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HEADER IMMUNE SYSTEM 25-AUG-03 1Q9R TITLE S25-2- A(2-8)KDO DISACCHARIDE COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: S25-2 FAB (IGG1K) LIGHT CHAIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FAB LIGHT CHAIN KAPPA; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: S25-2 FAB (IGG1K) HEAVY CHAIN; COMPND 7 CHAIN: B; COMPND 8 FRAGMENT: FAB HEAVY CHAIN G1 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 6 ORGANISM_COMMON: MOUSE KEYWDS ANTIGEN-BINDING FRAGMENT, FAB, ANTI-CARBOHYDRATE, ANTI-LPS, KEYWDS 2 ANTIBODY, IMMUNOGLOBULIN, KDO, COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR H.P.NGUYEN,N.O.SETO,C.R.MACKENZIE,L.BRADE,P.KOSMA,H.BRADE, AUTHOR 2 S.V.EVANS REVDAT 1 27-JAN-04 1Q9R 0 JRNL AUTH H.P.NGUYEN,N.O.SETO,C.R.MACKENZIE,L.BRADE,P.KOSMA, JRNL AUTH 2 H.BRADE,S.V.EVANS JRNL TITL GERMLINE ANTIBODY RECOGNITION OF DISTINCT JRNL TITL 2 CARBOHYDRATE EPITOPES. JRNL REF NAT.STRUCT.BIOL. V. 10 1019 2003 JRNL REFN ASTM NSBIEW US ISSN 1072-8368 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.45 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.78 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.9 REMARK 3 NUMBER OF REFLECTIONS : 82091 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.203 REMARK 3 FREE R VALUE : 0.224 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100 REMARK 3 FREE R VALUE TEST SET COUNT : 8262 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 10 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.45 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.50 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.00 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7065 REMARK 3 BIN R VALUE (WORKING SET) : 0.2400 REMARK 3 BIN FREE R VALUE : 0.2600 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.20 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 804 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.009 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3399 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 38 REMARK 3 SOLVENT ATOMS : 512 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 17.80 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.80 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.43000 REMARK 3 B22 (A**2) : -0.67000 REMARK 3 B33 (A**2) : -1.76000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.16 REMARK 3 ESD FROM SIGMAA (A) : 0.08 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.18 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.09 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.60 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : CNS BULK SOLVENT MODEL USED REMARK 3 KSOL : 0.36 REMARK 3 BSOL : 43.90 REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : CARBOHYDRATE.PARAM REMARK 3 PARAMETER FILE 3 : ION.PARAM REMARK 3 PARAMETER FILE 4 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 5 : KDO6.PAR REMARK 3 PARAMETER FILE 6 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP REMARK 3 TOPOLOGY FILE 3 : ION.TOP REMARK 3 TOPOLOGY FILE 4 : WATER.TOP REMARK 3 TOPOLOGY FILE 5 : KDO6.TOP REMARK 3 TOPOLOGY FILE 6 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1Q9R COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE RCSB ID CODE IS RCSB020094. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-SEP-2001 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 8.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS REMARK 200 BEAMLINE : X8C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.15 REMARK 200 MONOCHROMATOR : SI 111 CHANNEL REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 82091 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450 REMARK 200 RESOLUTION RANGE LOW (A) : 19.780 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL 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) : 1.50 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9 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: CNS REMARK 200 STARTING MODEL: PDB ENTRY 1Q9O, S45-18 FAB UNLIGANDED REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.67 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: KDO DISACCHARIDE, MAGNESIUM REMARK 280 CHLORIDE, ZINC CHLORIDE, ETHYLENE GLYCOL, GLYCEROL, PEG 4000, REMARK 280 TRIS, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-Z REMARK 290 4555 1/2+X,1/2-Y,-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 22.95000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.75000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.80000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.75000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.95000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.80000 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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 APPLY THE FOLLOWING TO CHAINS: B, A, C 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 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 REMARK 500 O8 KDA C 302 O6 KDO C 303 2.13 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OD2 ASP A 150 O HOH 746 2564 2.03 REMARK 500 ND1 HIS A 188 O HOH 746 2564 2.19 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 MET B 80 SD MET B 80 CE -0.167 REMARK 500 MET A 21 SD MET A 21 CE -0.163 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 TYR B 32 N - CA - C ANGL. DEV. = 9.8 DEGREES REMARK 500 TYR B 33 N - CA - C ANGL. DEV. =-10.6 DEGREES REMARK 500 PHE B 100C N - CA - C ANGL. DEV. =-10.3 DEGREES REMARK 500 SER B 118 N - CA - C ANGL. DEV. =-12.9 DEGREES REMARK 500 THR A 113 N - CA - C ANGL. DEV. = -9.8 DEGREES REMARK 500 LEU A 135 N - CA - C ANGL. DEV. =-10.2 DEGREES REMARK 500 ASP A 164 N - CA - C ANGL. DEV. =-11.0 DEGREES 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 M RES CSSEQI PSI PHI REMARK 500 GLN B 129 -33.84 71.05 REMARK 500 SER B 132 -61.63 74.10 REMARK 500 ALA A 51 -38.19 66.15 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1Q9Q RELATED DB: PDB REMARK 900 SAME PROTEIN, BUT HERE LIGANDED WITH A(2-8)KDO DISACCHARIDE REMARK 900 RELATED ID: 1Q9K RELATED DB: PDB REMARK 900 SAME PROTEIN, BUT HERE LIGANDED WITH A(2-8)KDO DISACCHARIDE REMARK 900 RELATED ID: 1Q9L RELATED DB: PDB REMARK 900 SAME PROTEIN, BUT HERE LIGANDED WITH A(2-8)KDO DISACCHARIDE REMARK 900 RELATED ID: 1Q9O RELATED DB: PDB REMARK 900 S45-18 HAS MORE MUTATIONS FROM GERMLINE THAN DOES S25-2 REMARK 900 RELATED ID: 1Q9T RELATED DB: PDB REMARK 900 AB S25-2 LIGANDED WITH A(2-4) KDO DISACCHARIDE REMARK 900 RELATED ID: 1Q9V RELATED DB: PDB REMARK 900 AB S25-2 LIGANDED WITH KDO MONOSACCHARIDE REMARK 900 RELATED ID: 1Q9W RELATED DB: PDB REMARK 900 S45-18 FAB PENTASACCHARIDE BISPHOSPHATE COMPLEX REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE SEQUENCE OF THE PROTEIN WAS NOT DEPOSITED REMARK 999 INTO ANY SEQUENCE DATABASE. SEQRES 1 A 219 ASP ILE VAL MET SER GLN SER PRO SER SER LEU ALA VAL SEQRES 2 A 219 SER ALA GLY GLU LYS VAL THR MET SER CYS LYS SER SER SEQRES 3 A 219 GLN SER LEU LEU ASN SER ARG THR ARG LYS ASN TYR LEU SEQRES 4 A 219 ALA TRP TYR GLN GLN LYS PRO GLY GLN SER PRO LYS LEU SEQRES 5 A 219 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 A 219 ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 A 219 LEU THR ILE THR SER VAL GLN ALA GLU ASP LEU ALA VAL SEQRES 8 A 219 TYR TYR CYS LYS GLN SER TYR ASN LEU ARG THR PHE GLY SEQRES 9 A 219 GLY GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA ALA SEQRES 10 A 219 PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU SEQRES 11 A 219 THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN SEQRES 12 A 219 PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP SEQRES 13 A 219 GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR SEQRES 14 A 219 ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SER SEQRES 15 A 219 THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SEQRES 16 A 219 SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER SEQRES 17 A 219 PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS SEQRES 1 B 222 GLU VAL LYS LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 222 SER GLY GLY SER LEU ARG LEU SER CYS ALA THR SER GLY SEQRES 3 B 222 PHE THR PHE THR ASP TYR TYR MET SER TRP VAL ARG GLN SEQRES 4 B 222 PRO PRO GLY LYS ALA LEU GLU TRP LEU GLY PHE ILE ARG SEQRES 5 B 222 ASN LYS ALA ASN GLY TYR THR THR GLU TYR SER PRO SER SEQRES 6 B 222 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SER GLN SEQRES 7 B 222 SER ILE LEU TYR LEU GLN MET ASN THR LEU ARG ALA GLU SEQRES 8 B 222 ASP SER ALA THR TYR TYR CYS ALA ARG ASP HIS ASP GLY SEQRES 9 B 222 TYR TYR GLU ARG PHE SER TYR TRP GLY GLN GLY THR LEU SEQRES 10 B 222 VAL THR VAL SER ALA ALA LYS THR THR PRO PRO SER VAL SEQRES 11 B 222 TYR PRO LEU ALA PRO GLY SER ALA ALA GLN THR ASN SER SEQRES 12 B 222 MET VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO SEQRES 13 B 222 GLU PRO VAL THR VAL THR TRP ASN SER GLY SER LEU SER SEQRES 14 B 222 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP SEQRES 15 B 222 LEU TYR THR LEU SER SER SER VAL THR VAL PRO SER SER SEQRES 16 B 222 THR TRP PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS SEQRES 17 B 222 PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO SEQRES 18 B 222 ARG HET KDA C 302 19 HET KDO C 303 15 HET MG 201 1 HET MG 202 1 HET MG 203 1 HET ZN 205 1 HETNAM KDA (3-DEOXY-D-MANNO-OCT-2-ULOSONIC ACID)-2-O-ALLYL HETNAM KDO 3-DEOXY-D-MANNO-OCT-2-ULOSONIC ACID HETNAM MG MAGNESIUM ION HETNAM ZN ZINC ION FORMUL 3 KDA C11 H18 O8 FORMUL 3 KDO C8 H14 O8 FORMUL 4 MG 3(MG 2+) FORMUL 7 ZN ZN 2+ FORMUL 8 HOH *512(H2 O) HELIX 1 1 THR B 28 TYR B 32 5 5 HELIX 2 2 ASN B 52A GLY B 52E 5 5 HELIX 3 3 ARG B 83 SER B 87 5 5 HELIX 4 4 SER B 154 SER B 156 5 3 HELIX 5 5 PRO B 198 SER B 201 5 4 HELIX 6 6 GLN A 79 LEU A 83 5 5 HELIX 7 7 SER A 120 THR A 125 1 6 HELIX 8 8 LYS A 182 GLU A 186 1 5 HELIX 9 9 ASN A 211 CYS A 213 5 3 SHEET 1 A 4 LYS B 3 SER B 7 0 SHEET 2 A 4 LEU B 18 SER B 25 -1 O SER B 25 N LYS B 3 SHEET 3 A 4 ILE B 75 MET B 80 -1 O LEU B 78 N LEU B 20 SHEET 4 A 4 PHE B 65 ASP B 70 -1 N THR B 66 O GLN B 79 SHEET 1 B 6 LEU B 11 VAL B 12 0 SHEET 2 B 6 THR B 105 VAL B 109 1 O THR B 108 N VAL B 12 SHEET 3 B 6 ALA B 88 ARG B 94 -1 N ALA B 88 O VAL B 107 SHEET 4 B 6 MET B 34 GLN B 39 -1 N VAL B 37 O TYR B 91 SHEET 5 B 6 GLU B 46 ILE B 51 -1 O LEU B 48 N TRP B 36 SHEET 6 B 6 THR B 55 TYR B 57 -1 O GLU B 56 N PHE B 50 SHEET 1 C 4 SER B 118 LEU B 122 0 SHEET 2 C 4 MET B 133 TYR B 143 -1 O LEU B 139 N TYR B 120 SHEET 3 C 4 LEU B 172 PRO B 182 -1 O TYR B 173 N TYR B 143 SHEET 4 C 4 VAL B 161 GLN B 169 -1 N HIS B 162 O SER B 178 SHEET 1 D 3 THR B 149 TRP B 152 0 SHEET 2 D 3 THR B 192 HIS B 197 -1 O ASN B 194 N THR B 151 SHEET 3 D 3 THR B 202 LYS B 207 -1 O VAL B 204 N VAL B 195 SHEET 1 E 4 MET A 4 SER A 7 0 SHEET 2 E 4 VAL A 19 SER A 25 -1 O SER A 22 N SER A 7 SHEET 3 E 4 ASP A 70 ILE A 75 -1 O PHE A 71 N CYS A 23 SHEET 4 E 4 PHE A 62 SER A 67 -1 N THR A 63 O THR A 74 SHEET 1 F 6 SER A 10 SER A 14 0 SHEET 2 F 6 THR A 101 LYS A 106 1 O GLU A 104 N LEU A 11 SHEET 3 F 6 ALA A 84 GLN A 90 -1 N ALA A 84 O LEU A 103 SHEET 4 F 6 LEU A 33 GLN A 38 -1 N TYR A 36 O TYR A 87 SHEET 5 F 6 LYS A 45 TYR A 49 -1 O LEU A 47 N TRP A 35 SHEET 6 F 6 THR A 53 ARG A 54 -1 O THR A 53 N TYR A 49 SHEET 1 G 4 SER A 10 SER A 14 0 SHEET 2 G 4 THR A 101 LYS A 106 1 O GLU A 104 N LEU A 11 SHEET 3 G 4 ALA A 84 GLN A 90 -1 N ALA A 84 O LEU A 103 SHEET 4 G 4 THR A 96 PHE A 97 -1 O THR A 96 N GLN A 90 SHEET 1 H 2 LEU A 30 ASN A 30A 0 SHEET 2 H 2 LYS A 30F ASN A 31 -1 O LYS A 30F N ASN A 30A SHEET 1 I 4 THR A 113 PHE A 117 0 SHEET 2 I 4 GLY A 128 PHE A 138 -1 O ASN A 136 N THR A 113 SHEET 3 I 4 TYR A 172 THR A 181 -1 O LEU A 178 N VAL A 131 SHEET 4 I 4 VAL A 158 TRP A 162 -1 N SER A 161 O SER A 175 SHEET 1 J 4 SER A 152 ARG A 154 0 SHEET 2 J 4 ASN A 144 ILE A 149 -1 N ILE A 149 O SER A 152 SHEET 3 J 4 SER A 190 THR A 196 -1 O GLU A 194 N LYS A 146 SHEET 4 J 4 ILE A 204 ASN A 209 -1 O ILE A 204 N ALA A 195 SSBOND 1 CYS B 22 CYS B 92 SSBOND 2 CYS B 138 CYS B 193 SSBOND 3 CYS A 23 CYS A 88 SSBOND 4 CYS A 133 CYS A 193 LINK O8 KDA C 302 C2 KDO C 303 CISPEP 1 PHE B 144 PRO B 145 0 -0.70 CISPEP 2 GLU B 146 PRO B 147 0 -0.03 CISPEP 3 TRP B 186 PRO B 187 0 0.34 CISPEP 4 SER A 7 PRO A 8 0 -0.72 CISPEP 5 TYR A 139 PRO A 140 0 0.23 CRYST1 45.900 81.600 131.500 90.00 90.00 90.00 P 21 21 21 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 0.021786 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012255 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007605 0.00000