HEADER IMMUNE SYSTEM 18-APR-20 6WLA TITLE ANTIGEN BINDING FRAGMENT OF CH128.1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB CH128.1 HEAVY CHAIN; COMPND 3 CHAIN: H1, H2, H3; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB CH128.1 LIGHT CHAIN; COMPND 7 CHAIN: L1, L3, L2; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ANTIBODY, ANTI-HUTFR1, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR G.HELGUERA,J.A.RODRIGUEZ,M.SAWAYA,D.CASCIO,S.ZINK,J.ZIEGENBEIN, AUTHOR 2 C.SHORT JRNL AUTH B.T.HICKERSON,T.R.DANIELS-WELLS,C.PAYES,L.E.CLARK, JRNL AUTH 2 P.V.CANDELARIA,K.W.BAILEY,E.J.SEFING,S.ZINK,J.ZIEGENBEIN, JRNL AUTH 3 J.ABRAHAM,G.HELGUERA,M.L.PENICHET,B.B.GOWEN JRNL TITL HOST RECEPTOR-TARGETED THERAPEUTIC APPROACH TO COUNTER JRNL TITL 2 PATHOGENIC NEW WORLD MAMMARENAVIRUS INFECTIONS. JRNL REF NAT COMMUN V. 13 558 2022 JRNL REFN ESSN 2041-1723 JRNL PMID 35091550 JRNL DOI 10.1038/S41467-021-27949-3 REMARK 2 REMARK 2 RESOLUTION. 2.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX DEV_3724 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.13 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 51861 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.212 REMARK 3 R VALUE (WORKING SET) : 0.207 REMARK 3 FREE R VALUE : 0.258 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 5185 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 63.1300 - 8.0800 1.00 1560 174 0.1644 0.1742 REMARK 3 2 8.0700 - 6.4100 0.98 1517 168 0.2044 0.2239 REMARK 3 3 6.4100 - 5.6000 1.00 1564 174 0.1987 0.2322 REMARK 3 4 5.6000 - 5.0900 1.00 1549 172 0.1976 0.2339 REMARK 3 5 5.0900 - 4.7200 1.00 1581 176 0.1842 0.2233 REMARK 3 6 4.7200 - 4.4400 1.00 1560 173 0.1766 0.2207 REMARK 3 7 4.4400 - 4.2200 1.00 1534 170 0.1829 0.2326 REMARK 3 8 4.2200 - 4.0400 1.00 1573 175 0.1993 0.2731 REMARK 3 9 4.0400 - 3.8800 1.00 1573 175 0.1986 0.2577 REMARK 3 10 3.8800 - 3.7500 1.00 1537 171 0.2042 0.2469 REMARK 3 11 3.7500 - 3.6300 1.00 1582 175 0.1912 0.2700 REMARK 3 12 3.6300 - 3.5300 0.98 1524 170 0.2085 0.2400 REMARK 3 13 3.5300 - 3.4400 1.00 1564 174 0.2041 0.2491 REMARK 3 14 3.4300 - 3.3500 1.00 1556 173 0.2319 0.2909 REMARK 3 15 3.3500 - 3.2700 1.00 1528 169 0.2232 0.3083 REMARK 3 16 3.2700 - 3.2100 1.00 1572 175 0.2227 0.2624 REMARK 3 17 3.2000 - 3.1400 1.00 1569 174 0.2217 0.2786 REMARK 3 18 3.1400 - 3.0800 1.00 1526 170 0.2309 0.3186 REMARK 3 19 3.0800 - 3.0300 1.00 1583 176 0.2324 0.3100 REMARK 3 20 3.0300 - 2.9800 1.00 1561 173 0.2251 0.3447 REMARK 3 21 2.9800 - 2.9300 1.00 1556 173 0.2423 0.3008 REMARK 3 22 2.9300 - 2.8800 1.00 1545 172 0.2468 0.3388 REMARK 3 23 2.8800 - 2.8400 1.00 1606 178 0.2552 0.3518 REMARK 3 24 2.8400 - 2.8000 1.00 1562 173 0.2783 0.3149 REMARK 3 25 2.8000 - 2.7600 1.00 1538 171 0.2742 0.3569 REMARK 3 26 2.7600 - 2.7300 1.00 1572 174 0.2766 0.3354 REMARK 3 27 2.7300 - 2.6900 1.00 1557 173 0.2612 0.3267 REMARK 3 28 2.6900 - 2.6600 1.00 1551 172 0.2658 0.3695 REMARK 3 29 2.6600 - 2.6300 1.00 1551 172 0.2690 0.3215 REMARK 3 30 2.6300 - 2.6000 0.96 1525 170 0.2828 0.3251 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL 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) : 0.400 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.750 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 55.58 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.88 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 : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL 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 6WLA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000248554. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-MAR-17 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 24-ID-E REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918 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 : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51879 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 63.130 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 5.294 REMARK 200 R MERGE (I) : 0.12900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.3100 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.67 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2 REMARK 200 DATA REDUNDANCY IN SHELL : 5.28 REMARK 200 R MERGE FOR SHELL (I) : 1.27700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.500 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: FIXED/FIXED.PDB REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 60.47 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1M LITHIUM CHLORIDE, 0.1 CITRIC ACID REMARK 280 PH 4.0, 20% (W/V) PEG 6000, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,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 31.61667 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 63.23333 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4720 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19050 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H1, L1 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4310 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19510 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H2, L2 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4090 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19170 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H3, L3 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 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 GLU L 211 CB CG CD OE1 OE2 REMARK 470 GLU H 1 CB CG CD OE1 OE2 REMARK 470 THR H 136 OG1 CG2 REMARK 470 SER L 7 OG 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 HISH1 41 44.61 -91.08 REMARK 500 ASNH1 44 -141.55 63.36 REMARK 500 ALAH1 92 -178.22 -172.05 REMARK 500 SERH1 132 -153.94 -95.38 REMARK 500 ASPH1 149 61.27 61.90 REMARK 500 PROH1 152 -169.25 -101.49 REMARK 500 PROH1 154 -169.10 -106.40 REMARK 500 THRH1 165 -42.58 -140.18 REMARK 500 THRH1 196 -62.31 -107.99 REMARK 500 THRL1 50 -35.96 69.95 REMARK 500 SERL1 51 -5.10 -141.27 REMARK 500 ASNL1 137 81.02 56.43 REMARK 500 PROL1 140 -166.68 -78.83 REMARK 500 LYSL1 189 -61.81 -129.31 REMARK 500 ASNH2 44 -132.56 63.24 REMARK 500 SERH2 85 73.44 51.17 REMARK 500 ALAH2 92 -177.24 -176.68 REMARK 500 ASPH2 149 66.24 67.53 REMARK 500 PROH2 152 -153.25 -97.61 REMARK 500 ASNH3 44 -129.13 60.86 REMARK 500 SERH3 132 -143.07 -127.57 REMARK 500 ASPH3 149 67.70 62.90 REMARK 500 THRH3 165 -46.20 -152.35 REMARK 500 THRL3 50 -48.90 67.17 REMARK 500 ASNL3 137 84.39 55.56 REMARK 500 LYSL3 189 -63.02 -107.14 REMARK 500 THRL2 50 -50.96 67.36 REMARK 500 ASNL2 137 69.35 60.38 REMARK 500 ASNL2 151 -1.20 68.63 REMARK 500 ARGL2 210 97.99 -69.22 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 GOL H1 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H1 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL L1 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL L1 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H2 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H2 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H3 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL L3 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL L2 301 DBREF 6WLAH1 1 219 PDB 6WLA 6WLA 1 219 DBREF 6WLAL1 1 211 PDB 6WLA 6WLA 1 211 DBREF 6WLAH2 1 219 PDB 6WLA 6WLA 1 219 DBREF 6WLAH3 1 219 PDB 6WLA 6WLA 1 219 DBREF 6WLAL3 1 211 PDB 6WLA 6WLA 1 211 DBREF 6WLAL2 1 211 PDB 6WLA 6WLA 1 211 SEQRES 1H1 219 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2H1 219 PRO GLY ALA SER MET LYS ILE SER CYS LYS ALA SER GLY SEQRES 3H1 219 TYR SER PHE THR GLY TYR THR MET ASN TRP VAL LYS GLN SEQRES 4H1 219 SER HIS GLY GLU ASN LEU GLU TRP ILE GLY ARG ILE ASN SEQRES 5H1 219 PRO HIS ASN GLY GLY THR ASP TYR ASN GLN LYS PHE LYS SEQRES 6H1 219 ASP LYS ALA PRO LEU THR VAL ASP LYS SER SER ASN THR SEQRES 7H1 219 ALA TYR MET GLU LEU LEU SER LEU THR SER GLY ASP SER SEQRES 8H1 219 ALA VAL TYR TYR CYS ALA ARG GLY TYR TYR TYR TYR SER SEQRES 9H1 219 LEU ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SER SEQRES 10H1 219 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11H1 219 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12H1 219 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13H1 219 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14H1 219 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15H1 219 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16H1 219 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17H1 219 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 1L1 211 GLN ILE VAL LEU THR GLN SER PRO ALA ILE MET SER VAL SEQRES 2L1 211 SER PRO GLY GLU LYS VAL THR MET THR CYS SER ALA SER SEQRES 3L1 211 SER SER ILE ARG TYR ILE HIS TRP TYR GLN GLN ARG PRO SEQRES 4L1 211 GLY THR SER PRO LYS ARG TRP ILE TYR ASP THR SER ASN SEQRES 5L1 211 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6L1 211 SER GLY THR SER TYR SER LEU THR ILE SER SER MET GLU SEQRES 7L1 211 ALA GLU ASP ALA ALA THR TYR TYR CYS HIS GLN ARG ASN SEQRES 8L1 211 SER TYR PRO TRP THR PHE GLY GLY GLY THR ARG LEU GLU SEQRES 9L1 211 ILE ARG ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10L1 211 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11L1 211 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12L1 211 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13L1 211 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14L1 211 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15L1 211 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16L1 211 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17L1 211 ASN ARG GLU SEQRES 1H2 219 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2H2 219 PRO GLY ALA SER MET LYS ILE SER CYS LYS ALA SER GLY SEQRES 3H2 219 TYR SER PHE THR GLY TYR THR MET ASN TRP VAL LYS GLN SEQRES 4H2 219 SER HIS GLY GLU ASN LEU GLU TRP ILE GLY ARG ILE ASN SEQRES 5H2 219 PRO HIS ASN GLY GLY THR ASP TYR ASN GLN LYS PHE LYS SEQRES 6H2 219 ASP LYS ALA PRO LEU THR VAL ASP LYS SER SER ASN THR SEQRES 7H2 219 ALA TYR MET GLU LEU LEU SER LEU THR SER GLY ASP SER SEQRES 8H2 219 ALA VAL TYR TYR CYS ALA ARG GLY TYR TYR TYR TYR SER SEQRES 9H2 219 LEU ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SER SEQRES 10H2 219 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11H2 219 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12H2 219 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13H2 219 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14H2 219 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15H2 219 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16H2 219 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17H2 219 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 1H3 219 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2H3 219 PRO GLY ALA SER MET LYS ILE SER CYS LYS ALA SER GLY SEQRES 3H3 219 TYR SER PHE THR GLY TYR THR MET ASN TRP VAL LYS GLN SEQRES 4H3 219 SER HIS GLY GLU ASN LEU GLU TRP ILE GLY ARG ILE ASN SEQRES 5H3 219 PRO HIS ASN GLY GLY THR ASP TYR ASN GLN LYS PHE LYS SEQRES 6H3 219 ASP LYS ALA PRO LEU THR VAL ASP LYS SER SER ASN THR SEQRES 7H3 219 ALA TYR MET GLU LEU LEU SER LEU THR SER GLY ASP SER SEQRES 8H3 219 ALA VAL TYR TYR CYS ALA ARG GLY TYR TYR TYR TYR SER SEQRES 9H3 219 LEU ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SER SEQRES 10H3 219 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11H3 219 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12H3 219 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13H3 219 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14H3 219 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15H3 219 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16H3 219 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17H3 219 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 1L3 211 GLN ILE VAL LEU THR GLN SER PRO ALA ILE MET SER VAL SEQRES 2L3 211 SER PRO GLY GLU LYS VAL THR MET THR CYS SER ALA SER SEQRES 3L3 211 SER SER ILE ARG TYR ILE HIS TRP TYR GLN GLN ARG PRO SEQRES 4L3 211 GLY THR SER PRO LYS ARG TRP ILE TYR ASP THR SER ASN SEQRES 5L3 211 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6L3 211 SER GLY THR SER TYR SER LEU THR ILE SER SER MET GLU SEQRES 7L3 211 ALA GLU ASP ALA ALA THR TYR TYR CYS HIS GLN ARG ASN SEQRES 8L3 211 SER TYR PRO TRP THR PHE GLY GLY GLY THR ARG LEU GLU SEQRES 9L3 211 ILE ARG ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10L3 211 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11L3 211 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12L3 211 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13L3 211 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14L3 211 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15L3 211 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16L3 211 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17L3 211 ASN ARG GLU SEQRES 1L2 211 GLN ILE VAL LEU THR GLN SER PRO ALA ILE MET SER VAL SEQRES 2L2 211 SER PRO GLY GLU LYS VAL THR MET THR CYS SER ALA SER SEQRES 3L2 211 SER SER ILE ARG TYR ILE HIS TRP TYR GLN GLN ARG PRO SEQRES 4L2 211 GLY THR SER PRO LYS ARG TRP ILE TYR ASP THR SER ASN SEQRES 5L2 211 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6L2 211 SER GLY THR SER TYR SER LEU THR ILE SER SER MET GLU SEQRES 7L2 211 ALA GLU ASP ALA ALA THR TYR TYR CYS HIS GLN ARG ASN SEQRES 8L2 211 SER TYR PRO TRP THR PHE GLY GLY GLY THR ARG LEU GLU SEQRES 9L2 211 ILE ARG ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10L2 211 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11L2 211 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12L2 211 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13L2 211 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14L2 211 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15L2 211 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16L2 211 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17L2 211 ASN ARG GLU HET GOL H1 301 6 HET GOL H1 302 6 HET GOL L1 301 6 HET GOL L1 302 6 HET GOL H2 301 6 HET GOL H2 302 6 HET GOL H3 301 6 HET GOL L3 301 6 HET GOL L2 301 6 HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 7 GOL 9(C3 H8 O3) FORMUL 16 HOH *122(H2 O) HELIX 1 AA1 SERH1 28 TYRH1 32 5 5 HELIX 2 AA2 LYSH1 74 SERH1 76 5 3 HELIX 3 AA3 THRH1 87 SERH1 91 5 5 HELIX 4 AA4 SERH1 161 ALAH1 163 5 3 HELIX 5 AA5 SERH1 192 LEUH1 194 5 3 HELIX 6 AA6 LYSH1 206 ASNH1 209 5 4 HELIX 7 AA7 GLUL1 78 ALAL1 82 5 5 HELIX 8 AA8 SERL1 120 GLYL1 127 1 8 HELIX 9 AA9 LYSL1 182 LYSL1 187 1 6 HELIX 10 AB1 SERH2 28 TYRH2 32 5 5 HELIX 11 AB2 GLNH2 62 LYSH2 65 5 4 HELIX 12 AB3 THRH2 87 SERH2 91 5 5 HELIX 13 AB4 SERH2 132 THRH2 136 5 5 HELIX 14 AB5 SERH2 161 ALAH2 163 5 3 HELIX 15 AB6 SERH2 192 LEUH2 194 5 3 HELIX 16 AB7 LYSH2 206 ASNH2 209 5 4 HELIX 17 AB8 SERH3 28 TYRH3 32 5 5 HELIX 18 AB9 GLNH3 62 LYSH3 65 5 4 HELIX 19 AC1 THRH3 87 SERH3 91 5 5 HELIX 20 AC2 SERH3 192 LEUH3 194 5 3 HELIX 21 AC3 LYSH3 206 ASNH3 209 5 4 HELIX 22 AC4 GLUL3 78 ALAL3 82 5 5 HELIX 23 AC5 SERL3 120 LYSL3 125 1 6 HELIX 24 AC6 LYSL3 182 GLUL3 186 1 5 HELIX 25 AC7 GLUL2 78 ALAL2 82 5 5 HELIX 26 AC8 SERL2 120 LYSL2 125 1 6 HELIX 27 AC9 LYSL2 182 LYSL2 187 1 6 SHEET 1 AA1 4 GLNH1 3 GLNH1 6 0 SHEET 2 AA1 4 METH1 18 SERH1 25 -1 O LYSH1 23 N GLNH1 5 SHEET 3 AA1 4 THRH1 78 LEUH1 83 -1 O METH1 81 N ILEH1 20 SHEET 4 AA1 4 LEUH1 70 ASPH1 73 -1 N THRH1 71 O TYRH1 80 SHEET 1 AA2 6 GLUH1 10 VALH1 12 0 SHEET 2 AA2 6 THRH1 112 VALH1 116 1 O THRH1 115 N VALH1 12 SHEET 3 AA2 6 ALAH1 92 GLYH1 99 -1 N ALAH1 92 O VALH1 114 SHEET 4 AA2 6 THRH1 33 SERH1 40 -1 N ASNH1 35 O ALAH1 97 SHEET 5 AA2 6 ASNH1 44 ILEH1 51 -1 O ILEH1 48 N TRPH1 36 SHEET 6 AA2 6 THRH1 58 TYRH1 60 -1 O ASPH1 59 N ARGH1 50 SHEET 1 AA3 4 SERH1 125 LEUH1 129 0 SHEET 2 AA3 4 THRH1 140 TYRH1 150 -1 O LEUH1 146 N PHEH1 127 SHEET 3 AA3 4 TYRH1 181 PROH1 190 -1 O VALH1 189 N ALAH1 141 SHEET 4 AA3 4 VALH1 168 THRH1 170 -1 N HISH1 169 O VALH1 186 SHEET 1 AA4 4 SERH1 125 LEUH1 129 0 SHEET 2 AA4 4 THRH1 140 TYRH1 150 -1 O LEUH1 146 N PHEH1 127 SHEET 3 AA4 4 TYRH1 181 PROH1 190 -1 O VALH1 189 N ALAH1 141 SHEET 4 AA4 4 VALH1 174 LEUH1 175 -1 N VALH1 174 O SERH1 182 SHEET 1 AA5 3 THRH1 156 TRPH1 159 0 SHEET 2 AA5 3 ILEH1 200 HISH1 205 -1 O ASNH1 202 N SERH1 158 SHEET 3 AA5 3 THRH1 210 LYSH1 215 -1 O VALH1 212 N VALH1 203 SHEET 1 AA6 4 LEUL1 4 THRL1 5 0 SHEET 2 AA6 4 VALL1 19 ALAL1 25 -1 O SERL1 24 N THRL1 5 SHEET 3 AA6 4 SERL1 69 ILEL1 74 -1 O TYRL1 70 N CYSL1 23 SHEET 4 AA6 4 PHEL1 61 SERL1 66 -1 N SERL1 64 O SERL1 71 SHEET 1 AA7 6 ILEL1 10 VALL1 13 0 SHEET 2 AA7 6 THRL1 101 ILEL1 105 1 O GLUL1 104 N VALL1 13 SHEET 3 AA7 6 THRL1 84 GLNL1 89 -1 N TYRL1 85 O THRL1 101 SHEET 4 AA7 6 HISL1 33 GLNL1 37 -1 N TYRL1 35 O TYRL1 86 SHEET 5 AA7 6 LYSL1 44 TYRL1 48 -1 O ILEL1 47 N TRPL1 34 SHEET 6 AA7 6 ASNL1 52 LEUL1 53 -1 O ASNL1 52 N TYRL1 48 SHEET 1 AA8 4 ILEL1 10 VALL1 13 0 SHEET 2 AA8 4 THRL1 101 ILEL1 105 1 O GLUL1 104 N VALL1 13 SHEET 3 AA8 4 THRL1 84 GLNL1 89 -1 N TYRL1 85 O THRL1 101 SHEET 4 AA8 4 THRL1 96 PHEL1 97 -1 O THRL1 96 N GLNL1 89 SHEET 1 AA9 4 SERL1 113 PHEL1 117 0 SHEET 2 AA9 4 THRL1 128 PHEL1 138 -1 O LEUL1 134 N PHEL1 115 SHEET 3 AA9 4 TYRL1 172 SERL1 181 -1 O LEUL1 180 N ALAL1 129 SHEET 4 AA9 4 SERL1 158 VALL1 162 -1 N GLNL1 159 O THRL1 177 SHEET 1 AB1 4 ALAL1 152 LEUL1 153 0 SHEET 2 AB1 4 LYSL1 144 VALL1 149 -1 N VALL1 149 O ALAL1 152 SHEET 3 AB1 4 VALL1 190 THRL1 196 -1 O GLUL1 194 N GLNL1 146 SHEET 4 AB1 4 VALL1 204 ASNL1 209 -1 O LYSL1 206 N CYSL1 193 SHEET 1 AB2 4 GLNH2 3 GLNH2 6 0 SHEET 2 AB2 4 METH2 18 SERH2 25 -1 O LYSH2 23 N GLNH2 5 SHEET 3 AB2 4 THRH2 78 LEUH2 83 -1 O METH2 81 N ILEH2 20 SHEET 4 AB2 4 LEUH2 70 ASPH2 73 -1 N THRH2 71 O TYRH2 80 SHEET 1 AB3 6 GLUH2 10 VALH2 12 0 SHEET 2 AB3 6 THRH2 112 VALH2 116 1 O THRH2 115 N VALH2 12 SHEET 3 AB3 6 ALAH2 92 GLYH2 99 -1 N ALAH2 92 O VALH2 114 SHEET 4 AB3 6 THRH2 33 SERH2 40 -1 N ASNH2 35 O ALAH2 97 SHEET 5 AB3 6 ASNH2 44 ASNH2 52 -1 O ILEH2 48 N TRPH2 36 SHEET 6 AB3 6 GLYH2 57 TYRH2 60 -1 O GLYH2 57 N ASNH2 52 SHEET 1 AB4 4 SERH2 125 LEUH2 129 0 SHEET 2 AB4 4 THRH2 140 TYRH2 150 -1 O GLYH2 144 N LEUH2 129 SHEET 3 AB4 4 TYRH2 181 PROH2 190 -1 O VALH2 189 N ALAH2 141 SHEET 4 AB4 4 VALH2 168 THRH2 170 -1 N HISH2 169 O VALH2 186 SHEET 1 AB5 4 SERH2 125 LEUH2 129 0 SHEET 2 AB5 4 THRH2 140 TYRH2 150 -1 O GLYH2 144 N LEUH2 129 SHEET 3 AB5 4 TYRH2 181 PROH2 190 -1 O VALH2 189 N ALAH2 141 SHEET 4 AB5 4 VALH2 174 LEUH2 175 -1 N VALH2 174 O SERH2 182 SHEET 1 AB6 3 THRH2 156 TRPH2 159 0 SHEET 2 AB6 3 TYRH2 199 HISH2 205 -1 O ASNH2 202 N SERH2 158 SHEET 3 AB6 3 THRH2 210 VALH2 216 -1 O LYSH2 214 N CYSH2 201 SHEET 1 AB7 4 GLNH3 3 GLNH3 6 0 SHEET 2 AB7 4 METH3 18 SERH3 25 -1 O LYSH3 23 N GLNH3 5 SHEET 3 AB7 4 THRH3 78 LEUH3 83 -1 O METH3 81 N ILEH3 20 SHEET 4 AB7 4 LEUH3 70 ASPH3 73 -1 N THRH3 71 O TYRH3 80 SHEET 1 AB8 6 GLUH3 10 VALH3 12 0 SHEET 2 AB8 6 THRH3 112 VALH3 116 1 O THRH3 115 N VALH3 12 SHEET 3 AB8 6 ALAH3 92 GLYH3 99 -1 N TYRH3 94 O THRH3 112 SHEET 4 AB8 6 THRH3 33 GLNH3 39 -1 N VALH3 37 O TYRH3 95 SHEET 5 AB8 6 LEUH3 45 ILEH3 51 -1 O GLUH3 46 N LYSH3 38 SHEET 6 AB8 6 THRH3 58 TYRH3 60 -1 O ASPH3 59 N ARGH3 50 SHEET 1 AB9 4 SERH3 125 LEUH3 129 0 SHEET 2 AB9 4 THRH3 140 TYRH3 150 -1 O GLYH3 144 N LEUH3 129 SHEET 3 AB9 4 TYRH3 181 PROH3 190 -1 O VALH3 189 N ALAH3 141 SHEET 4 AB9 4 VALH3 168 THRH3 170 -1 N HISH3 169 O VALH3 186 SHEET 1 AC1 4 SERH3 125 LEUH3 129 0 SHEET 2 AC1 4 THRH3 140 TYRH3 150 -1 O GLYH3 144 N LEUH3 129 SHEET 3 AC1 4 TYRH3 181 PROH3 190 -1 O VALH3 189 N ALAH3 141 SHEET 4 AC1 4 VALH3 174 LEUH3 175 -1 N VALH3 174 O SERH3 182 SHEET 1 AC2 3 THRH3 156 TRPH3 159 0 SHEET 2 AC2 3 TYRH3 199 HISH3 205 -1 O ASNH3 202 N SERH3 158 SHEET 3 AC2 3 THRH3 210 VALH3 216 -1 O VALH3 212 N VALH3 203 SHEET 1 AC3 4 LEUL3 4 SERL3 7 0 SHEET 2 AC3 4 VALL3 19 ALAL3 25 -1 O SERL3 24 N THRL3 5 SHEET 3 AC3 4 SERL3 69 ILEL3 74 -1 O TYRL3 70 N CYSL3 23 SHEET 4 AC3 4 PHEL3 61 SERL3 66 -1 N SERL3 62 O THRL3 73 SHEET 1 AC4 6 ILEL3 10 VALL3 13 0 SHEET 2 AC4 6 THRL3 101 ILEL3 105 1 O GLUL3 104 N VALL3 13 SHEET 3 AC4 6 THRL3 84 GLNL3 89 -1 N TYRL3 85 O THRL3 101 SHEET 4 AC4 6 HISL3 33 GLNL3 37 -1 N GLNL3 37 O THRL3 84 SHEET 5 AC4 6 LYSL3 44 TYRL3 48 -1 O ILEL3 47 N TRPL3 34 SHEET 6 AC4 6 ASNL3 52 LEUL3 53 -1 O ASNL3 52 N TYRL3 48 SHEET 1 AC5 4 ILEL3 10 VALL3 13 0 SHEET 2 AC5 4 THRL3 101 ILEL3 105 1 O GLUL3 104 N VALL3 13 SHEET 3 AC5 4 THRL3 84 GLNL3 89 -1 N TYRL3 85 O THRL3 101 SHEET 4 AC5 4 THRL3 96 PHEL3 97 -1 O THRL3 96 N GLNL3 89 SHEET 1 AC6 4 SERL3 113 PHEL3 117 0 SHEET 2 AC6 4 THRL3 128 PHEL3 138 -1 O LEUL3 134 N PHEL3 115 SHEET 3 AC6 4 TYRL3 172 SERL3 181 -1 O LEUL3 178 N VALL3 131 SHEET 4 AC6 4 SERL3 158 VALL3 162 -1 N SERL3 161 O SERL3 175 SHEET 1 AC7 4 ALAL3 152 LEUL3 153 0 SHEET 2 AC7 4 ALAL3 143 VALL3 149 -1 N VALL3 149 O ALAL3 152 SHEET 3 AC7 4 VALL3 190 HISL3 197 -1 O GLUL3 194 N GLNL3 146 SHEET 4 AC7 4 VALL3 204 ASNL3 209 -1 O LYSL3 206 N CYSL3 193 SHEET 1 AC8 4 LEUL2 4 SERL2 7 0 SHEET 2 AC8 4 VALL2 19 ALAL2 25 -1 O SERL2 24 N THRL2 5 SHEET 3 AC8 4 SERL2 69 ILEL2 74 -1 O LEUL2 72 N METL2 21 SHEET 4 AC8 4 PHEL2 61 SERL2 66 -1 N SERL2 64 O SERL2 71 SHEET 1 AC9 6 ILEL2 10 VALL2 13 0 SHEET 2 AC9 6 THRL2 101 ILEL2 105 1 O GLUL2 104 N VALL2 13 SHEET 3 AC9 6 THRL2 84 GLNL2 89 -1 N TYRL2 85 O THRL2 101 SHEET 4 AC9 6 HISL2 33 GLNL2 37 -1 N GLNL2 37 O THRL2 84 SHEET 5 AC9 6 LYSL2 44 TYRL2 48 -1 O ILEL2 47 N TRPL2 34 SHEET 6 AC9 6 ASNL2 52 LEUL2 53 -1 O ASNL2 52 N TYRL2 48 SHEET 1 AD1 4 ILEL2 10 VALL2 13 0 SHEET 2 AD1 4 THRL2 101 ILEL2 105 1 O GLUL2 104 N VALL2 13 SHEET 3 AD1 4 THRL2 84 GLNL2 89 -1 N TYRL2 85 O THRL2 101 SHEET 4 AD1 4 THRL2 96 PHEL2 97 -1 O THRL2 96 N GLNL2 89 SHEET 1 AD2 4 SERL2 113 PHEL2 117 0 SHEET 2 AD2 4 THRL2 128 PHEL2 138 -1 O LEUL2 134 N PHEL2 115 SHEET 3 AD2 4 TYRL2 172 SERL2 181 -1 O LEUL2 178 N VALL2 131 SHEET 4 AD2 4 SERL2 158 VALL2 162 -1 N SERL2 161 O SERL2 175 SHEET 1 AD3 4 ALAL2 152 LEUL2 153 0 SHEET 2 AD3 4 LYSL2 144 VALL2 149 -1 N VALL2 149 O ALAL2 152 SHEET 3 AD3 4 VALL2 190 THRL2 196 -1 O GLUL2 194 N GLNL2 146 SHEET 4 AD3 4 VALL2 204 ASNL2 209 -1 O VALL2 204 N VALL2 195 SSBOND 1 CYSH1 22 CYSH1 96 1555 1555 2.04 SSBOND 2 CYSH1 145 CYSH1 201 1555 1555 2.03 SSBOND 3 CYSL1 23 CYSL1 87 1555 1555 2.04 SSBOND 4 CYSL1 133 CYSL1 193 1555 1555 2.03 SSBOND 5 CYSH2 22 CYSH2 96 1555 1555 2.03 SSBOND 6 CYSH2 145 CYSH2 201 1555 1555 1.91 SSBOND 7 CYSH3 22 CYSH3 96 1555 1555 2.04 SSBOND 8 CYSH3 145 CYSH3 201 1555 1555 2.03 SSBOND 9 CYSL3 23 CYSL3 87 1555 1555 2.04 SSBOND 10 CYSL3 133 CYSL3 193 1555 1555 2.03 SSBOND 11 CYSL2 23 CYSL2 87 1555 1555 2.04 SSBOND 12 CYSL2 133 CYSL2 193 1555 1555 2.04 CISPEP 1 PHEH1 151 PROH1 152 0 1.55 CISPEP 2 GLUH1 153 PROH1 154 0 -1.96 CISPEP 3 TYRL1 93 PROL1 94 0 2.07 CISPEP 4 TYRL1 139 PROL1 140 0 1.72 CISPEP 5 PHEH2 151 PROH2 152 0 -1.11 CISPEP 6 GLUH2 153 PROH2 154 0 -1.29 CISPEP 7 PHEH3 151 PROH3 152 0 -3.19 CISPEP 8 GLUH3 153 PROH3 154 0 -3.23 CISPEP 9 SERL3 7 PROL3 8 0 -3.99 CISPEP 10 TYRL3 93 PROL3 94 0 -5.44 CISPEP 11 TYRL3 139 PROL3 140 0 1.37 CISPEP 12 SERL2 7 PROL2 8 0 -2.90 CISPEP 13 TYRL2 93 PROL2 94 0 -0.48 CISPEP 14 TYRL2 139 PROL2 140 0 4.76 SITE 1 AC1 7 PHEH1 171 PROH1 172 SERH1 182 LEUH1 183 SITE 2 AC1 7 SERH1 184 SERL1 175 THRL1 177 SITE 1 AC2 4 PROH1 9 GLYH1 111 SERH1 113 PROH1 154 SITE 1 AC3 5 TYRH1 102 TYRL1 31 ASPL1 49 ARGL1 90 SITE 2 AC3 5 ASNL1 91 SITE 1 AC4 3 SERH1 177 ARGL1 141 GLUL1 142 SITE 1 AC5 8 PROH2 14 SERH2 88 VALH2 116 SERH2 117 SITE 2 AC5 8 SERH2 118 ARGL2 107 ALAL2 110 ASPL2 169 SITE 1 AC6 6 ASNH1 55 LYSH1 74 LYSH2 122 GLYH2 123 SITE 2 AC6 6 SERH2 208 THRH2 210 SITE 1 AC7 8 PROH3 172 VALH3 174 SERH3 182 LEUH3 183 SITE 2 AC7 8 SERH3 184 SERL3 161 SERL3 175 THRL3 177 SITE 1 AC8 5 ARGL3 90 ASNL3 91 SERL3 92 TYRL3 93 SITE 2 AC8 5 TRPL3 95 SITE 1 AC9 8 PROH2 172 SERH2 182 LEUH2 183 SERH2 184 SITE 2 AC9 8 GLNL2 159 SERL2 161 SERL2 175 THRL2 177 CRYST1 126.270 126.270 94.850 90.00 90.00 120.00 P 31 9 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 0.007920 0.004572 0.000000 0.00000 SCALE2 0.000000 0.009145 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010543 0.00000