HEADER VIRAL PROTEIN/IMMUNE SYSTEM 23-DEC-24 9MNT TITLE STRUCTURE OF HEPATITIS C VIRUS ENVELOPE GLYCOPROTEIN E2 CORE FROM TITLE 2 GENOTYPE 6A BOUND TO BROADLY NEUTRALIZING ANTIBODY RM1-73 COMPND MOL_ID: 1; COMPND 2 MOLECULE: RM1-73 FAB LIGHT CHAIN; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: RM1-73 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,R.L.STANFIELD,I.A.WILSON REVDAT 1 14-JAN-26 9MNT 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 RM1-73 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.55 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) : 2.55 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.70 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 3 NUMBER OF REFLECTIONS : 31037 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.232 REMARK 3 R VALUE (WORKING SET) : 0.231 REMARK 3 FREE R VALUE : 0.252 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.790 REMARK 3 FREE R VALUE TEST SET COUNT : 1488 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 46.7000 - 5.6600 1.00 2916 130 0.2035 0.1873 REMARK 3 2 5.6600 - 4.4900 1.00 2772 134 0.1725 0.1781 REMARK 3 3 4.4900 - 3.9300 1.00 2731 129 0.1880 0.1959 REMARK 3 4 3.9200 - 3.5700 1.00 2684 151 0.2443 0.2784 REMARK 3 5 3.5700 - 3.3100 1.00 2689 149 0.2554 0.2815 REMARK 3 6 3.3100 - 3.1200 1.00 2694 126 0.2612 0.3271 REMARK 3 7 3.1200 - 2.9600 1.00 2652 153 0.2793 0.3261 REMARK 3 8 2.9600 - 2.8300 0.99 2640 128 0.2961 0.3320 REMARK 3 9 2.8300 - 2.7200 0.99 2630 140 0.2824 0.3107 REMARK 3 10 2.7200 - 2.6300 0.99 2619 132 0.3656 0.4538 REMARK 3 11 2.6300 - 2.5500 0.94 2522 116 0.3077 0.3056 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) : 0.347 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.234 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 51.45 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.98 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 : 0.678 6571 REMARK 3 CHIRALITY : 0.048 762 REMARK 3 PLANARITY : 0.007 830 REMARK 3 DIHEDRAL : 12.060 1720 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 9MNT 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_1000291413. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-NOV-22 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 : 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) : 0.979 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31223 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550 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 (%) : 99.9 REMARK 200 DATA REDUNDANCY : 12.20 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.3900 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64 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 (%): 63.78 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, PH 8.5, 0.2 M LITHIUM REMARK 280 SULFATE, 40% V/V PEG400, 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 30.31350 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 104.45300 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.61150 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 104.45300 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.31350 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.61150 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: 7660 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 28170 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, E, A, B 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 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 GLN E 412 REMARK 465 LEU E 413 REMARK 465 ILE E 414 REMARK 465 ASN E 415 REMARK 465 THR E 416 REMARK 465 GLU E 476 REMARK 465 ARG E 477 REMARK 465 MET E 478 REMARK 465 ALA E 479 REMARK 465 ALA E 480 REMARK 465 CYS E 481 REMARK 465 GLY E 482 REMARK 465 SER E 483 REMARK 465 SER E 484 REMARK 465 GLY E 485 REMARK 465 CYS E 486 REMARK 465 TRP E 487 REMARK 465 HIS E 488 REMARK 465 TYR E 489 REMARK 465 ALA E 490 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 SER H 100a OG 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 CB TYR E 527 O7 NAG B 1 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O ALA H 9 NZ LYS H 129 3454 2.15 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 LYS L 30 -117.31 53.35 REMARK 500 ALA L 51 -34.37 68.19 REMARK 500 ALA L 84 -179.42 -171.27 REMARK 500 ASN L 138 76.10 55.49 REMARK 500 ASP H 144 68.88 60.34 REMARK 500 ALA E 444 57.36 -94.86 REMARK 500 LYS E 445 -151.58 -77.76 REMARK 500 ASN E 446 -158.78 -96.74 REMARK 500 ASP E 448 28.95 -79.74 REMARK 500 ASP E 495 -104.86 -139.01 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG B 1 DBREF 9MNT L 1 212 PDB 9MNT 9MNT 1 212 DBREF 9MNT H 1 218 PDB 9MNT 9MNT 1 218 DBREF 9MNT E 412 645 PDB 9MNT 9MNT 412 645 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 LYS ASN TYR LEU HIS TRP TYR GLN GLN LYS SEQRES 4 L 212 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR GLY ALA SER SEQRES 5 L 212 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 212 GLY SER GLY THR ASP PHE ILE LEU THR ILE SER SER LEU SEQRES 7 L 212 GLN SER GLU ASP VAL ALA THR TYR TYR CYS GLN HIS SER SEQRES 8 L 212 TYR ASP THR PRO TYR SER PHE GLY GLU 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 235 PCA VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 235 PRO GLY ALA SER VAL ARG LEU SER CYS LYS ALA SER GLY SEQRES 3 H 235 PHE THR PHE SER ILE SER ALA ILE GLY TRP VAL ARG GLN SEQRES 4 H 235 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLU ILE ILE SEQRES 5 H 235 PRO LEU VAL GLY ILE THR ASN TYR ALA GLN LYS PHE GLN SEQRES 6 H 235 GLY ARG VAL THR ILE THR ALA ASP THR SER THR SER THR SEQRES 7 H 235 ALA TYR MET ASP LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 235 ALA VAL TYR TYR CYS ALA ARG GLY ASP SER LYS LEU GLN SEQRES 9 H 235 SER VAL ALA ALA GLY GLY THR GLU GLY GLY ASN GLY LEU SEQRES 10 H 235 ASP SER TRP GLY GLN GLY VAL VAL VAL THR VAL SER SER SEQRES 11 H 235 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 12 H 235 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 13 H 235 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 14 H 235 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 15 H 235 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 16 H 235 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 17 H 235 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 18 H 235 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP SEQRES 19 H 235 LYS SEQRES 1 E 189 GLN LEU ILE ASN THR ASN GLY SER TRP HIS ILE ASN ARG SEQRES 2 E 189 THR ALA LEU ASN CYS ASN ASP SER LEU GLN THR GLY PHE SEQRES 3 E 189 ILE THR SER LEU PHE TYR ALA LYS ASN VAL ASP SER SER SEQRES 4 E 189 GLY CYS PRO GLU ARG MET ALA ALA CYS GLY SER SER GLY SEQRES 5 E 189 CYS TRP HIS TYR ALA PRO ARG PRO CYS ASP VAL VAL SER SEQRES 6 E 189 ALA ARG THR VAL CYS GLY PRO VAL TYR CYS PHE THR PRO SEQRES 7 E 189 SER PRO VAL VAL VAL GLY THR THR ASP LYS LEU GLY ILE SEQRES 8 E 189 PRO THR TYR ASN TRP GLY GLU ASN GLU THR ASP VAL PHE SEQRES 9 E 189 MET LEU GLU SER LEU ARG PRO PRO THR GLY GLY TRP PHE SEQRES 10 E 189 GLY CYS THR TRP MET ASN SER THR GLY PHE THR LYS THR SEQRES 11 E 189 CYS GLY ALA PRO PRO GLY GLY PRO THR ASP GLY GLY SER SEQRES 12 E 189 GLY PRO TRP ILE THR PRO ARG CYS LEU VAL ASP TYR PRO SEQRES 13 E 189 TYR ARG LEU TRP HIS TYR PRO CYS THR VAL ASN PHE THR SEQRES 14 E 189 LEU HIS LYS VAL ARG MET PHE VAL GLY GLY ILE GLU HIS SEQRES 15 E 189 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 SO4 L 301 5 HET NAG E 701 14 HET NAG E 702 14 HET NAG E 703 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM SO4 SULFATE ION 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 FORMUL 6 SO4 O4 S 2- FORMUL 10 HOH *21(H2 O) HELIX 1 AA1 GLN L 79 VAL L 83 5 5 HELIX 2 AA2 SER L 121 SER L 127 1 7 HELIX 3 AA3 LYS L 183 HIS L 189 1 7 HELIX 4 AA4 GLN H 61 GLN H 64 5 4 HELIX 5 AA5 ARG H 83 THR H 87 5 5 HELIX 6 AA6 SER H 97 ALA H 100D 1 8 HELIX 7 AA7 SER H 187 LEU H 189 5 3 HELIX 8 AA8 LYS H 201 ASN H 204 5 4 HELIX 9 AA9 HIS E 421 THR E 425 5 5 HELIX 10 AB1 ILE E 438 TYR E 443 1 6 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 LYS L 103 N LEU L 11 SHEET 3 AA2 6 ALA L 84 HIS L 90 -1 N ALA L 84 O VAL L 104 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 LEU L 47 N TRP L 35 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 LYS L 103 N LEU L 11 SHEET 3 AA3 4 ALA L 84 HIS L 90 -1 N ALA L 84 O VAL L 104 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 179 N VAL L 132 SHEET 4 AA4 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176 SHEET 1 AA5 4 ALA L 153 LEU L 154 0 SHEET 2 AA5 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AA5 4 VAL L 191 GLN L 198 -1 O GLU L 195 N GLN L 147 SHEET 4 AA5 4 THR L 201 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 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AA6 4 THR H 77 LEU H 82 -1 O MET H 80 N LEU H 20 SHEET 4 AA6 4 VAL H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AA7 6 ALA H 9 LYS H 12 0 SHEET 2 AA7 6 VAL H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AA7 6 ALA H 88 GLY H 95 -1 N TYR H 90 O VAL H 107 SHEET 4 AA7 6 ALA H 33 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA7 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA7 6 THR H 57 TYR H 59 -1 O ASN H 58 N GLU H 50 SHEET 1 AA8 4 ALA H 9 LYS H 12 0 SHEET 2 AA8 4 VAL H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AA8 4 ALA H 88 GLY H 95 -1 N TYR H 90 O VAL H 107 SHEET 4 AA8 4 LEU H 100M TRP H 103 -1 O SER H 102 N ARG H 94 SHEET 1 AA9 4 SER H 120 LEU H 124 0 SHEET 2 AA9 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AA9 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145 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 GLY H 139 N LEU H 124 SHEET 3 AB1 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145 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 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AB2 3 THR H 205 LYS H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AB3 3 ALA E 426 LEU E 427 0 SHEET 2 AB3 3 VAL E 502 PHE E 509 -1 O GLY E 504 N ALA E 426 SHEET 3 AB3 3 PRO E 513 VAL E 516 -1 O VAL E 516 N VAL E 506 SHEET 1 AB4 4 ALA E 426 LEU E 427 0 SHEET 2 AB4 4 VAL E 502 PHE E 509 -1 O GLY E 504 N ALA E 426 SHEET 3 AB4 4 GLY E 551 ASN E 556 -1 O MET E 555 N CYS E 503 SHEET 4 AB4 4 THR E 561 GLY E 565 -1 O LYS E 562 N TRP E 554 SHEET 1 AB5 2 VAL E 496 SER E 498 0 SHEET 2 AB5 2 VAL E 536 MET E 538 -1 O PHE E 537 N VAL E 497 SHEET 1 AB6 3 CYS E 607 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 2.03 SSBOND 4 CYS H 140 CYS H 196 1555 1555 2.03 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 2.04 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 430 C1 NAG E 701 1555 1555 1.44 LINK ND2 ASN E 532 C1 NAG E 702 1555 1555 1.44 LINK ND2 ASN E 556 C1 NAG A 1 1555 1555 1.45 LINK ND2 ASN E 623 C1 NAG E 703 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 1.44 CISPEP 1 SER L 7 PRO L 8 0 -0.23 CISPEP 2 THR L 94 PRO L 95 0 -0.54 CISPEP 3 TYR L 140 PRO L 141 0 1.43 CISPEP 4 PHE H 146 PRO H 147 0 -3.16 CISPEP 5 GLU H 148 PRO H 149 0 -0.90 CISPEP 6 THR E 510 PRO E 511 0 11.78 CRYST1 60.627 73.223 208.906 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 0.016494 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013657 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004787 0.00000