HEADER IMMUNE SYSTEM 28-FEB-25 9NJY TITLE TERMINAL TWO DOMAINS OF CLFA002 WITH BOUND FAB OF AZD7745 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CLUMPING FACTOR A; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: FIBRINOGEN RECEPTOR A,FIBRINOGEN-BINDING PROTEIN A; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 OTHER_DETAILS: CELL SURFACE-ASSOCIATED PROTEIN IMPLICATED IN COMPND 8 VIRULENCE. PROMOTES BACTERIAL ATTACHMENT EXCLUSIVELY TO THE GAMMA- COMPND 9 CHAIN OF HUMAN FIBRINOGEN. INDUCES FORMATION OF BACTERIAL CLUMPS, COMPND 10 WHICH DIMINISH THE ABILITY OF GROUP IIA PHOSPHOLIPASE A2 TO CAUSE COMPND 11 BACTERIAL PHOSPHOLIPID HYDROLYSIS AND KILLING. SIGNIFICANTLY COMPND 12 DECREASES MACROPHAGE PHAGOCYTOSIS POSSIBLY THANKS TO THE CLUMPS, COMPND 13 CLUMPED BACTERIA BEING TOO LARGE TO BE PHAGOCYTOSED. DOMINANT FACTOR COMPND 14 RESPONSIBLE FOR HUMAN PLATELET AGGREGATION, WHICH MAY BE AN IMPORTANT COMPND 15 MECHANISM FOR INITIATING INFECTIVE ENDOCARDITIS; COMPND 16 MOL_ID: 2; COMPND 17 MOLECULE: HUMAN ANTIBODY, HEAVY CHAIN FRAGMENT, ANTIGEN BINDING; COMPND 18 CHAIN: H; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 3; COMPND 21 MOLECULE: HUMAN ANTIBODY, LIGHT CHAIN, ANTIGEN BINDING; COMPND 22 CHAIN: L; COMPND 23 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS; SOURCE 3 ORGANISM_TAXID: 1280; SOURCE 4 STRAIN: N315; SOURCE 5 VARIANT: 002; SOURCE 6 GENE: CLFA, SA0742; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: MAMMALIA; SOURCE 11 ORGANISM_TAXID: 40674; SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: MAMMALIA; SOURCE 16 ORGANISM_TAXID: 40674; SOURCE 17 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS STAPHYLOCOCCUS AUREUS, VIRULENCE FACTORS, MONOCLONAL ANTIBODY, KEYWDS 2 PROPHYLACTIC TREATMENT, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR V.Y.OGANESYAN REVDAT 1 30-JUL-25 9NJY 0 JRNL AUTH C.TKACZYK,T.KEREN-KAPLAN,A.GAMSON,P.WARRENER,E.SEMENOVA, JRNL AUTH 2 K.ROSENTHAL,A.BARNES,B.AHANI,B.R.SELLMAN,O.PODLAHA, JRNL AUTH 3 V.OGANESYAN JRNL TITL STRUCTURE OF CLFA002 IN COMPLEX WITH NEUTRALIZING ANTIBODY JRNL TITL 2 AZD7745 PROVIDES INSIGHT INTO ITS BROAD NEUTRALIZATION JRNL TITL 3 MECHANISM IN STAPHYLOCOCCUS AUREUS INFECTION. JRNL REF J.INFECT.DIS. 2025 JRNL REFN ESSN 1537-6613 JRNL PMID 40632825 JRNL DOI 10.1093/INFDIS/JIAF357 REMARK 2 REMARK 2 RESOLUTION. 1.58 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0425 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.58 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 116697 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.199 REMARK 3 FREE R VALUE : 0.219 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.963 REMARK 3 FREE R VALUE TEST SET COUNT : 5792 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.58 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.62 REMARK 3 REFLECTION IN BIN (WORKING SET) : 8153 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.97 REMARK 3 BIN R VALUE (WORKING SET) : 0.2850 REMARK 3 BIN FREE R VALUE SET COUNT : 408 REMARK 3 BIN FREE R VALUE : 0.2920 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 5641 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 12 REMARK 3 SOLVENT ATOMS : 364 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.62 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.09800 REMARK 3 B22 (A**2) : 0.84000 REMARK 3 B33 (A**2) : -0.71500 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -1.32900 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.084 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.082 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.058 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.644 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5812 ; 0.003 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 5300 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7939 ; 1.056 ; 1.796 REMARK 3 BOND ANGLES OTHERS (DEGREES): 12277 ; 0.385 ; 1.736 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 744 ; 6.759 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 15 ; 4.510 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 911 ;10.139 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 915 ; 0.053 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6793 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1271 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 827 ; 0.188 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 51 ; 0.147 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2856 ; 0.169 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 250 ; 0.195 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2973 ; 1.023 ; 2.119 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2973 ; 1.023 ; 2.119 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3718 ; 1.724 ; 3.805 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3719 ; 1.724 ; 3.806 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2839 ; 1.372 ; 2.238 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2838 ; 1.373 ; 2.236 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4221 ; 2.249 ; 4.035 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4222 ; 2.249 ; 4.036 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK BULK SOLVENT REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 9NJY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAR-25. REMARK 100 THE DEPOSITION ID IS D_1000293533. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-FEB-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 19-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 : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 117495 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.580 REMARK 200 RESOLUTION RANGE LOW (A) : 35.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 6.600 REMARK 200 R MERGE (I) : 0.06000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58 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: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 9 MM MGCL2, 90 MM HEPES, 18% PEG 6000 REMARK 280 (W/V), 1% GLYCEROL (V/V), PH 7.0, VAPOR DIFFUSION, TEMPERATURE REMARK 280 295K 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 33.08200 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5760 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 32550 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 GLU H 1 REMARK 465 CYS L 214 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 GLU A 370 -161.22 63.57 REMARK 500 HIS A 376 -123.89 53.89 REMARK 500 SER H 15 -11.40 86.69 REMARK 500 ASP H 112 127.94 -177.67 REMARK 500 SER H 143 140.17 -175.87 REMARK 500 ASP H 155 64.67 69.71 REMARK 500 THR L 30 -112.68 54.08 REMARK 500 SER L 51 -48.71 80.59 REMARK 500 ASN L 138 64.91 66.07 REMARK 500 REMARK 500 REMARK: NULL DBREF 9NJY A 228 529 UNP Q99VJ4 CLFA_STAAN 228 529 DBREF 9NJY H 1 225 PDB 9NJY 9NJY 1 225 DBREF 9NJY L 1 214 PDB 9NJY 9NJY 1 214 SEQRES 1 A 302 ALA GLY THR ASP ILE THR ASN GLN LEU THR ASP VAL LYS SEQRES 2 A 302 VAL THR ILE ASP SER GLY THR THR VAL TYR PRO HIS GLN SEQRES 3 A 302 ALA GLY TYR VAL LYS LEU ASN TYR GLY PHE SER VAL PRO SEQRES 4 A 302 ASN SER ALA VAL LYS GLY ASP THR PHE LYS ILE THR VAL SEQRES 5 A 302 PRO LYS GLU LEU ASN LEU ASN GLY VAL THR SER THR ALA SEQRES 6 A 302 LYS VAL PRO PRO ILE MET ALA GLY ASP GLN VAL LEU ALA SEQRES 7 A 302 ASN GLY VAL ILE ASP SER ASP GLY ASN VAL ILE TYR THR SEQRES 8 A 302 PHE THR ASP TYR VAL ASP ASN LYS GLU ASN VAL THR ALA SEQRES 9 A 302 ASN ILE THR MET PRO ALA TYR ILE ASP PRO GLU ASN VAL SEQRES 10 A 302 THR LYS THR GLY ASN VAL THR LEU THR THR GLY ILE GLY SEQRES 11 A 302 THR ASN THR ALA SER LYS THR VAL LEU ILE ASP TYR GLU SEQRES 12 A 302 LYS TYR GLY GLN PHE HIS ASN LEU SER ILE LYS GLY THR SEQRES 13 A 302 ILE ASP GLN ILE ASP LYS THR ASN ASN THR TYR ARG GLN SEQRES 14 A 302 THR ILE TYR VAL ASN PRO SER GLY ASP ASN VAL VAL LEU SEQRES 15 A 302 PRO ALA LEU THR GLY ASN LEU ILE PRO ASN THR LYS SER SEQRES 16 A 302 ASN ALA LEU ILE ASP ALA LYS ASN THR ASP ILE LYS VAL SEQRES 17 A 302 TYR ARG VAL ASP ASN ALA ASN ASP LEU SER GLU SER TYR SEQRES 18 A 302 TYR VAL ASN PRO SER ASP PHE GLU ASP VAL THR ASN GLN SEQRES 19 A 302 VAL ARG ILE SER PHE PRO ASN ALA ASN GLN TYR LYS VAL SEQRES 20 A 302 GLU PHE PRO THR ASP ASP ASP GLN ILE THR THR PRO TYR SEQRES 21 A 302 ILE VAL VAL VAL ASN GLY HIS ILE ASP PRO ALA SER THR SEQRES 22 A 302 GLY ASP LEU ALA LEU ARG SER THR PHE TYR GLY TYR ASP SEQRES 23 A 302 SER ASN PHE ILE TRP ARG SER MET SER TRP ASP ASN GLU SEQRES 24 A 302 VAL ALA PHE SEQRES 1 H 225 GLU VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 225 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 225 GLY SER ILE ASN ASN SER TYR TRP SER TRP ILE ARG GLN SEQRES 4 H 225 PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR LEU TYR SEQRES 5 H 225 SER SER GLY ARG THR ASN TYR THR PRO SER LEU LYS SER SEQRES 6 H 225 ARG VAL THR MET SER VAL ASP THR SER LYS ASN GLN PHE SEQRES 7 H 225 SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR ALA SEQRES 8 H 225 LEU TYR TYR CYS ALA ARG THR HIS LEU GLY GLY PHE HIS SEQRES 9 H 225 TYR GLY GLY GLY PHE TRP PHE ASP PRO TRP GLY GLN GLY SEQRES 10 H 225 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 H 225 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 H 225 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 H 225 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 H 225 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 H 225 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 H 225 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 H 225 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 H 225 VAL GLU PRO LYS SEQRES 1 L 214 ASP ILE VAL MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 214 GLN SER ILE THR SER TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA SER SER SEQRES 5 L 214 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 214 GLN PRO GLU ASP PHE ALA THR PHE TYR CYS GLN GLU SER SEQRES 8 L 214 TYR SER THR PRO PRO THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 L 214 GLU ILE LYS ARG THR 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 SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS HET GOL A 601 6 HET GOL H 301 6 HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 4 GOL 2(C3 H8 O3) FORMUL 6 HOH *364(H2 O) HELIX 1 AA1 ILE A 232 LEU A 236 5 5 HELIX 2 AA2 TYR A 250 ALA A 254 5 5 HELIX 3 AA3 ASP A 321 ASP A 324 5 4 HELIX 4 AA4 ASN A 440 LEU A 444 5 5 HELIX 5 AA5 ASN A 451 PHE A 455 5 5 HELIX 6 AA6 THR A 459 VAL A 462 5 4 HELIX 7 AA7 LEU H 63 SER H 65 5 3 HELIX 8 AA8 THR H 73 LYS H 75 5 3 HELIX 9 AA9 THR H 86 THR H 90 5 5 HELIX 10 AB1 GLY H 101 GLY H 106 1 6 HELIX 11 AB2 SER H 138 LYS H 140 5 3 HELIX 12 AB3 SER H 167 ALA H 169 5 3 HELIX 13 AB4 SER H 198 THR H 202 5 5 HELIX 14 AB5 LYS H 212 ASN H 215 5 4 HELIX 15 AB6 GLN L 79 PHE L 83 5 5 HELIX 16 AB7 SER L 121 SER L 127 1 7 HELIX 17 AB8 LYS L 183 GLU L 187 1 5 SHEET 1 AA1 4 THR A 237 ASP A 244 0 SHEET 2 AA1 4 VAL A 257 SER A 264 -1 O SER A 264 N THR A 237 SHEET 3 AA1 4 THR A 330 ILE A 339 -1 O MET A 335 N LEU A 259 SHEET 4 AA1 4 LEU A 283 ASN A 284 -1 N ASN A 284 O TYR A 338 SHEET 1 AA2 3 THR A 248 VAL A 249 0 SHEET 2 AA2 3 ASN A 359 ILE A 367 1 O LEU A 366 N VAL A 249 SHEET 3 AA2 3 GLY A 348 ILE A 356 -1 N LEU A 352 O LYS A 363 SHEET 1 AA3 4 THR A 274 ILE A 277 0 SHEET 2 AA3 4 VAL A 315 PHE A 319 -1 O VAL A 315 N ILE A 277 SHEET 3 AA3 4 GLN A 302 ILE A 309 -1 N ASN A 306 O THR A 318 SHEET 4 AA3 4 ILE A 297 ALA A 299 -1 N ALA A 299 O GLN A 302 SHEET 1 AA4 5 GLY A 373 PHE A 375 0 SHEET 2 AA4 5 LEU A 378 ASP A 388 -1 O LEU A 378 N PHE A 375 SHEET 3 AA4 5 THR A 393 VAL A 400 -1 O TYR A 399 N LYS A 381 SHEET 4 AA4 5 TYR A 487 ILE A 495 -1 O TYR A 487 N VAL A 400 SHEET 5 AA4 5 ALA A 424 LEU A 425 -1 N LEU A 425 O HIS A 494 SHEET 1 AA5 6 GLY A 373 PHE A 375 0 SHEET 2 AA5 6 LEU A 378 ASP A 388 -1 O LEU A 378 N PHE A 375 SHEET 3 AA5 6 THR A 393 VAL A 400 -1 O TYR A 399 N LYS A 381 SHEET 4 AA5 6 TYR A 487 ILE A 495 -1 O TYR A 487 N VAL A 400 SHEET 5 AA5 6 ASP A 432 ARG A 437 -1 N ASP A 432 O ASN A 492 SHEET 6 AA5 6 GLU A 456 ASP A 457 -1 O GLU A 456 N ARG A 437 SHEET 1 AA6 4 ARG A 463 SER A 465 0 SHEET 2 AA6 4 TYR A 472 GLU A 475 -1 O LYS A 473 N SER A 465 SHEET 3 AA6 4 VAL A 407 LEU A 416 -1 N LEU A 412 O VAL A 474 SHEET 4 AA6 4 GLN A 482 ILE A 483 -1 O ILE A 483 N VAL A 407 SHEET 1 AA7 5 ARG A 463 SER A 465 0 SHEET 2 AA7 5 TYR A 472 GLU A 475 -1 O LYS A 473 N SER A 465 SHEET 3 AA7 5 VAL A 407 LEU A 416 -1 N LEU A 412 O VAL A 474 SHEET 4 AA7 5 LEU A 503 TYR A 512 -1 O TYR A 510 N ALA A 411 SHEET 5 AA7 5 TRP A 518 VAL A 527 -1 O ASN A 525 N LEU A 505 SHEET 1 AA8 4 GLN H 3 SER H 7 0 SHEET 2 AA8 4 LEU H 18 SER H 25 -1 O THR H 23 N GLN H 5 SHEET 3 AA8 4 GLN H 77 LEU H 82 -1 O PHE H 78 N CYS H 22 SHEET 4 AA8 4 VAL H 67 ASP H 72 -1 N ASP H 72 O GLN H 77 SHEET 1 AA9 6 LEU H 11 VAL H 12 0 SHEET 2 AA9 6 THR H 118 VAL H 122 1 O THR H 121 N VAL H 12 SHEET 3 AA9 6 ALA H 91 LEU H 100 -1 N TYR H 93 O THR H 118 SHEET 4 AA9 6 TYR H 33 GLN H 39 -1 N ILE H 37 O TYR H 94 SHEET 5 AA9 6 GLU H 46 TYR H 52 -1 O ILE H 48 N TRP H 36 SHEET 6 AA9 6 THR H 57 TYR H 59 -1 O ASN H 58 N TYR H 50 SHEET 1 AB1 4 LEU H 11 VAL H 12 0 SHEET 2 AB1 4 THR H 118 VAL H 122 1 O THR H 121 N VAL H 12 SHEET 3 AB1 4 ALA H 91 LEU H 100 -1 N TYR H 93 O THR H 118 SHEET 4 AB1 4 PHE H 109 TRP H 114 -1 O TRP H 110 N HIS H 99 SHEET 1 AB2 4 SER H 131 LEU H 135 0 SHEET 2 AB2 4 THR H 146 TYR H 156 -1 O LEU H 152 N PHE H 133 SHEET 3 AB2 4 TYR H 187 PRO H 196 -1 O LEU H 189 N VAL H 153 SHEET 4 AB2 4 VAL H 174 THR H 176 -1 N HIS H 175 O VAL H 192 SHEET 1 AB3 4 THR H 142 SER H 143 0 SHEET 2 AB3 4 THR H 146 TYR H 156 -1 O THR H 146 N SER H 143 SHEET 3 AB3 4 TYR H 187 PRO H 196 -1 O LEU H 189 N VAL H 153 SHEET 4 AB3 4 VAL H 180 LEU H 181 -1 N VAL H 180 O SER H 188 SHEET 1 AB4 3 THR H 162 TRP H 165 0 SHEET 2 AB4 3 TYR H 205 HIS H 211 -1 O ASN H 208 N SER H 164 SHEET 3 AB4 3 THR H 216 VAL H 222 -1 O VAL H 218 N VAL H 209 SHEET 1 AB5 4 MET L 4 SER L 7 0 SHEET 2 AB5 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AB5 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AB5 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB6 6 SER L 10 SER L 14 0 SHEET 2 AB6 6 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 AB6 6 ALA L 84 GLU L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AB6 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AB6 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AB6 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AB7 4 SER L 114 PHE L 118 0 SHEET 2 AB7 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB7 4 TYR L 173 SER L 182 -1 O TYR L 173 N PHE L 139 SHEET 4 AB7 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB8 4 ALA L 153 LEU L 154 0 SHEET 2 AB8 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB8 4 VAL L 191 THR L 197 -1 O ALA L 193 N LYS L 149 SHEET 4 AB8 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SSBOND 1 CYS H 22 CYS H 95 1555 1555 2.29 SSBOND 2 CYS H 151 CYS H 207 1555 1555 2.14 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.47 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.30 CISPEP 1 ASP H 112 PRO H 113 0 -6.90 CISPEP 2 PHE H 157 PRO H 158 0 -8.04 CISPEP 3 GLU H 159 PRO H 160 0 -6.12 CISPEP 4 GLU H 159 PRO H 160 0 1.68 CISPEP 5 SER L 7 PRO L 8 0 -3.81 CISPEP 6 THR L 94 PRO L 95 0 -6.98 CISPEP 7 TYR L 140 PRO L 141 0 2.12 CRYST1 60.582 66.164 107.875 90.00 90.58 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 0.016507 0.000000 0.000168 0.00000 SCALE2 0.000000 0.015114 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009270 0.00000