HEADER IMMUNE SYSTEM 18-FEB-14 4OUO TITLE ANTI-BLA G 1 SCFV COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTI BLA G 1 SCFV; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS; SOURCE 3 ORGANISM_TAXID: 9031; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: ROSETTA2; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PDEST566 KEYWDS COCKROACH ALLERGEN, IGG, SCFV ANTIBODY FRAGMENT, BLA G 1, IMMUNE KEYWDS 2 SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR G.A.MUELLER,J.A.ANKNEY,J.GLESNER,T.KHURANA,L.L.EDWARDS,L.C.PEDERSEN, AUTHOR 2 L.PERERA,J.E.SLATER,A.POMES,R.E.LONDON REVDAT 2 09-APR-14 4OUO 1 JRNL REVDAT 1 05-MAR-14 4OUO 0 JRNL AUTH G.A.MUELLER,J.A.ANKNEY,J.GLESNER,T.KHURANA,L.L.EDWARDS, JRNL AUTH 2 L.C.PEDERSEN,L.PERERA,J.E.SLATER,A.POMES,R.E.LONDON JRNL TITL CHARACTERIZATION OF AN ANTI-BLA G 1 SCFV: EPITOPE MAPPING JRNL TITL 2 AND CROSS-REACTIVITY. JRNL REF MOL.IMMUNOL. V. 59 200 2014 JRNL REFN ISSN 0161-5890 JRNL PMID 24667070 JRNL DOI 10.1016/J.MOLIMM.2014.02.003 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.65 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 92.1 REMARK 3 NUMBER OF REFLECTIONS : 19291 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.166 REMARK 3 R VALUE (WORKING SET) : 0.165 REMARK 3 FREE R VALUE : 0.191 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 965 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 29.6583 - 3.4420 0.98 2859 152 0.1457 0.1492 REMARK 3 2 3.4420 - 2.7326 0.98 2795 150 0.1634 0.1994 REMARK 3 3 2.7326 - 2.3873 0.97 2761 142 0.1823 0.2147 REMARK 3 4 2.3873 - 2.1691 0.96 2736 145 0.1786 0.2202 REMARK 3 5 2.1691 - 2.0137 0.95 2654 137 0.1806 0.2110 REMARK 3 6 2.0137 - 1.8950 0.88 2483 132 0.1902 0.2557 REMARK 3 7 1.8950 - 1.8001 0.72 2038 107 0.1998 0.2836 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) : 0.170 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.250 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 22.45 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 1704 REMARK 3 ANGLE : 1.358 2323 REMARK 3 CHIRALITY : 0.081 262 REMARK 3 PLANARITY : 0.006 302 REMARK 3 DIHEDRAL : 11.539 578 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 4OUO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-FEB-14. REMARK 100 THE RCSB ID CODE IS RCSB084970. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-DEC-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : SI-220 REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19780 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.6 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.04800 REMARK 200 FOR THE DATA SET : 18.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83 REMARK 200 COMPLETENESS FOR SHELL (%) : 72.0 REMARK 200 DATA REDUNDANCY IN SHELL : 2.50 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.17600 REMARK 200 FOR SHELL : 4.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MLPHARE REMARK 200 STARTING MODEL: PDB ENTRY 3UX9 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.88 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AMMONIUM SULFATE, 100MM NACL, REMARK 280 50MM TRIS, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K 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 51.25000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.55000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 51.25000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.55000 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 300 REMARK: SCFV BIOLOGICAL UNIT IS A MONOMER BUT DUE TO A TOO SHORT REMARK 300 LINKER BETWEEN THE TWO IGG DOMAINS, THE N-TERMINAL DOMAIN OF ONE REMARK 300 MOLECULE FORMS THE BIOLOGICAL SCFV STRUCTURE WITH THE C-TERMINAL REMARK 300 DOMAIN OF ANOTHER MOLECULE (AND VISE-VERSA) THAT IS RELATED BY A REMARK 300 180 DEGREE ROTATION. 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: 5340 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19470 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -150.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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 BIOMT1 2 -1.000000 0.000000 0.000000 181.75805 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 86.74014 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 GLY A -3 REMARK 465 GLY A 108 REMARK 465 GLN A 109 REMARK 465 SER A 110 REMARK 465 SER A 111 REMARK 465 ARG A 112 REMARK 465 SER A 113 REMARK 465 SER A 114 REMARK 465 SER A 232 REMARK 465 SER A 233 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 SER A -2 OG REMARK 470 SER A 55 OG REMARK 470 ASP A 80 CG OD1 OD2 REMARK 470 ASP A 119 CG OD1 OD2 REMARK 470 THR A 127 OG1 CG2 REMARK 470 LYS A 157 CE NZ REMARK 470 LYS A 178 CG CD CE NZ REMARK 470 LYS A 219 NZ REMARK 470 GLU A 228 CG CD OE1 OE2 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 A 460 O HOH A 479 2.08 REMARK 500 O HOH A 482 O HOH A 490 2.11 REMARK 500 O HOH A 404 O HOH A 536 2.11 REMARK 500 O HOH A 527 O HOH A 536 2.14 REMARK 500 O HOH A 509 O HOH A 513 2.15 REMARK 500 O HOH A 526 O HOH A 539 2.16 REMARK 500 O HOH A 488 O HOH A 515 2.16 REMARK 500 O HOH A 485 O HOH A 534 2.16 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 ASN A 50 -42.05 73.13 REMARK 500 ALA A 83 169.96 175.98 REMARK 500 THR A 142 93.20 -69.55 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 SO4 A 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 304 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 305 DBREF 4OUO A -3 233 PDB 4OUO 4OUO -3 233 SEQRES 1 A 237 GLY SER PHE THR GLN ALA ALA LEU THR GLN PRO SER SER SEQRES 2 A 237 VAL SER ALA ASN PRO GLY GLU THR VAL LYS ILE THR CYS SEQRES 3 A 237 SER GLY GLY GLY SER SER SER ASN TYR GLY TRP PHE GLN SEQRES 4 A 237 GLN LYS SER PRO GLY SER ALA PRO VAL THR VAL ILE TYR SEQRES 5 A 237 ASN ASN ASN ASN ARG PRO SER ASP ILE PRO SER ARG PHE SEQRES 6 A 237 SER GLY SER LYS SER GLY SER THR ALA THR LEU THR ILE SEQRES 7 A 237 THR GLY VAL GLN ALA ASP ASP GLU ALA VAL TYR PHE CYS SEQRES 8 A 237 GLY GLY ARG ASP SER THR TYR ALA GLY MET PHE GLY ALA SEQRES 9 A 237 GLY THR THR LEU THR VAL LEU GLY GLN SER SER ARG SER SEQRES 10 A 237 SER ALA VAL THR LEU ASP GLU SER GLY GLY GLY LEU GLN SEQRES 11 A 237 THR PRO GLY GLY ALA LEU SER LEU VAL CYS LYS ALA SER SEQRES 12 A 237 GLY PHE THR PHE SER VAL TYR ASP MET MET TRP VAL ARG SEQRES 13 A 237 GLN ALA PRO SER LYS GLY LEU GLU TRP VAL ALA GLY ILE SEQRES 14 A 237 GLY ILE THR GLY SER THR TYR TYR ALA SER ALA VAL LYS SEQRES 15 A 237 GLY ARG ALA THR ILE SER ARG ASP ASN GLY GLN SER THR SEQRES 16 A 237 VAL ARG LEU GLN LEU ASN ASN LEU ARG ALA GLU ASP THR SEQRES 17 A 237 GLY THR TYR TYR CYS ALA ARG GLY GLY ALA TYR SER ILE SEQRES 18 A 237 ASN LYS LEU ASP THR TRP GLY GLN GLY THR GLU VAL ILE SEQRES 19 A 237 VAL SER SER HET SO4 A 301 5 HET SO4 A 302 5 HET CL A 303 1 HET CL A 304 1 HET CL A 305 1 HETNAM SO4 SULFATE ION HETNAM CL CHLORIDE ION FORMUL 2 SO4 2(O4 S 2-) FORMUL 4 CL 3(CL 1-) FORMUL 7 HOH *157(H2 O) HELIX 1 1 GLN A 78 GLU A 82 5 5 HELIX 2 2 THR A 142 TYR A 146 5 5 HELIX 3 3 SER A 175 LYS A 178 5 4 HELIX 4 4 ARG A 200 THR A 204 5 5 HELIX 5 5 SER A 216 LEU A 220 5 5 SHEET 1 A 5 SER A 9 ALA A 12 0 SHEET 2 A 5 THR A 102 VAL A 106 1 O THR A 105 N VAL A 10 SHEET 3 A 5 ALA A 83 ARG A 90 -1 N ALA A 83 O LEU A 104 SHEET 4 A 5 GLY A 32 GLN A 36 -1 N PHE A 34 O PHE A 86 SHEET 5 A 5 VAL A 44 ILE A 47 -1 O VAL A 44 N GLN A 35 SHEET 1 B 4 SER A 9 ALA A 12 0 SHEET 2 B 4 THR A 102 VAL A 106 1 O THR A 105 N VAL A 10 SHEET 3 B 4 ALA A 83 ARG A 90 -1 N ALA A 83 O LEU A 104 SHEET 4 B 4 GLY A 96 PHE A 98 -1 O MET A 97 N GLY A 89 SHEET 1 C 3 VAL A 18 SER A 23 0 SHEET 2 C 3 THR A 69 ILE A 74 -1 O LEU A 72 N ILE A 20 SHEET 3 C 3 PHE A 61 SER A 66 -1 N SER A 62 O THR A 73 SHEET 1 D 4 THR A 117 SER A 121 0 SHEET 2 D 4 ALA A 131 SER A 139 -1 O SER A 139 N THR A 117 SHEET 3 D 4 THR A 191 ASN A 197 -1 O LEU A 194 N LEU A 134 SHEET 4 D 4 ALA A 181 ASP A 186 -1 N THR A 182 O GLN A 195 SHEET 1 E 5 THR A 171 TYR A 173 0 SHEET 2 E 5 LEU A 159 ILE A 165 -1 N GLY A 164 O TYR A 172 SHEET 3 E 5 MET A 148 GLN A 153 -1 N TRP A 150 O ALA A 163 SHEET 4 E 5 GLY A 205 ARG A 211 -1 O TYR A 208 N VAL A 151 SHEET 5 E 5 THR A 222 TRP A 223 -1 O THR A 222 N ARG A 211 SHEET 1 F 5 THR A 171 TYR A 173 0 SHEET 2 F 5 LEU A 159 ILE A 165 -1 N GLY A 164 O TYR A 172 SHEET 3 F 5 MET A 148 GLN A 153 -1 N TRP A 150 O ALA A 163 SHEET 4 F 5 GLY A 205 ARG A 211 -1 O TYR A 208 N VAL A 151 SHEET 5 F 5 THR A 227 VAL A 229 -1 O THR A 227 N TYR A 207 SSBOND 1 CYS A 22 CYS A 87 1555 1555 2.06 SITE 1 AC1 5 ASN A 30 ARG A 90 SER A 216 ASN A 218 SITE 2 AC1 5 LYS A 219 SITE 1 AC2 10 ASN A 49 ASN A 50 ASN A 51 THR A 171 SITE 2 AC2 10 TYR A 173 HOH A 423 HOH A 436 HOH A 449 SITE 3 AC2 10 HOH A 495 HOH A 519 SITE 1 AC3 4 ALA A 214 TYR A 215 SER A 216 HOH A 451 SITE 1 AC4 6 ARG A 53 GLY A 166 ILE A 167 THR A 168 SITE 2 AC4 6 SER A 170 HOH A 406 SITE 1 AC5 4 SER A 27 SER A 28 ARG A 90 SER A 92 CRYST1 102.500 51.100 44.900 90.00 105.00 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 0.009756 0.000000 0.002614 0.00000 SCALE2 0.000000 0.019569 0.000000 0.00000 SCALE3 0.000000 0.000000 0.023057 0.00000