HEADER IMMUNE SYSTEM 13-SEP-24 9DMF TITLE CRYSTAL STRUCTURE OF LJF-0085 FAB, A NON-HUMAN PRIMATE ANTIBODY TITLE 2 TARGETS HIV-1 ENVELOPE PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: LJF-0085 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: LJF-0085 FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 3 ORGANISM_TAXID: 9544; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 9 ORGANISM_TAXID: 9544; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV-1 ENVELOPE ANTIBODY, HIV CD4 BINDING SITE ANTIBODY, NON-HUMAN KEYWDS 2 PRIMATE ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR X.LIN,I.A.WILSON REVDAT 1 23-JUL-25 9DMF 0 JRNL AUTH F.A.SCHLEICH,S.BALE,J.GUENAGA,G.OZOROWSKI,M.ADORI,X.LIN, JRNL AUTH 2 X.CASTRO DOPICO,R.WILSON,M.CHERNYSHEV,A.T.COTGREAVE, JRNL AUTH 3 M.MANDOLESI,J.CLUFF,E.D.DOYLE,L.M.SEWALL,W.H.LEE,S.ZHANG, JRNL AUTH 4 S.O'DELL,B.S.HEALY,D.LIM,V.R.LEWIS,E.BEN-AKIVA,D.J.IRVINE, JRNL AUTH 5 N.A.DORIA-ROSE,M.CORCORAN,D.CARNATHAN,G.SILVESTRI, JRNL AUTH 6 I.A.WILSON,A.B.WARD,G.B.KARLSSON HEDESTAM,R.T.WYATT JRNL TITL VACCINATION OF NONHUMAN PRIMATES ELICITS A BROADLY JRNL TITL 2 NEUTRALIZING ANTIBODY LINEAGE TARGETING A QUATERNARY EPITOPE JRNL TITL 3 ON THE HIV-1 ENV TRIMER. JRNL REF IMMUNITY V. 58 1598 2025 JRNL REFN ISSN 1074-7613 JRNL PMID 40339576 JRNL DOI 10.1016/J.IMMUNI.2025.04.010 REMARK 2 REMARK 2 RESOLUTION. 1.48 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) : 1.48 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 78472 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.189 REMARK 3 R VALUE (WORKING SET) : 0.188 REMARK 3 FREE R VALUE : 0.200 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.550 REMARK 3 FREE R VALUE TEST SET COUNT : 1998 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 29.6800 - 3.5700 1.00 5786 151 0.1664 0.1754 REMARK 3 2 3.5700 - 2.8300 1.00 5559 144 0.1871 0.1847 REMARK 3 3 2.8300 - 2.4700 1.00 5522 145 0.1998 0.1980 REMARK 3 4 2.4700 - 2.2500 1.00 5481 143 0.1993 0.1951 REMARK 3 5 2.2500 - 2.0900 1.00 5472 143 0.1918 0.2287 REMARK 3 6 2.0900 - 1.9600 1.00 5445 143 0.1905 0.2135 REMARK 3 7 1.9600 - 1.8600 1.00 5443 143 0.1896 0.2213 REMARK 3 8 1.8600 - 1.7800 1.00 5417 141 0.1981 0.2169 REMARK 3 9 1.7800 - 1.7200 1.00 5422 142 0.1900 0.1909 REMARK 3 10 1.7200 - 1.6600 1.00 5413 141 0.1929 0.1969 REMARK 3 11 1.6600 - 1.6000 1.00 5412 141 0.1915 0.2129 REMARK 3 12 1.6000 - 1.5600 1.00 5395 141 0.2011 0.2403 REMARK 3 13 1.5600 - 1.5200 1.00 5388 141 0.2093 0.2191 REMARK 3 14 1.5200 - 1.4800 0.99 5319 139 0.2242 0.2674 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) : 0.139 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.515 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 14.93 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.64 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 : 0.014 3422 REMARK 3 ANGLE : 1.371 4660 REMARK 3 CHIRALITY : 0.121 518 REMARK 3 PLANARITY : 0.011 603 REMARK 3 DIHEDRAL : 13.759 1228 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 9DMF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1000288401. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 26-FEB-24 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 : NSLS-II REMARK 200 BEAMLINE : 17-ID-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793 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 : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78472 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.480 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 : 13.50 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.08000 REMARK 200 FOR THE DATA SET : 21.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.52 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) : 0.67000 REMARK 200 FOR SHELL : 3.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.46 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.04 M POTASSIUM DIHYDROGEN PHOSPHATE, REMARK 280 20% (V/V) GLYCEROL, AND 16% (W/V) POLYETHYLENE GLYCOL 8000, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K 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 26.72850 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.62850 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.67750 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.62850 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.72850 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.67750 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3920 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20080 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L 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 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 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 O HOH H 540 O HOH H 547 1.88 REMARK 500 O HOH H 318 O HOH H 477 1.94 REMARK 500 O HOH H 338 O HOH H 384 2.07 REMARK 500 O HOH L 329 O HOH L 349 2.08 REMARK 500 O HOH H 309 O HOH H 497 2.13 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 SER H 15 -14.60 84.64 REMARK 500 ASP H 30 -157.03 -130.96 REMARK 500 ALA L 51 -41.40 70.35 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH H 556 DISTANCE = 6.37 ANGSTROMS REMARK 525 HOH H 557 DISTANCE = 6.51 ANGSTROMS DBREF 9DMF H 1 217 PDB 9DMF 9DMF 1 217 DBREF 9DMF L 1 214 PDB 9DMF 9DMF 1 214 SEQRES 1 H 227 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 227 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 227 GLY SER ILE ASP ASP TYR PHE TRP ASN TRP VAL ARG GLN SEQRES 4 H 227 PRO PRO GLY LYS PRO LEU GLU CYS ILE GLY TYR ILE PHE SEQRES 5 H 227 GLY ARG GLY GLY GLY THR LYS TYR ASN PRO SER LEU ASP SEQRES 6 H 227 ASN ARG VAL THR ILE SER THR ASP THR PRO ASN GLN PHE SEQRES 7 H 227 SER LEU LYS LEU ARG SER VAL THR VAL ALA ASP THR ALA SEQRES 8 H 227 ILE TYR TYR CYS ALA ARG TRP ASN LEU TYR ASP ASP ASP SEQRES 9 H 227 PHE GLY TYR ASN SER PHE ALA VAL TRP GLY ARG GLY VAL SEQRES 10 H 227 LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 H 227 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 H 227 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 H 227 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 H 227 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 H 227 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 H 227 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 H 227 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 H 227 GLU PRO LYS SER CYS ASP SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY ASP THR VAL THR ILE THR CYS GLN ALA ARG SEQRES 3 L 214 HIS ALA VAL GLY LYS ASN LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY ARG GLY PRO GLN LEU LEU ILE TYR MET ALA SER SEQRES 5 L 214 SER ARG HIS SER GLY VAL PRO SER ARG PHE ARG GLY SER SEQRES 6 L 214 GLY SER GLY ARG GLU PHE THR LEU THR ILE ASN ASN LEU SEQRES 7 L 214 GLN PRO GLU ASP PHE ALA THR TYR SER CYS GLN GLN GLY SEQRES 8 L 214 TYR THR TYR PRO TRP THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 L 214 GLU MET LYS GLY ALA VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU ARG SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS FORMUL 3 HOH *441(H2 O) HELIX 1 AA1 PRO H 61 ASP H 64 5 4 HELIX 2 AA2 THR H 83 THR H 87 5 5 HELIX 3 AA3 SER H 156 ALA H 158 5 3 HELIX 4 AA4 SER H 187 THR H 191 5 5 HELIX 5 AA5 LYS H 201 ASN H 204 5 4 HELIX 6 AA6 GLN L 79 PHE L 83 5 5 HELIX 7 AA7 SER L 121 LYS L 126 1 6 HELIX 8 AA8 LYS L 183 LYS L 188 1 6 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O THR H 21 N SER H 7 SHEET 3 AA1 4 GLN H 76 LEU H 81 -1 O PHE H 77 N CYS H 22 SHEET 4 AA1 4 VAL H 67 THR H 73 -1 N SER H 70 O SER H 78 SHEET 1 AA2 6 LEU H 11 VAL H 12 0 SHEET 2 AA2 6 VAL H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA2 6 ALA H 88 TRP H 95 -1 N TYR H 90 O VAL H 107 SHEET 4 AA2 6 PHE H 33 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA2 6 GLU H 46 PHE H 52 -1 O ILE H 51 N TRP H 34 SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O LYS H 58 N TYR H 50 SHEET 1 AA3 4 LEU H 11 VAL H 12 0 SHEET 2 AA3 4 VAL H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA3 4 ALA H 88 TRP H 95 -1 N TYR H 90 O VAL H 107 SHEET 4 AA3 4 PHE H 100G TRP H 103 -1 O VAL H 102 N ARG H 94 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 SER H 120 LEU H 124 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145 SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA6 3 THR H 151 TRP H 154 0 SHEET 2 AA6 3 TYR H 194 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA6 3 THR H 205 VAL H 211 -1 O VAL H 207 N VAL H 198 SHEET 1 AA7 4 MET L 4 SER L 7 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O GLN L 24 N THR L 5 SHEET 3 AA7 4 GLU L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA7 4 PHE L 62 SER L 67 -1 N ARG L 63 O THR L 74 SHEET 1 AA8 6 SER L 10 ALA L 13 0 SHEET 2 AA8 6 THR L 102 MET L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AA8 6 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AA8 6 LEU L 33 LYS L 39 -1 N ASN L 34 O GLN L 89 SHEET 5 AA8 6 ARG L 42 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA8 6 SER L 53 ARG L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AA9 4 SER L 114 PHE L 118 0 SHEET 2 AA9 4 THR L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AA9 4 TYR L 173 SER L 182 -1 O LEU L 175 N LEU L 136 SHEET 4 AA9 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB1 4 ALA L 153 LEU L 154 0 SHEET 2 AB1 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB1 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AB1 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.14 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.04 SSBOND 3 CYS H 216 CYS L 214 1555 1555 2.03 SSBOND 4 CYS L 23 CYS L 88 1555 1555 2.10 SSBOND 5 CYS L 134 CYS L 194 1555 1555 2.02 CISPEP 1 PHE H 146 PRO H 147 0 -10.55 CISPEP 2 GLU H 148 PRO H 149 0 1.79 CISPEP 3 SER L 7 PRO L 8 0 -3.19 CISPEP 4 TYR L 94 PRO L 95 0 -0.77 CISPEP 5 TYR L 140 PRO L 141 0 2.43 CRYST1 53.457 65.355 133.257 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 0.018707 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015301 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007504 0.00000