER GLY PHE SER TRP SER PHE GLY GLY ALA THR ARG SEQRES 9 I 214 LEU THR VAL LEU SER GLN PRO LYS ALA ALA PRO SER VAL SEQRES 10 I 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN SEQRES 11 I 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO SEQRES 12 I 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO SEQRES 13 I 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SEQRES 14 I 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU SEQRES 15 I 214 THR PRO GLU GLN TRP LYS SER HIS LYS SER TYR SER CYS SEQRES 16 I 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL SEQRES 17 I 214 ALA PRO THR GLU CYS SER SEQRES 1 J 236 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL ARG SEQRES 2 J 236 PRO SER GLU THR LEU SER VAL THR CYS ILE VAL SER GLY SEQRES 3 J 236 GLY SER ILE SER ASN TYR TYR TRP THR TRP ILE ARG GLN SEQRES 4 J 236 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SER SEQRES 5 J 236 ASP ARG GLU THR THR THR TYR ASN PRO SER LEU ASN SER SEQRES 6 J 236 ARG ALA VAL ILE SER ARG ASP THR SER LYS ASN GLN LEU SEQRES 7 J 236 SER LEU GLN LEU ARG SER VAL THR THR ALA ASP THR ALA SEQRES 8 J 236 ILE TYR PHE CYS ALA THR ALA ARG ARG GLY GLN ARG ILE SEQRES 9 J 236 TYR GLY VAL VAL SER PHE GLY GLU PHE PHE TYR TYR TYR SEQRES 10 J 236 TYR MET ASP VAL TRP GLY LYS GLY THR ALA VAL THR VAL SEQRES 11 J 236 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 12 J 236 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 13 J 236 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 14 J 236 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 15 J 236 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 16 J 236 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 17 J 236 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 18 J 236 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 19 J 236 CYS ASP SEQRES 1 L 184 MET LYS LYS VAL VAL LEU GLY LYS LYS GLY ASP THR VAL SEQRES 2 L 184 GLU LEU THR CYS THR ALA SER GLN LYS LYS SER ILE GLN SEQRES 3 L 184 PHE HIS TRP LYS ASN SER ASN GLN ILE LYS ILE LEU GLY SEQRES 4 L 184 ASN GLN GLY SER PHE LEU THR LYS GLY PRO SER LYS LEU SEQRES 5 L 184 ASN ASP ARG ALA ASP SER ARG ARG SER LEU TRP ASP GLN SEQRES 6 L 184 GLY ASN PHE PRO LEU ILE ILE LYS ASN LEU LYS ILE GLU SEQRES 7 L 184 ASP SER ASP THR TYR ILE CYS GLU VAL GLU ASP GLN LYS SEQRES 8 L 184 GLU GLU VAL GLN LEU LEU VAL PHE GLY LEU THR ALA ASN SEQRES 9 L 184 SER ASP THR HIS LEU LEU GLN GLY GLN SER LEU THR LEU SEQRES 10 L 184 THR LEU GLU SER PRO PRO GLY SER SER PRO SER VAL GLN SEQRES 11 L 184 CYS ARG SER PRO ARG GLY LYS ASN ILE GLN GLY GLY LYS SEQRES 12 L 184 THR LEU SER VAL SER GLN LEU GLU LEU GLN ASP SER GLY SEQRES 13 L 184 THR TRP THR CYS THR VAL LEU GLN ASN GLN LYS LYS VAL SEQRES 14 L 184 GLU PHE LYS ILE ASP ILE VAL VAL LEU ALA PHE GLN LYS SEQRES 15 L 184 ALA SER SEQRES 1 M 214 SER TYR VAL SER PRO LEU SER VAL ALA LEU GLY GLU THR SEQRES 2 M 214 ALA ARG ILE SER CYS GLY ARG GLN ALA LEU GLY SER ARG SEQRES 3 M 214 ALA VAL GLN TRP TYR GLN HIS LYS PRO GLY GLN ALA PRO SEQRES 4 M 214 ILE LEU LEU ILE TYR ASN ASN GLN ASP ARG PRO SER GLY SEQRES 5 M 214 ILE PRO GLU ARG PHE SER GLY THR PRO ASP ILE ASN PHE SEQRES 6 M 214 GLY THR THR ALA THR LEU THR ILE SER GLY VAL GLU VAL SEQRES 7 M 214 GLY ASP GLU ALA ASP TYR TYR CYS HIS MET TRP ASP SER SEQRES 8 M 214 ARG SER GLY PHE SER TRP SER PHE GLY GLY ALA THR ARG SEQRES 9 M 214 LEU THR VAL LEU SER GLN PRO LYS ALA ALA PRO SER VAL SEQRES 10 M 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN SEQRES 11 M 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO SEQRES 12 M 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO SEQRES 13 M 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SEQRES 14 M 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU SEQRES 15 M 214 THR PRO GLU GLN TRP LYS SER HIS LYS SER TYR SER CYS SEQRES 16 M 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL SEQRES 17 M 214 ALA PRO THR GLU CYS SER SEQRES 1 N 236 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL ARG SEQRES 2 N 236 PRO SER GLU THR LEU SER VAL THR CYS ILE VAL SER GLY SEQRES 3 N 236 GLY SER ILE SER ASN TYR TYR TRP THR TRP ILE ARG GLN SEQRES 4 N 236 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SER SEQRES 5 N 236 ASP ARG GLU THR THR THR TYR ASN PRO SER LEU ASN SER SEQRES 6 N 236 ARG ALA VAL ILE SER ARG ASP THR SER LYS ASN GLN LEU SEQRES 7 N 236 SER LEU GLN LEU ARG SER VAL THR THR ALA ASP THR ALA SEQRES 8 N 236 ILE TYR PHE CYS ALA THR ALA ARG ARG GLY GLN ARG ILE SEQRES 9 N 236 TYR GLY VAL VAL SER PHE GLY GLU PHE PHE TYR TYR TYR SEQRES 10 N 236 TYR MET ASP VAL TRP GLY LYS GLY THR ALA VAL THR VAL SEQRES 11 N 236 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 12 N 236 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 13 N 236 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 14 N 236 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 15 N 236 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 16 N 236 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 17 N 236 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 18 N 236 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 19 N 236 CYS ASP SEQRES 1 O 309 ASP PHE ASN MET TRP LYS ASN ASN MET VAL GLU GLN MET SEQRES 2 O 309 GLN GLU ASP VAL ILE ASN LEU TRP ASP GLN SER LEU LYS SEQRES 3 O 309 PRO CYS VAL LYS LEU THR GLY GLY SER VAL ILE THR GLN SEQRES 4 O 309 ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE HIS SEQRES 5 O 309 TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS ASN SEQRES 6 O 309 ASN LYS THR PHE ASN GLY LYS GLY GLN CYS LYS ASN VAL SEQRES 7 O 309 SER THR VAL GLN CYS THR HIS GLY ILE ARG PRO VAL VAL SEQRES 8 O 309 SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU GLU SEQRES 9 O 309 LYS VAL VAL ILE ARG SER ASP ASN PHE THR ASP ASN ALA SEQRES 10 O 309 LYS THR ILE ILE VAL GLN LEU ASN GLU SER VAL LYS ILE SEQRES 11 O 309 ASN CYS THR ARG PRO SER ASN ASN THR ARG PRO GLY GLU SEQRES 12 O 309 ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN ILE SER SEQRES 13 O 309 ARG ALA GLN TRP ASN ASN THR LEU LYS GLN ILE VAL GLU SEQRES 14 O 309 LYS LEU ARG GLU GLN PHE ASN ASN LYS THR ILE VAL PHE SEQRES 15 O 309 THR HIS SER SER GLY GLY ASP PRO GLU ILE VAL MET HIS SEQRES 16 O 309 SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN SER SEQRES 17 O 309 THR GLN LEU PHE ASN SER THR TRP ASN ASP THR GLU LYS SEQRES 18 O 309 SER SER GLY THR GLU GLY ASN ASP THR ILE ILE LEU PRO SEQRES 19 O 309 CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN GLU VAL SEQRES 20 O 309 GLY LYS ALA MET TYR ALA PRO PRO ILE LYS GLY GLN ILE SEQRES 21 O 309 ARG CYS SER SER ASN ILE THR GLY LEU LEU LEU THR ARG SEQRES 22 O 309 ASP GLY GLY LYS ASN GLU SER GLU ILE GLU ILE PHE ARG SEQRES 23 O 309 PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU SEQRES 24 O 309 LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU SEQRES 1 A 309 ASP PHE ASN MET TRP LYS ASN ASN MET VAL GLU GLN MET SEQRES 2 A 309 GLN GLU ASP VAL ILE ASN LEU TRP ASP GLN SER LEU LYS SEQRES 3 A 309 PRO CYS VAL LYS LEU THR GLY GLY SER VAL ILE THR GLN SEQRES 4 A 309 ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE HIS SEQRES 5 A 309 TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS ASN SEQRES 6 A 309 ASN LYS THR PHE ASN GLY LYS GLY GLN CYS LYS ASN VAL SEQRES 7 A 309 SER THR VAL GLN CYS THR HIS GLY ILE ARG PRO VAL VAL SEQRES 8 A 309 SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU GLU SEQRES 9 A 309 LYS VAL VAL ILE ARG SER ASP ASN PHE THR ASP ASN ALA SEQRES 10 A 309 LYS THR ILE ILE VAL GLN LEU ASN GLU SER VAL LYS ILE SEQRES 11 A 309 ASN CYS THR ARG PRO SER ASN ASN THR ARG PRO GLY GLU SEQRES 12 A 309 ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN ILE SER SEQRES 13 A 309 ARG ALA GLN TRP ASN ASN THR LEU LYS GLN ILE VAL GLU SEQRES 14 A 309 LYS LEU ARG GLU GLN PHE ASN ASN LYS THR ILE VAL PHE SEQRES 15 A 309 THR HIS SER SER GLY GLY ASP PRO GLU ILE VAL MET HIS SEQRES 16 A 309 SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN SER SEQRES 17 A 309 THR GLN LEU PHE ASN SER THR TRP ASN ASP THR GLU LYS SEQRES 18 A 309 SER SER GLY THR GLU GLY ASN ASP THR ILE ILE LEU PRO SEQRES 19 A 309 CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN GLU VAL SEQRES 20 A 309 GLY LYS ALA MET TYR ALA PRO PRO ILE LYS GLY GLN ILE SEQRES 21 A 309 ARG CYS SER SER ASN ILE THR GLY LEU LEU LEU THR ARG SEQRES 22 A 309 ASP GLY GLY LYS ASN GLU SER GLU ILE GLU ILE PHE ARG SEQRES 23 A 309 PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU SEQRES 24 A 309 LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU SEQRES 1 K 309 ASP PHE ASN MET TRP LYS ASN ASN MET VAL GLU GLN MET SEQRES 2 K 309 GLN GLU ASP VAL ILE ASN LEU TRP ASP GLN SER LEU LYS SEQRES 3 K 309 PRO CYS VAL LYS LEU THR GLY GLY SER VAL ILE THR GLN SEQRES 4 K 309 ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE HIS SEQRES 5 K 309 TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS ASN SEQRES 6 K 309 ASN LYS THR PHE ASN GLY LYS GLY GLN CYS LYS ASN VAL SEQRES 7 K 309 SER THR VAL GLN CYS THR HIS GLY ILE ARG PRO VAL VAL SEQRES 8 K 309 SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU GLU SEQRES 9 K 309 LYS VAL VAL ILE ARG SER ASP ASN PHE THR ASP ASN ALA SEQRES 10 K 309 LYS THR ILE ILE VAL GLN LEU ASN GLU SER VAL LYS ILE SEQRES 11 K 309 ASN CYS THR ARG PRO SER ASN ASN THR ARG PRO GLY GLU SEQRES 12 K 309 ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN ILE SER SEQRES 13 K 309 ARG ALA GLN TRP ASN ASN THR LEU LYS GLN ILE VAL GLU SEQRES 14 K 309 LYS LEU ARG GLU GLN PHE ASN ASN LYS THR ILE VAL PHE SEQRES 15 K 309 THR HIS SER SER GLY GLY ASP PRO GLU ILE VAL MET HIS SEQRES 16 K 309 SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN SER SEQRES 17 K 309 THR GLN LEU PHE ASN SER THR TRP ASN ASP THR GLU LYS SEQRES 18 K 309 SER SER GLY THR GLU GLY ASN ASP THR ILE ILE LEU PRO SEQRES 19 K 309 CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN GLU VAL SEQRES 20 K 309 GLY LYS ALA MET TYR ALA PRO PRO ILE LYS GLY GLN ILE SEQRES 21 K 309 ARG CYS SER SER ASN ILE THR GLY LEU LEU LEU THR ARG SEQRES 22 K 309 ASP GLY GLY LYS ASN GLU SER GLU ILE GLU ILE PHE ARG SEQRES 23 K 309 PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU SEQRES 24 K 309 LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU MODRES 4R2G ASN O 332 ASN GLYCOSYLATION SITE MODRES 4R2G ASN E 386 ASN GLYCOSYLATION SITE MODRES 4R2G ASN A 276 ASN GLYCOSYLATION SITE MODRES 4R2G ASN A 339 ASN GLYCOSYLATION SITE MODRES 4R2G ASN O 448 ASN GLYCOSYLATION SITE MODRES 4R2G ASN E 392 ASN GLYCOSYLATION SITE MODRES 4R2G ASN A 448 ASN GLYCOSYLATION SITE MODRES 4R2G ASN E 411 ASN GLYCOSYLATION SITE MODRES 4R2G ASN A 392 ASN GLYCOSYLATION SITE MODRES 4R2G ASN E 262 ASN GLYCOSYLATION SITE MODRES 4R2G ASN O 276 ASN GLYCOSYLATION SITE MODRES 4R2G ASN E 295 ASN GLYCOSYLATION SITE MODRES 4R2G ASN O 386 ASN GLYCOSYLATION SITE MODRES 4R2G ASN E 339 ASN GLYCOSYLATION SITE MODRES 4R2G ASN K 339 ASN GLYCOSYLATION SITE MODRES 4R2G ASN K 276 ASN GLYCOSYLATION SITE MODRES 4R2G ASN E 276 ASN GLYCOSYLATION SITE MODRES 4R2G ASN O 262 ASN GLYCOSYLATION SITE MODRES 4R2G ASN A 386 ASN GLYCOSYLATION SITE MODRES 4R2G ASN K 332 ASN GLYCOSYLATION SITE MODRES 4R2G ASN K 295 ASN GLYCOSYLATION SITE MODRES 4R2G ASN E 332 ASN GLYCOSYLATION SITE MODRES 4R2G ASN K 386 ASN GLYCOSYLATION SITE MODRES 4R2G ASN A 356 ASN GLYCOSYLATION SITE MODRES 4R2G ASN E 448 ASN GLYCOSYLATION SITE MODRES 4R2G ASN O 295 ASN GLYCOSYLATION SITE MODRES 4R2G ASN A 295 ASN GLYCOSYLATION SITE MODRES 4R2G ASN O 339 ASN GLYCOSYLATION SITE MODRES 4R2G ASN K 262 ASN GLYCOSYLATION SITE MODRES 4R2G ASN A 262 ASN GLYCOSYLATION SITE MODRES 4R2G ASN O 392 ASN GLYCOSYLATION SITE MODRES 4R2G ASN A 332 ASN GLYCOSYLATION SITE MODRES 4R2G THR K 404 THR GLYCOSYLATION SITE HET NAG E 501 14 HET NAG E 502 14 HET BMA E 503 11 HET MAN E 504 11 HET MAN E 505 11 HET MAN E 506 11 HET MAN E 507 11 HET MAN E 508 11 HET MAN E 509 11 HET MAN E 510 11 HET NAG E 511 14 HET NAG E 512 14 HET NAG E 513 14 HET NAG E 514 14 HET NAG E 515 14 HET NAG E 516 14 HET NAG E 517 14 HET NAG E 518 14 HET CL E 519 1 HET GOL Q 301 6 HET GOL D 301 6 HET GOL J 301 6 HET GOL N 301 6 HET NAG O 501 14 HET NAG O 502 14 HET BMA O 503 11 HET MAN O 504 11 HET MAN O 505 11 HET MAN O 506 11 HET MAN O 507 11 HET MAN O 508 11 HET MAN O 509 11 HET MAN O 510 11 HET NAG O 511 14 HET NAG O 512 14 HET NAG O 513 14 HET NAG O 514 14 HET NAG O 515 14 HET NAG O 516 14 HET NAG O 517 14 HET CL O 518 1 HET NAG A 501 14 HET NAG A 502 14 HET BMA A 503 11 HET MAN A 504 11 HET MAN A 505 11 HET MAN A 506 11 HET MAN A 507 11 HET MAN A 508 11 HET MAN A 509 11 HET MAN A 510 11 HET NAG A 511 14 HET NAG A 512 14 HET NAG A 513 14 HET NAG A 514 14 HET NAG A 515 14 HET NAG A 516 14 HET NAG A 517 14 HET NAG A 518 14 HET NAG A 519 14 HET NAG A 520 14 HET CL A 521 1 HET NAG K 501 14 HET NAG K 502 14 HET BMA K 503 11 HET MAN K 504 11 HET MAN K 505 11 HET MAN K 506 11 HET MAN K 507 11 HET MAN K 508 11 HET MAN K 509 11 HET MAN K 510 11 HET NAG K 511 14 HET NAG K 512 14 HET NAG K 513 14 HET NAG K 514 14 HET NAG K 515 14 HET CL K 516 1 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE HETNAM CL CHLORIDE ION HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 17 NAG 38(C8 H15 N O6) FORMUL 17 BMA 4(C6 H12 O6) FORMUL 17 MAN 28(C6 H12 O6) FORMUL 26 CL 4(CL 1-) FORMUL 27 GOL 4(C3 H8 O3) HELIX 1 1 ASN E 94 ASN E 98 5 5 HELIX 2 2 ASN E 99 LEU E 116 1 18 HELIX 3 3 ARG E 335 PHE E 353 1 19 HELIX 4 4 ASP E 368 MET E 373 1 6 HELIX 5 5 SER E 387 PHE E 391 5 5 HELIX 6 6 ASP E 474 TYR E 484 1 11 HELIX 7 7 ARG F 58 GLY F 65 5 8 HELIX 8 8 LYS F 75 SER F 79 5 5 HELIX 9 9 GLU P 79 GLU P 83 5 5 HELIX 10 10 SER P 122 ALA P 128 1 7 HELIX 11 11 THR P 182 SER P 188 1 7 HELIX 12 12 SER Q 28 TYR Q 32 5 5 HELIX 13 13 PRO Q 61 ASN Q 64 5 4 HELIX 14 14 THR Q 83 THR Q 87 5 5 HELIX 15 15 VAL Q 100D GLY Q 100H 5 5 HELIX 16 16 SER Q 205 LEU Q 207 5 3 HELIX 17 17 SER B 49 ASP B 53 5 5 HELIX 18 18 ARG B 58 GLY B 65 5 8 HELIX 19 19 GLU B 150 SER B 154 5 5 HELIX 20 20 GLU C 79 GLU C 83 5 5 HELIX 21 21 SER C 122 ALA C 128 1 7 HELIX 22 22 THR C 182 HIS C 189 1 8 HELIX 23 23 PRO D 61 ASN D 64 5 4 HELIX 24 24 THR D 83 THR D 87 5 5 HELIX 25 25 ARG H 58 ASP H 63 1 6 HELIX 26 26 LYS H 75 SER H 79 5 5 HELIX 27 27 GLU I 79 GLU I 83 5 5 HELIX 28 28 SER I 122 ALA I 128 1 7 HELIX 29 29 THR I 182 SER I 188 1 7 HELIX 30 30 SER J 28 TYR J 32 5 5 HELIX 31 31 PRO J 61 ASN J 64 5 4 HELIX 32 32 VAL J 100D GLY J 100H 5 5 HELIX 33 33 SER J 205 LEU J 207 5 3 HELIX 34 34 ARG L 58 GLY L 65 5 8 HELIX 35 35 LYS L 75 SER L 79 5 5 HELIX 36 36 GLU L 150 SER L 154 5 5 HELIX 37 37 GLU M 79 GLU M 83 5 5 HELIX 38 38 SER M 122 GLN M 127 1 6 HELIX 39 39 THR M 182 SER M 188 1 7 HELIX 40 40 PRO N 61 ASN N 64 5 4 HELIX 41 41 THR N 83 THR N 87 5 5 HELIX 42 42 SER N 174 LEU N 177 5 4 HELIX 43 43 ASN O 99 LEU O 116 1 18 HELIX 44 44 ARG O 335 PHE O 353 1 19 HELIX 45 45 ASP O 368 MET O 373 1 6 HELIX 46 46 ASP O 474 TYR O 484 1 11 HELIX 47 47 TRP A 96 ASN A 98 5 3 HELIX 48 48 ASN A 99 LEU A 116 1 18 HELIX 49 49 ARG A 335 PHE A 353 1 19 HELIX 50 50 ASP A 368 MET A 373 1 6 HELIX 51 51 ASP A 474 TYR A 484 1 11 HELIX 52 52 MET K 100 LEU K 116 1 17 HELIX 53 53 ARG K 335 PHE K 353 1 19 HELIX 54 54 ASP K 368 MET K 373 1 6 HELIX 55 55 ASP K 474 TYR K 484 1 11 SHEET 1 A 3 VAL E 120 LEU E 122 0 SHEET 2 A 3 LYS E 432 MET E 434 -1 O LYS E 432 N LEU E 122 SHEET 3 A 3 ILE E 423 ASN E 425 -1 N ILE E 424 O ALA E 433 SHEET 1 B 3 VAL E 242 VAL E 245 0 SHEET 2 B 3 PHE E 223 CYS E 228 -1 N LYS E 227 O SER E 243 SHEET 3 B 3 LYS E 487 LYS E 490 -1 O LYS E 487 N LEU E 226 SHEET 1 C 7 LEU E 259 LEU E 261 0 SHEET 2 C 7 ILE E 443 ARG E 456 -1 O GLY E 451 N LEU E 260 SHEET 3 C 7 ILE E 284 ARG E 298 -1 N ILE E 294 O SER E 447 SHEET 4 C 7 HIS E 330 SER E 334 -1 O ASN E 332 N ASN E 295 SHEET 5 C 7 THR E 413 LYS E 421 -1 O LEU E 416 N CYS E 331 SHEET 6 C 7 GLU E 381 CYS E 385 -1 N TYR E 384 O ARG E 419 SHEET 7 C 7 HIS E 374 CYS E 378 -1 N HIS E 374 O CYS E 385 SHEET 1 D 7 VAL E 271 ARG E 273 0 SHEET 2 D 7 ILE E 284 ARG E 298 -1 O GLN E 287 N VAL E 271 SHEET 3 D 7 ILE E 443 ARG E 456 -1 O SER E 447 N ILE E 294 SHEET 4 D 7 ILE E 465 PRO E 470 -1 O ARG E 469 N THR E 455 SHEET 5 D 7 THR E 358 PHE E 361 1 N VAL E 360 O PHE E 468 SHEET 6 D 7 SER E 393 TRP E 395 -1 O TRP E 395 N ILE E 359 SHEET 7 D 7 SER E 401 SER E 402 -1 O SER E 402 N THR E 394 SHEET 1 E 6 LYS F 2 LYS F 7 0 SHEET 2 E 6 LYS F 90 THR F 101 1 O LEU F 96 N VAL F 4 SHEET 3 E 6 ASP F 80 VAL F 86 -1 N ASP F 80 O LEU F 95 SHEET 4 E 6 PHE F 26 ASN F 30 -1 N LYS F 29 O ILE F 83 SHEET 5 E 6 LYS F 35 GLN F 40 -1 O LEU F 37 N TRP F 28 SHEET 6 E 6 PHE F 43 LYS F 46 -1 O THR F 45 N GLY F 38 SHEET 1 F 4 LYS F 2 LYS F 7 0 SHEET 2 F 4 LYS F 90 THR F 101 1 O LEU F 96 N VAL F 4 SHEET 3 F 4 THR F 115 GLU F 119 -1 O THR F 117 N THR F 101 SHEET 4 F 4 THR F 143 SER F 145 -1 O LEU F 144 N LEU F 116 SHEET 1 G 3 VAL F 12 LEU F 14 0 SHEET 2 G 3 LEU F 69 ILE F 71 -1 O LEU F 69 N LEU F 14 SHEET 3 G 3 ALA F 55 ASP F 56 -1 N ASP F 56 O ILE F 70 SHEET 1 H 4 ASN F 137 GLY F 140 0 SHEET 2 H 4 SER F 127 ARG F 131 -1 N CYS F 130 O ILE F 138 SHEET 3 H 4 GLY F 155 GLN F 163 -1 O THR F 160 N GLN F 129 SHEET 4 H 4 LYS F 166 ILE F 174 -1 O ILE F 174 N GLY F 155 SHEET 1 I 5 PRO P 8 ALA P 14 0 SHEET 2 I 5 ALA P 101 LEU P 106A 1 O LEU P 106A N VAL P 13 SHEET 3 I 5 ASP P 85 HIS P 89 -1 N TYR P 86 O THR P 102 SHEET 4 I 5 GLN P 34 HIS P 38 -1 N GLN P 34 O HIS P 89 SHEET 5 I 5 ILE P 45 ILE P 48 -1 O ILE P 45 N GLN P 37 SHEET 1 J 3 ALA P 19 SER P 22 0 SHEET 2 J 3 THR P 72 ILE P 75 -1 O ILE P 75 N ALA P 19 SHEET 3 J 3 PHE P 62 SER P 63 -1 N SER P 63 O THR P 74 SHEET 1 K 3 ALA P 131 PHE P 140 0 SHEET 2 K 3 TYR P 173 LEU P 181 -1 O LEU P 181 N ALA P 131 SHEET 3 K 3 VAL P 160 THR P 162 -1 N GLU P 161 O TYR P 178 SHEET 1 L 3 ALA P 131 PHE P 140 0 SHEET 2 L 3 TYR P 173 LEU P 181 -1 O LEU P 181 N ALA P 131 SHEET 3 L 3 SER P 166 LYS P 167 -1 N SER P 166 O ALA P 174 SHEET 1 M 3 THR P 146 TRP P 149 0 SHEET 2 M 3 TYR P 192 THR P 197 -1 O GLN P 195 N ALA P 148 SHEET 3 M 3 THR P 202 VAL P 207 -1 O VAL P 203 N VAL P 196 SHEET 1 N 4 GLN Q 3 SER Q 7 0 SHEET 2 N 4 LEU Q 18 SER Q 25 -1 O THR Q 21 N SER Q 7 SHEET 3 N 4 GLN Q 77 LEU Q 82 -1 O LEU Q 80 N VAL Q 20 SHEET 4 N 4 ALA Q 67 ASP Q 72 -1 N ASP Q 72 O GLN Q 77 SHEET 1 O 6 LEU Q 11 VAL Q 12 0 SHEET 2 O 6 THR Q 107 VAL Q 111 1 O THR Q 110 N VAL Q 12 SHEET 3 O 6 ALA Q 88 ILE Q 100A-1 N TYR Q 90 O THR Q 107 SHEET 4 O 6 TYR Q 33 GLN Q 39 -1 N ILE Q 37 O PHE Q 91 SHEET 5 O 6 LEU Q 45 ILE Q 51 -1 O ILE Q 51 N TRP Q 34 SHEET 6 O 6 THR Q 57 TYR Q 59 -1 O THR Q 58 N TYR Q 50 SHEET 1 P 4 LEU Q 11 VAL Q 12 0 SHEET 2 P 4 THR Q 107 VAL Q 111 1 O THR Q 110 N VAL Q 12 SHEET 3 P 4 ALA Q 88 ILE Q 100A-1 N TYR Q 90 O THR Q 107 SHEET 4 P 4 PHE Q 100J TYR Q 100O-1 O PHE Q 100K N ARG Q 100 SHEET 1 Q 4 SER Q 138 LEU Q 142 0 SHEET 2 Q 4 THR Q 153 TYR Q 163 -1 O GLY Q 157 N LEU Q 142 SHEET 3 Q 4 TYR Q 194 PRO Q 203 -1 O VAL Q 202 N ALA Q 154 SHEET 4 Q 4 VAL Q 181 THR Q 183 -1 N HIS Q 182 O VAL Q 199 SHEET 1 R 4 SER Q 138 LEU Q 142 0 SHEET 2 R 4 THR Q 153 TYR Q 163 -1 O GLY Q 157 N LEU Q 142 SHEET 3 R 4 TYR Q 194 PRO Q 203 -1 O VAL Q 202 N ALA Q 154 SHEET 4 R 4 VAL Q 187 LEU Q 188 -1 N VAL Q 187 O SER Q 195 SHEET 1 S 3 THR Q 169 TRP Q 172 0 SHEET 2 S 3 TYR Q 212 HIS Q 218 -1 O ASN Q 217 N THR Q 169 SHEET 3 S 3 THR Q 223 VAL Q 229 -1 O VAL Q 225 N VAL Q 216 SHEET 1 T 6 LYS B 2 LYS B 7 0 SHEET 2 T 6 LYS B 90 THR B 101 1 O GLN B 94 N LYS B 2 SHEET 3 T 6 ASP B 80 VAL B 86 -1 N ASP B 80 O LEU B 95 SHEET 4 T 6 PHE B 26 LYS B 29 -1 N LYS B 29 O ILE B 83 SHEET 5 T 6 LYS B 35 GLN B 40 -1 O LEU B 37 N TRP B 28 SHEET 6 T 6 PHE B 43 LYS B 46 -1 O THR B 45 N GLY B 38 SHEET 1 U 4 LYS B 2 LYS B 7 0 SHEET 2 U 4 LYS B 90 THR B 101 1 O GLN B 94 N LYS B 2 SHEET 3 U 4 LEU B 114 GLU B 119 -1 O THR B 117 N THR B 101 SHEET 4 U 4 THR B 143 VAL B 146 -1 O LEU B 144 N LEU B 116 SHEET 1 V 3 VAL B 12 LEU B 14 0 SHEET 2 V 3 LEU B 69 ILE B 71 -1 O LEU B 69 N LEU B 14 SHEET 3 V 3 ALA B 55 ASP B 56 -1 N ASP B 56 O ILE B 70 SHEET 1 W 4 ASN B 137 GLY B 140 0 SHEET 2 W 4 SER B 127 ARG B 131 -1 N CYS B 130 O ILE B 138 SHEET 3 W 4 GLY B 155 GLN B 163 -1 O THR B 160 N GLN B 129 SHEET 4 W 4 LYS B 166 ILE B 174 -1 O ILE B 174 N GLY B 155 SHEET 1 X 5 SER C 7 ALA C 14 0 SHEET 2 X 5 ALA C 101 LEU C 106A 1 O ARG C 103 N SER C 7 SHEET 3 X 5 ALA C 84 TRP C 91 -1 N ALA C 84 O LEU C 104 SHEET 4 X 5 ALA C 32 HIS C 38 -1 N ALA C 32 O TRP C 91 SHEET 5 X 5 ILE C 45 ILE C 48 -1 O ILE C 45 N GLN C 37 SHEET 1 Y 3 ALA C 19 SER C 22 0 SHEET 2 Y 3 THR C 72 ILE C 75 -1 O LEU C 73 N ILE C 21 SHEET 3 Y 3 PHE C 62 SER C 63 -1 N SER C 63 O THR C 74 SHEET 1 Z 4 THR C 117 PHE C 119 0 SHEET 2 Z 4 ALA C 131 PHE C 140 -1 O LEU C 136 N THR C 117 SHEET 3 Z 4 TYR C 173 LEU C 181 -1 O TYR C 173 N PHE C 140 SHEET 4 Z 4 VAL C 160 THR C 162 -1 N GLU C 161 O TYR C 178 SHEET 1 AA 4 SER C 154 PRO C 155 0 SHEET 2 AA 4 THR C 146 ALA C 151 -1 N ALA C 151 O SER C 154 SHEET 3 AA 4 TYR C 192 HIS C 198 -1 O GLN C 195 N ALA C 148 SHEET 4 AA 4 SER C 201 VAL C 207 -1 O LYS C 205 N CYS C 194 SHEET 1 AB 4 LEU D 4 SER D 7 0 SHEET 2 AB 4 LEU D 18 VAL D 24 -1 O THR D 21 N SER D 7 SHEET 3 AB 4 GLN D 77 LEU D 82 -1 O LEU D 80 N VAL D 20 SHEET 4 AB 4 ALA D 67 ASP D 72 -1 N SER D 70 O SER D 79 SHEET 1 AC 6 LEU D 11 VAL D 12 0 SHEET 2 AC 6 THR D 107 VAL D 111 1 O THR D 110 N VAL D 12 SHEET 3 AC 6 ALA D 88 ARG D 100 -1 N TYR D 90 O THR D 107 SHEET 4 AC 6 TYR D 33 GLN D 39 -1 N ILE D 37 O PHE D 91 SHEET 5 AC 6 LEU D 45 ILE D 51 -1 O ILE D 51 N TRP D 34 SHEET 6 AC 6 THR D 57 TYR D 59 -1 O THR D 58 N TYR D 50 SHEET 1 AD 4 LEU D 11 VAL D 12 0 SHEET 2 AD 4 THR D 107 VAL D 111 1 O THR D 110 N VAL D 12 SHEET 3 AD 4 ALA D 88 ARG D 100 -1 N TYR D 90 O THR D 107 SHEET 4 AD 4 PHE D 100K TRP D 103 -1 O PHE D 100K N ARG D 100 SHEET 1 AE 4 VAL D 139 LEU D 142 0 SHEET 2 AE 4 THR D 153 TYR D 163 -1 O LEU D 159 N PHE D 140 SHEET 3 AE 4 TYR D 194 PRO D 203 -1 O TYR D 194 N TYR D 163 SHEET 4 AE 4 VAL D 181 THR D 183 -1 N HIS D 182 O VAL D 199 SHEET 1 AF 3 THR D 169 TRP D 172 0 SHEET 2 AF 3 ILE D 213 ASN D 217 -1 O ASN D 217 N THR D 169 SHEET 3 AF 3 LYS D 227 LYS D 228 -1 O LYS D 227 N CYS D 214 SHEET 1 AG 6 VAL H 3 LYS H 7 0 SHEET 2 AG 6 LYS H 90 ALA H 102 1 O LEU H 96 N GLY H 6 SHEET 3 AG 6 ASP H 80 GLU H 85 -1 N TYR H 82 O VAL H 93 SHEET 4 AG 6 HIS H 27 LYS H 29 -1 N LYS H 29 O ILE H 83 SHEET 5 AG 6 LYS H 35 GLN H 40 -1 O ILE H 36 N TRP H 28 SHEET 6 AG 6 PHE H 43 LYS H 46 -1 O THR H 45 N GLY H 38 SHEET 1 AH 3 VAL H 3 LYS H 7 0 SHEET 2 AH 3 LYS H 90 ALA H 102 1 O LEU H 96 N GLY H 6 SHEET 3 AH 3 LEU H 116 GLU H 119 -1 O THR H 117 N THR H 101 SHEET 1 AI 3 VAL H 12 LEU H 14 0 SHEET 2 AI 3 LEU H 69 ILE H 71 -1 O ILE H 71 N VAL H 12 SHEET 3 AI 3 ALA H 55 ASP H 56 -1 N ASP H 56 O ILE H 70 SHEET 1 AJ 4 ASN H 137 GLY H 140 0 SHEET 2 AJ 4 SER H 127 ARG H 131 -1 N CYS H 130 O ILE H 138 SHEET 3 AJ 4 THR H 156 GLN H 163 -1 O THR H 158 N ARG H 131 SHEET 4 AJ 4 LYS H 166 ASP H 173 -1 O ILE H 172 N TRP H 157 SHEET 1 AK 5 SER I 7 ALA I 14 0 SHEET 2 AK 5 ALA I 101 LEU I 106A 1 O ALA I 101 N SER I 7 SHEET 3 AK 5 ALA I 84 ASP I 92 -1 N ALA I 84 O LEU I 104 SHEET 4 AK 5 ARG I 31 HIS I 38 -1 N TYR I 36 O TYR I 87 SHEET 5 AK 5 ILE I 45 ILE I 48 -1 O ILE I 45 N GLN I 37 SHEET 1 AL 3 ALA I 19 SER I 22 0 SHEET 2 AL 3 THR I 72 ILE I 75 -1 O ILE I 75 N ALA I 19 SHEET 3 AL 3 PHE I 62 SER I 63 -1 N SER I 63 O THR I 74 SHEET 1 AM 4 SER I 115 PHE I 119 0 SHEET 2 AM 4 ALA I 131 PHE I 140 -1 O SER I 138 N SER I 115 SHEET 3 AM 4 TYR I 173 LEU I 181 -1 O LEU I 179 N LEU I 133 SHEET 4 AM 4 VAL I 160 THR I 162 -1 N GLU I 161 O TYR I 178 SHEET 1 AN 4 SER I 154 PRO I 155 0 SHEET 2 AN 4 THR I 146 ALA I 151 -1 N ALA I 151 O SER I 154 SHEET 3 AN 4 TYR I 192 THR I 197 -1 O THR I 197 N THR I 146 SHEET 4 AN 4 THR I 202 VAL I 207 -1 O VAL I 203 N VAL I 196 SHEET 1 AO 4 LEU J 4 SER J 7 0 SHEET 2 AO 4 LEU J 18 VAL J 24 -1 O ILE J 23 N GLN J 5 SHEET 3 AO 4 GLN J 77 LEU J 82 -1 O LEU J 80 N VAL J 20 SHEET 4 AO 4 ALA J 67 ASP J 72 -1 N SER J 70 O SER J 79 SHEET 1 AP 6 LEU J 11 VAL J 12 0 SHEET 2 AP 6 THR J 107 VAL J 111 1 O THR J 110 N VAL J 12 SHEET 3 AP 6 ALA J 88 THR J 94 -1 N TYR J 90 O THR J 107 SHEET 4 AP 6 TRP J 34 GLN J 39 -1 N ILE J 37 O PHE J 91 SHEET 5 AP 6 LEU J 45 ILE J 51 -1 O GLU J 46 N ARG J 38 SHEET 6 AP 6 THR J 57 TYR J 59 -1 O THR J 58 N TYR J 50 SHEET 1 AQ 2 ARG J 96 ILE J 100A 0 SHEET 2 AQ 2 PHE J 100J TYR J 100O-1 O TYR J 100O N ARG J 96 SHEET 1 AR 4 SER J 138 LEU J 142 0 SHEET 2 AR 4 THR J 153 LYS J 161 -1 O GLY J 157 N LEU J 142 SHEET 3 AR 4 SER J 197 PRO J 203 -1 O VAL J 202 N ALA J 154 SHEET 4 AR 4 HIS J 182 THR J 183 -1 N HIS J 182 O VAL J 199 SHEET 1 AS 3 THR J 169 TRP J 172 0 SHEET 2 AS 3 TYR J 212 HIS J 218 -1 O ASN J 215 N SER J 171 SHEET 3 AS 3 THR J 223 VAL J 229 -1 O VAL J 225 N VAL J 216 SHEET 1 AT 6 VAL L 4 LYS L 7 0 SHEET 2 AT 6 LYS L 90 PHE L 98 1 O LEU L 96 N GLY L 6 SHEET 3 AT 6 ASP L 80 VAL L 86 -1 N CYS L 84 O GLU L 91 SHEET 4 AT 6 PHE L 26 LYS L 29 -1 N HIS L 27 O GLU L 85 SHEET 5 AT 6 LYS L 35 GLN L 40 -1 O LEU L 37 N TRP L 28 SHEET 6 AT 6 PHE L 43 LYS L 46 -1 O THR L 45 N GLY L 38 SHEET 1 AU 3 VAL L 12 LEU L 14 0 SHEET 2 AU 3 LEU L 69 ILE L 71 -1 O LEU L 69 N LEU L 14 SHEET 3 AU 3 ALA L 55 ASP L 56 -1 N ASP L 56 O ILE L 70 SHEET 1 AV 2 LEU L 114 THR L 117 0 SHEET 2 AV 2 THR L 143 VAL L 146 -1 O VAL L 146 N LEU L 114 SHEET 1 AW 4 ASN L 137 GLY L 141 0 SHEET 2 AW 4 SER L 127 ARG L 131 -1 N CYS L 130 O ILE L 138 SHEET 3 AW 4 GLY L 155 GLN L 163 -1 O THR L 160 N GLN L 129 SHEET 4 AW 4 LYS L 166 ILE L 174 -1 O PHE L 170 N CYS L 159 SHEET 1 AX 5 VAL M 6 ALA M 14 0 SHEET 2 AX 5 ALA M 101 LEU M 106A 1 O ALA M 101 N SER M 7 SHEET 3 AX 5 ASP M 85 ASP M 92 -1 N TYR M 86 O THR M 102 SHEET 4 AX 5 ARG M 31 HIS M 38 -1 N TYR M 36 O TYR M 87 SHEET 5 AX 5 ILE M 45 ILE M 48 -1 O ILE M 48 N TRP M 35 SHEET 1 AY 3 ALA M 19 SER M 22 0 SHEET 2 AY 3 THR M 72 ILE M 75 -1 O ILE M 75 N ALA M 19 SHEET 3 AY 3 PHE M 62 SER M 63 -1 N SER M 63 O THR M 74 SHEET 1 AZ 4 SER M 115 PHE M 119 0 SHEET 2 AZ 4 ALA M 131 PHE M 140 -1 O LEU M 136 N THR M 117 SHEET 3 AZ 4 TYR M 173 LEU M 181 -1 O TYR M 173 N PHE M 140 SHEET 4 AZ 4 VAL M 160 THR M 162 -1 N GLU M 161 O TYR M 178 SHEET 1 BA 4 SER M 115 PHE M 119 0 SHEET 2 BA 4 ALA M 131 PHE M 140 -1 O LEU M 136 N THR M 117 SHEET 3 BA 4 TYR M 173 LEU M 181 -1 O TYR M 173 N PHE M 140 SHEET 4 BA 4 SER M 166 LYS M 167 -1 N SER M 166 O ALA M 174 SHEET 1 BB 4 SER M 154 PRO M 155 0 SHEET 2 BB 4 THR M 146 ALA M 151 -1 N ALA M 151 O SER M 154 SHEET 3 BB 4 TYR M 192 HIS M 198 -1 O GLN M 195 N ALA M 148 SHEET 4 BB 4 SER M 201 VAL M 207 -1 O VAL M 203 N VAL M 196 SHEET 1 BC 4 GLN N 3 SER N 7 0 SHEET 2 BC 4 LEU N 18 SER N 25 -1 O SER N 25 N GLN N 3 SHEET 3 BC 4 GLN N 77 LEU N 82 -1 O LEU N 78 N CYS N 22 SHEET 4 BC 4 ALA N 67 ASP N 72 -1 N ASP N 72 O GLN N 77 SHEET 1 BD 6 LEU N 11 VAL N 12 0 SHEET 2 BD 6 THR N 107 VAL N 111 1 O THR N 110 N VAL N 12 SHEET 3 BD 6 ALA N 88 ILE N 100A-1 N TYR N 90 O THR N 107 SHEET 4 BD 6 TRP N 34 GLN N 39 -1 N ILE N 37 O PHE N 91 SHEET 5 BD 6 LEU N 45 ILE N 51 -1 O GLU N 46 N ARG N 38 SHEET 6 BD 6 THR N 57 TYR N 59 -1 O THR N 58 N TYR N 50 SHEET 1 BE 4 LEU N 11 VAL N 12 0 SHEET 2 BE 4 THR N 107 VAL N 111 1 O THR N 110 N VAL N 12 SHEET 3 BE 4 ALA N 88 ILE N 100A-1 N TYR N 90 O THR N 107 SHEET 4 BE 4 PHE N 100J TRP N 103 -1 O PHE N 100K N ARG N 100 SHEET 1 BF 4 SER N 138 LEU N 142 0 SHEET 2 BF 4 THR N 153 TYR N 163 -1 O GLY N 157 N LEU N 142 SHEET 3 BF 4 TYR N 194 PRO N 203 -1 O LEU N 196 N VAL N 160 SHEET 4 BF 4 VAL N 181 THR N 183 -1 N HIS N 182 O VAL N 199 SHEET 1 BG 4 SER N 138 LEU N 142 0 SHEET 2 BG 4 THR N 153 TYR N 163 -1 O GLY N 157 N LEU N 142 SHEET 3 BG 4 TYR N 194 PRO N 203 -1 O LEU N 196 N VAL N 160 SHEET 4 BG 4 VAL N 187 LEU N 188 -1 N VAL N 187 O SER N 195 SHEET 1 BH 3 THR N 169 TRP N 172 0 SHEET 2 BH 3 ILE N 213 HIS N 218 -1 O ASN N 215 N SER N 171 SHEET 3 BH 3 THR N 223 LYS N 228 -1 O THR N 223 N HIS N 218 SHEET 1 BI 4 SER O 199 THR O 202 0 SHEET 2 BI 4 VAL O 120 THR O 123 -1 N LYS O 121 O ILE O 201 SHEET 3 BI 4 LYS O 432 MET O 434 -1 O LYS O 432 N LEU O 122 SHEET 4 BI 4 ILE O 423 ASN O 425 -1 N ILE O 424 O ALA O 433 SHEET 1 BJ 3 VAL O 242 VAL O 245 0 SHEET 2 BJ 3 PHE O 223 CYS O 228 -1 N LYS O 227 O SER O 243 SHEET 3 BJ 3 TYR O 486 LYS O 490 -1 O VAL O 489 N ALA O 224 SHEET 1 BK 7 LEU O 259 LEU O 261 0 SHEET 2 BK 7 ILE O 443 ARG O 456 -1 O THR O 450 N LEU O 260 SHEET 3 BK 7 ILE O 284 ARG O 298 -1 N ILE O 294 O SER O 447 SHEET 4 BK 7 HIS O 330 SER O 334 -1 O ASN O 332 N ASN O 295 SHEET 5 BK 7 THR O 413 LYS O 421 -1 O ILE O 414 N ILE O 333 SHEET 6 BK 7 GLU O 381 CYS O 385 -1 N TYR O 384 O ARG O 419 SHEET 7 BK 7 HIS O 374 CYS O 378 -1 N HIS O 374 O CYS O 385 SHEET 1 BL 7 VAL O 271 ARG O 273 0 SHEET 2 BL 7 ILE O 284 ARG O 298 -1 O ILE O 285 N ARG O 273 SHEET 3 BL 7 ILE O 443 ARG O 456 -1 O SER O 447 N ILE O 294 SHEET 4 BL 7 ILE O 465 PRO O 470 -1 O ARG O 469 N THR O 455 SHEET 5 BL 7 THR O 358 PHE O 361 1 N VAL O 360 O PHE O 468 SHEET 6 BL 7 SER O 393 TRP O 395 -1 O SER O 393 N PHE O 361 SHEET 7 BL 7 SER O 401 SER O 402 -1 O SER O 402 N THR O 394 SHEET 1 BM 2 PHE A 93 ASN A 94 0 SHEET 2 BM 2 LYS A 236 GLY A 237 -1 O GLY A 237 N PHE A 93 SHEET 1 BN 4 VAL A 200 THR A 202 0 SHEET 2 BN 4 VAL A 120 LEU A 122 -1 N LYS A 121 O ILE A 201 SHEET 3 BN 4 LYS A 432 MET A 434 -1 O LYS A 432 N LEU A 122 SHEET 4 BN 4 ILE A 423 ASN A 425 -1 N ILE A 424 O ALA A 433 SHEET 1 BO 3 VAL A 242 VAL A 245 0 SHEET 2 BO 3 PHE A 223 CYS A 228 -1 N LYS A 227 O SER A 243 SHEET 3 BO 3 VAL A 488 LYS A 490 -1 O VAL A 489 N ALA A 224 SHEET 1 BP 7 LEU A 259 LEU A 261 0 SHEET 2 BP 7 ILE A 443 ARG A 456 -1 O GLY A 451 N LEU A 260 SHEET 3 BP 7 ILE A 284 ARG A 298 -1 N VAL A 292 O ILE A 449 SHEET 4 BP 7 HIS A 330 SER A 334 -1 O ASN A 332 N ASN A 295 SHEET 5 BP 7 THR A 413 LYS A 421 -1 O LEU A 416 N CYS A 331 SHEET 6 BP 7 GLU A 381 CYS A 385 -1 N TYR A 384 O ARG A 419 SHEET 7 BP 7 HIS A 374 CYS A 378 -1 N CYS A 378 O GLU A 381 SHEET 1 BQ 6 VAL A 271 ARG A 273 0 SHEET 2 BQ 6 ILE A 284 ARG A 298 -1 O GLN A 287 N VAL A 271 SHEET 3 BQ 6 ILE A 443 ARG A 456 -1 O ILE A 449 N VAL A 292 SHEET 4 BQ 6 ILE A 465 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 5 BQ 6 THR A 358 PHE A 361 1 N VAL A 360 O PHE A 468 SHEET 6 BQ 6 SER A 393 TRP A 395 -1 O SER A 393 N PHE A 361 SHEET 1 BR 4 ILE K 201 THR K 202 0 SHEET 2 BR 4 VAL K 120 LEU K 122 -1 N LYS K 121 O ILE K 201 SHEET 3 BR 4 LYS K 432 MET K 434 -1 O LYS K 432 N LEU K 122 SHEET 4 BR 4 ILE K 423 ASN K 425 -1 N ILE K 424 O ALA K 433 SHEET 1 BS 2 PHE K 223 ILE K 225 0 SHEET 2 BS 2 VAL K 488 LYS K 490 -1 O VAL K 489 N ALA K 224 SHEET 1 BT 7 LEU K 259 LEU K 261 0 SHEET 2 BT 7 ARG K 444 ARG K 456 -1 O THR K 450 N LEU K 260 SHEET 3 BT 7 ILE K 284 THR K 297 -1 N ILE K 294 O SER K 447 SHEET 4 BT 7 HIS K 330 SER K 334 -1 O ASN K 332 N ASN K 295 SHEET 5 BT 7 THR K 413 LYS K 421 -1 O ILE K 414 N ILE K 333 SHEET 6 BT 7 GLU K 381 CYS K 385 -1 N TYR K 384 O ARG K 419 SHEET 7 BT 7 HIS K 374 CYS K 378 -1 N HIS K 374 O CYS K 385 SHEET 1 BU 7 VAL K 271 ARG K 273 0 SHEET 2 BU 7 ILE K 284 THR K 297 -1 O GLN K 287 N VAL K 271 SHEET 3 BU 7 ARG K 444 ARG K 456 -1 O SER K 447 N ILE K 294 SHEET 4 BU 7 GLU K 466 PRO K 470 -1 O ARG K 469 N THR K 455 SHEET 5 BU 7 ILE K 359 PHE K 361 1 N VAL K 360 O PHE K 468 SHEET 6 BU 7 SER K 393 TRP K 395 -1 O SER K 393 N PHE K 361 SHEET 7 BU 7 SER K 401 SER K 402 -1 O SER K 402 N THR K 394 SSBOND 1 CYS E 119 CYS E 205 1555 1555 2.04 SSBOND 2 CYS E 218 CYS E 247 1555 1555 2.04 SSBOND 3 CYS E 228 CYS E 239 1555 1555 2.07 SSBOND 4 CYS E 296 CYS E 331 1555 1555 1.98 SSBOND 5 CYS E 378 CYS E 445 1555 1555 2.04 SSBOND 6 CYS E 385 CYS E 418 1555 1555 2.10 SSBOND 7 CYS F 16 CYS F 84 1555 1555 2.05 SSBOND 8 CYS F 130 CYS F 159 1555 1555 2.03 SSBOND 9 CYS P 23 CYS P 88 1555 1555 2.05 SSBOND 10 CYS P 135 CYS P 194 1555 1555 2.03 SSBOND 11 CYS Q 22 CYS Q 92 1555 1555 2.03 SSBOND 12 CYS Q 158 CYS Q 214 1555 1555 2.03 SSBOND 13 CYS B 16 CYS B 84 1555 1555 1.92 SSBOND 14 CYS B 130 CYS B 159 1555 1555 2.04 SSBOND 15 CYS C 23 CYS C 88 1555 1555 2.05 SSBOND 16 CYS C 135 CYS C 194 1555 1555 2.03 SSBOND 17 CYS D 22 CYS D 92 1555 1555 2.03 SSBOND 18 CYS D 158 CYS D 214 1555 1555 2.04 SSBOND 19 CYS H 16 CYS H 84 1555 1555 2.05 SSBOND 20 CYS H 130 CYS H 159 1555 1555 2.03 SSBOND 21 CYS I 23 CYS I 88 1555 1555 2.51 SSBOND 22 CYS I 135 CYS I 194 1555 1555 2.03 SSBOND 23 CYS J 22 CYS J 92 1555 1555 2.04 SSBOND 24 CYS J 158 CYS J 214 1555 1555 2.04 SSBOND 25 CYS L 16 CYS L 84 1555 1555 2.04 SSBOND 26 CYS L 130 CYS L 159 1555 1555 2.04 SSBOND 27 CYS M 23 CYS M 88 1555 1555 2.06 SSBOND 28 CYS M 135 CYS M 194 1555 1555 2.09 SSBOND 29 CYS N 22 CYS N 92 1555 1555 2.04 SSBOND 30 CYS N 158 CYS N 214 1555 1555 2.04 SSBOND 31 CYS O 119 CYS O 205 1555 1555 2.03 SSBOND 32 CYS O 218 CYS O 247 1555 1555 1.83 SSBOND 33 CYS O 228 CYS O 239 1555 1555 2.03 SSBOND 34 CYS O 296 CYS O 331 1555 1555 2.21 SSBOND 35 CYS O 331 CYS O 385 1555 1555 2.57 SSBOND 36 CYS O 378 CYS O 445 1555 1555 2.04 SSBOND 37 CYS O 385 CYS O 418 1555 1555 2.06 SSBOND 38 CYS A 119 CYS A 205 1555 1555 2.45 SSBOND 39 CYS A 228 CYS A 239 1555 1555 2.04 SSBOND 40 CYS A 296 CYS A 331 1555 1555 2.20 SSBOND 41 CYS A 331 CYS A 385 1555 1555 2.53 SSBOND 42 CYS A 378 CYS A 445 1555 1555 2.04 SSBOND 43 CYS A 385 CYS A 418 1555 1555 2.00 SSBOND 44 CYS K 119 CYS K 205 1555 1555 2.04 SSBOND 45 CYS K 218 CYS K 247 1555 1555 2.03 SSBOND 46 CYS K 228 CYS K 239 1555 1555 2.48 SSBOND 47 CYS K 296 CYS K 331 1555 1555 2.21 SSBOND 48 CYS K 331 CYS K 385 1555 1555 2.94 SSBOND 49 CYS K 378 CYS K 445 1555 1555 2.04 SSBOND 50 CYS K 385 CYS K 418 1555 1555 2.05 LINK ND2 ASN O 332 C1 NAG O 501 1555 1555 1.24 LINK O3 BMA E 503 C1 MAN E 508 1555 1555 1.31 LINK O3 BMA O 503 C1 MAN O 508 1555 1555 1.32 LINK O3 BMA K 503 C1 MAN K 508 1555 1555 1.32 LINK O4 NAG A 502 C1 BMA A 503 1555 1555 1.34 LINK O4 NAG E 502 C1 BMA E 503 1555 1555 1.34 LINK O4 NAG K 502 C1 BMA K 503 1555 1555 1.34 LINK O4 NAG O 502 C1 BMA O 503 1555 1555 1.34 LINK ND2 ASN E 386 C1 NAG E 515 1555 1555 1.35 LINK ND2 ASN A 276 C1 NAG A 516 1555 1555 1.35 LINK ND2 ASN A 339 C1 NAG A 513 1555 1555 1.35 LINK ND2 ASN O 448 C1 NAG O 517 1555 1555 1.38 LINK ND2 ASN E 392 C1 NAG E 516 1555 1555 1.39 LINK ND2 ASN A 448 C1 NAG A 520 1555 1555 1.40 LINK ND2 ASN E 411 C1 NAG E 517 1555 1555 1.41 LINK ND2 ASN A 392 C1 NAG A 519 1555 1555 1.42 LINK ND2 ASN E 262 C1 NAG E 511 1555 1555 1.43 LINK ND2 ASN O 276 C1 NAG O 512 1555 1555 1.43 LINK ND2 ASN E 295 C1 NAG E 513 1555 1555 1.43 LINK ND2 ASN O 386 C1 NAG O 515 1555 1555 1.44 LINK O2 MAN E 509 C1 MAN E 510 1555 1555 1.44 LINK O2 MAN E 508 C1 MAN E 509 1555 1555 1.44 LINK O6 BMA K 503 C1 MAN K 504 1555 1555 1.44 LINK ND2 ASN E 339 C1 NAG E 514 1555 1555 1.44 LINK O2 MAN A 508 C1 MAN A 509 1555 1555 1.44 LINK O2 MAN A 509 C1 MAN A 510 1555 1555 1.44 LINK O2 MAN O 509 C1 MAN O 510 1555 1555 1.44 LINK O6 BMA O 503 C1 MAN O 504 1555 1555 1.44 LINK O6 BMA E 503 C1 MAN E 504 1555 1555 1.44 LINK O6 BMA A 503 C1 MAN A 504 1555 1555 1.44 LINK O2 MAN K 509 C1 MAN K 510 1555 1555 1.44 LINK ND2 ASN K 339 C1 NAG K 514 1555 1555 1.44 LINK O2 MAN O 505 C1 MAN O 506 1555 1555 1.44 LINK O2 MAN E 505 C1 MAN E 506 1555 1555 1.44 LINK O2 MAN A 505 C1 MAN A 506 1555 1555 1.44 LINK O2 MAN K 505 C1 MAN K 506 1555 1555 1.44 LINK O4 NAG E 501 C1 NAG E 502 1555 1555 1.44 LINK O4 NAG O 501 C1 NAG O 502 1555 1555 1.44 LINK O4 NAG A 501 C1 NAG A 502 1555 1555 1.44 LINK O4 NAG K 501 C1 NAG K 502 1555 1555 1.44 LINK O6 MAN A 504 C1 MAN A 505 1555 1555 1.44 LINK O6 MAN O 504 C1 MAN O 505 1555 1555 1.44 LINK O6 MAN E 504 C1 MAN E 505 1555 1555 1.44 LINK O6 MAN K 504 C1 MAN K 505 1555 1555 1.44 LINK ND2 ASN K 276 C1 NAG K 511 1555 1555 1.44 LINK ND2 ASN E 276 C1 NAG E 512 1555 1555 1.45 LINK ND2 ASN O 262 C1 NAG O 511 1555 1555 1.45 LINK ND2 ASN A 386 C1 NAG A 518 1555 1555 1.45 LINK ND2 ASN K 332 C1 NAG K 501 1555 1555 1.45 LINK ND2 ASN K 295 C1 NAG K 513 1555 1555 1.46 LINK ND2 ASN E 332 C1 NAG E 501 1555 1555 1.46 LINK ND2 ASN K 386 C1 NAG K 515 1555 1555 1.46 LINK ND2 ASN A 356 C1 NAG A 517 1555 1555 1.46 LINK ND2 ASN E 448 C1 NAG E 518 1555 1555 1.46 LINK ND2 ASN O 295 C1 NAG O 513 1555 1555 1.47 LINK ND2 ASN A 295 C1 NAG A 511 1555 1555 1.47 LINK O4 NAG A 513 C1 NAG A 514 1555 1555 1.47 LINK ND2 ASN O 339 C1 NAG O 514 1555 1555 1.47 LINK ND2 ASN K 262 C1 NAG K 512 1555 1555 1.47 LINK O4 NAG A 511 C1 NAG A 512 1555 1555 1.48 LINK ND2 ASN A 262 C1 NAG A 515 1555 1555 1.48 LINK ND2 ASN O 392 C1 NAG O 516 1555 1555 1.50 LINK O3 BMA A 503 C1 MAN A 508 1555 1555 1.50 LINK ND2 ASN A 332 C1 NAG A 501 1555 1555 1.66 LINK O3 MAN O 504 C1 MAN O 507 1555 1555 1.57 LINK O3 MAN K 504 C1 MAN K 507 1555 1555 1.57 LINK O3 MAN E 504 C1 MAN E 507 1555 1555 1.57 LINK O3 MAN A 504 C1 MAN A 507 1555 1555 1.57 LINK O2 MAN O 508 C1 MAN O 509 1555 1555 1.59 LINK O2 MAN K 508 C1 MAN K 509 1555 1555 1.59 LINK OG1 THR K 404 O7 NAG K 514 1555 1555 2.03 CISPEP 1 GLY E 197 GLY E 198 0 -0.46 CISPEP 2 LEU F 114 THR F 115 0 13.01 CISPEP 3 TYR P 141 PRO P 142 0 8.62 CISPEP 4 GLY Q 151 GLY Q 152 0 5.17 CISPEP 5 PHE Q 164 PRO Q 165 0 -4.27 CISPEP 6 GLU Q 166 PRO Q 167 0 13.61 CISPEP 7 SER Q 179 GLY Q 180 0 -0.74 CISPEP 8 SER Q 221 ASN Q 222 0 -14.30 CISPEP 9 LEU C 106A SER C 107 0 -20.13 CISPEP 10 TYR C 141 PRO C 142 0 1.93 CISPEP 11 GLY D 27 SER D 28 0 -6.62 CISPEP 12 PHE D 100G GLY D 100H 0 1.05 CISPEP 13 PHE D 164 PRO D 165 0 -4.03 CISPEP 14 GLU D 166 PRO D 167 0 -1.60 CISPEP 15 ALA D 176 LEU D 177 0 4.80 CISPEP 16 SER D 179 GLY D 180 0 -0.31 CISPEP 17 SER D 205 SER D 206 0 -0.57 CISPEP 18 SER D 221 ASN D 222 0 -1.30 CISPEP 19 GLY H 141 LYS H 142 0 0.54 CISPEP 20 TYR I 5 VAL I 6 0 -1.02 CISPEP 21 TYR I 141 PRO I 142 0 5.12 CISPEP 22 GLY J 26 GLY J 27 0 5.87 CISPEP 23 GLY J 151 GLY J 152 0 -0.98 CISPEP 24 PHE J 164 PRO J 165 0 -2.35 CISPEP 25 GLU J 166 PRO J 167 0 2.31 CISPEP 26 SER J 179 GLY J 180 0 11.91 CISPEP 27 SER J 221 ASN J 222 0 -13.83 CISPEP 28 ASN L 103 SER L 104 0 -8.10 CISPEP 29 TYR M 141 PRO M 142 0 0.23 CISPEP 30 PHE N 100G GLY N 100H 0 -3.68 CISPEP 31 GLY N 151 GLY N 152 0 -1.82 CISPEP 32 PHE N 164 PRO N 165 0 -4.03 CISPEP 33 GLU N 166 PRO N 167 0 3.59 CISPEP 34 SER N 179 GLY N 180 0 1.85 CISPEP 35 SER N 221 ASN N 222 0 3.76 CISPEP 36 ILE O 323 GLY O 324 0 3.46 CISPEP 37 CYS A 205 PRO A 206 0 -14.96 CISPEP 38 HIS A 249 GLY A 250 0 -7.07 CISPEP 39 GLY K 197 GLY K 198 0 -4.97 CISPEP 40 ILE K 323 GLY K 324 0 -10.61 CISPEP 41 LYS K 460 ASN K 461 0 -0.28 SITE 1 AC1 5 ASN E 295 HIS E 330 ASN E 332 ILE E 415 SITE 2 AC1 5 NAG E 502 SITE 1 AC2 8 ARG E 327 NAG E 501 BMA E 503 CL E 519 SITE 2 AC2 8 ILE Q 100A GLY Q 100C VAL Q 100D VAL Q 100E SITE 1 AC3 6 NAG E 502 MAN E 504 MAN E 507 MAN E 508 SITE 2 AC3 6 ILE Q 100A GOL Q 301 SITE 1 AC4 4 BMA E 503 MAN E 505 MAN E 507 GOL Q 301 SITE 1 AC5 2 MAN E 504 MAN E 506 SITE 1 AC6 2 MAN E 505 GLN Q 99 SITE 1 AC7 3 BMA E 503 MAN E 504 GOL Q 301 SITE 1 AC8 6 BMA E 503 MAN E 509 MAN E 510 SER P 30 SITE 2 AC8 6 ILE P 66B ARG Q 100 SITE 1 AC9 7 MAN E 508 MAN E 510 ASN P 50 ASN P 51 SITE 2 AC9 7 GLN P 52 ASP P 66A ARG Q 100 SITE 1 BC1 3 MAN E 508 MAN E 509 GLN P 52 SITE 1 BC2 6 VAL E 254 LEU E 261 ASN E 262 SER E 446 SITE 2 BC2 6 SER E 447 NAG E 518 SITE 1 BC3 2 ASN E 276 ASP E 279 SITE 1 BC4 2 ASN E 295 SER E 446 SITE 1 BC5 6 ARG E 335 ASN E 339 THR E 404 GLU E 405 SITE 2 BC5 6 GLY E 410 ASP E 412 SITE 1 BC6 4 ASN E 386 THR E 388 GLN E 389 NAG E 516 SITE 1 BC7 3 GLN E 389 ASN E 392 NAG E 515 SITE 1 BC8 2 GLN E 389 ASN E 411 SITE 1 BC9 5 ARG E 252 ASN E 262 SER E 291 ASN E 448 SITE 2 BC9 5 NAG E 511 SITE 1 CC1 4 ARG E 327 GLN E 442 ARG E 444 NAG E 502 SITE 1 CC2 3 BMA E 503 MAN E 504 MAN E 507 SITE 1 CC3 4 NAG O 502 BMA O 503 MAN O 504 MAN O 507 SITE 1 CC4 4 NAG K 502 BMA K 503 MAN K 504 MAN K 507 SITE 1 CC5 4 NAG A 501 NAG A 502 MAN A 504 MAN A 507 SITE 1 CC6 4 ASN O 295 HIS O 330 ASN O 332 NAG O 502 SITE 1 CC7 7 ILE D 100A GLY D 100C VAL D 100D VAL D 100E SITE 2 CC7 7 GOL D 301 NAG O 501 BMA O 503 SITE 1 CC8 6 ILE D 100A GOL D 301 NAG O 502 MAN O 504 SITE 2 CC8 6 MAN O 507 MAN O 508 SITE 1 CC9 4 GOL D 301 BMA O 503 MAN O 505 MAN O 507 SITE 1 DC1 2 MAN O 504 MAN O 506 SITE 1 DC2 2 GLN D 99 MAN O 505 SITE 1 DC3 3 GOL D 301 BMA O 503 MAN O 504 SITE 1 DC4 7 SER C 30 ASP C 66A ILE C 66B ARG D 100 SITE 2 DC4 7 BMA O 503 MAN O 509 MAN O 510 SITE 1 DC5 8 ASN C 50 ASN C 51 GLN C 52 PRO C 66 SITE 2 DC5 8 ASP C 66A ARG D 100 MAN O 508 MAN O 510 SITE 1 DC6 3 GLN C 52 MAN O 508 MAN O 509 SITE 1 DC7 6 VAL O 254 ASN O 262 CYS O 445 SER O 446 SITE 2 DC7 6 SER O 447 NAG O 517 SITE 1 DC8 3 ASN O 276 THR O 278 ASP O 279 SITE 1 DC9 4 ASN O 295 ILE O 333 SER O 334 SER O 446 SITE 1 EC1 7 ARG O 335 ASN O 339 SER O 401 THR O 404 SITE 2 EC1 7 GLU O 405 ASN O 411 ASP O 412 SITE 1 EC2 4 VAL O 372 ASN O 386 THR O 388 NAG O 516 SITE 1 EC3 3 GLN O 389 ASN O 392 NAG O 515 SITE 1 EC4 3 ASN O 262 ASN O 448 NAG O 511 SITE 1 EC5 1 GLN O 442 SITE 1 EC6 5 ASN A 295 HIS A 330 ASN A 332 NAG A 502 SITE 2 EC6 5 GOL N 301 SITE 1 EC7 7 NAG A 501 BMA A 503 ILE N 100A GLY N 100C SITE 2 EC7 7 VAL N 100D VAL N 100E GOL N 301 SITE 1 EC8 5 NAG A 502 MAN A 504 MAN A 507 MAN A 508 SITE 2 EC8 5 ILE N 100A SITE 1 EC9 4 BMA A 503 MAN A 505 MAN A 507 GOL N 301 SITE 1 FC1 2 MAN A 504 MAN A 506 SITE 1 FC2 2 MAN A 505 GLN N 99 SITE 1 FC3 3 BMA A 503 MAN A 504 GOL N 301 SITE 1 FC4 6 BMA A 503 MAN A 509 SER M 30 ASP M 66A SITE 2 FC4 6 ILE M 66B ARG N 100 SITE 1 FC5 8 MAN A 508 MAN A 510 ASN M 50 ASN M 51 SITE 2 FC5 8 GLN M 52 PRO M 66 ASP M 66A ARG N 100 SITE 1 FC6 2 MAN A 509 GLN M 52 SITE 1 FC7 3 ASN A 295 ASN A 332 NAG A 512 SITE 1 FC8 1 NAG A 511 SITE 1 FC9 6 ARG A 335 ALA A 336 ASN A 339 TRP A 395 SITE 2 FC9 6 THR A 404 NAG A 514 SITE 1 GC1 2 ASP A 412 NAG A 513 SITE 1 GC2 7 VAL A 254 LEU A 261 ASN A 262 CYS A 445 SITE 2 GC2 7 SER A 446 SER A 447 NAG A 520 SITE 1 GC3 2 ASN A 276 ASP A 279 SITE 1 GC4 2 ARG A 350 ASN A 356 SITE 1 GC5 3 ASN A 386 THR A 388 NAG A 519 SITE 1 GC6 2 ASN A 392 NAG A 518 SITE 1 GC7 2 ASN A 448 NAG A 515 SITE 1 GC8 3 ARG A 327 GLN A 442 ARG A 444 SITE 1 GC9 5 ASN K 295 HIS K 330 ASN K 332 ILE K 415 SITE 2 GC9 5 NAG K 502 SITE 1 HC1 9 ILE J 100A GLY J 100C VAL J 100D VAL J 100E SITE 2 HC1 9 GOL J 301 ARG K 327 NAG K 501 BMA K 503 SITE 3 HC1 9 CL K 516 SITE 1 HC2 6 ILE J 100A GOL J 301 NAG K 502 MAN K 504 SITE 2 HC2 6 MAN K 507 MAN K 508 SITE 1 HC3 4 GOL J 301 BMA K 503 MAN K 505 MAN K 507 SITE 1 HC4 2 MAN K 504 MAN K 506 SITE 1 HC5 2 GLN J 99 MAN K 505 SITE 1 HC6 3 GOL J 301 BMA K 503 MAN K 504 SITE 1 HC7 7 SER I 30 ASP I 66A ILE I 66B ARG J 100 SITE 2 HC7 7 BMA K 503 MAN K 509 MAN K 510 SITE 1 HC8 7 ASN I 51 GLN I 52 PRO I 66 ASP I 66A SITE 2 HC8 7 ARG J 100 MAN K 508 MAN K 510 SITE 1 HC9 2 MAN K 508 MAN K 509 SITE 1 IC1 4 LYS H 29 ASN K 276 THR K 278 ASP K 279 SITE 1 IC2 5 VAL K 254 LEU K 261 ASN K 262 SER K 446 SITE 2 IC2 5 SER K 447 SITE 1 IC3 2 ASN K 295 SER K 334 SITE 1 IC4 5 ARG K 335 ALA K 336 ASN K 339 SER K 401 SITE 2 IC4 5 THR K 404 SITE 1 IC5 4 MET K 373 ASN K 386 THR K 388 ARG K 419 SITE 1 IC6 2 ARG K 444 NAG K 502 CRYST1 164.406 165.438 229.712 90.00 90.00 90.00 P 21 21 21 16 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 0.006083 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006045 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004353 0.00000