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HEADER IMMUNE SYSTEM 20-AUG-02 1MHH TITLE ANTIBODY-ANTIGEN COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB, LIGHT CHAIN; COMPND 3 CHAIN: A, C; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: FAB, HEAVY CHAIN; COMPND 6 CHAIN: B, D; COMPND 7 MOL_ID: 3; COMPND 8 MOLECULE: PROTEIN L DOMAIN C; COMPND 9 CHAIN: E, F; COMPND 10 ENGINEERED: YES; COMPND 11 MUTATION: YES 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; SOURCE 7 MOL_ID: 3; SOURCE 8 ORGANISM_SCIENTIFIC: PEPTOSTREPTOCOCCUS MAGNUS; SOURCE 9 ORGANISM_COMMON: BACTERIA; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 12 EXPRESSION_SYSTEM_STRAIN: JM103; SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PKK233-3 KEYWDS ANTIBODY-ANTIGEN COMPLEX, B CELL SUPERANTIGEN, KEYWDS 2 IMMUNOGLOBULIN BINDING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR M.GRAILLE,E.A.STURA REVDAT 1 14-JAN-03 1MHH 0 JRNL AUTH M.GRAILLE,S.HARRISON,M.P.CRUMP,S.C.FINDLOW, JRNL AUTH 2 N.G.HOUSDEN,B.H.MULLER,N.BATTAIL-POIROT,G.SIBAI, JRNL AUTH 3 B.J.SUTTON,M.J.TAUSSIG,C.JOLIVET-REYNAUD,M.G.GORE, JRNL AUTH 4 E.A.STURA JRNL TITL EVIDENCE FOR PLASTICITY AND STRUCTURAL MIMICRY AT JRNL TITL 2 THE IMMUNOGLOBULIN LIGHT CHAIN-PROTEIN L INTERFACE JRNL REF J.BIOL.CHEM. V. 277 47500 2002 JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.GRAILLE,E.A.STURA,N.G.HOUSDEN,J.A.BECKINGHAM, REMARK 1 AUTH 2 S.P.BOTTOMLEY,D.BEALE,M.J.TAUSSIG,B.J.SUTTON, REMARK 1 AUTH 3 M.G.GORE,J-B.CHARBONNIER REMARK 1 TITL COMPLEX BETWEEN PEPTOSTREPTOCOCCUS MAGNUS PROTEIN REMARK 1 TITL 2 L AND A HUMAN ANTIBODY REVEALS STRUCTURAL REMARK 1 TITL 3 CONVERGENCE IN THE INTERACTION MODES OF FAB REMARK 1 TITL 4 BINDING MODES REMARK 1 REF STRUCTURE V. 9 679 2001 REMARK 1 REFN ASTM STRUE6 UK ISSN 0969-2126 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 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) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.0 REMARK 3 NUMBER OF REFLECTIONS : 62052 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) : 0.197 REMARK 3 FREE R VALUE : 0.247 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 3138 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL 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) : 2.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.11 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2244 REMARK 3 BIN FREE R VALUE : 0.2349 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 54 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 7743 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 8 REMARK 3 SOLVENT ATOMS : 739 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 38.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -9.08000 REMARK 3 B22 (A**2) : 3.59600 REMARK 3 B33 (A**2) : 5.48400 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) : 0.24 REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.005 REMARK 3 BOND ANGLES (DEGREES) : 1.30 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 : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : NULL 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 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1MHH 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 3.101 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB016914. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 18-FEB-2001; 04-JUN-2001 REMARK 200 TEMPERATURE (KELVIN) : 100; 100 REMARK 200 PH : 4.50 REMARK 200 NUMBER OF CRYSTALS USED : 2 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : ESRF; ESRF REMARK 200 BEAMLINE : ID14-2; ID14-4 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.934; 0.91842 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD; CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69723 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6 REMARK 200 DATA REDUNDANCY : 6.770 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.06700 REMARK 200 FOR THE DATA SET : 26.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16 REMARK 200 COMPLETENESS FOR SHELL (%) : 85.0 REMARK 200 DATA REDUNDANCY IN SHELL : 5.86 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.41700 REMARK 200 FOR SHELL : 3.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.42 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10%(WT/WT) MPEG 5K, 100MM SODIUM REMARK 280 ACETATE, PH 4.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 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 39.24300 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.57350 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.47850 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.57350 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.24300 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.47850 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 6 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: A, B, E 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 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F 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 THR B 132 REMARK 465 ASN B 133 REMARK 465 ALA D 130 REMARK 465 GLN D 131 REMARK 465 THR D 132 REMARK 465 LYS F 1882 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 GLY F1881 O 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 34 SD MET B 34 CE 0.050 REMARK 500 MET B 48 SD MET B 48 CE 0.036 REMARK 500 PRO B 149 CG PRO B 149 CD 0.038 REMARK 500 PRO D 149 CG PRO D 149 CD 0.037 REMARK 500 LYS D 209 C ILE D 210 N 0.135 REMARK 500 ILE D 210 C VAL D 211 N 0.130 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 LEU A 33 CA - CB - CG ANGL. DEV. = -8.9 DEGREES REMARK 500 LEU A 73 N - CA - C ANGL. DEV. = -8.0 DEGREES REMARK 500 ILE A 75 N - CA - C ANGL. DEV. = -8.2 DEGREES REMARK 500 CYS A 88 N - CA - C ANGL. DEV. = -8.4 DEGREES REMARK 500 GLY A 99 N - CA - C ANGL. DEV. = -7.8 DEGREES REMARK 500 LYS A 107 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 THR A 114 N - CA - C ANGL. DEV. = -9.3 DEGREES REMARK 500 LEU A 136 N - CA - C ANGL. DEV. =-10.8 DEGREES REMARK 500 ASN A 137 N - CA - C ANGL. DEV. = 8.9 DEGREES REMARK 500 ASP A 165 N - CA - C ANGL. DEV. = -8.3 DEGREES REMARK 500 GLY B 65 N - CA - C ANGL. DEV. = 9.0 DEGREES REMARK 500 GLU B 72 N - CA - C ANGL. DEV. =-13.2 DEGREES REMARK 500 CYS B 92 N - CA - C ANGL. DEV. =-11.1 DEGREES REMARK 500 GLN B 99 N - CA - C ANGL. DEV. = 8.8 DEGREES REMARK 500 GLY B 104 N - CA - C ANGL. DEV. =-10.4 DEGREES REMARK 500 CYS B 140 CA - CB - SG ANGL. DEV. = 9.3 DEGREES REMARK 500 LEU C 11 CA - CB - CG ANGL. DEV. = 8.0 DEGREES REMARK 500 ASN C 31 N - CA - C ANGL. DEV. = -7.8 DEGREES REMARK 500 LEU C 73 N - CA - C ANGL. DEV. = -8.2 DEGREES REMARK 500 CYS C 88 N - CA - C ANGL. DEV. = -8.8 DEGREES REMARK 500 GLY C 99 N - CA - C ANGL. DEV. = -7.9 DEGREES REMARK 500 THR C 114 N - CA - C ANGL. DEV. = -8.5 DEGREES REMARK 500 LEU C 136 N - CA - C ANGL. DEV. = -9.7 DEGREES REMARK 500 ASN C 137 N - CA - C ANGL. DEV. = 9.0 DEGREES REMARK 500 LEU D 45 CA - CB - CG ANGL. DEV. = 9.8 DEGREES REMARK 500 ALA D 60 N - CA - C ANGL. DEV. = -8.5 DEGREES REMARK 500 GLY D 65 N - CA - C ANGL. DEV. = 9.4 DEGREES REMARK 500 GLU D 72 N - CA - C ANGL. DEV. =-12.4 DEGREES REMARK 500 CYS D 92 N - CA - C ANGL. DEV. =-11.8 DEGREES REMARK 500 GLN D 99 N - CA - C ANGL. DEV. = 9.9 DEGREES REMARK 500 GLY D 104 N - CA - C ANGL. DEV. =-10.2 DEGREES REMARK 500 SER D 120 N - CA - C ANGL. DEV. = -9.8 DEGREES REMARK 500 CYS D 140 CA - CB - SG ANGL. DEV. = 9.4 DEGREES REMARK 500 LEU D 177 CA - CB - CG ANGL. DEV. = 8.2 DEGREES REMARK 500 GLN E 835 N - CA - C ANGL. DEV. = -8.0 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 ALA A 51 -37.70 64.41 REMARK 500 ALA C 51 -41.02 73.72 REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE 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): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 2061 DISTANCE = 6.92 ANGSTROMS REMARK 525 HOH 2158 DISTANCE = 5.61 ANGSTROMS REMARK 525 HOH 2509 DISTANCE = 6.17 ANGSTROMS REMARK 525 HOH 2537 DISTANCE = 6.77 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1HEZ RELATED DB: PDB REMARK 900 1HEZ CONTAINS COMPLEX BETWEEN PEPTOSTREPTOCOCCUS MAGNUS REMARK 900 PROTEIN L AND A HUMAN ANTIBODY SEQRES 1 A 220 ASP ILE VAL MET SER GLN SER PRO SER SER LEU ALA VAL SEQRES 2 A 220 SER ALA GLY GLU LYS VAL THR MET SER CYS LYS SER SER SEQRES 3 A 220 GLN SER LEU LEU ASN SER ARG THR ARG LYS ASN TYR LEU SEQRES 4 A 220 ALA TRP TYR GLN GLN LYS PRO GLY GLN SER PRO LYS VAL SEQRES 5 A 220 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 A 220 ASP ARG PHE THR GLY ARG GLY SER GLY THR ASP PHE THR SEQRES 7 A 220 LEU THR ILE SER SER VAL GLN ALA GLU ASP GLN ALA VAL SEQRES 8 A 220 TYR TYR CYS LYS GLN ALA TYR ILE PRO PRO LEU THR PHE SEQRES 9 A 220 GLY ALA GLY THR LYS LEU GLU LEU LYS ARG ALA ASP ALA SEQRES 10 A 220 ALA PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN SEQRES 11 A 220 LEU THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN SEQRES 12 A 220 ASN PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE SEQRES 13 A 220 ASP GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP SEQRES 14 A 220 THR ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SEQRES 15 A 220 SER THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS SEQRES 16 A 220 ASN SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SEQRES 17 A 220 SER PRO ILE VAL LYS SER PHE ASN ARG ASN GLU AEA SEQRES 1 B 217 GLN ILE GLN LEU VAL GLN SER GLY PRO GLU LEU LYS LYS SEQRES 2 B 217 PRO GLY GLU THR VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 B 217 TYR THR PHE THR ASP PHE SER MET HIS TRP VAL ASN GLN SEQRES 4 B 217 ALA PRO GLY LYS GLY LEU ASN TRP MET GLY TRP VAL ASN SEQRES 5 B 217 THR GLU THR GLY GLU PRO THR TYR ALA ASP ASP PHE LYS SEQRES 6 B 217 GLY ARG PHE ALA PHE SER LEU GLU THR SER ALA SER THR SEQRES 7 B 217 ALA TYR LEU GLN ILE ASN SER LEU LYS ASN GLU ASP THR SEQRES 8 B 217 ALA THR TYR PHE CYS ALA ARG PHE LEU LEU ARG GLN TYR SEQRES 9 B 217 PHE ASP VAL TRP GLY ALA GLY THR THR VAL THR VAL SER SEQRES 10 B 217 SER ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA SEQRES 11 B 217 PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU SEQRES 12 B 217 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR SEQRES 13 B 217 VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS SEQRES 14 B 217 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SEQRES 15 B 217 SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SER SEQRES 16 B 217 GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER SEQRES 17 B 217 THR LYS VAL ASP LYS LYS ILE VAL PRO SEQRES 1 C 220 ASP ILE VAL MET SER GLN SER PRO SER SER LEU ALA VAL SEQRES 2 C 220 SER ALA GLY GLU LYS VAL THR MET SER CYS LYS SER SER SEQRES 3 C 220 GLN SER LEU LEU ASN SER ARG THR ARG LYS ASN TYR LEU SEQRES 4 C 220 ALA TRP TYR GLN GLN LYS PRO GLY GLN SER PRO LYS VAL SEQRES 5 C 220 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 C 220 ASP ARG PHE THR GLY ARG GLY SER GLY THR ASP PHE THR SEQRES 7 C 220 LEU THR ILE SER SER VAL GLN ALA GLU ASP GLN ALA VAL SEQRES 8 C 220 TYR TYR CYS LYS GLN ALA TYR ILE PRO PRO LEU THR PHE SEQRES 9 C 220 GLY ALA GLY THR LYS LEU GLU LEU LYS ARG ALA ASP ALA SEQRES 10 C 220 ALA PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN SEQRES 11 C 220 LEU THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN SEQRES 12 C 220 ASN PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE SEQRES 13 C 220 ASP GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP SEQRES 14 C 220 THR ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SEQRES 15 C 220 SER THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS SEQRES 16 C 220 ASN SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SEQRES 17 C 220 SER PRO ILE VAL LYS SER PHE ASN ARG ASN GLU AEA SEQRES 1 D 217 GLN ILE GLN LEU VAL GLN SER GLY PRO GLU LEU LYS LYS SEQRES 2 D 217 PRO GLY GLU THR VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 D 217 TYR THR PHE THR ASP PHE SER MET HIS TRP VAL ASN GLN SEQRES 4 D 217 ALA PRO GLY LYS GLY LEU ASN TRP MET GLY TRP VAL ASN SEQRES 5 D 217 THR GLU THR GLY GLU PRO THR TYR ALA ASP ASP PHE LYS SEQRES 6 D 217 GLY ARG PHE ALA PHE SER LEU GLU THR SER ALA SER THR SEQRES 7 D 217 ALA TYR LEU GLN ILE ASN SER LEU LYS ASN GLU ASP THR SEQRES 8 D 217 ALA THR TYR PHE CYS ALA ARG PHE LEU LEU ARG GLN TYR SEQRES 9 D 217 PHE ASP VAL TRP GLY ALA GLY THR THR VAL THR VAL SER SEQRES 10 D 217 SER ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA SEQRES 11 D 217 PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU SEQRES 12 D 217 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR SEQRES 13 D 217 VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS SEQRES 14 D 217 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SEQRES 15 D 217 SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SER SEQRES 16 D 217 GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER SEQRES 17 D 217 THR LYS VAL ASP LYS LYS ILE VAL PRO SEQRES 1 E 63 GLU VAL THR ILE LYS VAL ASN LEU ILE PHE ALA ASP GLY SEQRES 2 E 63 LYS ILE GLN THR ALA GLU PHE LYS GLY THR PHE GLU GLU SEQRES 3 E 63 ALA THR ALA GLU ALA TYR ARG TYR ALA ALA LEU LEU ALA SEQRES 4 E 63 LYS VAL ASN GLY GLU TRP THR ALA ASP LEU GLU ASP GLY SEQRES 5 E 63 GLY ASN HIS MET ASN ILE LYS PHE ALA GLY LYS SEQRES 1 F 63 GLU VAL THR ILE LYS VAL ASN LEU ILE PHE ALA ASP GLY SEQRES 2 F 63 LYS ILE GLN THR ALA GLU PHE LYS GLY THR PHE GLU GLU SEQRES 3 F 63 ALA THR ALA GLU ALA TYR ARG TYR ALA ALA LEU LEU ALA SEQRES 4 F 63 LYS VAL ASN GLY GLU TRP THR ALA ASP LEU GLU ASP GLY SEQRES 5 F 63 GLY ASN HIS MET ASN ILE LYS PHE ALA GLY LYS MODRES 1MHH AEA A 214 MODRES 1MHH AEA C 214 HET AEA A 214 10 HET AEA C 214 10 HET EDO 3001 4 HET EDO 4001 4 HETNAM AEA (2-AMINO-2-CARBAMOYL-ETHYLSULFANYL)-ACETIC ACID HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 1 AEA 2(C5 H10 N2 O3 S) FORMUL 7 EDO 2(C2 H6 O2) FORMUL 9 HOH *739(H2 O) HELIX 1 1 GLN A 79 GLN A 83 5 5 HELIX 2 2 SER A 121 THR A 126 1 6 HELIX 3 3 LYS A 183 ARG A 188 1 6 HELIX 4 4 THR B 28 PHE B 32 5 5 HELIX 5 5 ASP B 61 LYS B 64 5 4 HELIX 6 6 THR B 73 ALA B 75 5 3 HELIX 7 7 LYS B 83 THR B 87 5 5 HELIX 8 8 SER B 156 SER B 158 5 3 HELIX 9 9 PRO B 200 SER B 203 5 4 HELIX 10 10 GLN C 79 GLN C 83 5 5 HELIX 11 11 SER C 121 THR C 126 1 6 HELIX 12 12 LYS C 183 ARG C 188 1 6 HELIX 13 13 THR D 28 PHE D 32 5 5 HELIX 14 14 ASP D 61 LYS D 64 5 4 HELIX 15 15 THR D 73 ALA D 75 5 3 HELIX 16 16 LYS D 83 THR D 87 5 5 HELIX 17 17 SER D 156 SER D 158 5 3 HELIX 18 18 SER D 186 GLU D 191 1 6 HELIX 19 19 PRO D 200 SER D 203 5 4 HELIX 20 20 THR E 842 GLY E 862 1 21 HELIX 21 21 ASP E 870 GLY E 872 5 3 HELIX 22 22 THR F 1842 GLY F 1862 1 21 SHEET 1 A 4 MET A 4 SER A 7 0 SHEET 2 A 4 VAL A 19 SER A 25 -1 O LYS A 24 N SER A 5 SHEET 3 A 4 ASP A 70 ILE A 75 -1 O PHE A 71 N CYS A 23 SHEET 4 A 4 PHE A 62 SER A 67 -1 N THR A 63 O THR A 74 SHEET 1 B10 TRP E 864 GLU E 869 0 SHEET 2 B10 HIS E 874 PHE E 879 -1 O LYS E 878 N THR E 865 SHEET 3 B10 VAL E 821 ILE E 828 1 N ASN E 826 O ILE E 877 SHEET 4 B10 ILE E 834 GLY E 841 -1 O GLN E 835 N LEU E 827 SHEET 5 B10 SER A 10 SER A 14 -1 N ALA A 12 O THR E 836 SHEET 6 B10 THR A 102 LYS A 107 1 O GLU A 105 N LEU A 11 SHEET 7 B10 ALA A 84 GLN A 90 -1 N ALA A 84 O LEU A 104 SHEET 8 B10 LEU A 33 GLN A 38 -1 N TYR A 36 O TYR A 87 SHEET 9 B10 LYS A 45 TYR A 49 -1 O LYS A 45 N GLN A 37 SHEET 10 B10 THR A 53 ARG A 54 -1 O THR A 53 N TYR A 49 SHEET 1 C 8 TRP E 864 GLU E 869 0 SHEET 2 C 8 HIS E 874 PHE E 879 -1 O LYS E 878 N THR E 865 SHEET 3 C 8 VAL E 821 ILE E 828 1 N ASN E 826 O ILE E 877 SHEET 4 C 8 ILE E 834 GLY E 841 -1 O GLN E 835 N LEU E 827 SHEET 5 C 8 SER A 10 SER A 14 -1 N ALA A 12 O THR E 836 SHEET 6 C 8 THR A 102 LYS A 107 1 O GLU A 105 N LEU A 11 SHEET 7 C 8 ALA A 84 GLN A 90 -1 N ALA A 84 O LEU A 104 SHEET 8 C 8 THR A 97 PHE A 98 -1 O THR A 97 N GLN A 90 SHEET 1 D 2 LYS A 30 ASN A 31 0 SHEET 1 E 4 THR A 114 PHE A 118 0 SHEET 2 E 4 GLY A 129 PHE A 139 -1 O PHE A 135 N SER A 116 SHEET 3 E 4 TYR A 173 THR A 182 -1 O LEU A 181 N ALA A 130 SHEET 4 E 4 VAL A 159 TRP A 163 -1 N LEU A 160 O THR A 178 SHEET 1 F 4 SER A 153 ARG A 155 0 SHEET 2 F 4 ASN A 145 ILE A 150 -1 N ILE A 150 O SER A 153 SHEET 3 F 4 SER A 191 THR A 197 -1 O THR A 197 N ASN A 145 SHEET 4 F 4 ILE A 205 ASN A 210 -1 O LYS A 207 N CYS A 194 SHEET 1 G 4 GLN B 3 GLN B 6 0 SHEET 2 G 4 VAL B 18 SER B 25 -1 O LYS B 23 N VAL B 5 SHEET 3 G 4 THR B 77 ILE B 82 -1 O ILE B 82 N VAL B 18 SHEET 4 G 4 PHE B 67 GLU B 72 -1 N SER B 70 O TYR B 79 SHEET 1 H 5 PRO B 57 TYR B 59 0 SHEET 2 H 5 ASN B 46 VAL B 51 -1 N TRP B 50 O THR B 58 SHEET 3 H 5 MET B 34 GLN B 39 -1 N TRP B 36 O MET B 48 SHEET 4 H 5 ALA B 88 PHE B 95 -1 O PHE B 91 N VAL B 37 SHEET 1 I 6 PRO B 57 TYR B 59 0 SHEET 2 I 6 ASN B 46 VAL B 51 -1 N TRP B 50 O THR B 58 SHEET 3 I 6 MET B 34 GLN B 39 -1 N TRP B 36 O MET B 48 SHEET 4 I 6 ALA B 88 PHE B 95 -1 O PHE B 91 N VAL B 37 SHEET 5 I 6 THR B 107 VAL B 111 -1 O VAL B 109 N ALA B 88 SHEET 6 I 6 GLU B 10 LYS B 12 1 N GLU B 10 O THR B 110 SHEET 1 J 4 SER B 120 LEU B 124 0 SHEET 2 J 4 MET B 135 TYR B 145 -1 O LEU B 141 N TYR B 122 SHEET 3 J 4 TYR B 175 PRO B 184 -1 O LEU B 177 N VAL B 142 SHEET 4 J 4 VAL B 163 THR B 165 -1 N HIS B 164 O SER B 180 SHEET 1 K 4 SER B 120 LEU B 124 0 SHEET 2 K 4 MET B 135 TYR B 145 -1 O LEU B 141 N TYR B 122 SHEET 3 K 4 TYR B 175 PRO B 184 -1 O LEU B 177 N VAL B 142 SHEET 4 K 4 VAL B 169 LEU B 170 -1 N VAL B 169 O THR B 176 SHEET 1 L 3 THR B 151 TRP B 154 0 SHEET 2 L 3 THR B 194 HIS B 199 -1 O ASN B 196 N THR B 153 SHEET 3 L 3 THR B 204 LYS B 209 -1 O VAL B 206 N VAL B 197 SHEET 1 M 4 MET C 4 SER C 7 0 SHEET 2 M 4 VAL C 19 SER C 25 -1 O LYS C 24 N SER C 5 SHEET 3 M 4 ASP C 70 ILE C 75 -1 O PHE C 71 N CYS C 23 SHEET 4 M 4 PHE C 62 SER C 67 -1 N THR C 63 O THR C 74 SHEET 1 N10 TRP F1864 GLU F1869 0 SHEET 2 N10 HIS F1874 PHE F1879 -1 O ASN F1876 N ASP F1867 SHEET 3 N10 VAL F1821 ILE F1828 1 N ASN F1826 O ILE F1877 SHEET 4 N10 ILE F1834 GLY F1841 -1 O GLN F1835 N LEU F1827 SHEET 5 N10 SER C 10 SER C 14 -1 N ALA C 12 O THR F1836 SHEET 6 N10 THR C 102 LYS C 107 1 O GLU C 105 N LEU C 11 SHEET 7 N10 ALA C 84 GLN C 90 -1 N ALA C 84 O LEU C 104 SHEET 8 N10 LEU C 33 GLN C 38 -1 N TYR C 36 O TYR C 87 SHEET 9 N10 LYS C 45 TYR C 49 -1 O LEU C 47 N TRP C 35 SHEET 10 N10 THR C 53 ARG C 54 -1 O THR C 53 N TYR C 49 SHEET 1 O 8 TRP F1864 GLU F1869 0 SHEET 2 O 8 HIS F1874 PHE F1879 -1 O ASN F1876 N ASP F1867 SHEET 3 O 8 VAL F1821 ILE F1828 1 N ASN F1826 O ILE F1877 SHEET 4 O 8 ILE F1834 GLY F1841 -1 O GLN F1835 N LEU F1827 SHEET 5 O 8 SER C 10 SER C 14 -1 N ALA C 12 O THR F1836 SHEET 6 O 8 THR C 102 LYS C 107 1 O GLU C 105 N LEU C 11 SHEET 7 O 8 ALA C 84 GLN C 90 -1 N ALA C 84 O LEU C 104 SHEET 8 O 8 THR C 97 PHE C 98 -1 O THR C 97 N GLN C 90 SHEET 1 P 2 LYS C 30 ASN C 31 0 SHEET 1 Q 4 THR C 114 PHE C 118 0 SHEET 2 Q 4 GLY C 129 PHE C 139 -1 O VAL C 133 N PHE C 118 SHEET 3 Q 4 TYR C 173 THR C 182 -1 O LEU C 179 N VAL C 132 SHEET 4 Q 4 VAL C 159 TRP C 163 -1 N SER C 162 O SER C 176 SHEET 1 R 4 SER C 153 ARG C 155 0 SHEET 2 R 4 ASN C 145 ILE C 150 -1 N ILE C 150 O SER C 153 SHEET 3 R 4 SER C 191 THR C 197 -1 O THR C 197 N ASN C 145 SHEET 4 R 4 ILE C 205 ASN C 210 -1 O LYS C 207 N CYS C 194 SHEET 1 S 4 GLN D 3 GLN D 6 0 SHEET 2 S 4 VAL D 18 SER D 25 -1 O LYS D 23 N VAL D 5 SHEET 3 S 4 THR D 77 ILE D 82 -1 O ILE D 82 N VAL D 18 SHEET 4 S 4 PHE D 67 GLU D 72 -1 N SER D 70 O TYR D 79 SHEET 1 T 5 PRO D 57 TYR D 59 0 SHEET 2 T 5 LEU D 45 VAL D 51 -1 N TRP D 50 O THR D 58 SHEET 3 T 5 SER D 33 GLN D 39 -1 N TRP D 36 O MET D 48 SHEET 4 T 5 ALA D 88 PHE D 95 -1 O PHE D 91 N VAL D 37 SHEET 1 U 6 PRO D 57 TYR D 59 0 SHEET 2 U 6 LEU D 45 VAL D 51 -1 N TRP D 50 O THR D 58 SHEET 3 U 6 SER D 33 GLN D 39 -1 N TRP D 36 O MET D 48 SHEET 4 U 6 ALA D 88 PHE D 95 -1 O PHE D 91 N VAL D 37 SHEET 5 U 6 THR D 107 VAL D 111 -1 O THR D 107 N TYR D 90 SHEET 6 U 6 GLU D 10 LYS D 12 1 N GLU D 10 O THR D 110 SHEET 1 V 4 SER D 120 LEU D 124 0 SHEET 2 V 4 MET D 135 TYR D 145 -1 O LEU D 141 N TYR D 122 SHEET 3 V 4 LEU D 174 PRO D 184 -1 O LEU D 177 N VAL D 142 SHEET 4 V 4 VAL D 163 THR D 165 -1 N HIS D 164 O SER D 180 SHEET 1 W 4 SER D 120 LEU D 124 0 SHEET 2 W 4 MET D 135 TYR D 145 -1 O LEU D 141 N TYR D 122 SHEET 3 W 4 LEU D 174 PRO D 184 -1 O LEU D 177 N VAL D 142 SHEET 4 W 4 VAL D 169 GLN D 171 -1 N GLN D 171 O LEU D 174 SHEET 1 X 3 THR D 151 TRP D 154 0 SHEET 2 X 3 THR D 194 HIS D 199 -1 O ASN D 196 N THR D 153 SHEET 3 X 3 THR D 204 LYS D 209 -1 O VAL D 206 N VAL D 197 SSBOND 1 CYS A 23 CYS A 88 SSBOND 2 CYS A 134 CYS A 194 SSBOND 3 CYS B 22 CYS B 92 SSBOND 4 CYS B 140 CYS B 195 SSBOND 5 CYS C 23 CYS C 88 SSBOND 6 CYS C 134 CYS C 194 SSBOND 7 CYS D 22 CYS D 92 SSBOND 8 CYS D 140 CYS D 195 CISPEP 1 SER A 7 PRO A 8 0 -0.23 CISPEP 2 PRO A 94 PRO A 95 0 0.08 CISPEP 3 TYR A 140 PRO A 141 0 0.06 CISPEP 4 PHE B 146 PRO B 147 0 -0.30 CISPEP 5 GLU B 148 PRO B 149 0 -0.10 CISPEP 6 TRP B 188 PRO B 189 0 -0.10 CISPEP 7 SER C 7 PRO C 8 0 -0.11 CISPEP 8 PRO C 94 PRO C 95 0 -0.23 CISPEP 9 TYR C 140 PRO C 141 0 -0.15 CISPEP 10 PHE D 146 PRO D 147 0 -0.16 CISPEP 11 GLU D 148 PRO D 149 0 0.09 CISPEP 12 TRP D 188 PRO D 189 0 -0.01 CRYST1 78.486 100.957 149.147 90.00 90.00 90.00 P 21 21 21 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 0.012741 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009905 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006705 0.00000