HEADER IMMUNE SYSTEM 08-NOV-22 8F2T TITLE ANTIBODY FAB DIRECTED AGAINST SARS-COV-2 SPIKE PROTEIN RECEPTOR TITLE 2 BINDING DOMAIN (RBD) COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB HEAVY CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB LIGHT CHAIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL: HEK293; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_CELL: HEK293 KEYWDS ANTIBODY, FAB FRAGMENT, IMMUNOGLOBULIN, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.C.-H.CHEN REVDAT 1 13-DEC-23 8F2T 0 JRNL AUTH J.C.-H.CHEN JRNL TITL ANTIBODY FAB DIRECTED AGAINST SARS-COV-2 SPIKE PROTEIN JRNL TITL 2 RECEPTOR BINDING DOMAIN (RBD) JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.12 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) : 2.12 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.34 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 3 NUMBER OF REFLECTIONS : 22958 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.208 REMARK 3 R VALUE (WORKING SET) : 0.203 REMARK 3 FREE R VALUE : 0.257 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.670 REMARK 3 FREE R VALUE TEST SET COUNT : 1991 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 28.3400 - 5.1100 1.00 1558 148 0.1813 0.1991 REMARK 3 2 5.1100 - 4.0600 1.00 1516 144 0.1599 0.1992 REMARK 3 3 4.0600 - 3.5500 1.00 1521 145 0.1869 0.2373 REMARK 3 4 3.5500 - 3.2200 1.00 1513 144 0.2051 0.2611 REMARK 3 5 3.2200 - 2.9900 1.00 1512 143 0.2186 0.2767 REMARK 3 6 2.9900 - 2.8200 1.00 1505 144 0.2172 0.3275 REMARK 3 7 2.8200 - 2.6800 1.00 1498 142 0.2187 0.2614 REMARK 3 8 2.6700 - 2.5600 1.00 1489 142 0.2439 0.3158 REMARK 3 9 2.5600 - 2.4600 1.00 1521 144 0.2263 0.2787 REMARK 3 10 2.4600 - 2.3800 1.00 1496 143 0.2333 0.3046 REMARK 3 11 2.3700 - 2.3000 1.00 1502 143 0.2239 0.3058 REMARK 3 12 2.3000 - 2.2400 1.00 1483 141 0.2361 0.3344 REMARK 3 13 2.2300 - 2.1800 1.00 1505 140 0.2607 0.3298 REMARK 3 14 2.1800 - 2.1200 0.89 1348 128 0.3072 0.4090 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) : 0.311 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.421 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 34.19 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.34 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 : 0.008 3306 REMARK 3 ANGLE : 1.017 4511 REMARK 3 CHIRALITY : 0.059 513 REMARK 3 PLANARITY : 0.007 579 REMARK 3 DIHEDRAL : 6.086 463 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 8F2T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-NOV-22. REMARK 100 THE DEPOSITION ID IS D_1000269716. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-NOV-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 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) : 0.97934 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 : 23030 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.110 REMARK 200 RESOLUTION RANGE LOW (A) : 28.340 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 200 DATA REDUNDANCY : 6.590 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.11 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16 REMARK 200 COMPLETENESS FOR SHELL (%) : 65.4 REMARK 200 DATA REDUNDANCY IN SHELL : 5.50 REMARK 200 R MERGE FOR SHELL (I) : 0.86200 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: 7ORA REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 44.83 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, 25 %, 0.1 M TRIS, 0.2 M REMARK 280 SODIUM CHLORIDE, PH 8.5, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z 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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 46.97050 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.43400 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 46.97050 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.43400 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: 3440 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18600 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 SER A 220 REMARK 465 CYS A 221 REMARK 465 GLY B 212 REMARK 465 GLU B 213 REMARK 465 CYS B 214 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 TYR A 104 OH TYR B 36 2.08 REMARK 500 O HOH A 332 O HOH B 336 2.14 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 LEU A 183 CA - CB - CG ANGL. DEV. = 14.8 DEGREES REMARK 500 CYS B 194 CA - CB - SG ANGL. DEV. = 6.7 DEGREES 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 A 100 -4.03 56.54 REMARK 500 TRP A 103 100.06 66.62 REMARK 500 PHE A 105 73.14 50.67 REMARK 500 ASP A 149 68.30 69.78 REMARK 500 ASN A 209 67.66 14.79 REMARK 500 SER B 30 -128.28 59.75 REMARK 500 ALA B 51 -31.47 69.01 REMARK 500 ALA B 190 -60.87 -109.36 REMARK 500 REMARK 500 REMARK: NULL DBREF 8F2T A 1 221 PDB 8F2T 8F2T 1 221 DBREF 8F2T B 1 214 PDB 8F2T 8F2T 1 214 SEQRES 1 A 221 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 A 221 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 221 PHE THR VAL GLY SER ASN TYR MET SER TRP VAL ARG GLN SEQRES 4 A 221 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER VAL ILE TYR SEQRES 5 A 221 SER GLY GLY SER THR TYR TYR ALA ASP SER VAL LYS GLY SEQRES 6 A 221 ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR LEU SEQRES 7 A 221 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 A 221 VAL TYR TYR CYS ALA ARG GLY SER SER GLY ALA TRP TYR SEQRES 9 A 221 PHE ASP LEU TRP GLY ARG GLY THR LEU VAL THR VAL SER SEQRES 10 A 221 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 A 221 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 A 221 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 A 221 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 A 221 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 A 221 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 A 221 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 A 221 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO ALA SER CYS SEQRES 1 B 214 GLU ILE VAL MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 B 214 SER VAL GLY ASP SER VAL THR ILE THR CYS GLN ALA SER SEQRES 3 B 214 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 B 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP ALA SER SEQRES 5 B 214 ASN LEU GLU THR GLY VAL PRO SER ARG PHE SER GLY GLY SEQRES 6 B 214 GLY SER GLY THR ASP PHE THR LEU THR ILE THR SER LEU SEQRES 7 B 214 GLN PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 B 214 ASP ASN PHE PRO PRO THR PHE GLY PRO GLY THR LYS VAL SEQRES 9 B 214 ASP ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 B 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 B 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 B 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 B 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER ALA SEQRES 14 B 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 B 214 ALA ALA ASP TYR ALA ALA HIS ALA VAL TYR ALA CYS GLU SEQRES 16 B 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 B 214 PHE ASN ARG GLY GLU CYS FORMUL 3 HOH *88(H2 O) HELIX 1 AA1 THR A 28 ASN A 32 5 5 HELIX 2 AA2 ARG A 86 THR A 90 5 5 HELIX 3 AA3 SER A 161 ALA A 163 5 3 HELIX 4 AA4 SER A 192 LEU A 194 5 3 HELIX 5 AA5 LYS A 206 ASN A 209 5 4 HELIX 6 AA6 GLN B 79 ILE B 83 5 5 HELIX 7 AA7 SER B 121 LYS B 126 1 6 HELIX 8 AA8 ALA B 183 ALA B 187 1 5 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O SER A 21 N SER A 7 SHEET 3 AA1 4 THR A 77 MET A 82 -1 O MET A 82 N LEU A 18 SHEET 4 AA1 4 PHE A 67 ASP A 72 -1 N THR A 68 O GLN A 81 SHEET 1 AA2 6 LEU A 11 VAL A 12 0 SHEET 2 AA2 6 THR A 112 VAL A 116 1 O THR A 115 N VAL A 12 SHEET 3 AA2 6 ALA A 91 GLY A 98 -1 N TYR A 93 O THR A 112 SHEET 4 AA2 6 TYR A 33 ALA A 40 -1 N VAL A 37 O TYR A 94 SHEET 5 AA2 6 GLY A 44 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AA2 6 THR A 57 TYR A 59 -1 O TYR A 58 N VAL A 50 SHEET 1 AA3 4 LEU A 11 VAL A 12 0 SHEET 2 AA3 4 THR A 112 VAL A 116 1 O THR A 115 N VAL A 12 SHEET 3 AA3 4 ALA A 91 GLY A 98 -1 N TYR A 93 O THR A 112 SHEET 4 AA3 4 LEU A 107 TRP A 108 -1 O LEU A 107 N ARG A 97 SHEET 1 AA4 4 SER A 125 LEU A 129 0 SHEET 2 AA4 4 THR A 140 TYR A 150 -1 O LEU A 146 N PHE A 127 SHEET 3 AA4 4 TYR A 181 PRO A 190 -1 O LEU A 183 N VAL A 147 SHEET 4 AA4 4 VAL A 168 THR A 170 -1 N HIS A 169 O VAL A 186 SHEET 1 AA5 4 THR A 136 SER A 137 0 SHEET 2 AA5 4 THR A 140 TYR A 150 -1 O THR A 140 N SER A 137 SHEET 3 AA5 4 TYR A 181 PRO A 190 -1 O LEU A 183 N VAL A 147 SHEET 4 AA5 4 VAL A 174 LEU A 175 -1 N VAL A 174 O SER A 182 SHEET 1 AA6 3 THR A 156 TRP A 159 0 SHEET 2 AA6 3 ILE A 200 HIS A 205 -1 O ASN A 202 N SER A 158 SHEET 3 AA6 3 THR A 210 LYS A 215 -1 O VAL A 212 N VAL A 203 SHEET 1 AA7 4 MET B 4 SER B 7 0 SHEET 2 AA7 4 VAL B 19 ALA B 25 -1 O GLN B 24 N THR B 5 SHEET 3 AA7 4 ASP B 70 ILE B 75 -1 O LEU B 73 N ILE B 21 SHEET 4 AA7 4 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74 SHEET 1 AA8 6 SER B 10 ALA B 13 0 SHEET 2 AA8 6 THR B 102 ILE B 106 1 O ASP B 105 N LEU B 11 SHEET 3 AA8 6 ALA B 84 GLN B 90 -1 N ALA B 84 O VAL B 104 SHEET 4 AA8 6 LEU B 33 GLN B 38 -1 N TYR B 36 O TYR B 87 SHEET 5 AA8 6 LYS B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AA8 6 ASN B 53 LEU B 54 -1 O ASN B 53 N TYR B 49 SHEET 1 AA9 4 SER B 10 ALA B 13 0 SHEET 2 AA9 4 THR B 102 ILE B 106 1 O ASP B 105 N LEU B 11 SHEET 3 AA9 4 ALA B 84 GLN B 90 -1 N ALA B 84 O VAL B 104 SHEET 4 AA9 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90 SHEET 1 AB1 4 SER B 114 PHE B 118 0 SHEET 2 AB1 4 THR B 129 PHE B 139 -1 O ASN B 137 N SER B 114 SHEET 3 AB1 4 TYR B 173 SER B 182 -1 O LEU B 179 N VAL B 132 SHEET 4 AB1 4 SER B 159 VAL B 163 -1 N GLN B 160 O THR B 178 SHEET 1 AB2 4 ALA B 153 LEU B 154 0 SHEET 2 AB2 4 LYS B 145 VAL B 150 -1 N VAL B 150 O ALA B 153 SHEET 3 AB2 4 VAL B 191 THR B 197 -1 O GLU B 195 N GLN B 147 SHEET 4 AB2 4 VAL B 205 ASN B 210 -1 O VAL B 205 N VAL B 196 SSBOND 1 CYS A 22 CYS A 95 1555 1555 2.04 SSBOND 2 CYS A 145 CYS A 201 1555 1555 2.05 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.07 SSBOND 4 CYS B 134 CYS B 194 1555 1555 2.05 CISPEP 1 PHE A 151 PRO A 152 0 -6.65 CISPEP 2 GLU A 153 PRO A 154 0 0.01 CISPEP 3 SER B 7 PRO B 8 0 -8.58 CISPEP 4 PHE B 94 PRO B 95 0 -2.94 CISPEP 5 TYR B 140 PRO B 141 0 -0.31 CRYST1 93.941 60.868 73.005 90.00 98.75 90.00 C 1 2 1 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 0.010645 0.000000 0.001639 0.00000 SCALE2 0.000000 0.016429 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013859 0.00000