HEADER VIRAL PROTEIN/IMMUNE SYSTEM 09-JAN-25 9MSC TITLE STRUCTURE OF HEPATITIS C VIRUS ENVELOPE GLYCOPROTEIN HCV-1 E2ECTO FROM TITLE 2 GENOTYPE 1A BOUND TO NEUTRALIZING ANTIBODY RM5-16 COMPND MOL_ID: 1; COMPND 2 MOLECULE: RM5-16 FAB LC; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: RM5-16 FAN HC; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HEPC46 FAB LC; COMPND 11 CHAIN: B; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: HEPC46 FAB HC; COMPND 15 CHAIN: A; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: ENVELOPE GLYCOPROTEIN E2; COMPND 19 CHAIN: E; COMPND 20 SYNONYM: NS1,GP68,GP70; COMPND 21 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: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS (ISOLATE 1); SOURCE 31 ORGANISM_TAXID: 11104; SOURCE 32 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 33 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 34 EXPRESSION_SYSTEM_TAXID: 9606 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 9MSC 0 JRNL AUTH T.K.Y.NGUYEN JRNL TITL STRUCTURE OF HEPATITIS C VIRUS ENVELOPE GLYCOPROTEIN HCV-1 JRNL TITL 2 E2ECTO FROM GENOTYPE 1A BOUND TO NEUTRALIZING ANTIBODY JRNL TITL 3 RM5-16 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.39 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21RC1_5127 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.39 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.64 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4 REMARK 3 NUMBER OF REFLECTIONS : 24290 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.281 REMARK 3 R VALUE (WORKING SET) : 0.278 REMARK 3 FREE R VALUE : 0.317 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.290 REMARK 3 FREE R VALUE TEST SET COUNT : 1286 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 49.6400 - 7.0600 0.91 2823 161 0.2383 0.2906 REMARK 3 2 7.0500 - 5.6000 0.86 2468 161 0.2908 0.3515 REMARK 3 3 5.6000 - 4.9000 0.90 2545 149 0.2735 0.3082 REMARK 3 4 4.9000 - 4.4500 0.91 2556 127 0.2833 0.3197 REMARK 3 5 4.4500 - 4.1300 0.92 2576 155 0.2884 0.3265 REMARK 3 6 4.1300 - 3.8900 0.94 2589 126 0.3178 0.3495 REMARK 3 7 3.8900 - 3.6900 0.93 2537 108 0.3209 0.3229 REMARK 3 8 3.6900 - 3.5300 0.90 2513 123 0.3322 0.3617 REMARK 3 9 3.5300 - 3.3900 0.89 2443 130 0.3466 0.3481 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 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) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.988 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 162.6 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: 0.1100 REMARK 3 OPERATOR: -H,-K,L REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.003 8650 REMARK 3 ANGLE : 0.661 11813 REMARK 3 CHIRALITY : 0.046 1341 REMARK 3 PLANARITY : 0.005 1501 REMARK 3 DIHEDRAL : 12.061 2996 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 9MSC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1000291426. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-DEC-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 : 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 : 24462 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.390 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 (%) : 95.8 REMARK 200 DATA REDUNDANCY : 4.300 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.6400 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.39 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.50 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 (%): 65.13 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.3 M MAGNESIUM CHLORIDE, 15% W/V REMARK 280 PEG3350, EVAPORATION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+1/3 REMARK 290 6555 -X,-X+Y,-Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 376.51933 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 188.25967 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 188.25967 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 376.51933 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: PENTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 12320 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 50130 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, B, A, E, C, D, F REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLN L 1 REMARK 465 SER L 2 REMARK 465 ALA L 207 REMARK 465 PRO L 208 REMARK 465 THR L 209 REMARK 465 GLU L 210 REMARK 465 CYS L 211 REMARK 465 SER L 212 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 CYS A 216 REMARK 465 GLY A 217 REMARK 465 SER A 218 REMARK 465 GLU E 384 REMARK 465 THR E 385 REMARK 465 HIS E 386 REMARK 465 VAL E 387 REMARK 465 THR E 388 REMARK 465 GLY E 389 REMARK 465 GLY E 390 REMARK 465 SER E 391 REMARK 465 ALA E 392 REMARK 465 GLY E 393 REMARK 465 HIS E 394 REMARK 465 THR E 395 REMARK 465 VAL E 396 REMARK 465 SER E 397 REMARK 465 GLY E 398 REMARK 465 PHE E 399 REMARK 465 VAL E 400 REMARK 465 SER E 401 REMARK 465 LEU E 402 REMARK 465 LEU E 403 REMARK 465 ALA E 404 REMARK 465 PRO E 405 REMARK 465 GLY E 406 REMARK 465 ALA E 407 REMARK 465 LYS E 408 REMARK 465 GLN E 409 REMARK 465 ASN E 410 REMARK 465 VAL E 411 REMARK 465 GLN E 412 REMARK 465 LEU E 413 REMARK 465 ILE E 414 REMARK 465 ASN E 415 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 GLN L 194 CB CG 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 HIS L 26 -155.29 -138.60 REMARK 500 ASN L 27B -153.72 -129.49 REMARK 500 ILE L 28 -116.34 38.72 REMARK 500 ASP L 51 -53.64 66.76 REMARK 500 ASN L 52 22.69 -140.23 REMARK 500 ASP L 68 -111.38 56.48 REMARK 500 ASP L 151 -85.23 55.57 REMARK 500 LYS L 171 -155.85 -138.71 REMARK 500 SER H 132 87.57 -62.34 REMARK 500 ASP H 144 74.47 56.67 REMARK 500 THR H 160 -34.17 -132.24 REMARK 500 ASN B 27B -87.82 -109.51 REMARK 500 ASN B 31 -164.98 -127.17 REMARK 500 ASN B 51 -48.42 67.75 REMARK 500 ASN B 52 46.81 -156.48 REMARK 500 PRO B 55 -160.65 -77.34 REMARK 500 ASP B 82 36.26 -91.78 REMARK 500 ASN B 138 83.37 54.36 REMARK 500 SER B 156 138.65 -171.49 REMARK 500 LYS A 13 -77.99 -81.34 REMARK 500 PRO A 14 -171.99 -57.18 REMARK 500 CYS A 22 114.26 -171.75 REMARK 500 SER A 113 37.58 -67.22 REMARK 500 SER A 128 -80.18 -27.47 REMARK 500 ASP A 144 58.57 74.11 REMARK 500 PHE A 146 134.97 167.92 REMARK 500 ASN E 430 93.64 -163.15 REMARK 500 ASN E 434 62.93 64.48 REMARK 500 LYS E 446 40.67 -145.88 REMARK 500 SER E 449 78.49 -46.18 REMARK 500 SER E 450 -108.29 -66.88 REMARK 500 PRO E 461 -167.74 -74.72 REMARK 500 PHE E 465 40.80 -83.68 REMARK 500 GLN E 467 -151.09 -102.74 REMARK 500 PRO E 471 93.61 -22.84 REMARK 500 ASP E 520 63.79 -106.11 REMARK 500 ARG E 521 -34.91 59.61 REMARK 500 SER E 528 41.32 -101.29 REMARK 500 TRP E 529 18.85 49.41 REMARK 500 THR E 558 -162.46 -105.17 REMARK 500 ASN E 576 31.88 -96.46 REMARK 500 LEU E 579 71.09 -161.53 REMARK 500 THR E 583 -154.02 -141.06 REMARK 500 CYS E 585 57.80 -95.18 REMARK 500 PRO E 605 -16.66 -49.64 REMARK 500 TYR E 618 74.62 -116.79 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 MAN E 704 DBREF 9MSC L 1 212 PDB 9MSC 9MSC 1 212 DBREF 9MSC H 1 216 PDB 9MSC 9MSC 1 216 DBREF 9MSC B 1 212 PDB 9MSC 9MSC 1 212 DBREF 9MSC A 1 218 PDB 9MSC 9MSC 1 218 DBREF 9MSC E 384 645 UNP P26664 POLG_HCV1 384 645 SEQRES 1 L 216 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 L 216 PRO GLY GLN ARG VAL THR ILE SER CYS THR GLY HIS SER SEQRES 3 L 216 SER ASN ILE GLY GLY TYR PHE VAL SER TRP TYR GLN GLN SEQRES 4 L 216 LEU PRO GLY THR THR PRO LYS LEU LEU ILE TYR GLN ASP SEQRES 5 L 216 ASN LYS ARG PRO SER GLY VAL SER ASP ARG PHE SER GLY SEQRES 6 L 216 SER LYS SER ASP THR THR ALA SER LEU THR ILE THR GLY SEQRES 7 L 216 LEU GLN THR GLU ASP GLU ALA ASP TYR TYR CYS LEU SER SEQRES 8 L 216 TYR ASP ASN SER LEU SER ALA GLN VAL PHE GLY GLY GLY SEQRES 9 L 216 THR ARG LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SEQRES 10 L 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 L 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 L 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 L 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER SEQRES 14 L 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 L 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 16 L 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 L 216 THR VAL ALA PRO THR GLU CYS SER SEQRES 1 H 224 PCA LEU GLN LEU GLN GLU SER GLY PRO GLY LEU MET LYS SEQRES 2 H 224 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 H 224 GLY SER ILE SER SER HIS TYR TRP SER TRP ILE ARG GLN SEQRES 4 H 224 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE TYR SEQRES 5 H 224 GLY GLY THR GLY ARG THR ASN TYR ASN PRO SER LEU LYS SEQRES 6 H 224 SER ARG VAL THR ILE SER THR ASP THR SER LYS ASN GLN SEQRES 7 H 224 PHE SER LEU ASN LEU SER SER VAL THR ALA ALA ASP THR SEQRES 8 H 224 ALA MET TYR TYR CYS ALA ARG TYR PRO GLY SER HIS TRP SEQRES 9 H 224 GLU ASN SER LEU ASP VAL TRP GLY ARG GLY VAL LEU VAL SEQRES 10 H 224 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 H 224 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 H 224 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 H 224 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 H 224 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 H 224 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 H 224 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 H 224 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 H 224 LYS SER CYS SEQRES 1 B 217 GLN SER VAL LEU THR GLN PRO PRO SER ALA SER GLY THR SEQRES 2 B 217 PRO GLY GLN ARG VAL THR ILE SER CYS SER GLY SER SER SEQRES 3 B 217 SER ASN ILE GLY SER ASN TYR VAL TYR TRP TYR GLN GLN SEQRES 4 B 217 PHE PRO GLY THR ALA PRO LYS LEU LEU ILE TYR GLY ASN SEQRES 5 B 217 ASN GLN ARG PRO SER GLY VAL PRO ASP ARG PHE SER GLY SEQRES 6 B 217 SER LYS SER GLY THR SER ALA SER LEU ALA ILE SER GLY SEQRES 7 B 217 LEU ARG SER GLU ASP GLU ALA ASP TYR TYR CYS ALA ALA SEQRES 8 B 217 TRP ASP ASP SER LEU SER GLY PRO TRP VAL PHE GLY GLY SEQRES 9 B 217 GLY THR GLN VAL THR VAL LEU GLY GLN PRO VAL ALA ALA SEQRES 10 B 217 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 B 217 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 B 217 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 B 217 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 B 217 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 B 217 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 B 217 VAL TYR ALA CYS GLU VAL THR GLN GLY THR THR SER VAL SEQRES 17 B 217 THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 A 223 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 A 223 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 A 223 TYR ILE PHE THR SER HIS GLY ILE SER TRP VAL ARG GLN SEQRES 4 A 223 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE SER SEQRES 5 A 223 VAL TYR ASN GLY TYR THR ASN TYR ALA GLN ASN LEU GLN SEQRES 6 A 223 GLY ARG VAL THR MET THR THR ASP THR SER THR SER THR SEQRES 7 A 223 ALA TYR MET GLU LEU ARG SER LEU ARG SER ASP ASP THR SEQRES 8 A 223 ALA VAL TYR PHE CYS ALA ARG ALA SER GLN ILE ARG GLY SEQRES 9 A 223 VAL ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 A 223 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 A 223 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 A 223 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 A 223 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 A 223 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 A 223 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 A 223 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 A 223 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 18 A 223 GLY SER SEQRES 1 E 262 GLU THR HIS VAL THR GLY GLY SER ALA GLY HIS THR VAL SEQRES 2 E 262 SER GLY PHE VAL SER LEU LEU ALA PRO GLY ALA LYS GLN SEQRES 3 E 262 ASN VAL GLN LEU ILE ASN THR ASN GLY SER TRP HIS LEU SEQRES 4 E 262 ASN SER THR ALA LEU ASN CYS ASN ASP SER LEU ASN THR SEQRES 5 E 262 GLY TRP LEU ALA GLY LEU PHE TYR HIS HIS LYS PHE ASN SEQRES 6 E 262 SER SER GLY CYS PRO GLU ARG LEU ALA SER CYS ARG PRO SEQRES 7 E 262 LEU THR ASP PHE ASP GLN GLY TRP GLY PRO ILE SER TYR SEQRES 8 E 262 ALA ASN GLY SER GLY PRO ASP GLN ARG PRO TYR CYS TRP SEQRES 9 E 262 HIS TYR PRO PRO LYS PRO CYS GLY ILE VAL PRO ALA LYS SEQRES 10 E 262 SER VAL CYS GLY PRO VAL TYR CYS PHE THR PRO SER PRO SEQRES 11 E 262 VAL VAL VAL GLY THR THR ASP ARG SER GLY ALA PRO THR SEQRES 12 E 262 TYR SER TRP GLY GLU ASN ASP THR ASP VAL PHE VAL LEU SEQRES 13 E 262 ASN ASN THR ARG PRO PRO LEU GLY ASN TRP PHE GLY CYS SEQRES 14 E 262 THR TRP MET ASN SER THR GLY PHE THR LYS VAL CYS GLY SEQRES 15 E 262 ALA PRO PRO CYS VAL ILE GLY GLY ALA GLY ASN ASN THR SEQRES 16 E 262 LEU HIS CYS PRO THR ASP CYS PHE ARG LYS HIS PRO ASP SEQRES 17 E 262 ALA THR TYR SER ARG CYS GLY SER GLY PRO TRP ILE THR SEQRES 18 E 262 PRO ARG CYS LEU VAL ASP TYR PRO TYR ARG LEU TRP HIS SEQRES 19 E 262 TYR PRO CYS THR ILE ASN TYR THR ILE PHE LYS ILE ARG SEQRES 20 E 262 MET TYR VAL GLY GLY VAL GLU HIS ARG LEU GLU ALA ALA SEQRES 21 E 262 CYS ASN HET PCA H 1 8 HET NAG C 1 14 HET NAG C 2 14 HET NAG D 1 14 HET NAG D 2 14 HET NAG F 1 14 HET NAG F 2 14 HET BMA F 3 11 HET NAG E 701 14 HET NAG E 702 14 HET NAG E 703 14 HET MAN E 704 11 HETNAM PCA PYROGLUTAMIC ACID HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 2 PCA C5 H7 N O3 FORMUL 6 NAG 9(C8 H15 N O6) FORMUL 8 BMA C6 H12 O6 FORMUL 12 MAN C6 H12 O6 HELIX 1 AA1 ASN L 27B TYR L 31 5 5 HELIX 2 AA2 GLN L 79 GLU L 83 5 5 HELIX 3 AA3 SER L 121 GLN L 126 1 6 HELIX 4 AA4 THR L 181 HIS L 188 1 8 HELIX 5 AA5 THR H 83 THR H 87 5 5 HELIX 6 AA6 SER H 98 ASN H 100B 5 5 HELIX 7 AA7 SER H 156 ALA H 158 5 3 HELIX 8 AA8 SER H 187 LEU H 189 5 3 HELIX 9 AA9 LYS H 201 ASN H 204 5 4 HELIX 10 AB1 ARG B 79 GLU B 83 5 5 HELIX 11 AB2 SER B 121 LYS B 126 1 6 HELIX 12 AB3 LYS B 183 LYS B 188 1 6 HELIX 13 AB4 GLN A 61 GLN A 64 5 4 HELIX 14 AB5 ARG A 83 THR A 87 5 5 HELIX 15 AB6 SER A 187 LEU A 189 5 3 HELIX 16 AB7 LYS A 201 ASN A 204 5 4 HELIX 17 AB8 TRP E 437 PHE E 442 5 6 HELIX 18 AB9 CYS E 452 CYS E 459 1 8 HELIX 19 AC1 THR E 593 GLY E 598 1 6 HELIX 20 AC2 TYR E 613 TYR E 618 1 6 SHEET 1 AA1 5 SER L 9 GLY L 13 0 SHEET 2 AA1 5 THR L 102 VAL L 106 1 O THR L 105 N GLY L 13 SHEET 3 AA1 5 ASP L 85 ASP L 92 -1 N TYR L 86 O THR L 102 SHEET 4 AA1 5 SER L 34 GLN L 38 -1 N GLN L 38 O ASP L 85 SHEET 5 AA1 5 LYS L 45 ILE L 48 -1 O LEU L 47 N TRP L 35 SHEET 1 AA2 4 SER L 9 GLY L 13 0 SHEET 2 AA2 4 THR L 102 VAL L 106 1 O THR L 105 N GLY L 13 SHEET 3 AA2 4 ASP L 85 ASP L 92 -1 N TYR L 86 O THR L 102 SHEET 4 AA2 4 ALA L 95B PHE L 98 -1 O ALA L 95B N ASP L 92 SHEET 1 AA3 3 VAL L 19 THR L 24 0 SHEET 2 AA3 3 THR L 70 ILE L 75 -1 O ILE L 75 N VAL L 19 SHEET 3 AA3 3 PHE L 62 SER L 67 -1 N SER L 65 O SER L 72 SHEET 1 AA4 4 SER L 114 PHE L 118 0 SHEET 2 AA4 4 ALA L 130 PHE L 139 -1 O SER L 137 N SER L 114 SHEET 3 AA4 4 TYR L 172 LEU L 180 -1 O SER L 176 N CYS L 134 SHEET 4 AA4 4 VAL L 159 THR L 161 -1 N GLU L 160 O TYR L 177 SHEET 1 AA5 4 SER L 114 PHE L 118 0 SHEET 2 AA5 4 ALA L 130 PHE L 139 -1 O SER L 137 N SER L 114 SHEET 3 AA5 4 TYR L 172 LEU L 180 -1 O SER L 176 N CYS L 134 SHEET 4 AA5 4 SER L 165 LYS L 166 -1 N SER L 165 O ALA L 173 SHEET 1 AA6 4 SER L 153 VAL L 155 0 SHEET 2 AA6 4 THR L 145 ALA L 150 -1 N ALA L 150 O SER L 153 SHEET 3 AA6 4 TYR L 191 THR L 196 -1 O GLN L 194 N ALA L 147 SHEET 4 AA6 4 THR L 201 VAL L 206 -1 O VAL L 202 N VAL L 195 SHEET 1 AA7 4 GLN H 3 SER H 7 0 SHEET 2 AA7 4 LEU H 18 SER H 25 -1 O THR H 21 N SER H 7 SHEET 3 AA7 4 GLN H 77 LEU H 82 -1 O LEU H 82 N LEU H 18 SHEET 4 AA7 4 VAL H 67 ASP H 72 -1 N ASP H 72 O GLN H 77 SHEET 1 AA8 6 LEU H 11 MET H 12 0 SHEET 2 AA8 6 VAL H 107 VAL H 111 1 O THR H 110 N MET H 12 SHEET 3 AA8 6 ALA H 88 ARG H 94 -1 N TYR H 90 O VAL H 107 SHEET 4 AA8 6 TYR H 33 SER H 40 -1 N ILE H 37 O TYR H 91 SHEET 5 AA8 6 GLY H 44 TYR H 52 -1 O ILE H 51 N TRP H 34 SHEET 6 AA8 6 THR H 57 TYR H 59 -1 O ASN H 58 N TYR H 50 SHEET 1 AA9 4 LEU H 11 MET H 12 0 SHEET 2 AA9 4 VAL H 107 VAL H 111 1 O THR H 110 N MET H 12 SHEET 3 AA9 4 ALA H 88 ARG H 94 -1 N TYR H 90 O VAL H 107 SHEET 4 AA9 4 VAL H 102 TRP H 103 -1 O VAL H 102 N ARG H 94 SHEET 1 AB1 4 SER H 120 LEU H 124 0 SHEET 2 AB1 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 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 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AB2 4 SER H 120 LEU H 124 0 SHEET 2 AB2 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AB2 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145 SHEET 4 AB2 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AB3 3 THR H 151 TRP H 154 0 SHEET 2 AB3 3 TYR H 194 HIS H 200 -1 O ASN H 199 N THR H 151 SHEET 3 AB3 3 THR H 205 VAL H 211 -1 O THR H 205 N HIS H 200 SHEET 1 AB4 5 SER B 9 GLY B 13 0 SHEET 2 AB4 5 THR B 102 VAL B 106 1 O GLN B 103 N ALA B 11 SHEET 3 AB4 5 ASP B 85 TRP B 91 -1 N TYR B 86 O THR B 102 SHEET 4 AB4 5 VAL B 33 GLN B 38 -1 N TYR B 34 O ALA B 89 SHEET 5 AB4 5 LYS B 45 ILE B 48 -1 O LYS B 45 N GLN B 37 SHEET 1 AB5 4 SER B 9 GLY B 13 0 SHEET 2 AB5 4 THR B 102 VAL B 106 1 O GLN B 103 N ALA B 11 SHEET 3 AB5 4 ASP B 85 TRP B 91 -1 N TYR B 86 O THR B 102 SHEET 4 AB5 4 TRP B 96 VAL B 97 -1 O VAL B 97 N ALA B 90 SHEET 1 AB6 3 VAL B 19 SER B 24 0 SHEET 2 AB6 3 SER B 70 ILE B 75 -1 O ILE B 75 N VAL B 19 SHEET 3 AB6 3 PHE B 62 GLY B 64 -1 N SER B 63 O ALA B 74 SHEET 1 AB7 4 SER B 114 PHE B 118 0 SHEET 2 AB7 4 THR B 129 PHE B 139 -1 O VAL B 133 N PHE B 118 SHEET 3 AB7 4 TYR B 173 SER B 182 -1 O LEU B 181 N ALA B 130 SHEET 4 AB7 4 SER B 159 VAL B 163 -1 N GLN B 160 O THR B 178 SHEET 1 AB8 4 ALA B 153 LEU B 154 0 SHEET 2 AB8 4 LYS B 145 VAL B 150 -1 N VAL B 150 O ALA B 153 SHEET 3 AB8 4 VAL B 191 GLN B 198 -1 O THR B 197 N LYS B 145 SHEET 4 AB8 4 THR B 201 ASN B 208 -1 O THR B 201 N GLN B 198 SHEET 1 AB9 2 GLN A 3 GLN A 6 0 SHEET 2 AB9 2 CYS A 22 SER A 25 -1 O LYS A 23 N VAL A 5 SHEET 1 AC1 6 GLU A 10 VAL A 11 0 SHEET 2 AC1 6 THR A 107 THR A 110 1 O LEU A 108 N GLU A 10 SHEET 3 AC1 6 ALA A 88 SER A 96 -1 N TYR A 90 O THR A 107 SHEET 4 AC1 6 GLY A 33 GLN A 39 -1 N SER A 35 O ALA A 93 SHEET 5 AC1 6 LEU A 45 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AC1 6 THR A 57 TYR A 59 -1 O ASN A 58 N TRP A 50 SHEET 1 AC2 4 GLU A 10 VAL A 11 0 SHEET 2 AC2 4 THR A 107 THR A 110 1 O LEU A 108 N GLU A 10 SHEET 3 AC2 4 ALA A 88 SER A 96 -1 N TYR A 90 O THR A 107 SHEET 4 AC2 4 GLY A 100 TRP A 103 -1 O TYR A 102 N ARG A 94 SHEET 1 AC3 3 VAL A 18 VAL A 20 0 SHEET 2 AC3 3 THR A 77 LEU A 82 -1 O MET A 80 N VAL A 20 SHEET 3 AC3 3 VAL A 67 ASP A 72 -1 N THR A 70 O TYR A 79 SHEET 1 AC4 4 SER A 120 LEU A 124 0 SHEET 2 AC4 4 THR A 135 TYR A 145 -1 O LEU A 141 N PHE A 122 SHEET 3 AC4 4 TYR A 176 PRO A 185 -1 O TYR A 176 N TYR A 145 SHEET 4 AC4 4 HIS A 164 THR A 165 -1 N HIS A 164 O VAL A 181 SHEET 1 AC5 4 SER A 120 LEU A 124 0 SHEET 2 AC5 4 THR A 135 TYR A 145 -1 O LEU A 141 N PHE A 122 SHEET 3 AC5 4 TYR A 176 PRO A 185 -1 O TYR A 176 N TYR A 145 SHEET 4 AC5 4 VAL A 169 LEU A 170 -1 N VAL A 169 O SER A 177 SHEET 1 AC6 3 THR A 151 TRP A 154 0 SHEET 2 AC6 3 ILE A 195 HIS A 200 -1 O ASN A 197 N SER A 153 SHEET 3 AC6 3 THR A 205 LYS A 210 -1 O THR A 205 N HIS A 200 SHEET 1 AC7 2 SER E 473 TYR E 474 0 SHEET 2 AC7 2 CYS E 569 VAL E 570 -1 O VAL E 570 N SER E 473 SHEET 1 AC8 3 ILE E 496 PRO E 498 0 SHEET 2 AC8 3 ASP E 535 VAL E 538 -1 O PHE E 537 N VAL E 497 SHEET 3 AC8 3 THR E 519 ASP E 520 -1 N THR E 519 O VAL E 536 SHEET 1 AC9 4 PRO E 513 VAL E 516 0 SHEET 2 AC9 4 VAL E 502 PHE E 509 -1 N CYS E 508 O VAL E 514 SHEET 3 AC9 4 GLY E 551 ASN E 556 -1 O THR E 553 N TYR E 507 SHEET 4 AC9 4 THR E 561 GLY E 565 -1 O CYS E 564 N CYS E 552 SHEET 1 AD1 4 TRP E 602 THR E 604 0 SHEET 2 AD1 4 CYS E 607 VAL E 609 -1 O CYS E 607 N THR E 604 SHEET 3 AD1 4 VAL E 636 CYS E 644 -1 O ALA E 643 N LEU E 608 SHEET 4 AD1 4 THR E 625 VAL E 633 -1 N THR E 625 O CYS E 644 SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 2 CYS L 134 CYS L 193 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 2.04 SSBOND 5 CYS B 23 CYS B 88 1555 1555 2.03 SSBOND 6 CYS B 134 CYS B 194 1555 1555 2.03 SSBOND 7 CYS A 22 CYS A 92 1555 1555 2.04 SSBOND 8 CYS A 140 CYS A 196 1555 1555 2.04 SSBOND 9 CYS E 429 CYS E 503 1555 1555 2.03 SSBOND 10 CYS E 452 CYS E 620 1555 1555 2.03 SSBOND 11 CYS E 459 CYS E 486 1555 1555 2.03 SSBOND 12 CYS E 494 CYS E 564 1555 1555 2.03 SSBOND 13 CYS E 508 CYS E 552 1555 1555 2.04 SSBOND 14 CYS E 569 CYS E 597 1555 1555 2.03 SSBOND 15 CYS E 581 CYS E 585 1555 1555 2.03 SSBOND 16 CYS E 607 CYS E 644 1555 1555 2.03 LINK C PCA H 1 N LEU H 2 1555 1555 1.33 LINK ND2 ASN E 423 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN E 430 C1 NAG C 1 1555 1555 1.44 LINK ND2 ASN E 476 C1 NAG E 703 1555 1555 1.44 LINK ND2 ASN E 532 C1 NAG E 702 1555 1555 1.45 LINK ND2 ASN E 540 C1 NAG E 701 1555 1555 1.45 LINK ND2 ASN E 556 C1 NAG F 1 1555 1555 1.43 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.45 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.45 LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.45 CISPEP 1 TYR L 140 PRO L 141 0 -0.64 CISPEP 2 PHE H 146 PRO H 147 0 -6.35 CISPEP 3 GLU H 148 PRO H 149 0 -2.35 CISPEP 4 GLY B 95B PRO B 95C 0 15.00 CISPEP 5 TYR B 140 PRO B 141 0 4.17 CISPEP 6 PHE A 146 PRO A 147 0 2.05 CISPEP 7 GLU A 148 PRO A 149 0 0.75 CISPEP 8 THR E 510 PRO E 511 0 -21.72 CISPEP 9 PRO E 544 PRO E 545 0 3.82 CRYST1 72.709 72.709 564.779 90.00 90.00 120.00 P 32 2 1 6 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.013753 0.007941 0.000000 0.00000 SCALE2 0.000000 0.015881 0.000000 0.00000 SCALE3 0.000000 0.000000 0.001771 0.00000