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HEADER IMMUNE SYSTEM 28-AUG-02 1MJU TITLE 1.22 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE FAB TITLE 2 FRAGMENT OF ESTEROLYTIC ANTIBODY MS6-12 COMPND MOL_ID: 1; COMPND 2 MOLECULE: IMMUNOGLOBULIN MS6-12; COMPND 3 CHAIN: L; COMPND 4 FRAGMENT: FAB FRAGMENT, LIGHT CHAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: IMMUNOGLOBULIN MS6-12; 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 1MJU 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. 1.22 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5, 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 : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.22 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) (%) : 93.4 REMARK 3 NUMBER OF REFLECTIONS : 141368 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) : 0.123 REMARK 3 FREE R VALUE : 0.154 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 7075 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 : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.22 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.25 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6913 REMARK 3 BIN R VALUE (WORKING SET) : 0.1700 REMARK 3 BIN FREE R VALUE : 0.2120 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 352 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 : 3362 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 971 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.54 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.21000 REMARK 3 B22 (A**2) : 0.56000 REMARK 3 B33 (A**2) : -0.35000 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) : 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) : NULL REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : ANISOTROPIC 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 : BABINET MODEL WITH MASK 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: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 1MJU 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 RCSB . REMARK 100 THE RCSB ID CODE IS RCSB016966. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-NOV-2000 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 5.00 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 : 141368 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.220 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 (%) : 93.4 REMARK 200 DATA REDUNDANCY : 8.300 REMARK 200 R MERGE (I) : 0.03500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 32.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.22 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.24 REMARK 200 COMPLETENESS FOR SHELL (%) : 63.3 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.21900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR 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 (%): 52.89 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE, NACL, PH 5.0, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 290K 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 28.02300 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.28150 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.67450 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.28150 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.02300 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.67450 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: 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 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 SER H 136 REMARK 465 THR H 231 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 HOH 852 O HOH 933 1.52 REMARK 500 O HOH 374 O HOH 893 1.55 REMARK 500 O HOH 199 O HOH 598 1.56 REMARK 500 C CYS H 128 O HOH 894 1.58 REMARK 500 O HOH 178 O HOH 927 1.58 REMARK 500 OE1 GLN H 105 O HOH 928 1.59 REMARK 500 NE2 GLN H 203 O HOH 852 1.62 REMARK 500 O HOH 237 O HOH 930 1.62 REMARK 500 O HOH 138 O HOH 909 1.65 REMARK 500 O HOH 241 O HOH 826 1.66 REMARK 500 O HOH 410 O HOH 675 1.73 REMARK 500 O HOH 341 O HOH 456 1.74 REMARK 500 O HOH 312 O HOH 561 1.76 REMARK 500 O HOH 886 O HOH 887 1.77 REMARK 500 O HOH 460 O HOH 571 1.83 REMARK 500 O HOH 221 O HOH 416 1.85 REMARK 500 O HOH 201 O HOH 920 1.86 REMARK 500 O HOH 438 O HOH 757 1.86 REMARK 500 NH2 ARG L 24 O HOH 828 1.87 REMARK 500 O HOH 306 O HOH 935 1.88 REMARK 500 O HOH 182 O HOH 889 1.91 REMARK 500 O HOH 177 O HOH 930 1.92 REMARK 500 O HOH 533 O HOH 794 1.92 REMARK 500 O HOH 188 O HOH 906 1.93 REMARK 500 O GLN H 179 O HOH 572 1.96 REMARK 500 O HOH 433 O HOH 503 1.96 REMARK 500 O HOH 729 O HOH 900 1.97 REMARK 500 CG2 THR H 198 O HOH 932 1.98 REMARK 500 O HOH 213 O HOH 890 2.01 REMARK 500 O HOH 267 O HOH 763 2.01 REMARK 500 O HOH 407 O HOH 896 2.01 REMARK 500 N ALA L 7 O HOH 906 2.02 REMARK 500 OE2 GLU L 154 O HOH 405 2.04 REMARK 500 O HOH 226 O HOH 456 2.04 REMARK 500 O HOH 546 O HOH 897 2.04 REMARK 500 NH2 ARG L 77 O HOH 727 2.07 REMARK 500 OE2 GLU L 79 O HOH 406 2.07 REMARK 500 O HOH 620 O HOH 919 2.07 REMARK 500 O HOH 137 O HOH 769 2.08 REMARK 500 O HOH 659 O HOH 792 2.08 REMARK 500 O2 GOL 1402 O HOH 486 2.09 REMARK 500 O HOH 524 O HOH 922 2.09 REMARK 500 O HOH 552 O HOH 577 2.09 REMARK 500 OE1 GLU H 46 O HOH 459 2.11 REMARK 500 N SER H 137 O HOH 929 2.12 REMARK 500 O HOH 631 O HOH 732 2.13 REMARK 500 O HOH 750 O HOH 809 2.16 REMARK 500 NZ LYS L 183 OE2 GLU L 187 2.17 REMARK 500 O HOH 344 O HOH 663 2.19 REMARK 500 O HOH 402 O HOH 539 2.19 REMARK 500 O HOH 849 O HOH 871 2.19 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 391 O HOH 915 2555 1.67 REMARK 500 O HOH 384 O HOH 926 2555 1.88 REMARK 500 O HOH 850 O HOH 908 2554 1.95 REMARK 500 O HOH 880 O HOH 916 3655 2.03 REMARK 500 O HOH 306 O HOH 926 2555 2.04 REMARK 500 O HOH 850 O HOH 935 2554 2.06 REMARK 500 O HOH 303 O HOH 489 3645 2.09 REMARK 500 CG2 THR L 202 O HOH 927 3645 2.15 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 ASN L 190 CG ASN L 190 OD1 0.079 REMARK 500 VAL H 152 CA VAL H 152 CB 0.088 REMARK 500 VAL H 191 CA VAL H 191 CB 0.079 REMARK 500 SER H 196 C THR H 198 N 0.090 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. =-12.0 DEGREES REMARK 500 LEU L 104 CA - CB - CG ANGL. DEV. = 11.7 DEGREES REMARK 500 ASN L 145 N - CA - C ANGL. DEV. =-10.8 DEGREES REMARK 500 VAL L 146 N - CA - CB ANGL. DEV. =-11.7 DEGREES REMARK 500 VAL L 146 CG1 - CB - CG2 ANGL. DEV. = 13.2 DEGREES REMARK 500 MET L 175 CG - SD - CE ANGL. DEV. =-18.0 DEGREES REMARK 500 VAL H 177 CG1 - CB - CG2 ANGL. DEV. =-16.2 DEGREES REMARK 500 VAL H 177 CG1 - CB - CG2 ANGL. DEV. = 13.3 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 -38.81 74.07 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ASN L 145 VAL L 146 149.94 REMARK 500 PRO H 149 GLU H 150 144.16 REMARK 500 PRO H 151 VAL H 152 134.57 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 825 DISTANCE = 5.02 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: 1MJ8 RELATED DB: PDB REMARK 900 HIGH RESOLUTION CRYSTAL STRUCTURE OF THE COMPLEX OF THE FAB REMARK 900 FRAGMENT OF THE ESTEROLYTIC ANTIBODY MS6-126 AND A REMARK 900 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 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 ASP 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 227 PCA VAL GLN LEU GLN GLN PRO GLY ALA GLU LEU VAL LYS SEQRES 2 H 227 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY SEQRES 3 H 227 TYR THR PHE THR ASN TYR TRP ILE ASN TRP VAL LYS GLN SEQRES 4 H 227 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ASN ILE TYR SEQRES 5 H 227 PRO GLY SER SER TYR THR HIS TYR ASN GLU LYS PHE LYS SEQRES 6 H 227 ASN LYS ALA THR LEU THR VAL ASP THR SER SER SER THR SEQRES 7 H 227 ALA TYR MET GLN LEU SER SER LEU THR SER ASP ASP SER SEQRES 8 H 227 ALA VAL TYR TYR CYS ALA ASN LYS LEU GLY TRP PHE PRO SEQRES 9 H 227 TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER ALA ALA SEQRES 10 H 227 LYS THR THR ALA PRO SER VAL TYR PRO LEU ALA PRO VAL SEQRES 11 H 227 CYS GLY ASP THR SER GLY SER SER VAL THR LEU GLY CYS SEQRES 12 H 227 LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR LEU THR SEQRES 13 H 227 TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE SEQRES 14 H 227 PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SEQRES 15 H 227 SER VAL THR VAL THR SER SER THR TRP PRO SER GLN SER SEQRES 16 H 227 ILE THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS SEQRES 17 H 227 VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO THR ILE LYS SEQRES 18 H 227 PRO CYS PRO PRO CYS LYS MODRES 1MJU PCA H 1 GLU PYROGLUTAMIC ACID HET PCA H 1 8 HET GOL 1401 6 HET GOL 1402 6 HET GOL 1403 6 HET GOL 1404 6 HET GOL 1405 6 HET GOL 1406 6 HETNAM PCA PYROGLUTAMIC ACID HETNAM GOL GLYCEROL FORMUL 2 PCA C5 H7 N O3 FORMUL 3 GOL 6(C3 H8 O3) FORMUL 9 HOH *935(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 TYR H 32 5 5 HELIX 5 5 GLU H 61 LYS H 64 5 4 HELIX 6 6 THR H 83 SER H 87 5 5 HELIX 7 7 SER H 163 SER H 165 5 3 HELIX 8 8 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 PHE L 71 N CYS L 23 SHEET 4 A 4 PHE L 62 GLY L 66 -1 N SER L 63 O ARG L 74 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 VAL L 85 N GLN L 38 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 VAL L 85 N GLN L 38 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 ASN L 137 N THR L 114 SHEET 3 D 4 TYR L 173 THR L 182 -1 O TYR L 173 N PHE L 139 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 GLN H 3 GLN H 5 0 SHEET 2 F 4 VAL H 18 SER H 25 -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 LEU H 45 ILE H 51 -1 N ASN H 50 O HIS H 58 SHEET 3 G 5 ILE H 34 GLN H 39 -1 N TRP H 36 O ILE H 48 SHEET 4 G 5 ALA H 88 LEU H 96 -1 O ALA H 93 N ASN H 35 SHEET 5 G 5 PHE H 99 TRP H 103 -1 O PHE H 99 N LEU H 96 SHEET 1 H 6 THR H 57 TYR H 59 0 SHEET 2 H 6 LEU H 45 ILE H 51 -1 N ASN H 50 O HIS H 58 SHEET 3 H 6 ILE H 34 GLN H 39 -1 N TRP H 36 O ILE H 48 SHEET 4 H 6 ALA H 88 LEU H 96 -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 VAL H 12 O THR H 110 SHEET 1 I 4 SER H 120 LEU H 124 0 SHEET 2 I 4 VAL H 138 TYR H 147 -1 O LEU H 143 N TYR H 122 SHEET 3 I 4 LEU H 184 VAL H 193 -1 O TYR H 185 N TYR H 147 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 VAL H 138 TYR H 147 -1 O LEU H 143 N TYR H 122 SHEET 3 J 4 LEU H 184 VAL H 193 -1 O TYR H 185 N TYR H 147 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 -4.34 CISPEP 2 TYR L 140 PRO L 141 0 3.07 CISPEP 3 PHE H 148 PRO H 149 0 -8.52 CISPEP 4 GLU H 150 PRO H 151 0 -4.98 CISPEP 5 TRP H 199 PRO H 200 0 6.00 CRYST1 56.046 65.349 138.563 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 0.017842 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015302 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007217 0.00000