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. 1.22 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5, CNS 1.1 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON,BRUNGER,ADAMS, REMARK 3 : CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG, REMARK 3 : KUSZEWSKI,NILGES,PANNU,READ,RICE, REMARK 3 : 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 : 3314 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 36 REMARK 3 SOLVENT ATOMS : 935 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 RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 1MJU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-02. 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-00 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.0 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 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 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 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 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: 5260 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19740 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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 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 DISTANCE REMARK 500 O HOH H 1835 O HOH H 1868 1.52 REMARK 500 O HOH L 1601 O HOH L 1852 1.55 REMARK 500 O HOH L 1517 O HOH L 1710 1.56 REMARK 500 O HOH H 1483 O HOH H 1862 1.58 REMARK 500 C CYS H 128 O HOH H 1853 1.58 REMARK 500 OE1 GLN H 105 O HOH H 1863 1.59 REMARK 500 O HOH H 1508 O HOH H 1865 1.62 REMARK 500 NE2 GLN H 203 O HOH H 1835 1.62 REMARK 500 O HOH L 1482 O HOH L 1864 1.65 REMARK 500 O HOH L 1542 O HOH L 1817 1.66 REMARK 500 O HOH H 1740 O HOH L 1624 1.73 REMARK 500 O HOH L 1590 O HOH L 1647 1.74 REMARK 500 O HOH L 1580 O HOH L 1695 1.76 REMARK 500 O HOH L 1847 O HOH L 1848 1.77 REMARK 500 O HOH L 1649 O HOH L 1699 1.83 REMARK 500 O HOH L 1529 O HOH L 1627 1.85 REMARK 500 O HOH L 1519 O HOH L 1875 1.86 REMARK 500 O HOH L 1639 O HOH L 1788 1.86 REMARK 500 NH2 ARG L 24 O HOH L 1819 1.87 REMARK 500 O HOH H 1870 O HOH L 1578 1.88 REMARK 500 O HOH H 1487 O HOH H 1851 1.91 REMARK 500 O HOH H 1662 O HOH H 1801 1.92 REMARK 500 O HOH H 1482 O HOH H 1865 1.92 REMARK 500 O HOH L 1509 O HOH L 1862 1.93 REMARK 500 O GLN H 179 O HOH H 1684 1.96 REMARK 500 O HOH L 1636 O HOH L 1668 1.96 REMARK 500 O HOH H 1764 O HOH H 1854 1.97 REMARK 500 CG2 THR H 198 O HOH H 1867 1.98 REMARK 500 O HOH H 1519 O HOH H 1782 2.01 REMARK 500 O HOH L 1525 O HOH L 1850 2.01 REMARK 500 O HOH H 1596 O HOH L 1854 2.01 REMARK 500 N ALA L 7 O HOH L 1862 2.02 REMARK 500 O HOH L 1688 O HOH L 1855 2.04 REMARK 500 OE2 GLU L 154 O HOH L 1621 2.04 REMARK 500 O HOH L 1534 O HOH L 1647 2.04 REMARK 500 NH2 ARG L 77 O HOH L 1776 2.07 REMARK 500 O HOH L 1724 O HOH L 1874 2.07 REMARK 500 OE2 GLU L 79 O HOH L 1622 2.07 REMARK 500 O HOH H 1731 O HOH H 1800 2.08 REMARK 500 O HOH L 1481 O HOH L 1795 2.08 REMARK 500 O HOH H 1657 O HOH H 1857 2.09 REMARK 500 O2 GOL H 1402 O HOH H 1636 2.09 REMARK 500 O HOH H 1673 O HOH L 1702 2.09 REMARK 500 OE1 GLU H 46 O HOH H 1622 2.11 REMARK 500 N SER H 137 O HOH H 1864 2.12 REMARK 500 O HOH H 1713 O HOH H 1767 2.13 REMARK 500 O HOH H 1776 O HOH H 1810 2.16 REMARK 500 NZ LYS L 183 OE2 GLU L 187 2.17 REMARK 500 O HOH H 1565 O HOH H 1733 2.19 REMARK 500 O HOH L 1827 O HOH L 1838 2.19 REMARK 500 REMARK 500 THIS ENTRY HAS 51 CLOSE CONTACTS REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH H 1592 O HOH L 1870 2555 1.67 REMARK 500 O HOH H 1861 O HOH L 1605 2554 1.88 REMARK 500 O HOH H 1856 O HOH L 1828 2555 1.95 REMARK 500 O HOH H 1848 O HOH L 1871 3655 2.03 REMARK 500 O HOH H 1861 O HOH L 1578 2554 2.04 REMARK 500 O HOH H 1870 O HOH L 1828 2555 2.06 REMARK 500 O HOH H 1637 O HOH L 1576 3655 2.09 REMARK 500 CG2 THR L 202 O HOH H 1862 3645 2.15 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 VAL L 146 CG1 - CB - CG2 ANGL. DEV. = -10.4 DEGREES REMARK 500 MET L 175 CG - SD - CE ANGL. DEV. = -17.3 DEGREES REMARK 500 VAL L 206 CG1 - CB - CG2 ANGL. DEV. = 10.1 DEGREES REMARK 500 ARG H 40 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 VAL H 177 CG1 - CB - CG2 ANGL. DEV. = -16.3 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 MET L 51 -38.81 74.07 REMARK 500 SER L 67 -144.99 -94.02 REMARK 500 GLU L 213 56.06 -90.77 REMARK 500 REMARK 500 REMARK: NULL 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 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 H1531 DISTANCE = 5.02 ANGSTROMS REMARK 525 HOH H1626 DISTANCE = 5.07 ANGSTROMS REMARK 525 HOH H1664 DISTANCE = 5.13 ANGSTROMS REMARK 525 HOH H1672 DISTANCE = 5.13 ANGSTROMS REMARK 525 HOH H1675 DISTANCE = 5.09 ANGSTROMS REMARK 525 HOH H1693 DISTANCE = 5.58 ANGSTROMS REMARK 525 HOH H1697 DISTANCE = 5.18 ANGSTROMS REMARK 525 HOH H1702 DISTANCE = 5.03 ANGSTROMS REMARK 525 HOH H1768 DISTANCE = 5.03 ANGSTROMS REMARK 525 HOH H1775 DISTANCE = 5.91 ANGSTROMS REMARK 525 HOH H1780 DISTANCE = 5.21 ANGSTROMS REMARK 525 HOH H1799 DISTANCE = 5.36 ANGSTROMS REMARK 525 HOH H1811 DISTANCE = 5.10 ANGSTROMS REMARK 525 HOH H1814 DISTANCE = 5.29 ANGSTROMS REMARK 525 HOH H1820 DISTANCE = 5.02 ANGSTROMS REMARK 525 HOH H1823 DISTANCE = 6.30 ANGSTROMS REMARK 525 HOH H1832 DISTANCE = 7.16 ANGSTROMS REMARK 525 HOH H1846 DISTANCE = 5.80 ANGSTROMS REMARK 525 HOH H1847 DISTANCE = 5.12 ANGSTROMS REMARK 525 HOH L1685 DISTANCE = 5.65 ANGSTROMS REMARK 525 HOH L1751 DISTANCE = 5.26 ANGSTROMS REMARK 525 HOH L1769 DISTANCE = 5.53 ANGSTROMS REMARK 525 HOH L1784 DISTANCE = 6.17 ANGSTROMS REMARK 525 HOH L1800 DISTANCE = 5.85 ANGSTROMS REMARK 525 HOH L1822 DISTANCE = 6.49 ANGSTROMS REMARK 525 HOH L1823 DISTANCE = 5.33 ANGSTROMS REMARK 525 HOH L1826 DISTANCE = 5.15 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL L 1401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 1402 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL L 1403 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL L 1404 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL L 1405 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 1406 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.