HEADER IMMUNE SYSTEM 29-SEP-13 4C83 TITLE CRYSTAL STRUCTURE OF THE IGG2A LPT3 IN COMPLEX WITH AN 8- TITLE 2 SUGAR INNER CORE ANALOGUE OF NEISSERIA MENINGITIDIS COMPND MOL_ID: 1; COMPND 2 MOLECULE: LPT3 LIGHT CHAIN; COMPND 3 CHAIN: B, D; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: LPT3 HEAVY CHAIN; COMPND 6 CHAIN: A, C SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 7 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 8 ORGANISM_TAXID: 10090 KEYWDS IMMUNE SYSTEM, LIPOOLIGOSACCHARIDES, ANTIBODIES, ANTIGEN-ANTIBODY KEYWDS 2 COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR M.J.PARKER,K.GOMERY,G.RICHARD,C.R.MACKENZIE,A.D.COX,J.C.RICHARDS, AUTHOR 2 S.V.EVANS REVDAT 2 16-APR-14 4C83 1 JRNL REVDAT 1 12-FEB-14 4C83 0 JRNL AUTH M.J.PARKER,K.GOMERY,G.RICHARD,C.R.MACKENZIE,A.D.COX, JRNL AUTH 2 J.C.RICHARDS,S.V.EVANS JRNL TITL STRUCTURAL BASIS FOR SELECTIVE CROSS-REACTIVITY IN A JRNL TITL 2 BACTERICIDAL ANTIBODY AGAINST INNER CORE JRNL TITL 3 LIPOOLIGOSACCHARIDE FROM NEISSERIA MENINGITIDIS. JRNL REF GLYCOBIOLOGY V. 24 442 2014 JRNL REFN ISSN 0959-6658 JRNL PMID 24488440 JRNL DOI 10.1093/GLYCOB/CWU009 REMARK 2 REMARK 2 RESOLUTION. 2.69 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.7.0029 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU, REMARK 3 STEINER,NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.90 REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE REMARK 3 COMPLETENESS FOR RANGE (%) : 97.43 REMARK 3 NUMBER OF REFLECTIONS : 24686 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 + TEST SET) : 0.22845 REMARK 3 R VALUE (WORKING SET) : 0.22484 REMARK 3 FREE R VALUE : 0.29255 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1 REMARK 3 FREE R VALUE TEST SET COUNT : 1319 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.690 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.760 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1870 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.09 REMARK 3 BIN R VALUE (WORKING SET) : 0.356 REMARK 3 BIN FREE R VALUE SET COUNT : 77 REMARK 3 BIN FREE R VALUE : 0.447 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6543 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 144 REMARK 3 SOLVENT ATOMS : 4 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.986 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.94 REMARK 3 B22 (A**2) : -1.51 REMARK 3 B33 (A**2) : 3.63 REMARK 3 B12 (A**2) : -0.24 REMARK 3 B13 (A**2) : 2.31 REMARK 3 B23 (A**2) : 0.40 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.421 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.357 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.607 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.886 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6859 ; 0.010 ; 0.020 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9326 ; 1.321 ; 1.969 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 837 ; 5.954 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 257 ;34.043 ;23.385 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1062 ;22.611 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;23.027 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1061 ; 0.180 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5020 ; 0.009 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL 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 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 USED IF PRESENT IN REMARK 3 THE INPUT. REMARK 4 REMARK 4 4C83 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-NOV-13. REMARK 100 THE PDBE ID CODE IS EBI-58513. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : CLSI REMARK 200 BEAMLINE : CMCF-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTAL CLEAR REMARK 200 DATA SCALING SOFTWARE : CRYSTAL CLEAR REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26006 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.69 REMARK 200 RESOLUTION RANGE LOW (A) : 40.00 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5 REMARK 200 DATA REDUNDANCY : 1.96 REMARK 200 R MERGE (I) : 0.05 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.30 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.79 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1 REMARK 200 DATA REDUNDANCY IN SHELL : 1.95 REMARK 200 R MERGE FOR SHELL (I) : 0.14 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.30 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: 1MF2 REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.22 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5650 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19460 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.8 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5670 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19620 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.8 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 ASP A 1 REMARK 465 GLY A 129 REMARK 465 ASP A 130 REMARK 465 THR A 131 REMARK 465 THR A 132 REMARK 465 ASP C 1 REMARK 465 GLY C 129 REMARK 465 ASP C 130 REMARK 465 THR C 131 REMARK 465 THR C 132 REMARK 465 GLN D 1 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 NH1 ARG A 94 OE2 GLU A 96 2.14 REMARK 500 OG SER B 12 CG LYS B 107 2.18 REMARK 500 O VAL B 30 OH TYR B 71 1.93 REMARK 500 OG SER B 191 OD1 ASN B 210 2.07 REMARK 500 NH1 ARG C 66 O SER C 82B 2.03 REMARK 500 NH2 ARG C 66 OD2 ASP C 86 1.99 REMARK 500 NH1 ARG C 94 OE2 GLU C 96 2.00 REMARK 500 NH1 ARG D 61 OD2 ASP D 82 2.13 REMARK 500 O SER D 63 CD PRO D 74 2.06 REMARK 500 OG SER D 191 OD1 ASN D 210 2.04 REMARK 500 REMARK 500 REMARK: NULL 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 OG SER B 26 OD1 ASN D 157 2556 2.12 REMARK 500 REMARK 500 REMARK: NULL 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 PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS A 128 CA - CB - SG ANGL. DEV. = -8.9 DEGREES REMARK 500 PRO B 74 C - N - CD ANGL. DEV. = -22.7 DEGREES REMARK 500 CYS C 128 CA - CB - SG ANGL. DEV. = -16.6 DEGREES REMARK 500 CYS D 214 CA - CB - SG ANGL. DEV. = -6.9 DEGREES 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 LYS A 43 -1.12 83.72 REMARK 500 TRP B 47 -61.34 -123.89 REMARK 500 THR B 51 -60.33 75.48 REMARK 500 ALA B 84 -162.70 -169.16 REMARK 500 SER C 54 -5.80 84.69 REMARK 500 ASN C 76 20.99 82.43 REMARK 500 TRP D 47 -58.87 -122.61 REMARK 500 THR D 51 -58.49 75.81 REMARK 500 GLU D 213 -3.95 84.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND ARE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): THESE HAVE BEEN REPOSITIONED REMARK 525 BY APPLYING THE SYMMETRY TRANSFORMATION INDICATED. REMARK 525 REMARK 525 M RES CSSEQI ORIGINAL COORDINATES SYMMETRY TRANS. DIST. REMARK 525 X Y Z REMARK 525 HOH A2001 10.434 58.741 1.889 001 545 3.63 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1221 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1221 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NDG A1216 THROUGH KDO A1220 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NDG C1216 THROUGH KDO C1220 REMARK 999 REMARK 999 SEQUENCE REMARK 999 SEQUENCE NOT AVAILABLE ON DATABASES DBREF 4C83 A 1 215 PDB 4C83 4C83 1 215 DBREF 4C83 B 1 214 PDB 4C83 4C83 1 214 DBREF 4C83 C 1 215 PDB 4C83 4C83 1 215 DBREF 4C83 D 1 214 PDB 4C83 4C83 1 214 SEQRES 1 A 220 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 220 PRO GLY GLY SER ARG LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 A 220 PHE THR PHE ARG ARG PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 A 220 SER PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE GLY SEQRES 5 A 220 GLY GLY SER SER THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 A 220 GLY ARG PHE THR ILE SER ARG ASP ASN PRO LYS ASN THR SEQRES 7 A 220 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 A 220 ALA MET TYR TYR CYS THR ARG ASP GLU THR GLY SER TRP SEQRES 9 A 220 PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 A 220 ALA ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU ALA SEQRES 11 A 220 PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR LEU SEQRES 12 A 220 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR SEQRES 13 A 220 LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS SEQRES 14 A 220 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SEQRES 15 A 220 SER SER SER VAL THR VAL THR SER SER THR TRP PRO SER SEQRES 16 A 220 GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER SER SEQRES 17 A 220 THR LYS VAL ASP LYS LYS ILE GLU PRO ARG VAL PRO SEQRES 1 B 214 GLN ILE VAL LEU SER GLN SER PRO ALA ILE MET SER ALA SEQRES 2 B 214 SER PRO GLY GLU LYS VAL THR MET THR CYS SER ALA SER SEQRES 3 B 214 SER SER VAL ARG TYR MET HIS TRP TYR GLN GLN LYS SER SEQRES 4 B 214 GLY THR SER PRO LYS ARG TRP ILE TYR ASP THR SER LYS SEQRES 5 B 214 LEU ALA SER GLY VAL PRO THR ARG PHE SER GLY SER GLY SEQRES 6 B 214 SER GLY THR SER TYR SER LEU PRO ILE SER SER MET GLU SEQRES 7 B 214 ALA GLU ASP GLY ALA SER TYR TYR CYS GLN GLN TRP ASN SEQRES 8 B 214 GLY TYR PRO PRO LEU THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 B 214 GLU MET LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 B 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 B 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 B 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 B 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 B 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 B 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 B 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 B 214 PHE ASN ARG ASN GLU CYS SEQRES 1 C 220 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 220 PRO GLY GLY SER ARG LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 C 220 PHE THR PHE ARG ARG PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 C 220 SER PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE GLY SEQRES 5 C 220 GLY GLY SER SER THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 C 220 GLY ARG PHE THR ILE SER ARG ASP ASN PRO LYS ASN THR SEQRES 7 C 220 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 C 220 ALA MET TYR TYR CYS THR ARG ASP GLU THR GLY SER TRP SEQRES 9 C 220 PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 C 220 ALA ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU ALA SEQRES 11 C 220 PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR LEU SEQRES 12 C 220 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR SEQRES 13 C 220 LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS SEQRES 14 C 220 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SEQRES 15 C 220 SER SER SER VAL THR VAL THR SER SER THR TRP PRO SER SEQRES 16 C 220 GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER SER SEQRES 17 C 220 THR LYS VAL ASP LYS LYS ILE GLU PRO ARG VAL PRO SEQRES 1 D 214 GLN ILE VAL LEU SER GLN SER PRO ALA ILE MET SER ALA SEQRES 2 D 214 SER PRO GLY GLU LYS VAL THR MET THR CYS SER ALA SER SEQRES 3 D 214 SER SER VAL ARG TYR MET HIS TRP TYR GLN GLN LYS SER SEQRES 4 D 214 GLY THR SER PRO LYS ARG TRP ILE TYR ASP THR SER LYS SEQRES 5 D 214 LEU ALA SER GLY VAL PRO THR ARG PHE SER GLY SER GLY SEQRES 6 D 214 SER GLY THR SER TYR SER LEU PRO ILE SER SER MET GLU SEQRES 7 D 214 ALA GLU ASP GLY ALA SER TYR TYR CYS GLN GLN TRP ASN SEQRES 8 D 214 GLY TYR PRO PRO LEU THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 D 214 GLU MET LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 D 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 D 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 D 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 D 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 D 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 D 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 D 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 D 214 PHE ASN ARG ASN GLU CYS HET NDG A1216 14 HET GMH A1217 13 HET GMH A1218 13 HET BGC A1219 11 HET KDO A1220 16 HET SO4 A1221 5 HET NDG C1216 14 HET GMH C1217 13 HET GMH C1218 13 HET BGC C1219 11 HET KDO C1220 16 HET SO4 C1221 5 HETNAM SO4 SULFATE ION HETNAM GMH L-GLYCERO-D-MANNO-HEPTOPYRANOSE HETNAM KDO 3-DEOXY-D-MANNO-OCT-2-ULOSONIC ACID HETNAM BGC BETA-D-GLUCOSE HETNAM NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE FORMUL 5 SO4 2(O4 S 2-) FORMUL 6 GMH 4(C7 H14 O7) FORMUL 7 KDO 2(C8 H14 O8) FORMUL 8 BGC 2(C6 H12 O6) FORMUL 9 NDG 2(C8 H15 N O6) FORMUL 10 HOH *4(H2 O) HELIX 1 1 THR A 28 PHE A 32 5 5 HELIX 2 2 ARG A 83 THR A 87 5 5 HELIX 3 3 SER A 156 SER A 158 5 3 HELIX 4 4 SER B 121 SER B 127 1 7 HELIX 5 5 LYS B 183 HIS B 189 1 7 HELIX 6 6 THR C 28 PHE C 32 5 5 HELIX 7 7 ARG C 83 THR C 87 5 5 HELIX 8 8 SER C 156 SER C 158 5 3 HELIX 9 9 GLU D 79 GLY D 83 5 5 HELIX 10 10 SER D 121 SER D 127 1 7 HELIX 11 11 LYS D 183 GLU D 187 1 5 SHEET 1 AA 4 GLN A 3 SER A 7 0 SHEET 2 AA 4 ARG A 18 SER A 25 -1 O SER A 21 N SER A 7 SHEET 3 AA 4 THR A 77 MET A 82 -1 O LEU A 78 N CYS A 22 SHEET 4 AA 4 PHE A 67 ASP A 72 -1 O THR A 68 N GLN A 81 SHEET 1 AB 4 GLY A 10 VAL A 12 0 SHEET 2 AB 4 THR A 107 VAL A 111 -1 O LEU A 108 N GLY A 10 SHEET 3 AB 4 ALA A 88 ASP A 95 -1 O ALA A 88 N VAL A 109 SHEET 4 AB 4 PHE A 100A TRP A 103 -1 O TYR A 102 N ARG A 94 SHEET 1 AC 6 GLY A 10 VAL A 12 0 SHEET 2 AC 6 THR A 107 VAL A 111 -1 O LEU A 108 N GLY A 10 SHEET 3 AC 6 ALA A 88 ASP A 95 -1 O ALA A 88 N VAL A 109 SHEET 4 AC 6 GLY A 33 GLN A 39 -1 O GLY A 33 N ASP A 95 SHEET 5 AC 6 LEU A 45 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AC 6 ILE A 57 TYR A 59 -1 O TYR A 58 N TYR A 50 SHEET 1 AD 2 PHE A 100A TRP A 103 0 SHEET 2 AD 2 ALA A 88 ASP A 95 -1 N ARG A 94 O TYR A 102 SHEET 1 AE 4 SER A 120 LEU A 124 0 SHEET 2 AE 4 SER A 135 TYR A 145 -1 O GLY A 139 N LEU A 124 SHEET 3 AE 4 LEU A 174 THR A 184 -1 O TYR A 175 N TYR A 145 SHEET 4 AE 4 VAL A 163 GLN A 171 -1 O HIS A 164 N SER A 180 SHEET 1 AF 3 THR A 151 TRP A 154 0 SHEET 2 AF 3 THR A 194 HIS A 199 -1 O ASN A 196 N THR A 153 SHEET 3 AF 3 THR A 204 LYS A 209 -1 O THR A 204 N HIS A 199 SHEET 1 BA 3 LEU B 4 SER B 7 0 SHEET 2 BA 3 VAL B 19 ALA B 25 -1 O THR B 22 N SER B 7 SHEET 3 BA 3 SER B 72 ILE B 75 -1 O LEU B 73 N MET B 21 SHEET 1 BB 4 ILE B 10 ALA B 13 0 SHEET 2 BB 4 THR B 102 MET B 106 1 O LYS B 103 N MET B 11 SHEET 3 BB 4 SER B 85 TRP B 91 -1 O TYR B 86 N THR B 102 SHEET 4 BB 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90 SHEET 1 BC 6 ILE B 10 ALA B 13 0 SHEET 2 BC 6 THR B 102 MET B 106 1 O LYS B 103 N MET B 11 SHEET 3 BC 6 SER B 85 TRP B 91 -1 O TYR B 86 N THR B 102 SHEET 4 BC 6 TYR B 32 GLN B 38 -1 O TYR B 32 N TRP B 91 SHEET 5 BC 6 LYS B 45 TYR B 49 -1 O LYS B 45 N GLN B 37 SHEET 6 BC 6 LYS B 53 LEU B 54 -1 O LYS B 53 N TYR B 49 SHEET 1 BD 2 THR B 97 PHE B 98 0 SHEET 2 BD 2 SER B 85 TRP B 91 -1 O GLN B 90 N THR B 97 SHEET 1 BE 4 THR B 114 PHE B 118 0 SHEET 2 BE 4 GLY B 129 PHE B 139 -1 O VAL B 133 N PHE B 118 SHEET 3 BE 4 TYR B 173 THR B 182 -1 O TYR B 173 N PHE B 139 SHEET 4 BE 4 VAL B 159 TRP B 163 -1 O LEU B 160 N THR B 178 SHEET 1 BF 4 SER B 153 ARG B 155 0 SHEET 2 BF 4 ASN B 145 ILE B 150 -1 O TRP B 148 N ARG B 155 SHEET 3 BF 4 SER B 191 THR B 197 -1 O THR B 193 N LYS B 149 SHEET 4 BF 4 ILE B 205 ASN B 210 -1 O ILE B 205 N ALA B 196 SHEET 1 CA 4 GLN C 3 SER C 7 0 SHEET 2 CA 4 ARG C 18 SER C 25 -1 O SER C 21 N SER C 7 SHEET 3 CA 4 THR C 77 MET C 82 -1 O LEU C 78 N CYS C 22 SHEET 4 CA 4 PHE C 67 ASP C 72 -1 O THR C 68 N GLN C 81 SHEET 1 CB 4 GLY C 10 VAL C 12 0 SHEET 2 CB 4 THR C 107 VAL C 111 -1 O LEU C 108 N GLY C 10 SHEET 3 CB 4 ALA C 88 ASP C 95 -1 O ALA C 88 N VAL C 109 SHEET 4 CB 4 PHE C 100A TRP C 103 -1 O TYR C 102 N ARG C 94 SHEET 1 CC 6 GLY C 10 VAL C 12 0 SHEET 2 CC 6 THR C 107 VAL C 111 -1 O LEU C 108 N GLY C 10 SHEET 3 CC 6 ALA C 88 ASP C 95 -1 O ALA C 88 N VAL C 109 SHEET 4 CC 6 MET C 34 SER C 40 -1 O HIS C 35 N THR C 93 SHEET 5 CC 6 GLY C 44 ILE C 51 -1 O GLY C 44 N SER C 40 SHEET 6 CC 6 ILE C 57 TYR C 59 -1 O TYR C 58 N TYR C 50 SHEET 1 CD 2 PHE C 100A TRP C 103 0 SHEET 2 CD 2 ALA C 88 ASP C 95 -1 O ARG C 94 N ALA C 101 SHEET 1 CE 4 SER C 120 LEU C 124 0 SHEET 2 CE 4 VAL C 136 TYR C 145 -1 O GLY C 139 N LEU C 124 SHEET 3 CE 4 LEU C 174 VAL C 183 -1 O TYR C 175 N TYR C 145 SHEET 4 CE 4 VAL C 163 GLN C 171 -1 O HIS C 164 N SER C 180 SHEET 1 CF 3 THR C 151 TRP C 154 0 SHEET 2 CF 3 THR C 194 HIS C 199 -1 O ASN C 196 N THR C 153 SHEET 3 CF 3 THR C 204 LYS C 209 -1 O THR C 204 N HIS C 199 SHEET 1 DA 4 LEU D 4 SER D 7 0 SHEET 2 DA 4 VAL D 19 ALA D 25 -1 O THR D 22 N SER D 7 SHEET 3 DA 4 SER D 70 ILE D 75 -1 O TYR D 71 N CYS D 23 SHEET 4 DA 4 SER D 65 SER D 67 -1 O SER D 65 N SER D 72 SHEET 1 DB 4 ILE D 10 ALA D 13 0 SHEET 2 DB 4 THR D 102 MET D 106 1 O LYS D 103 N MET D 11 SHEET 3 DB 4 ALA D 84 GLN D 90 -1 O ALA D 84 N LEU D 104 SHEET 4 DB 4 THR D 97 PHE D 98 -1 O THR D 97 N GLN D 90 SHEET 1 DC 6 ILE D 10 ALA D 13 0 SHEET 2 DC 6 THR D 102 MET D 106 1 O LYS D 103 N MET D 11 SHEET 3 DC 6 ALA D 84 GLN D 90 -1 O ALA D 84 N LEU D 104 SHEET 4 DC 6 MET D 33 GLN D 38 -1 O HIS D 34 N GLN D 89 SHEET 5 DC 6 LYS D 45 TYR D 49 -1 O LYS D 45 N GLN D 37 SHEET 6 DC 6 LYS D 53 LEU D 54 -1 O LYS D 53 N TYR D 49 SHEET 1 DD 2 THR D 97 PHE D 98 0 SHEET 2 DD 2 ALA D 84 GLN D 90 -1 O GLN D 90 N THR D 97 SHEET 1 DE 4 THR D 114 PHE D 118 0 SHEET 2 DE 4 GLY D 129 PHE D 139 -1 O VAL D 133 N PHE D 118 SHEET 3 DE 4 TYR D 173 THR D 182 -1 O TYR D 173 N PHE D 139 SHEET 4 DE 4 VAL D 159 TRP D 163 -1 O LEU D 160 N THR D 178 SHEET 1 DF 4 SER D 153 ARG D 155 0 SHEET 2 DF 4 ASN D 145 ILE D 150 -1 O TRP D 148 N ARG D 155 SHEET 3 DF 4 SER D 191 THR D 197 -1 O THR D 193 N LYS D 149 SHEET 4 DF 4 ILE D 205 ASN D 210 -1 O ILE D 205 N ALA D 196 SSBOND 1 CYS A 22 CYS A 92 1555 1555 2.09 SSBOND 2 CYS A 128 CYS B 214 1555 1555 1.96 SSBOND 3 CYS A 140 CYS A 195 1555 1555 2.11 SSBOND 4 CYS B 23 CYS B 88 1555 1555 2.09 SSBOND 5 CYS B 134 CYS B 194 1555 1555 2.03 SSBOND 6 CYS C 22 CYS C 92 1555 1555 2.05 SSBOND 7 CYS C 128 CYS D 214 1555 1555 2.10 SSBOND 8 CYS C 140 CYS C 195 1555 1555 2.05 SSBOND 9 CYS D 23 CYS D 88 1555 1555 2.07 SSBOND 10 CYS D 134 CYS D 194 1555 1555 1.97 LINK C1 NDG A1216 O2 GMH A1217 1555 1555 1.45 LINK C1 GMH A1217 O3 GMH A1218 1555 1555 1.43 LINK C1 GMH A1218 O5 KDO A1220 1555 1555 1.48 LINK O4 GMH A1218 C1 BGC A1219 1555 1555 1.44 LINK C1 NDG C1216 O2 GMH C1217 1555 1555 1.43 LINK C1 GMH C1217 O3 GMH C1218 1555 1555 1.40 LINK O4 GMH C1218 C1 BGC C1219 1555 1555 1.45 LINK C1 GMH C1218 O5 KDO C1220 1555 1555 1.38 CISPEP 1 PHE A 146 PRO A 147 0 -9.00 CISPEP 2 GLU A 148 PRO A 149 0 8.48 CISPEP 3 TRP A 188 PRO A 189 0 11.89 CISPEP 4 SER B 7 PRO B 8 0 -2.95 CISPEP 5 PRO B 95 PRO B 95A 0 5.20 CISPEP 6 TYR B 140 PRO B 141 0 2.60 CISPEP 7 PHE C 146 PRO C 147 0 -10.23 CISPEP 8 GLU C 148 PRO C 149 0 6.14 CISPEP 9 TRP C 188 PRO C 189 0 8.88 CISPEP 10 SER D 7 PRO D 8 0 -4.73 CISPEP 11 PRO D 95 PRO D 95A 0 6.77 CISPEP 12 TYR D 140 PRO D 141 0 0.36 SITE 1 AC1 6 GLY A 52 GLY A 52A GLY A 53 SER A 54 SITE 2 AC1 6 SER A 55 THR A 56 SITE 1 AC2 7 GLY C 52 GLY C 52A GLY C 53 SER C 54 SITE 2 AC2 7 SER C 55 THR C 56 BGC C1219 SITE 1 AC3 8 PHE A 32 GLY A 33 TYR A 50 THR A 56 SITE 2 AC3 8 ASP A 95 THR A 97 GLY A 98 SER A 99 SITE 1 AC4 20 PHE A 32 GLY A 33 TYR A 50 THR A 56 SITE 2 AC4 20 ASP A 95 THR A 97 GLY A 98 SER A 99 SITE 3 AC4 20 ARG C 31 PHE C 32 GLY C 33 TYR C 50 SITE 4 AC4 20 THR C 56 ASP C 95 GLU C 96 THR C 97 SITE 5 AC4 20 GLY C 98 SER C 99 SO4 C1221 TRP D 91 CRYST1 62.628 64.192 64.403 87.51 89.82 73.41 P 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 0.015967 -0.004757 0.000161 0.00000 SCALE2 0.000000 0.016255 -0.000722 0.00000 SCALE3 0.000000 0.000000 0.015543 0.00000