HEADER CARBOHYDRATE 26-JAN-22 7QXC TITLE RECOGNITION OF STAPHYLOCOCCUS AUREUS WALL TEICHOIC ACID ANALOGUE SA533 TITLE 2 (COMPOUND 1) BY FAB4461 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB 4461 HEAVY CHAIN; COMPND 3 CHAIN: HHH; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB 4461 LIGHT CHAIN; COMPND 7 CHAIN: LLL; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ANTIBODY, FAB FRAGMENT, TEICHOIC ACID ANALOGUE, CARBOHYDRATE EXPDTA X-RAY DIFFRACTION AUTHOR P.SORIANO-MALDONADO,M.J.VAN RAAIJ JRNL AUTH C.DI CARLUCCIO,P.SORIANO MALDONADO,F.BERNI,C.J.C.DE HAAS, JRNL AUTH 2 A.R.TEMMING,A.HENDRIKS,S.ALI,A.MOLINARO,A.SILIPO, JRNL AUTH 3 N.M.VAN SORGE,M.J.VAN RAAIJ,J.D.C.CODEE,R.MARCHETTI JRNL TITL ANTIBODY RECOGNITION OF DIFFERENT STAPHYLOCOCCUS AUREUS WALL JRNL TITL 2 TEICHOIC ACID GLYCOFORMS JRNL REF ACS CENT.SCI. 2022 JRNL REFN ESSN 2374-7951 JRNL DOI 10.1021/ACSCENTSCI.2C00125 REMARK 2 REMARK 2 RESOLUTION. 1.45 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0267 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) : 1.45 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.51 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5 REMARK 3 NUMBER OF REFLECTIONS : 87588 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.174 REMARK 3 FREE R VALUE : 0.200 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.987 REMARK 3 FREE R VALUE TEST SET COUNT : 4368 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) : 1.45 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.53 REMARK 3 REFLECTION IN BIN (WORKING SET) : 10122 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.79 REMARK 3 BIN R VALUE (WORKING SET) : 0.3350 REMARK 3 BIN FREE R VALUE SET COUNT : 529 REMARK 3 BIN FREE R VALUE : 0.3420 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3317 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 88 REMARK 3 SOLVENT ATOMS : 424 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 21.80 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.02 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.41500 REMARK 3 B22 (A**2) : 0.10100 REMARK 3 B33 (A**2) : 0.26900 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.06100 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.062 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.064 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.046 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.231 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3489 ; 0.009 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 3183 ; 0.001 ; 0.015 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4738 ; 1.498 ; 1.652 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7374 ; 1.352 ; 1.578 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 434 ; 7.152 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 155 ;34.742 ;23.032 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 540 ;11.908 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;21.132 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 461 ; 0.069 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3906 ; 0.008 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 782 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 495 ; 0.197 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 48 ; 0.121 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1653 ; 0.163 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 302 ; 0.221 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.084 ; 0.200 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): 1739 ; 1.943 ; 2.199 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1738 ; 1.940 ; 2.197 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2169 ; 3.201 ; 3.291 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2170 ; 3.200 ; 3.293 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1750 ; 2.613 ; 2.516 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1751 ; 2.613 ; 2.518 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2568 ; 4.080 ; 3.626 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2569 ; 4.079 ; 3.628 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 7QXC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292120484. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-DEC-20 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 9.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALBA REMARK 200 BEAMLINE : XALOC REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97926 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 : XDS JANUARY 2020 REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 87656 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450 REMARK 200 RESOLUTION RANGE LOW (A) : 53.510 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6 REMARK 200 DATA REDUNDANCY : 3.100 REMARK 200 R MERGE (I) : 0.02800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53 REMARK 200 COMPLETENESS FOR SHELL (%) : 80.6 REMARK 200 DATA REDUNDANCY IN SHELL : 2.50 REMARK 200 R MERGE FOR SHELL (I) : 0.43000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 2.8.3 REMARK 200 STARTING MODEL: SEPARATE CONSTANT AND VARIABLE DOMAINS OF PDB REMARK 200 ENTRY 5I1D REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MM TRIS-HCL; 250 MM SODIUM REMARK 280 CHLORIDE; 12.9 % W/V POLYETHYLENE GLYCOL 20,000; 150 MM CAPSO PH REMARK 280 9.5; 6 % V/V POLYETHYLENE GLYCOL 300, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 294K 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 32.72400 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: HHH, LLL 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 H 134 REMARK 465 LYS H 135 REMARK 465 SER H 136 REMARK 465 THR H 137 REMARK 465 SER H 221 REMARK 465 CYS H 222 REMARK 465 GLY H 223 REMARK 465 GLY H 224 REMARK 465 GLY H 225 REMARK 465 GLY H 226 REMARK 465 SER H 227 REMARK 465 LEU H 228 REMARK 465 PRO H 229 REMARK 465 GLU H 230 REMARK 465 THR H 231 REMARK 465 GLY H 232 REMARK 465 GLY H 233 REMARK 465 HIS H 234 REMARK 465 HIS H 235 REMARK 465 HIS H 236 REMARK 465 HIS H 237 REMARK 465 HIS H 238 REMARK 465 HIS H 239 REMARK 465 CYS L 220 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 H 28 OG 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 OE1 GLNLL 106 O HOHLL 401 1.55 REMARK 500 OE1 GLUHH 154 O HOHHH 401 1.62 REMARK 500 O HOHLL 521 O HOHLL 586 1.73 REMARK 500 OG SERHH 185 O HOHHH 402 1.89 REMARK 500 NE2 GLNHH 1 O HOHHH 403 1.96 REMARK 500 OH TYRLL 42 O HOHLL 402 1.97 REMARK 500 O HOHLL 401 O HOHLL 587 2.06 REMARK 500 O HOHHH 463 O HOHLL 560 2.10 REMARK 500 NH1 ARGLL 18 OD1 ASNLL 82 2.12 REMARK 500 O HOHHH 402 O HOHLL 418 2.13 REMARK 500 OD2 ASPHH 107 O HOHLL 402 2.14 REMARK 500 O4 PEGLL 303 O4 PEGLL 304 2.15 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 SERHH 28 172.84 68.38 REMARK 500 PHEHH 29 -8.07 -155.69 REMARK 500 THRHH 30 -95.00 -117.56 REMARK 500 ALALL 57 -35.11 67.90 REMARK 500 ASNLL 144 63.75 61.05 REMARK 500 REMARK 500 REMARK: NULL DBREF 7QXCHH 1 239 PDB 7QXC 7QXC 1 239 DBREF 7QXCLL 1 220 PDB 7QXC 7QXC 1 220 SEQRES 1HH 239 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL ARG LYS SEQRES 2HH 239 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3HH 239 TYR SER PHE THR ASP TYR TYR MET HIS TRP VAL ARG GLN SEQRES 4HH 239 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5HH 239 PRO LYS SER GLY GLY THR ASN TYR ALA GLN ARG PHE GLN SEQRES 6HH 239 GLY ARG VAL THR MET THR GLY ASP THR SER ILE SER ALA SEQRES 7HH 239 ALA TYR MET ASP LEU ALA SER LEU THR SER ASP ASP THR SEQRES 8HH 239 ALA VAL TYR TYR CYS VAL LYS ASP CYS GLY SER GLY GLY SEQRES 9HH 239 LEU ARG ASP PHE TRP GLY GLN GLY THR THR VAL THR VAL SEQRES 10HH 239 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11HH 239 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12HH 239 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13HH 239 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14HH 239 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15HH 239 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16HH 239 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17HH 239 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 18HH 239 CYS GLY GLY GLY GLY SER LEU PRO GLU THR GLY GLY HIS SEQRES 19HH 239 HIS HIS HIS HIS HIS SEQRES 1LL 220 ASP ILE GLN MET THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2LL 220 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER SEQRES 3LL 220 GLN SER VAL LEU SER ARG ALA ASN ASN ASN TYR TYR VAL SEQRES 4LL 220 ALA TRP TYR GLN HIS LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 5LL 220 LEU ILE TYR TRP ALA SER THR ARG GLU PHE GLY VAL PRO SEQRES 6LL 220 ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7LL 220 LEU THR ILE ASN SER LEU GLN ALA GLU ASP VAL ALA VAL SEQRES 8LL 220 TYR TYR CYS GLN GLN TYR TYR THR SER ARG ARG THR PHE SEQRES 9LL 220 GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA SEQRES 10LL 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11LL 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12LL 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13LL 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14LL 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15LL 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16LL 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17LL 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS HET 3CX HH 301 15 HET PEG HH 302 7 HET G6N LL 301 45 HET PEG LL 302 7 HET PEG LL 303 7 HET PEG LL 304 7 HETNAM 3CX (2S)-3-(CYCLOHEXYLAMINO)-2-HYDROXYPROPANE-1-SULFONIC HETNAM 2 3CX ACID HETNAM PEG DI(HYDROXYETHYL)ETHER FORMUL 3 3CX C9 H19 N O4 S FORMUL 4 PEG 4(C4 H10 O3) FORMUL 5 G6N FORMUL 9 HOH *424(H2 O) HELIX 1 AA1 GLNHH 62 GLNHH 65 5 4 HELIX 2 AA2 THRHH 74 ILEHH 76 5 3 HELIX 3 AA3 THRHH 87 THRHH 91 5 5 HELIX 4 AA4 SERHH 162 ALAHH 164 5 3 HELIX 5 AA5 SERHH 193 GLNHH 198 1 6 HELIX 6 AA6 LYSHH 207 ASNHH 210 5 4 HELIX 7 AA7 GLNLL 85 VALLL 89 5 5 HELIX 8 AA8 SERLL 127 LYSLL 132 1 6 HELIX 9 AA9 LYSLL 189 HISLL 195 1 7 SHEET 1 AA1 4 GLNHH 3 GLNHH 6 0 SHEET 2 AA1 4 VALHH 18 SERHH 25 -1 O LYSHH 23 N VALHH 5 SHEET 3 AA1 4 ALAHH 78 LEUHH 83 -1 O METHH 81 N VALHH 20 SHEET 4 AA1 4 VALHH 68 ASPHH 73 -1 N THRHH 71 O TYRHH 80 SHEET 1 AA2 6 GLUHH 10 ARGHH 12 0 SHEET 2 AA2 6 THRHH 113 VALHH 117 1 O THRHH 116 N GLUHH 10 SHEET 3 AA2 6 ALAHH 92 ASPHH 99 -1 N TYRHH 94 O THRHH 113 SHEET 4 AA2 6 TYRHH 33 GLNHH 39 -1 N VALHH 37 O TYRHH 95 SHEET 5 AA2 6 GLUHH 46 ILEHH 51 -1 O METHH 48 N TRPHH 36 SHEET 6 AA2 6 THRHH 58 TYRHH 60 -1 O ASNHH 59 N TRPHH 50 SHEET 1 AA3 4 GLUHH 10 ARGHH 12 0 SHEET 2 AA3 4 THRHH 113 VALHH 117 1 O THRHH 116 N GLUHH 10 SHEET 3 AA3 4 ALAHH 92 ASPHH 99 -1 N TYRHH 94 O THRHH 113 SHEET 4 AA3 4 ASPHH 107 TRPHH 109 -1 O PHEHH 108 N LYSHH 98 SHEET 1 AA4 4 SERHH 126 LEUHH 130 0 SHEET 2 AA4 4 THRHH 141 TYRHH 151 -1 O LYSHH 149 N SERHH 126 SHEET 3 AA4 4 TYRHH 182 PROHH 191 -1 O LEUHH 184 N VALHH 148 SHEET 4 AA4 4 VALHH 169 THRHH 171 -1 N HISHH 170 O VALHH 187 SHEET 1 AA5 4 SERHH 126 LEUHH 130 0 SHEET 2 AA5 4 THRHH 141 TYRHH 151 -1 O LYSHH 149 N SERHH 126 SHEET 3 AA5 4 TYRHH 182 PROHH 191 -1 O LEUHH 184 N VALHH 148 SHEET 4 AA5 4 VALHH 175 LEUHH 176 -1 N VALHH 175 O SERHH 183 SHEET 1 AA6 3 THRHH 157 TRPHH 160 0 SHEET 2 AA6 3 ILEHH 201 HISHH 206 -1 O ASNHH 203 N SERHH 159 SHEET 3 AA6 3 THRHH 211 LYSHH 216 -1 O VALHH 213 N VALHH 204 SHEET 1 AA7 4 METLL 4 SERLL 7 0 SHEET 2 AA7 4 ALALL 19 SERLL 25 -1 O ASNLL 22 N SERLL 7 SHEET 3 AA7 4 ASPLL 76 ILELL 81 -1 O PHELL 77 N CYSLL 23 SHEET 4 AA7 4 PHELL 68 SERLL 73 -1 N SERLL 69 O THRLL 80 SHEET 1 AA8 6 SERLL 10 VALLL 13 0 SHEET 2 AA8 6 THRLL 108 ILELL 112 1 O LYSLL 109 N LEULL 11 SHEET 3 AA8 6 ALALL 90 GLNLL 96 -1 N ALALL 90 O VALLL 110 SHEET 4 AA8 6 VALLL 39 HISLL 44 -1 N HISLL 44 O VALLL 91 SHEET 5 AA8 6 LYSLL 51 TYRLL 55 -1 O LEULL 53 N TRPLL 41 SHEET 6 AA8 6 THRLL 59 ARGLL 60 -1 O THRLL 59 N TYRLL 55 SHEET 1 AA9 4 SERLL 10 VALLL 13 0 SHEET 2 AA9 4 THRLL 108 ILELL 112 1 O LYSLL 109 N LEULL 11 SHEET 3 AA9 4 ALALL 90 GLNLL 96 -1 N ALALL 90 O VALLL 110 SHEET 4 AA9 4 THRLL 103 PHELL 104 -1 O THRLL 103 N GLNLL 96 SHEET 1 AB1 4 SERLL 120 PHELL 124 0 SHEET 2 AB1 4 THRLL 135 PHELL 145 -1 O ASNLL 143 N SERLL 120 SHEET 3 AB1 4 TYRLL 179 SERLL 188 -1 O LEULL 181 N LEULL 142 SHEET 4 AB1 4 SERLL 165 VALLL 169 -1 N GLNLL 166 O THRLL 184 SHEET 1 AB2 4 ALALL 159 LEULL 160 0 SHEET 2 AB2 4 LYSLL 151 VALLL 156 -1 N VALLL 156 O ALALL 159 SHEET 3 AB2 4 VALLL 197 THRLL 203 -1 O GLULL 201 N GLNLL 153 SHEET 4 AB2 4 VALLL 211 ASNLL 216 -1 O VALLL 211 N VALLL 202 SSBOND 1 CYSHH 22 CYSHH 96 1555 1555 2.08 SSBOND 2 CYSHH 146 CYSHH 202 1555 1555 2.01 SSBOND 3 CYSLL 23 CYSLL 94 1555 1555 2.13 SSBOND 4 CYSLL 140 CYSLL 200 1555 1555 1.99 CISPEP 1 PHEHH 152 PROHH 153 0 -8.25 CISPEP 2 GLUHH 154 PROHH 155 0 -3.68 CISPEP 3 GLUHH 154 PROHH 155 0 -4.59 CISPEP 4 SERLL 7 PROLL 8 0 -5.93 CISPEP 5 TYRLL 146 PROLL 147 0 -0.38 CRYST1 58.191 65.448 74.338 90.00 112.90 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 0.017185 0.000000 0.007259 0.00000 SCALE2 0.000000 0.015279 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014603 0.00000