HEADER IMMUNE SYSTEM 07-FEB-23 8IA6 TITLE CRYSTAL STRUCTURE OF SCFV ANTIBODY AGAINST PHOSPHOLIPASE A2 OF ECHIS TITLE 2 CARINATUS VENOM COMPND MOL_ID: 1; COMPND 2 MOLECULE: SCFV ANTIBODY; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET-22B(+) KEYWDS SCFV, SNAKE VENOM, PHOSPHOLIPASE A2, ECHIS CARINATUS, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.KUMAR,Z.K.MADNI,D.M.SALUNKE REVDAT 1 14-FEB-24 8IA6 0 JRNL AUTH A.KUMAR,Z.K.MADNI,D.M.SALUNKE JRNL TITL CRYSTAL STRUCTURE OF SCFV ANTIBODY AGAINST PHOSPHOLIPASE A2 JRNL TITL 2 OF ECHIS CARINATUS VENOM JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.75 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) : 2.75 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.23 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5 REMARK 3 NUMBER OF REFLECTIONS : 15192 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.234 REMARK 3 R VALUE (WORKING SET) : 0.232 REMARK 3 FREE R VALUE : 0.264 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010 REMARK 3 FREE R VALUE TEST SET COUNT : 761 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 29.2300 - 4.7000 0.99 3056 192 0.2210 0.2373 REMARK 3 2 4.7000 - 3.7300 0.95 2846 147 0.1968 0.2261 REMARK 3 3 3.7300 - 3.2600 0.85 2579 139 0.2346 0.2753 REMARK 3 4 3.2600 - 2.9600 0.99 2966 143 0.2704 0.3370 REMARK 3 5 2.9600 - 2.7500 0.99 2984 140 0.2912 0.3423 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) : 0.332 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.385 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 33.08 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.08 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 : 0.003 3498 REMARK 3 ANGLE : 0.614 4734 REMARK 3 CHIRALITY : 0.042 520 REMARK 3 PLANARITY : 0.005 601 REMARK 3 DIHEDRAL : 5.799 508 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 8IA6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-FEB-23. REMARK 100 THE DEPOSITION ID IS D_1300035234. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-JUL-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ELETTRA REMARK 200 BEAMLINE : 11.2C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.988 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15296 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750 REMARK 200 RESOLUTION RANGE LOW (A) : 33.350 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1 REMARK 200 DATA REDUNDANCY : 3.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8 REMARK 200 DATA REDUNDANCY IN SHELL : 3.70 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.100 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 (%): 56.57 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M CITRIC ACID, 0.05 M BIS-TRIS REMARK 280 PROPANE PH 5.0, 16% W/V POLYETHYLENE GLYCOL 3350, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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+1/2 REMARK 290 4555 -X+1/2,Y+1/2,-Z+1/2 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 26.90554 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.94000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 84.41006 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 26.90554 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 26.94000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 84.41006 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: MONOMERIC 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 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 ALA A 1 REMARK 465 SER A 117 REMARK 465 GLY A 118 REMARK 465 GLY A 119 REMARK 465 GLY A 120 REMARK 465 GLY A 121 REMARK 465 SER A 122 REMARK 465 GLY A 123 REMARK 465 GLY A 124 REMARK 465 GLY A 125 REMARK 465 GLY A 126 REMARK 465 SER A 127 REMARK 465 GLY A 128 REMARK 465 GLY A 129 REMARK 465 GLY A 130 REMARK 465 GLY A 131 REMARK 465 SER A 132 REMARK 465 LYS A 240 REMARK 465 ARG A 241 REMARK 465 ALA A 242 REMARK 465 ALA A 243 REMARK 465 ALA A 244 REMARK 465 LEU A 245 REMARK 465 GLU A 246 REMARK 465 HIS A 247 REMARK 465 HIS A 248 REMARK 465 HIS A 249 REMARK 465 HIS A 250 REMARK 465 HIS A 251 REMARK 465 HIS A 252 REMARK 465 ALA B 1 REMARK 465 GLY B 118 REMARK 465 GLY B 119 REMARK 465 GLY B 120 REMARK 465 GLY B 121 REMARK 465 SER B 122 REMARK 465 GLY B 123 REMARK 465 GLY B 124 REMARK 465 GLY B 125 REMARK 465 GLY B 126 REMARK 465 SER B 127 REMARK 465 GLY B 128 REMARK 465 GLY B 129 REMARK 465 GLY B 130 REMARK 465 GLY B 131 REMARK 465 SER B 132 REMARK 465 THR B 133 REMARK 465 LYS B 240 REMARK 465 ARG B 241 REMARK 465 ALA B 242 REMARK 465 ALA B 243 REMARK 465 ALA B 244 REMARK 465 LEU B 245 REMARK 465 GLU B 246 REMARK 465 HIS B 247 REMARK 465 HIS B 248 REMARK 465 HIS B 249 REMARK 465 HIS B 250 REMARK 465 HIS B 251 REMARK 465 HIS B 252 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 PRO A 101 CG CD REMARK 470 GLN A 109 CG CD OE1 NE2 REMARK 470 ASP A 134 CG OD1 OD2 REMARK 470 ARG A 157 CG CD NE CZ NH1 NH2 REMARK 470 SER A 200 OG REMARK 470 GLU A 238 CG CD OE1 OE2 REMARK 470 GLN B 109 CG CD OE1 NE2 REMARK 470 SER B 117 OG REMARK 470 ARG B 157 CG CD NE CZ NH1 NH2 REMARK 470 SER B 193 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 THR A 100 150.11 72.90 REMARK 500 SER A 163 -132.46 54.22 REMARK 500 ALA A 184 -39.75 69.31 REMARK 500 ARG A 194 0.70 -69.48 REMARK 500 SER A 200 -51.37 -134.69 REMARK 500 THR B 92 107.68 -58.85 REMARK 500 THR B 100 94.36 59.01 REMARK 500 TYR B 102 -45.96 72.89 REMARK 500 PHE B 104 60.78 62.69 REMARK 500 SER B 163 -121.39 53.88 REMARK 500 ALA B 184 -51.75 69.34 REMARK 500 ALA B 217 -166.74 -162.32 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 A 477 DISTANCE = 5.85 ANGSTROMS REMARK 525 HOH A 478 DISTANCE = 6.01 ANGSTROMS REMARK 525 HOH A 479 DISTANCE = 6.04 ANGSTROMS REMARK 525 HOH A 480 DISTANCE = 6.41 ANGSTROMS REMARK 525 HOH A 481 DISTANCE = 6.64 ANGSTROMS REMARK 525 HOH A 482 DISTANCE = 8.67 ANGSTROMS REMARK 525 HOH B 580 DISTANCE = 6.48 ANGSTROMS REMARK 525 HOH B 581 DISTANCE = 6.50 ANGSTROMS REMARK 525 HOH B 582 DISTANCE = 7.43 ANGSTROMS REMARK 525 HOH B 583 DISTANCE = 8.76 ANGSTROMS DBREF 8IA6 A 1 252 PDB 8IA6 8IA6 1 252 DBREF 8IA6 B 1 252 PDB 8IA6 8IA6 1 252 SEQRES 1 A 252 ALA GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL SEQRES 2 A 252 GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER SEQRES 3 A 252 GLY PHE THR PHE SER SER TYR ALA MET SER TRP VAL ARG SEQRES 4 A 252 GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE SEQRES 5 A 252 SER ASP ASN GLY GLN THR THR THR TYR ALA ASP SER VAL SEQRES 6 A 252 LYS GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN SEQRES 7 A 252 THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP SEQRES 8 A 252 THR ALA VAL TYR TYR CYS ALA LYS THR PRO TYR LEU PHE SEQRES 9 A 252 ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 10 A 252 GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY SEQRES 11 A 252 GLY SER THR ASP ILE GLN MET THR GLN SER PRO SER SER SEQRES 12 A 252 LEU SER ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS SEQRES 13 A 252 ARG ALA SER GLN SER ILE SER SER TYR LEU ASN TRP TYR SEQRES 14 A 252 GLN GLN LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SEQRES 15 A 252 SER ALA SER HIS LEU GLN SER GLY VAL PRO SER ARG PHE SEQRES 16 A 252 SER GLY SER GLY SER GLY THR ASP PHE THR LEU THR ILE SEQRES 17 A 252 SER SER LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS SEQRES 18 A 252 GLN GLN HIS ARG ARG PRO PRO PRO THR PHE GLY GLN GLY SEQRES 19 A 252 THR LYS VAL GLU ILE LYS ARG ALA ALA ALA LEU GLU HIS SEQRES 20 A 252 HIS HIS HIS HIS HIS SEQRES 1 B 252 ALA GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL SEQRES 2 B 252 GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER SEQRES 3 B 252 GLY PHE THR PHE SER SER TYR ALA MET SER TRP VAL ARG SEQRES 4 B 252 GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE SEQRES 5 B 252 SER ASP ASN GLY GLN THR THR THR TYR ALA ASP SER VAL SEQRES 6 B 252 LYS GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN SEQRES 7 B 252 THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP SEQRES 8 B 252 THR ALA VAL TYR TYR CYS ALA LYS THR PRO TYR LEU PHE SEQRES 9 B 252 ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 10 B 252 GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY SEQRES 11 B 252 GLY SER THR ASP ILE GLN MET THR GLN SER PRO SER SER SEQRES 12 B 252 LEU SER ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS SEQRES 13 B 252 ARG ALA SER GLN SER ILE SER SER TYR LEU ASN TRP TYR SEQRES 14 B 252 GLN GLN LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SEQRES 15 B 252 SER ALA SER HIS LEU GLN SER GLY VAL PRO SER ARG PHE SEQRES 16 B 252 SER GLY SER GLY SER GLY THR ASP PHE THR LEU THR ILE SEQRES 17 B 252 SER SER LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS SEQRES 18 B 252 GLN GLN HIS ARG ARG PRO PRO PRO THR PHE GLY GLN GLY SEQRES 19 B 252 THR LYS VAL GLU ILE LYS ARG ALA ALA ALA LEU GLU HIS SEQRES 20 B 252 HIS HIS HIS HIS HIS HET GOL A 301 6 HET GOL A 302 6 HET GOL A 303 6 HET GOL A 304 6 HET GOL A 305 6 HET PEG A 306 7 HET GOL B 401 6 HET PEG B 402 7 HET PEG B 403 7 HETNAM GOL GLYCEROL HETNAM PEG DI(HYDROXYETHYL)ETHER HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 3 GOL 6(C3 H8 O3) FORMUL 8 PEG 3(C4 H10 O3) FORMUL 12 HOH *165(H2 O) HELIX 1 AA1 THR A 29 TYR A 33 5 5 HELIX 2 AA2 ARG A 88 THR A 92 5 5 HELIX 3 AA3 GLN A 212 PHE A 216 5 5 HELIX 4 AA4 THR B 29 TYR B 33 5 5 HELIX 5 AA5 ARG B 88 THR B 92 5 5 HELIX 6 AA6 GLN B 212 PHE B 216 5 5 SHEET 1 AA1 4 GLN A 4 SER A 8 0 SHEET 2 AA1 4 LEU A 19 SER A 26 -1 O SER A 22 N SER A 8 SHEET 3 AA1 4 THR A 79 MET A 84 -1 O MET A 84 N LEU A 19 SHEET 4 AA1 4 PHE A 69 ASP A 74 -1 N THR A 70 O GLN A 83 SHEET 1 AA2 6 GLY A 11 VAL A 13 0 SHEET 2 AA2 6 THR A 111 VAL A 115 1 O THR A 114 N GLY A 11 SHEET 3 AA2 6 ALA A 93 LYS A 99 -1 N TYR A 95 O THR A 111 SHEET 4 AA2 6 MET A 35 GLN A 40 -1 N VAL A 38 O TYR A 96 SHEET 5 AA2 6 LEU A 46 ILE A 52 -1 O GLU A 47 N ARG A 39 SHEET 6 AA2 6 THR A 59 TYR A 61 -1 O THR A 60 N SER A 51 SHEET 1 AA3 4 MET A 137 SER A 140 0 SHEET 2 AA3 4 VAL A 152 ALA A 158 -1 O ARG A 157 N THR A 138 SHEET 3 AA3 4 ASP A 203 ILE A 208 -1 O LEU A 206 N ILE A 154 SHEET 4 AA3 4 PHE A 195 GLY A 199 -1 N SER A 196 O THR A 207 SHEET 1 AA4 6 SER A 143 SER A 145 0 SHEET 2 AA4 6 THR A 235 GLU A 238 1 O GLU A 238 N LEU A 144 SHEET 3 AA4 6 ALA A 217 GLN A 223 -1 N ALA A 217 O VAL A 237 SHEET 4 AA4 6 LEU A 166 GLN A 171 -1 N GLN A 171 O THR A 218 SHEET 5 AA4 6 LYS A 178 TYR A 182 -1 O LYS A 178 N GLN A 170 SHEET 6 AA4 6 HIS A 186 LEU A 187 -1 O HIS A 186 N TYR A 182 SHEET 1 AA5 4 SER A 143 SER A 145 0 SHEET 2 AA5 4 THR A 235 GLU A 238 1 O GLU A 238 N LEU A 144 SHEET 3 AA5 4 ALA A 217 GLN A 223 -1 N ALA A 217 O VAL A 237 SHEET 4 AA5 4 THR A 230 PHE A 231 -1 O THR A 230 N GLN A 223 SHEET 1 AA6 4 GLN B 4 SER B 8 0 SHEET 2 AA6 4 LEU B 19 SER B 26 -1 O ALA B 24 N LEU B 6 SHEET 3 AA6 4 THR B 79 MET B 84 -1 O LEU B 82 N LEU B 21 SHEET 4 AA6 4 PHE B 69 ASP B 74 -1 N THR B 70 O GLN B 83 SHEET 1 AA7 6 LEU B 12 VAL B 13 0 SHEET 2 AA7 6 THR B 111 VAL B 115 1 O THR B 114 N VAL B 13 SHEET 3 AA7 6 ALA B 93 LYS B 99 -1 N TYR B 95 O THR B 111 SHEET 4 AA7 6 MET B 35 GLN B 40 -1 N VAL B 38 O TYR B 96 SHEET 5 AA7 6 LEU B 46 ILE B 52 -1 O ILE B 52 N MET B 35 SHEET 6 AA7 6 THR B 59 TYR B 61 -1 O THR B 60 N SER B 51 SHEET 1 AA8 4 LEU B 12 VAL B 13 0 SHEET 2 AA8 4 THR B 111 VAL B 115 1 O THR B 114 N VAL B 13 SHEET 3 AA8 4 ALA B 93 LYS B 99 -1 N TYR B 95 O THR B 111 SHEET 4 AA8 4 TYR B 106 TRP B 107 -1 O TYR B 106 N LYS B 99 SHEET 1 AA9 4 MET B 137 SER B 140 0 SHEET 2 AA9 4 VAL B 152 ALA B 158 -1 O THR B 155 N SER B 140 SHEET 3 AA9 4 ASP B 203 ILE B 208 -1 O PHE B 204 N CYS B 156 SHEET 4 AA9 4 PHE B 195 SER B 200 -1 N SER B 196 O THR B 207 SHEET 1 AB1 6 SER B 143 SER B 145 0 SHEET 2 AB1 6 THR B 235 GLU B 238 1 O GLU B 238 N LEU B 144 SHEET 3 AB1 6 THR B 218 GLN B 223 -1 N TYR B 219 O THR B 235 SHEET 4 AB1 6 LEU B 166 GLN B 171 -1 N TYR B 169 O TYR B 220 SHEET 5 AB1 6 LYS B 178 TYR B 182 -1 O LYS B 178 N GLN B 170 SHEET 6 AB1 6 HIS B 186 LEU B 187 -1 O HIS B 186 N TYR B 182 SHEET 1 AB2 4 SER B 143 SER B 145 0 SHEET 2 AB2 4 THR B 235 GLU B 238 1 O GLU B 238 N LEU B 144 SHEET 3 AB2 4 THR B 218 GLN B 223 -1 N TYR B 219 O THR B 235 SHEET 4 AB2 4 THR B 230 PHE B 231 -1 O THR B 230 N GLN B 223 SSBOND 1 CYS A 23 CYS A 97 1555 1555 2.04 SSBOND 2 CYS A 156 CYS A 221 1555 1555 2.04 SSBOND 3 CYS B 23 CYS B 97 1555 1555 2.04 SSBOND 4 CYS B 156 CYS B 221 1555 1555 2.04 CISPEP 1 SER A 140 PRO A 141 0 -3.34 CISPEP 2 PRO A 227 PRO A 228 0 0.68 CISPEP 3 SER B 140 PRO B 141 0 -2.49 CISPEP 4 PRO B 227 PRO B 228 0 1.13 CRYST1 66.890 53.880 169.326 90.00 94.43 90.00 I 1 2 1 8 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 0.014950 0.000000 0.001158 0.00000 SCALE2 0.000000 0.018560 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005923 0.00000