HEADER VIRAL PROTEIN/IMMUNE SYSTEM 23-DEC-24 9MNQ TITLE STRUCTURE OF HEPATITIS C VIRUS ENVELOPE GLYCOPROTEIN E2 CORE FROM TITLE 2 GENOTYPE 6A BOUND TO BROADLY NEUTRALIZING ANTIBODY RM10-30 CAVEAT 9MNQ COMPND MOL_ID: 1; COMPND 2 MOLECULE: RM10-30 FAB LIGHT CHAIN; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: RM10-30 FAB HEAVY CHAIN; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HEPATITIS C VIRUS ENVELOPE GLYCOPROTEIN E2 CORE FROM COMPND 11 GENOTYPE 6A; COMPND 12 CHAIN: E; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 3 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 4 ORGANISM_TAXID: 9544; 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: MACACA MULATTA; SOURCE 10 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 11 ORGANISM_TAXID: 9544; 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: RECOMBINANT HEPATITIS C VIRUS HK6A/JFH-1; SOURCE 17 ORGANISM_TAXID: 595609; SOURCE 18 EXPRESSION_SYSTEM: UNIDENTIFIED; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 32644 KEYWDS IMMUNE SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR T.K.Y.NGUYEN,I.A.WILSON REVDAT 1 14-JAN-26 9MNQ 0 JRNL AUTH T.K.Y.NGUYEN JRNL TITL STRUCTURE OF HEPATITIS C VIRUS ENVELOPE GLYCOPROTEIN E2 CORE JRNL TITL 2 FROM GENOTYPE 6A BOUND TO BROADLY NEUTRALIZING ANTIBODY JRNL TITL 3 RM10-30 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.83 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2_4158 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.83 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.52 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4 REMARK 3 NUMBER OF REFLECTIONS : 24965 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.259 REMARK 3 R VALUE (WORKING SET) : 0.258 REMARK 3 FREE R VALUE : 0.287 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.170 REMARK 3 FREE R VALUE TEST SET COUNT : 1291 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 41.5200 - 5.8800 1.00 2860 157 0.2153 0.2332 REMARK 3 2 5.8800 - 4.6700 1.00 2698 140 0.2190 0.2381 REMARK 3 3 4.6700 - 4.0800 0.99 2674 135 0.2436 0.2565 REMARK 3 4 4.0800 - 3.7100 0.99 2633 148 0.3284 0.3729 REMARK 3 5 3.7100 - 3.4400 1.00 2637 145 0.3226 0.3680 REMARK 3 6 3.4400 - 3.2400 0.99 2605 158 0.3370 0.3768 REMARK 3 7 3.2400 - 3.0800 1.00 2596 165 0.3610 0.4579 REMARK 3 8 3.0800 - 2.9400 0.99 2638 116 0.3762 0.3919 REMARK 3 9 2.9400 - 2.8300 0.89 2333 127 0.3793 0.4056 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) : 0.540 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.677 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 105.7 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 117.6 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 : 0.004 4824 REMARK 3 ANGLE : 0.733 6577 REMARK 3 CHIRALITY : 0.048 765 REMARK 3 PLANARITY : 0.006 829 REMARK 3 DIHEDRAL : 11.498 1724 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 9MNQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1000291410. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-MAR-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25251 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.830 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 12.00 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 23.2700 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.83 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.93 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 68.53 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.91 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.5, 0.8 M POTASSIUM REMARK 280 DIHYDROGEN PHOSPHATE, 0.8 M SODIUM DIHYDROGEN PHOSPHATE, REMARK 280 EVAPORATION, 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 30.51700 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.28750 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.07000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.28750 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.51700 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.07000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7300 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 28530 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, E, A, B, C 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 PCA H 1 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 L 30 -117.70 57.77 REMARK 500 TYR L 32 35.69 -94.64 REMARK 500 LEU L 47 -63.07 -102.16 REMARK 500 ALA L 51 16.69 56.45 REMARK 500 SER L 52 -50.87 -159.66 REMARK 500 THR L 56 109.68 -59.80 REMARK 500 THR L 69 -61.55 -101.73 REMARK 500 ALA L 84 -164.13 -169.19 REMARK 500 TYR L 92 -92.25 -63.40 REMARK 500 ASN L 138 78.37 58.65 REMARK 500 SER H 7 -159.09 -73.51 REMARK 500 ALA H 16 -164.06 -100.87 REMARK 500 SER H 30 -130.12 55.24 REMARK 500 MET H 48 -76.85 -92.52 REMARK 500 SER H 113 34.51 -95.15 REMARK 500 SER H 132 37.60 -145.60 REMARK 500 ASP H 144 77.37 62.50 REMARK 500 SER E 449 -67.81 34.96 REMARK 500 ASP E 495 -101.44 -91.74 REMARK 500 THR E 519 -156.15 -129.70 REMARK 500 GLU E 540 -69.92 -19.56 REMARK 500 SER E 541 -58.39 -22.81 REMARK 500 ARG E 543 108.03 -34.88 REMARK 500 REMARK 500 REMARK: NULL DBREF 9MNQ L 1 212 PDB 9MNQ 9MNQ 1 212 DBREF 9MNQ H 1 215 PDB 9MNQ 9MNQ 1 215 DBREF 9MNQ E 421 645 PDB 9MNQ 9MNQ 421 645 SEQRES 1 L 212 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 212 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 212 GLU ASN VAL ASN ASN TYR LEU HIS TRP TYR GLN GLN LYS SEQRES 4 L 212 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 L 212 THR LEU GLN THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 212 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 212 GLN PRO GLU ASP VAL ALA THR TYR TYR CYS GLN HIS SER SEQRES 8 L 212 TYR GLY THR PRO TYR SER PHE GLY LEU GLY THR LYS VAL SEQRES 9 L 212 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 212 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 212 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 212 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 212 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 212 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 212 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 212 VAL THR GLN GLY THR THR SER VAL THR LYS SER PHE ASN SEQRES 17 L 212 ARG GLY GLU CYS SEQRES 1 H 225 PCA VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 225 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY SEQRES 3 H 225 PHE THR PHE SER ILE ASP ALA ILE SER TRP VAL ARG GLN SEQRES 4 H 225 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLU ILE ILE SEQRES 5 H 225 PRO ARG VAL GLY ILE THR VAL TYR ALA GLN LYS PHE HIS SEQRES 6 H 225 ASP ARG VAL THR ILE THR ALA ASP THR SER THR SER THR SEQRES 7 H 225 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 225 ALA VAL TYR TYR CYS ALA ARG GLY GLN ALA GLU GLY SER SEQRES 9 H 225 LEU ARG LEU ARG TRP PHE ASP VAL TRP GLY PRO GLY VAL SEQRES 10 H 225 LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 H 225 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 H 225 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 H 225 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 H 225 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 H 225 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 H 225 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 H 225 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 H 225 GLU PRO LYS SER SEQRES 1 E 169 HIS ILE ASN ARG THR ALA LEU ASN CYS ASN ASP SER LEU SEQRES 2 E 169 GLN THR GLY PHE ILE THR SER LEU PHE TYR ALA LYS ASN SEQRES 3 E 169 VAL ASP SER SER GLY CYS PRO GLU HIS TYR ALA PRO ARG SEQRES 4 E 169 PRO CYS ASP VAL VAL SER ALA ARG THR VAL CYS GLY PRO SEQRES 5 E 169 VAL TYR CYS PHE THR PRO SER PRO VAL VAL VAL GLY THR SEQRES 6 E 169 THR ASP LYS LEU GLY ILE PRO THR TYR ASN TRP GLY GLU SEQRES 7 E 169 ASN GLU THR ASP VAL PHE MET LEU GLU SER LEU ARG PRO SEQRES 8 E 169 PRO THR GLY GLY TRP PHE GLY CYS THR TRP MET ASN SER SEQRES 9 E 169 THR GLY PHE THR LYS THR CYS GLY ALA PRO PRO GLY GLY SEQRES 10 E 169 PRO THR ASP GLY GLY SER GLY PRO TRP ILE THR PRO ARG SEQRES 11 E 169 CYS LEU VAL ASP TYR PRO TYR ARG LEU TRP HIS TYR PRO SEQRES 12 E 169 CYS THR VAL ASN PHE THR LEU HIS LYS VAL ARG MET PHE SEQRES 13 E 169 VAL GLY GLY ILE GLU HIS ARG PHE ASP ALA ALA CYS ASN HET NAG A 1 14 HET NAG A 2 14 HET NAG B 1 14 HET NAG B 2 14 HET BMA B 3 11 HET NAG C 1 14 HET NAG C 2 14 HET NAG E 701 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-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 FORMUL 4 NAG 7(C8 H15 N O6) FORMUL 5 BMA C6 H12 O6 HELIX 1 AA1 GLN L 79 VAL L 83 5 5 HELIX 2 AA2 SER L 121 LYS L 126 1 6 HELIX 3 AA3 LYS L 183 HIS L 189 1 7 HELIX 4 AA4 ARG H 83 THR H 87 5 5 HELIX 5 AA5 SER H 156 ALA H 158 5 3 HELIX 6 AA6 SER H 187 LEU H 189 5 3 HELIX 7 AA7 LYS H 201 ASN H 204 5 4 HELIX 8 AA8 HIS E 421 THR E 425 5 5 HELIX 9 AA9 ILE E 438 TYR E 443 1 6 HELIX 10 AB1 ASP E 448 CYS E 452 5 5 HELIX 11 AB2 GLU E 540 ARG E 543 5 4 HELIX 12 AB3 TYR E 613 TYR E 618 1 6 HELIX 13 AB4 PRO E 619 PHE E 624 5 6 SHEET 1 AA1 4 MET L 4 SER L 7 0 SHEET 2 AA1 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA1 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA1 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA2 6 SER L 10 SER L 14 0 SHEET 2 AA2 6 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 AA2 6 THR L 85 HIS L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA2 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AA2 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AA2 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AA3 4 SER L 10 SER L 14 0 SHEET 2 AA3 4 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 AA3 4 THR L 85 HIS L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA3 4 SER L 97 PHE L 98 -1 O SER L 97 N HIS L 90 SHEET 1 AA4 4 SER L 114 PHE L 118 0 SHEET 2 AA4 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AA4 4 TYR L 173 SER L 182 -1 O LEU L 181 N ALA L 130 SHEET 4 AA4 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AA5 3 LYS L 145 VAL L 150 0 SHEET 2 AA5 3 VAL L 191 THR L 197 -1 O THR L 197 N LYS L 145 SHEET 3 AA5 3 SER L 202 ASN L 208 -1 O VAL L 203 N VAL L 196 SHEET 1 AA6 4 GLN H 3 GLN H 6 0 SHEET 2 AA6 4 SER H 17 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AA6 4 THR H 77 SER H 82A-1 O ALA H 78 N CYS H 22 SHEET 4 AA6 4 VAL H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 AA7 6 GLU H 10 LYS H 12 0 SHEET 2 AA7 6 LEU H 108 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AA7 6 ALA H 88 GLN H 96 -1 N ALA H 88 O VAL H 109 SHEET 4 AA7 6 ALA H 33 GLN H 39 -1 N ALA H 33 O GLY H 95 SHEET 5 AA7 6 GLU H 46 ILE H 52 -1 O MET H 48 N TRP H 36 SHEET 6 AA7 6 ILE H 56 TYR H 59 -1 O VAL H 58 N GLU H 50 SHEET 1 AA8 4 GLU H 10 LYS H 12 0 SHEET 2 AA8 4 LEU H 108 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AA8 4 ALA H 88 GLN H 96 -1 N ALA H 88 O VAL H 109 SHEET 4 AA8 4 TRP H 100E TRP H 103 -1 O TRP H 100E N GLN H 96 SHEET 1 AA9 4 SER H 120 LEU H 124 0 SHEET 2 AA9 4 THR H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AA9 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AA9 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AB1 4 SER H 120 LEU H 124 0 SHEET 2 AB1 4 THR H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AB1 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AB1 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AB2 3 THR H 151 TRP H 154 0 SHEET 2 AB2 3 TYR H 194 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AB2 3 THR H 205 VAL H 211 -1 O THR H 205 N HIS H 200 SHEET 1 AB3 2 ALA E 426 LEU E 427 0 SHEET 2 AB3 2 CYS E 503 GLY E 504 -1 O GLY E 504 N ALA E 426 SHEET 1 AB4 2 VAL E 496 SER E 498 0 SHEET 2 AB4 2 VAL E 536 MET E 538 -1 O PHE E 537 N VAL E 497 SHEET 1 AB5 4 PRO E 513 VAL E 516 0 SHEET 2 AB5 4 VAL E 506 PHE E 509 -1 N VAL E 506 O VAL E 516 SHEET 3 AB5 4 GLY E 551 MET E 555 -1 O THR E 553 N TYR E 507 SHEET 4 AB5 4 THR E 561 GLY E 565 -1 O LYS E 562 N TRP E 554 SHEET 1 AB6 3 LEU E 608 VAL E 609 0 SHEET 2 AB6 3 GLU E 637 CYS E 644 -1 O ALA E 643 N LEU E 608 SHEET 3 AB6 3 THR E 625 PHE E 632 -1 N MET E 631 O HIS E 638 SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 2 CYS L 134 CYS L 194 1555 1555 2.03 SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 4 CYS H 140 CYS H 196 1555 1555 2.04 SSBOND 5 CYS E 429 CYS E 503 1555 1555 2.03 SSBOND 6 CYS E 452 CYS E 620 1555 1555 2.03 SSBOND 7 CYS E 494 CYS E 564 1555 1555 2.03 SSBOND 8 CYS E 508 CYS E 552 1555 1555 2.03 SSBOND 9 CYS E 607 CYS E 644 1555 1555 2.03 LINK ND2 ASN E 423 C1 NAG B 1 1555 1555 1.44 LINK ND2 ASN E 532 C1 NAG E 701 1555 1555 1.44 LINK ND2 ASN E 556 C1 NAG A 1 1555 1555 1.45 LINK ND2 ASN E 623 C1 NAG C 1 1555 1555 1.44 LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.45 LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44 LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.45 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.45 CISPEP 1 SER L 7 PRO L 8 0 -4.43 CISPEP 2 THR L 94 PRO L 95 0 2.65 CISPEP 3 TYR L 140 PRO L 141 0 2.89 CISPEP 4 PHE H 146 PRO H 147 0 -4.63 CISPEP 5 GLU H 148 PRO H 149 0 0.32 CISPEP 6 THR E 510 PRO E 511 0 -5.75 CRYST1 61.034 74.140 226.575 90.00 90.00 90.00 P 21 21 21 4 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 0.016384 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013488 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004414 0.00000