REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH T.A.MURANOVA,S.N.RUZHEINIKOV,S.E.SEDELNIKOVA,A.MOIR, REMARK 1 AUTH 2 L.J.PARTRIDGE,H.KAKINUMA,N.TAKASHI,K.SHIMAZAKI,J.SUN, REMARK 1 AUTH 3 Y.NISHI,D.W.RICE REMARK 1 TITL THE PREPARATION AND CRYSTALLIZATION OF FAB FRAGMENTS OF A REMARK 1 TITL 2 FAMILY OF MOUSE ESTEROLYTIC CATALYTIC ANTIBODIES AND THEIR REMARK 1 TITL 3 COMPLEXES WITH A TRANSITION-STATE ANALOGUE REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 57 1192 2001 REMARK 1 REFN ISSN 0907-4449 REMARK 1 DOI 10.1107/S0907444901010149 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) : 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 : 51508 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) : 0.218 REMARK 3 FREE R VALUE : 0.288 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2585 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 : 5966 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 76 REMARK 3 SOLVENT ATOMS : 517 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.00 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) : 0.010 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 : ISOTROPIC REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 4.858 ; 3.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 7.301 ; 4.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 6.642 ; 4.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 9.198 ; 4.500 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 : HAP.PARAM 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 1MH5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-SEP-02. REMARK 100 THE RCSB ID CODE IS RCSB016907. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-JUN-00 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 3.3 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SRS REMARK 200 BEAMLINE : PX14.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.244 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 : 51508 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 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 (%) : 88.5 REMARK 200 DATA REDUNDANCY : 3.100 REMARK 200 R MERGE (I) : 0.05200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 18.0000 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) : 2.15 REMARK 200 COMPLETENESS FOR SHELL (%) : 47.5 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.30600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.000 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 1A3L REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.90 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, LITIUM SULPHATE, ACETIC REMARK 280 ACID, PH 3.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 38.17300 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.55200 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 38.17300 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 58.55200 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 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4090 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 17540 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4210 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18050 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH L 215 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 285 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 292 LIES ON A SPECIAL POSITION. 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 SER A 121 REMARK 465 SER A 122 REMARK 465 GLU A 123 REMARK 465 GLN A 124 REMARK 465 LEU A 125 REMARK 465 THR A 126 REMARK 465 SER A 127 REMARK 465 GLY A 128 REMARK 465 GLY A 129 REMARK 465 ASP A 184 REMARK 465 GLU A 185 REMARK 465 TYR A 186 REMARK 465 GLU A 187 REMARK 465 HIS A 198 REMARK 465 LYS A 199 REMARK 465 THR A 200 REMARK 465 SER A 201 REMARK 465 THR A 202 REMARK 465 ARG A 211 REMARK 465 ASN A 212 REMARK 465 GLU A 213 REMARK 465 CYS A 214 REMARK 465 GLN B 1 REMARK 465 CYS B 130 REMARK 465 GLY B 131 REMARK 465 ASP B 132 REMARK 465 THR B 133 REMARK 465 SER B 134 REMARK 465 GLY B 135 REMARK 465 SER B 136 REMARK 465 SER B 137 REMARK 465 ASN B 163 REMARK 465 SER B 164 REMARK 465 GLY B 165 REMARK 465 SER B 166 REMARK 465 LEU B 167 REMARK 465 SER B 168 REMARK 465 SER B 169 REMARK 465 GLY B 170 REMARK 465 THR B 194 REMARK 465 SER B 195 REMARK 465 SER B 196 REMARK 465 THR B 197 REMARK 465 TRP B 198 REMARK 465 PRO B 199 REMARK 465 SER B 200 REMARK 465 GLN B 201 REMARK 465 SER B 202 REMARK 465 ILE B 203 REMARK 465 THR B 204 REMARK 465 CYS B 205 REMARK 465 ASN B 206 REMARK 465 VAL B 207 REMARK 465 ALA B 208 REMARK 465 HIS B 209 REMARK 465 PRO B 210 REMARK 465 ALA B 211 REMARK 465 SER B 212 REMARK 465 SER B 213 REMARK 465 THR B 214 REMARK 465 LYS B 215 REMARK 465 VAL B 216 REMARK 465 ASP B 217 REMARK 465 LYS B 218 REMARK 465 LYS B 219 REMARK 465 ILE B 220 REMARK 465 GLU B 221 REMARK 465 PRO B 222 REMARK 465 ARG B 223 REMARK 465 GLY B 224 REMARK 465 PRO B 225 REMARK 465 THR B 226 REMARK 465 ILE B 227 REMARK 465 LYS B 228 REMARK 465 PRO B 229 REMARK 465 CYS B 230 REMARK 465 PRO B 231 REMARK 465 PRO B 232 REMARK 465 CYS B 233 REMARK 465 LYS B 234 REMARK 465 HIS L 198 REMARK 465 LYS L 199 REMARK 465 THR L 200 REMARK 465 SER L 201 REMARK 465 THR L 202 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 465 GLN H 1 REMARK 465 VAL H 129 REMARK 465 CYS H 130 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 THR H 196 REMARK 465 SER H 197 REMARK 465 SER H 198 REMARK 465 THR H 199 REMARK 465 TRP H 200 REMARK 465 PRO H 201 REMARK 465 SER H 202 REMARK 465 GLN H 203 REMARK 465 SER H 204 REMARK 465 SER H 215 REMARK 465 SER H 216 REMARK 465 THR H 217 REMARK 465 LYS H 218 REMARK 465 VAL H 219 REMARK 465 ASP H 220 REMARK 465 LYS H 221 REMARK 465 LYS H 222 REMARK 465 ILE H 223 REMARK 465 GLU H 224 REMARK 465 PRO H 225 REMARK 465 ARG H 226 REMARK 465 GLY H 227 REMARK 465 PRO H 228 REMARK 465 THR H 229 REMARK 465 ILE H 230 REMARK 465 LYS H 231 REMARK 465 PRO H 232 REMARK 465 CYS H 233 REMARK 465 PRO H 234 REMARK 465 PRO H 235 REMARK 465 CYS H 236 REMARK 465 LYS H 237 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 O HOH A 269 O HOH B 751 2.01 REMARK 500 O HOH H 746 O HOH H 821 2.11 REMARK 500 O HOH B 736 O HOH B 758 2.13 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 ASN A 28 1.67 -66.77 REMARK 500 LEU A 47 -54.31 -127.22 REMARK 500 ARG A 50 -155.33 57.11 REMARK 500 MET A 51 -76.45 -44.31 REMARK 500 SER A 52 46.46 -149.58 REMARK 500 ASP A 60 -1.25 -56.80 REMARK 500 SER A 67 -118.35 -65.04 REMARK 500 SER A 76 -81.47 -60.74 REMARK 500 ARG A 77 73.94 -114.10 REMARK 500 VAL A 78 126.20 -33.45 REMARK 500 ASN A 138 66.97 38.75 REMARK 500 THR A 182 97.85 -55.83 REMARK 500 ALA A 196 -152.93 -97.43 REMARK 500 SER B 25 140.41 -178.82 REMARK 500 SER B 82B 78.48 30.36 REMARK 500 ALA B 88 -177.80 -178.09 REMARK 500 SER B 98 -63.02 -105.81 REMARK 500 PRO B 119 -135.12 -65.07 REMARK 500 SER B 120 67.06 170.02 REMARK 500 VAL B 121 159.70 -49.69 REMARK 500 PRO B 123 -105.03 -57.32 REMARK 500 LEU B 124 65.97 83.82 REMARK 500 PRO B 126 116.56 -36.12 REMARK 500 PHE B 148 133.93 -178.47 REMARK 500 SER B 180 94.82 38.44 REMARK 500 ASP B 183 24.72 44.76 REMARK 500 ARG L 50 -162.39 59.89 REMARK 500 SER L 52 36.29 -164.98 REMARK 500 SER L 67 -128.72 -66.53 REMARK 500 SER L 76 -90.99 -53.28 REMARK 500 SER L 122 -72.42 -47.96 REMARK 500 GLN L 124 -80.88 -25.44 REMARK 500 TYR L 140 137.10 -172.93 REMARK 500 ILE L 144 141.72 177.85 REMARK 500 ASP L 184 17.95 -57.93 REMARK 500 GLU L 185 -42.23 -130.86 REMARK 500 ARG L 211 23.64 -59.16 REMARK 500 SER H 82B 80.21 28.78 REMARK 500 SER H 98 -62.63 -100.87 REMARK 500 PRO H 119 -136.77 -64.75 REMARK 500 SER H 120 84.26 172.43 REMARK 500 SER H 137 -160.80 -127.17 REMARK 500 PRO H 151 -159.04 -111.04 REMARK 500 ASN H 162 73.85 65.19 REMARK 500 SER H 163 18.70 49.36 REMARK 500 SER H 168 -117.64 -54.16 REMARK 500 SER H 180 82.02 39.78 REMARK 500 ASP H 183 -4.53 63.02 REMARK 500 PRO H 213 91.68 -56.70 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 264 DISTANCE = 6.85 ANGSTROMS REMARK 525 HOH A 297 DISTANCE = 6.32 ANGSTROMS REMARK 525 HOH A 319 DISTANCE = 6.72 ANGSTROMS REMARK 525 HOH A 333 DISTANCE = 7.21 ANGSTROMS REMARK 525 HOH A 334 DISTANCE = 5.95 ANGSTROMS REMARK 525 HOH A 335 DISTANCE = 8.81 ANGSTROMS REMARK 525 HOH A 348 DISTANCE = 7.16 ANGSTROMS REMARK 525 HOH A 352 DISTANCE = 8.10 ANGSTROMS REMARK 525 HOH B 784 DISTANCE = 5.32 ANGSTROMS REMARK 525 HOH B 788 DISTANCE = 6.87 ANGSTROMS REMARK 525 HOH B 789 DISTANCE = 5.99 ANGSTROMS REMARK 525 HOH B 801 DISTANCE = 6.93 ANGSTROMS REMARK 525 HOH B 802 DISTANCE = 7.04 ANGSTROMS REMARK 525 HOH B 804 DISTANCE = 7.71 ANGSTROMS REMARK 525 HOH B 805 DISTANCE = 8.22 ANGSTROMS REMARK 525 HOH B 806 DISTANCE = 7.49 ANGSTROMS REMARK 525 HOH B 825 DISTANCE = 6.69 ANGSTROMS REMARK 525 HOH B 826 DISTANCE = 8.04 ANGSTROMS REMARK 525 HOH B 827 DISTANCE = 7.61 ANGSTROMS REMARK 525 HOH B 829 DISTANCE = 5.41 ANGSTROMS REMARK 525 HOH B 835 DISTANCE = 6.46 ANGSTROMS REMARK 525 HOH B 840 DISTANCE = 7.45 ANGSTROMS REMARK 525 HOH B 842 DISTANCE = 5.91 ANGSTROMS REMARK 525 HOH B 843 DISTANCE = 5.15 ANGSTROMS REMARK 525 HOH B 850 DISTANCE = 7.48 ANGSTROMS REMARK 525 HOH B 851 DISTANCE = 10.82 ANGSTROMS REMARK 525 HOH H 797 DISTANCE = 6.81 ANGSTROMS REMARK 525 HOH H 798 DISTANCE = 6.59 ANGSTROMS REMARK 525 HOH H 825 DISTANCE = 7.34 ANGSTROMS REMARK 525 HOH H 834 DISTANCE = 5.97 ANGSTROMS REMARK 525 HOH H 835 DISTANCE = 6.09 ANGSTROMS REMARK 525 HOH L 215 DISTANCE = 5.42 ANGSTROMS REMARK 525 HOH L 277 DISTANCE = 5.81 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 703 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 704 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HAL B 601 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HAL H 602 REMARK 900 REMARK 900 RELATED ENTRIES 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 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.