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HEADER IMMUNE SYSTEM 27-AUG-02 1MJ8 TITLE HIGH RESOLUTION CRYSTAL STRUCTURE OF THE FAB FRAGMENT OF TITLE 2 THE ESTEROLYTIC ANTIBODY MS6-126 COMPND MOL_ID: 1; COMPND 2 MOLECULE: IMMUNOGLOBULIN MS6-126; COMPND 3 CHAIN: L; COMPND 4 FRAGMENT: FAB FRAGMENT, LIGHT CHAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: IMMUNOGLOBULIN MS6-126; COMPND 8 CHAIN: H; COMPND 9 FRAGMENT: FAB FRAGMENT, HEAVY CHAIN; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 CELL_LINE: HYBRIDOMA; SOURCE 5 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: MOUSE; SOURCE 7 OTHER_DETAILS: FUSING OF MOUSE SPLENOCYTES WITH MYELOMA SOURCE 8 CELL; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 11 ORGANISM_COMMON: MOUSE; SOURCE 12 CELL_LINE: HYBRIDOMA; SOURCE 13 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: MOUSE; SOURCE 15 OTHER_DETAILS: FUSING OF MOUSE SPLENOCYTES WITH MYELOMA SOURCE 16 CELL KEYWDS CATALYTIC ANTIBODY, ESTER HYDROLYSIS, ESTEROLYTIC, FAB, KEYWDS 2 IMMUNOGLOBULIN EXPDTA X-RAY DIFFRACTION AUTHOR S.N.RUZHEINIKOV,T.A.MURANOVA,S.E.SEDELNIKOVA,L.J.PARTRIDGE, AUTHOR 2 G.M.BLACKBURN,I.A.MURRAY,H.KAKINUMA,N.TAKASHI,K.SHIMAZAKI, AUTHOR 3 J.SUN,Y.NISHI,D.W.RICE REVDAT 1 23-SEP-03 1MJ8 0 JRNL AUTH S.N.RUZHEINIKOV,T.A.MURANOVA,S.E.SEDELNIKOVA, JRNL AUTH 2 L.J.PARTRIDGE,G.M.BLACKBURN,I.A.MURRAY,H.KAKINUMA, JRNL AUTH 3 N.TAKASHI,K.SHIMAZAKI,J.SUN,Y.NISHI,D.W.RICE JRNL TITL HIGH-RESOLUTION CRYSTAL STRUCTURE OF THE JRNL TITL 2 FAB-FRAGMENTS OF A FAMILY OF MOUSE CATALYTIC JRNL TITL 3 ANTIBODIES WITH ESTERASE ACTIVITY JRNL REF J.MOL.BIOL. V. 332 423 2003 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH T.A.MURANOVA,S.N.RUZHEINIKOV,S.E.SEDELNIKOVA, REMARK 1 AUTH 2 A.MOIR,L.J.PARTRIDGE,H.KAKINUMA,N.TAKASHI, REMARK 1 AUTH 3 K.SHIMAZAKI,J.SUN,Y.NISHI,D.W.RICE REMARK 1 TITL THE PREPARATION AND CRYSTALLIZATION OF FAB REMARK 1 TITL 2 FRAGMENTS OF A FAMILY OF MOUSE ESTEROLYTIC REMARK 1 TITL 3 CATALYTIC ANTIBODIES AND THEIR COMPLEXES WITH A REMARK 1 TITL 4 TRANSITION-STATE ANALOGUE REMARK 1 REF ACTA CRYSTALLOGR., SECT.D V. 57 1192 2001 REMARK 1 REFN ASTM ABCRE6 DK ISSN 0907-4449 REMARK 2 REMARK 2 RESOLUTION. 1.75 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) : 1.75 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00 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) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 39166 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) : 0.155 REMARK 3 FREE R VALUE : 0.221 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1960 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) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL 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 : 3349 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 25 REMARK 3 SOLVENT ATOMS : 665 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.80 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL 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) : NULL REMARK 3 BOND ANGLES (DEGREES) : 1.78 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC 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 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : ION.PARAM REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 4 : GOL.PAR REMARK 3 PARAMETER FILE 5 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1MJ8 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 RCSB016952. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-SEP-2000 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 8.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SRS REMARK 200 BEAMLINE : PX9.6 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.870 REMARK 200 MONOCHROMATOR : SI 111 REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39166 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750 REMARK 200 RESOLUTION RANGE LOW (A) : 10.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 89.1 REMARK 200 DATA REDUNDANCY : 3.500 REMARK 200 R MERGE (I) : 0.03700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 31.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78 REMARK 200 COMPLETENESS FOR SHELL (%) : 58.4 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.18300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 4.700 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 1MH5 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 45.85 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM PHOSPHATE, TRIS-HCL, PH REMARK 280 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K 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,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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 69.14200 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 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: L, H 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 LYS L 199 REMARK 465 THR L 200 REMARK 465 SER L 201 REMARK 465 THR L 202 REMARK 465 SER L 203 REMARK 465 GLN H 1 REMARK 465 GLY H 131 REMARK 465 ASP H 132 REMARK 465 THR H 133 REMARK 465 SER H 134 REMARK 465 GLY H 135 REMARK 465 ILE H 232 REMARK 465 LYS H 233 REMARK 465 PRO H 234 REMARK 465 CYS H 235 REMARK 465 PRO H 236 REMARK 465 PRO H 237 REMARK 465 CYS H 238 REMARK 465 LYS H 239 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 O PRO L 40 O HOH 516 2.06 REMARK 500 O HOH 119 O HOH 652 2.13 REMARK 500 O HOH 57 O HOH 455 2.16 REMARK 500 O HOH 118 O HOH 371 2.18 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 O HOH 231 O HOH 412 1454 2.13 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 L 51 SD MET L 51 CE -0.090 REMARK 500 MET L 175 SD MET L 175 CE -0.083 REMARK 500 CYS H 128 CA CYS H 128 CB 0.086 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 GLN L 6 N - CA - C ANGL. DEV. =-12.1 DEGREES REMARK 500 MET L 51 N - CA - C ANGL. DEV. = 10.0 DEGREES REMARK 500 THR L 114 N - CA - C ANGL. DEV. =-10.7 DEGREES REMARK 500 PRO H 52A N - CA - C ANGL. DEV. = 10.2 DEGREES REMARK 500 SER H 120 N - CA - C ANGL. DEV. =-11.3 DEGREES REMARK 500 CYS H 128 CB - CA - C ANGL. DEV. = 14.1 DEGREES REMARK 500 CYS H 128 N - CA - CB ANGL. DEV. =-10.1 DEGREES REMARK 500 VAL H 152 N - CA - C ANGL. DEV. = -9.8 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 MET L 51 -38.02 63.70 REMARK 500 SER H 65 -34.37 76.77 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 174 DISTANCE = 5.98 ANGSTROMS REMARK 525 HOH 439 DISTANCE = 5.05 ANGSTROMS REMARK 525 HOH 472 DISTANCE = 7.21 ANGSTROMS REMARK 525 HOH 602 DISTANCE = 7.34 ANGSTROMS REMARK 525 HOH 610 DISTANCE = 5.90 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1MH5 RELATED DB: PDB REMARK 900 THE STRUCTURE OF THE COMPLEX OF THE FAB FRAGMENT OF REMARK 900 THEESTEROLYTIC ANTIBODY MS6-164 AND A TRANSITION-STATE REMARK 900 ANALOG REMARK 900 RELATED ID: 1MIE RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE FAB FRAGMENT OF ESTEROLYTIC REMARK 900 ANTIBODY MS5-393 REMARK 900 RELATED ID: 1MJ7 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF THE FAB FRAGMENT OF REMARK 900 ESTEROLYTIC ANTIBODY MS5-393D9 AND A TRANSITION-STATE ANALOG REMARK 900 RELATED ID: 1MJJ RELATED DB: PDB REMARK 900 HIGH RESOLUTION CRYSTAL STRUCTURE OF THE COMPLEX OF THE FAB REMARK 900 FRAGMENT OF ESTEROLYTIC ANTIBODY MS6-12 AND A TRANSITION- REMARK 900 STATE ANALOG REMARK 900 RELATED ID: 1MJU RELATED DB: PDB REMARK 900 1.22 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE COMPLEX REMARK 900 OF THE FAB FRAGMENT OF ESTEROLYTIC ANTIBODY MS6-12 REMARK 999 REMARK 999 SEQUENCE REMARK 999 AN APPROPRIATE SEQUENCE DATABASE REFERENCE WAS REMARK 999 NOT AVAILABLE AT THE TIME OF PROCESSING. SEQRES 1 L 219 GLU ILE VAL MET THR GLN ALA ALA PRO SER VAL PRO VAL SEQRES 2 L 219 THR PRO GLY GLU SER VAL SER ILE SER CYS ARG SER SER SEQRES 3 L 219 LYS SER LEU LEU HIS SER ASN GLY ASN THR TYR LEU TYR SEQRES 4 L 219 TRP PHE LEU GLN ARG PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 L 219 ILE TYR ARG MET SER ASN LEU ALA SER GLY VAL PRO ASP SEQRES 6 L 219 ARG PHE SER GLY SER GLY SER GLY THR ALA PHE THR LEU SEQRES 7 L 219 ARG ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 L 219 TYR CYS LEU GLN HIS LEU GLU TYR PRO PHE THR PHE GLY SEQRES 9 L 219 ALA GLY THR LYS LEU GLU LEU LYS ARG ALA ASP ALA ALA SEQRES 10 L 219 PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU SEQRES 11 L 219 THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN SEQRES 12 L 219 PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP SEQRES 13 L 219 GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR SEQRES 14 L 219 ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SER SEQRES 15 L 219 THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SEQRES 16 L 219 SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER SEQRES 17 L 219 PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS SEQRES 1 H 230 GLN VAL GLN LEU GLN GLN PRO GLY ALA GLU LEU VAL LYS SEQRES 2 H 230 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY SEQRES 3 H 230 TYR THR PHE THR SER ASN TRP ILE ASN TRP VAL LYS GLN SEQRES 4 H 230 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ASN ILE TYR SEQRES 5 H 230 PRO GLY SER GLY TYR THR ASN TYR ASN GLU ARG PHE LYS SEQRES 6 H 230 SER LYS ALA THR LEU THR VAL ASP THR SER SER SER THR SEQRES 7 H 230 ALA TYR MET GLN LEU SER SER LEU THR SER ASP ASP SER SEQRES 8 H 230 ALA VAL TYR TYR CYS ALA ARG LYS HIS TYR PHE TYR ASP SEQRES 9 H 230 GLY VAL VAL TYR TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 10 H 230 SER ALA ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU SEQRES 11 H 230 ALA PRO VAL CYS GLY ASP THR SER GLY SER SER VAL THR SEQRES 12 H 230 LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL SEQRES 13 H 230 THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL SEQRES 14 H 230 HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR SEQRES 15 H 230 LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO SEQRES 16 H 230 SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER SEQRES 17 H 230 SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO SEQRES 18 H 230 THR ILE LYS PRO CYS PRO PRO CYS LYS HET PO4 801 5 HET PO4 802 5 HET PO4 803 5 HET PO4 804 5 HET PO4 805 5 HET GOL 700 6 HET GOL 701 6 HETNAM PO4 PHOSPHATE ION HETNAM GOL GLYCEROL FORMUL 3 PO4 5(O4 P 3-) FORMUL 8 GOL 2(C3 H8 O3) FORMUL 10 HOH *653(H2 O) HELIX 1 1 GLU L 79 VAL L 83 5 5 HELIX 2 2 SER L 121 THR L 126 1 6 HELIX 3 3 LYS L 183 ARG L 188 1 6 HELIX 4 4 THR H 28 ASN H 32 5 5 HELIX 5 5 GLU H 61 LYS H 64 5 4 HELIX 6 6 THR H 73 SER H 75 5 3 HELIX 7 7 THR H 83 SER H 87 5 5 HELIX 8 8 SER H 163 SER H 165 5 3 HELIX 9 9 PRO H 213 SER H 216 5 4 SHEET 1 A 4 MET L 4 THR L 5 0 SHEET 2 A 4 VAL L 19 SER L 25 -1 O ARG L 24 N THR L 5 SHEET 3 A 4 ALA L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 A 4 PHE L 62 GLY L 66 -1 N SER L 65 O THR L 72 SHEET 1 B 5 ASN L 53 LEU L 54 0 SHEET 2 B 5 GLN L 45 TYR L 49 -1 N TYR L 49 O ASN L 53 SHEET 3 B 5 LEU L 33 GLN L 38 -1 N LEU L 37 O GLN L 45 SHEET 4 B 5 GLY L 84 GLN L 90 -1 O LEU L 89 N TYR L 34 SHEET 5 B 5 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 C 6 ASN L 53 LEU L 54 0 SHEET 2 C 6 GLN L 45 TYR L 49 -1 N TYR L 49 O ASN L 53 SHEET 3 C 6 LEU L 33 GLN L 38 -1 N LEU L 37 O GLN L 45 SHEET 4 C 6 GLY L 84 GLN L 90 -1 O LEU L 89 N TYR L 34 SHEET 5 C 6 THR L 102 LEU L 106 -1 O THR L 102 N TYR L 86 SHEET 6 C 6 SER L 10 VAL L 13 1 N VAL L 11 O GLU L 105 SHEET 1 D 4 THR L 114 PHE L 118 0 SHEET 2 D 4 GLY L 129 PHE L 139 -1 O PHE L 135 N SER L 116 SHEET 3 D 4 TYR L 173 THR L 182 -1 O MET L 175 N LEU L 136 SHEET 4 D 4 VAL L 159 TRP L 163 -1 N LEU L 160 O THR L 178 SHEET 1 E 4 SER L 153 ARG L 155 0 SHEET 2 E 4 ASN L 145 ILE L 150 -1 N ILE L 150 O SER L 153 SHEET 3 E 4 SER L 191 THR L 197 -1 O GLU L 195 N LYS L 147 SHEET 4 E 4 ILE L 205 ASN L 210 -1 O ILE L 205 N ALA L 196 SHEET 1 F 4 LEU H 4 GLN H 5 0 SHEET 2 F 4 VAL H 18 ALA H 24 -1 O LYS H 23 N GLN H 5 SHEET 3 F 4 THR H 77 LEU H 82 -1 O MET H 80 N LEU H 20 SHEET 4 F 4 ALA H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 G 5 THR H 57 TYR H 59 0 SHEET 2 G 5 GLU H 46 ILE H 51 -1 N ASN H 50 O ASN H 58 SHEET 3 G 5 ILE H 34 GLN H 39 -1 N LYS H 38 O GLU H 46 SHEET 4 G 5 ALA H 88 LYS H 95 -1 O ALA H 93 N ASN H 35 SHEET 5 G 5 VAL H 101 TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 H 6 THR H 57 TYR H 59 0 SHEET 2 H 6 GLU H 46 ILE H 51 -1 N ASN H 50 O ASN H 58 SHEET 3 H 6 ILE H 34 GLN H 39 -1 N LYS H 38 O GLU H 46 SHEET 4 H 6 ALA H 88 LYS H 95 -1 O ALA H 93 N ASN H 35 SHEET 5 H 6 THR H 107 VAL H 111 -1 O VAL H 109 N ALA H 88 SHEET 6 H 6 ALA H 9 VAL H 12 1 N GLU H 10 O THR H 110 SHEET 1 I 4 SER H 120 LEU H 124 0 SHEET 2 I 4 SER H 137 TYR H 147 -1 O LEU H 143 N TYR H 122 SHEET 3 I 4 LEU H 184 THR H 194 -1 O LEU H 187 N VAL H 144 SHEET 4 I 4 VAL H 171 THR H 173 -1 N HIS H 172 O SER H 190 SHEET 1 J 4 SER H 120 LEU H 124 0 SHEET 2 J 4 SER H 137 TYR H 147 -1 O LEU H 143 N TYR H 122 SHEET 3 J 4 LEU H 184 THR H 194 -1 O LEU H 187 N VAL H 144 SHEET 4 J 4 VAL H 177 GLN H 179 -1 N GLN H 179 O LEU H 184 SHEET 1 K 3 THR H 153 TRP H 158 0 SHEET 2 K 3 THR H 206 HIS H 212 -1 O ASN H 209 N THR H 157 SHEET 3 K 3 THR H 217 LYS H 222 -1 O VAL H 219 N VAL H 210 SSBOND 1 CYS L 23 CYS L 88 SSBOND 2 CYS L 134 CYS L 194 SSBOND 3 CYS L 214 CYS H 128 SSBOND 4 CYS H 22 CYS H 92 SSBOND 5 CYS H 142 CYS H 208 CISPEP 1 TYR L 94 PRO L 95 0 0.48 CISPEP 2 TYR L 140 PRO L 141 0 0.27 CISPEP 3 PHE H 148 PRO H 149 0 -0.67 CISPEP 4 GLU H 150 PRO H 151 0 0.87 CISPEP 5 TRP H 199 PRO H 200 0 0.65 CRYST1 37.020 138.284 45.186 90.00 106.11 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 0.027012 0.000000 0.007802 0.00000 SCALE2 0.000000 0.007231 0.000000 0.00000 SCALE3 0.000000 0.000000 0.023035 0.00000