HEADER VIRAL PROTEIN 19-SEP-23 8WFH TITLE CRYSTAL STRUCTURE OF OMICRON BA.4/5 IN COMPLEX WITH A NEUTRALIZING TITLE 2 ANTIBODY SCFV D1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE PROTEIN S1; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: D1 SCFV; COMPND 7 CHAIN: E; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2; SOURCE 4 ORGANISM_TAXID: 2697049; SOURCE 5 GENE: S, 2; SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7110; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: TRICHOPLUSIA; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7110 KEYWDS RBD, ANTIBODY, SCFV, BA.4/5, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR M.ZHANG,N.ZHANG,A.GABIBOV,Y.GUO REVDAT 1 25-SEP-24 8WFH 0 JRNL AUTH M.ZHANG,N.ZHANG,A.GABIBOV,Y.GUO JRNL TITL CRYSTAL STRUCTURE OF OMICRON BA.4/5 IN COMPLEX WITH A JRNL TITL 2 NEUTRALIZING ANTIBODY SCFV D1 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.72 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.72 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.54 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 12062 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.215 REMARK 3 R VALUE (WORKING SET) : 0.211 REMARK 3 FREE R VALUE : 0.250 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.010 REMARK 3 FREE R VALUE TEST SET COUNT : 1207 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 37.5400 - 5.6500 1.00 1234 138 0.2114 0.2624 REMARK 3 2 5.6500 - 4.4900 1.00 1200 133 0.1719 0.1787 REMARK 3 3 4.4900 - 3.9200 1.00 1212 135 0.1819 0.2326 REMARK 3 4 3.9200 - 3.5600 1.00 1203 133 0.1952 0.2172 REMARK 3 5 3.5600 - 3.3100 1.00 1195 134 0.2212 0.2785 REMARK 3 6 3.3100 - 3.1100 1.00 1204 133 0.2448 0.3315 REMARK 3 7 3.1100 - 2.9600 1.00 1184 132 0.2448 0.2676 REMARK 3 8 2.9600 - 2.8300 1.00 1223 136 0.2875 0.3227 REMARK 3 9 2.8300 - 2.7200 0.99 1200 133 0.3469 0.3884 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) : 0.440 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.800 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 : 0.011 3374 REMARK 3 ANGLE : 1.328 4590 REMARK 3 CHIRALITY : 0.073 486 REMARK 3 PLANARITY : 0.009 595 REMARK 3 DIHEDRAL : 17.190 1184 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 8WFH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-SEP-23. REMARK 100 THE DEPOSITION ID IS D_1300040984. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-JUN-23 REMARK 200 TEMPERATURE (KELVIN) : 80 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL18U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97853 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12082 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.720 REMARK 200 RESOLUTION RANGE LOW (A) : 44.330 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 3.290 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.72 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.79 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: SAD 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 (%): 43.78 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 25% W/V PEG 1500, SPG BUFFER/NAOH PH REMARK 280 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 47.75000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E 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 THR A 1 REMARK 465 ASN A 2 REMARK 465 LYS A 146 REMARK 465 LYS A 196 REMARK 465 LYS A 197 REMARK 465 SER A 198 REMARK 465 GLN E 123 REMARK 465 ALA E 124 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 GLU E 1 CG CD OE1 OE2 REMARK 480 GLU E 89 CG CD OE1 OE2 REMARK 480 SER E 133 OG REMARK 480 GLN E 138 CG CD OE1 NE2 REMARK 480 LYS E 166 CE NZ 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 OH TYR E 215 O ASN E 218 2.05 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 TRP A 21 153.33 -48.25 REMARK 500 ASN A 28 55.63 38.89 REMARK 500 ALA A 40 149.57 74.34 REMARK 500 PHE A 45 77.24 -159.12 REMARK 500 ASP A 96 46.83 -97.10 REMARK 500 ARG A 125 117.11 -161.13 REMARK 500 THR A 138 31.15 -145.05 REMARK 500 ASN A 149 -136.59 58.82 REMARK 500 LEU A 186 -169.44 -104.86 REMARK 500 LEU E 18 144.19 -170.22 REMARK 500 GLN E 138 -178.82 -69.94 REMARK 500 THR E 147 -169.73 -125.84 REMARK 500 ASP E 150 -91.29 -126.94 REMARK 500 TYR E 156 57.17 -116.91 REMARK 500 VAL E 175 -55.98 69.23 REMARK 500 ALA E 208 -165.70 -165.21 REMARK 500 ASN E 218 -136.39 47.53 REMARK 500 PHE E 223 -166.23 -119.87 REMARK 500 REMARK 500 REMARK: NULL DBREF 8WFH A 1 198 UNP P0DTC2 SPIKE_SARS2 333 530 DBREF 8WFH E 1 232 PDB 8WFH 8WFH 1 232 SEQADV 8WFH ASP A 7 UNP P0DTC2 GLY 339 VARIANT SEQADV 8WFH PHE A 39 UNP P0DTC2 SER 371 VARIANT SEQADV 8WFH PRO A 41 UNP P0DTC2 SER 373 VARIANT SEQADV 8WFH PHE A 43 UNP P0DTC2 SER 375 VARIANT SEQADV 8WFH ALA A 44 UNP P0DTC2 THR 376 VARIANT SEQADV 8WFH ASN A 73 UNP P0DTC2 ASP 405 VARIANT SEQADV 8WFH SER A 76 UNP P0DTC2 ARG 408 VARIANT SEQADV 8WFH ASN A 85 UNP P0DTC2 LYS 417 VARIANT SEQADV 8WFH LYS A 108 UNP P0DTC2 ASN 440 VARIANT SEQADV 8WFH ARG A 120 UNP P0DTC2 LEU 452 VARIANT SEQADV 8WFH ASN A 145 UNP P0DTC2 SER 477 VARIANT SEQADV 8WFH LYS A 146 UNP P0DTC2 THR 478 VARIANT SEQADV 8WFH ALA A 152 UNP P0DTC2 GLU 484 VARIANT SEQADV 8WFH VAL A 154 UNP P0DTC2 PHE 486 VARIANT SEQADV 8WFH ARG A 166 UNP P0DTC2 GLN 498 VARIANT SEQADV 8WFH TYR A 169 UNP P0DTC2 ASN 501 VARIANT SEQADV 8WFH HIS A 173 UNP P0DTC2 TYR 505 VARIANT SEQRES 1 A 198 THR ASN LEU CYS PRO PHE ASP GLU VAL PHE ASN ALA THR SEQRES 2 A 198 ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE SEQRES 3 A 198 SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN PHE SEQRES 4 A 198 ALA PRO PHE PHE ALA PHE LYS CYS TYR GLY VAL SER PRO SEQRES 5 A 198 THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA SEQRES 6 A 198 ASP SER PHE VAL ILE ARG GLY ASN GLU VAL SER GLN ILE SEQRES 7 A 198 ALA PRO GLY GLN THR GLY ASN ILE ALA ASP TYR ASN TYR SEQRES 8 A 198 LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP SEQRES 9 A 198 ASN SER ASN LYS LEU ASP SER LYS VAL GLY GLY ASN TYR SEQRES 10 A 198 ASN TYR ARG TYR ARG LEU PHE ARG LYS SER ASN LEU LYS SEQRES 11 A 198 PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA SEQRES 12 A 198 GLY ASN LYS PRO CYS ASN GLY VAL ALA GLY VAL ASN CYS SEQRES 13 A 198 TYR PHE PRO LEU GLN SER TYR GLY PHE ARG PRO THR TYR SEQRES 14 A 198 GLY VAL GLY HIS GLN PRO TYR ARG VAL VAL VAL LEU SER SEQRES 15 A 198 PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO SEQRES 16 A 198 LYS LYS SER SEQRES 1 E 232 GLU VAL GLN LEU VAL GLU SER GLY GLY VAL VAL VAL GLN SEQRES 2 E 232 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 E 232 PHE THR PHE ASP ASP TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 E 232 VAL PRO GLY LYS GLY LEU GLU TRP VAL SER LEU ILE SER SEQRES 5 E 232 TRP ASP GLY GLY SER ARG ASP TYR ALA ASP SER VAL LYS SEQRES 6 E 232 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN ALA SEQRES 7 E 232 LEU TYR LEU GLN MET HIS SER LEU ARG LEU GLU ASP THR SEQRES 8 E 232 ALA LEU TYR TYR CYS VAL ARG PRO VAL TYR PRO GLY TYR SEQRES 9 E 232 SER SER SER GLU PHE ASP SER TRP GLY GLN GLY THR MET SEQRES 10 E 232 VAL THR VAL SER SER GLN ALA VAL LEU THR GLN PRO ARG SEQRES 11 E 232 SER VAL SER GLY SER PRO GLY GLN SER VAL THR ILE SER SEQRES 12 E 232 CYS THR GLY THR ILE SER ASP VAL GLY ALA TYR ASN TYR SEQRES 13 E 232 VAL SER TRP TYR GLN GLN HIS PRO GLY LYS ALA PRO LYS SEQRES 14 E 232 LEU ILE ILE TYR ASP VAL ILE GLU ARG PRO SER GLY VAL SEQRES 15 E 232 PRO ASP ARG PHE SER GLY SER LYS SER GLY ASN THR ALA SEQRES 16 E 232 SER LEU THR ILE SER GLY LEU GLN ALA GLU ASP GLU ALA SEQRES 17 E 232 ASP TYR HIS CYS CYS SER TYR ALA GLY ASN TYR THR TRP SEQRES 18 E 232 MET PHE GLY GLY GLY THR THR LEU THR VAL LEU HELIX 1 AA1 PRO A 5 ALA A 12 1 8 HELIX 2 AA2 SER A 17 TRP A 21 5 5 HELIX 3 AA3 TYR A 33 ASN A 38 1 6 HELIX 4 AA4 SER A 51 LEU A 58 5 8 HELIX 5 AA5 ASN A 73 ILE A 78 5 6 HELIX 6 AA6 GLY A 84 ASN A 90 1 7 HELIX 7 AA7 SER A 106 SER A 111 1 6 HELIX 8 AA8 GLY A 170 HIS A 173 5 4 HELIX 9 AA9 THR E 28 TYR E 32 5 5 HELIX 10 AB1 ASP E 62 LYS E 65 5 4 HELIX 11 AB2 ASN E 74 LYS E 76 5 3 HELIX 12 AB3 ARG E 87 THR E 91 5 5 HELIX 13 AB4 ASP E 150 TYR E 154 5 5 HELIX 14 AB5 GLN E 203 GLU E 207 5 5 SHEET 1 AA1 5 ASN A 22 ILE A 26 0 SHEET 2 AA1 5 ASN A 62 ARG A 71 -1 O ALA A 65 N LYS A 24 SHEET 3 AA1 5 PRO A 175 GLU A 184 -1 O VAL A 180 N ASP A 66 SHEET 4 AA1 5 GLY A 99 ASN A 105 -1 N CYS A 100 O LEU A 181 SHEET 5 AA1 5 ALA A 44 TYR A 48 -1 N LYS A 46 O VAL A 101 SHEET 1 AA2 2 CYS A 29 VAL A 30 0 SHEET 2 AA2 2 VAL A 192 CYS A 193 1 O CYS A 193 N CYS A 29 SHEET 1 AA3 2 ARG A 120 ARG A 122 0 SHEET 2 AA3 2 LEU A 160 SER A 162 -1 O GLN A 161 N TYR A 121 SHEET 1 AA4 2 TYR A 141 GLN A 142 0 SHEET 2 AA4 2 CYS A 156 TYR A 157 -1 O TYR A 157 N TYR A 141 SHEET 1 AA5 4 GLN E 3 SER E 7 0 SHEET 2 AA5 4 LEU E 18 SER E 25 -1 O SER E 21 N SER E 7 SHEET 3 AA5 4 ALA E 78 MET E 83 -1 O MET E 83 N LEU E 18 SHEET 4 AA5 4 PHE E 68 ASP E 73 -1 N THR E 69 O GLN E 82 SHEET 1 AA6 6 VAL E 11 VAL E 12 0 SHEET 2 AA6 6 THR E 116 VAL E 120 1 O THR E 119 N VAL E 12 SHEET 3 AA6 6 ALA E 92 PRO E 99 -1 N ALA E 92 O VAL E 118 SHEET 4 AA6 6 MET E 34 VAL E 40 -1 N VAL E 37 O TYR E 95 SHEET 5 AA6 6 GLY E 44 ILE E 51 -1 O GLU E 46 N ARG E 38 SHEET 6 AA6 6 ARG E 58 TYR E 60 -1 O ASP E 59 N LEU E 50 SHEET 1 AA7 4 VAL E 11 VAL E 12 0 SHEET 2 AA7 4 THR E 116 VAL E 120 1 O THR E 119 N VAL E 12 SHEET 3 AA7 4 ALA E 92 PRO E 99 -1 N ALA E 92 O VAL E 118 SHEET 4 AA7 4 PHE E 109 TRP E 112 -1 O SER E 111 N ARG E 98 SHEET 1 AA8 5 SER E 131 GLY E 134 0 SHEET 2 AA8 5 GLY E 226 THR E 230 1 O THR E 227 N VAL E 132 SHEET 3 AA8 5 ASP E 209 TYR E 215 -1 N TYR E 210 O GLY E 226 SHEET 4 AA8 5 VAL E 157 GLN E 162 -1 N SER E 158 O CYS E 213 SHEET 5 AA8 5 LYS E 169 ILE E 172 -1 O LYS E 169 N GLN E 161 SHEET 1 AA9 4 SER E 131 GLY E 134 0 SHEET 2 AA9 4 GLY E 226 THR E 230 1 O THR E 227 N VAL E 132 SHEET 3 AA9 4 ASP E 209 TYR E 215 -1 N TYR E 210 O GLY E 226 SHEET 4 AA9 4 TRP E 221 PHE E 223 -1 O MET E 222 N SER E 214 SHEET 1 AB1 3 VAL E 140 THR E 145 0 SHEET 2 AB1 3 THR E 194 ILE E 199 -1 O ILE E 199 N VAL E 140 SHEET 3 AB1 3 PHE E 186 SER E 191 -1 N SER E 191 O THR E 194 SSBOND 1 CYS A 4 CYS A 29 1555 1555 2.02 SSBOND 2 CYS A 47 CYS A 100 1555 1555 2.07 SSBOND 3 CYS A 59 CYS A 193 1555 1555 2.07 SSBOND 4 CYS A 148 CYS A 156 1555 1555 2.04 SSBOND 5 CYS E 22 CYS E 96 1555 1555 2.03 SSBOND 6 CYS E 144 CYS E 212 1555 1555 2.05 CRYST1 47.570 95.500 53.070 90.00 109.41 90.00 P 1 21 1 2 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 0.021022 0.000000 0.007407 0.00000 SCALE2 0.000000 0.010471 0.000000 0.00000 SCALE3 0.000000 0.000000 0.019979 0.00000