REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 78.7 REMARK 3 NUMBER OF REFLECTIONS : 31830 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) : 0.196 REMARK 3 FREE R VALUE : 0.290 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.800 REMARK 3 FREE R VALUE TEST SET COUNT : 3074 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.017 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 : 6628 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 36 REMARK 3 SOLVENT ATOMS : 678 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.20 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) : 0.014 REMARK 3 BOND ANGLES (DEGREES) : 2.20 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.30 REMARK 3 IMPROPER ANGLES (DEGREES) : 2.10 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 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 2PCP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : AUG-97 REMARK 200 TEMPERATURE (KELVIN) : 298 REMARK 200 PH : 4.6 REMARK 200 NUMBER OF CRYSTALS USED : 2 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NI FILTER REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MACSCIENCE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33694 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200 REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 79.3 REMARK 200 DATA REDUNDANCY : 2.100 REMARK 200 R MERGE (I) : 0.09100 REMARK 200 R SYM (I) : 0.09100 REMARK 200 FOR THE DATA SET : 9.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40 REMARK 200 COMPLETENESS FOR SHELL (%) : 63.5 REMARK 200 DATA REDUNDANCY IN SHELL : 2.10 REMARK 200 R MERGE FOR SHELL (I) : 0.22100 REMARK 200 R SYM FOR SHELL (I) : 0.22100 REMARK 200 FOR SHELL : 3.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: X-PLOR 3.1 REMARK 200 STARTING MODEL: PDB ENTRY 4FAB AND 1GIG REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.33 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.6 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,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 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 300 REMARK: REMARK 300 THERE ARE TWO FAB MOLECULES IN THE ASYMMETRIC UNIT. THE REMARK 300 LIGHT CHAINS ARE NAMED A AND C, AND THE HEAVY CHAINS ARE REMARK 300 NAMED B AND D. 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: 4270 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19170 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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: 4070 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19560 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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 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 LEU A 104 CA - CB - CG ANGL. DEV. = 15.0 DEGREES REMARK 500 LEU A 160 CA - CB - CG ANGL. DEV. = 16.2 DEGREES REMARK 500 SER A 201 N - CA - C ANGL. DEV. = -17.3 DEGREES REMARK 500 ILE A 205 N - CA - C ANGL. DEV. = -16.4 DEGREES REMARK 500 PRO B 151 C - N - CA ANGL. DEV. = -9.0 DEGREES REMARK 500 LEU C 181 CA - CB - CG ANGL. DEV. = 14.9 DEGREES REMARK 500 LEU D 109 CA - CB - CG ANGL. DEV. = 14.7 DEGREES REMARK 500 ALA D 129 N - CA - C ANGL. DEV. = -26.0 DEGREES REMARK 500 ALA D 130 N - CA - C ANGL. DEV. = 18.1 DEGREES REMARK 500 PRO D 151 C - N - CA ANGL. DEV. = -11.7 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 THR A 27A 136.40 -39.60 REMARK 500 VAL A 51 -55.40 65.19 REMARK 500 ARG A 77 79.74 71.25 REMARK 500 GLU A 81 10.71 -69.00 REMARK 500 ARG A 108 -156.02 -162.91 REMARK 500 TYR A 140 138.43 176.11 REMARK 500 ILE A 144 110.05 -160.79 REMARK 500 GLN A 156 -47.21 -135.72 REMARK 500 SER A 171 30.37 76.95 REMARK 500 LYS A 183 -34.93 -36.48 REMARK 500 ARG A 188 28.08 -79.23 REMARK 500 ASN A 190 -67.72 -106.76 REMARK 500 SER A 203 125.70 -171.30 REMARK 500 VAL B 2 81.60 -60.39 REMARK 500 HIS B 41 51.15 73.70 REMARK 500 LYS B 43 -82.76 -115.58 REMARK 500 PRO B 52A 19.82 -64.97 REMARK 500 LEU B 82C 97.74 -56.00 REMARK 500 GLU B 85 -8.40 -52.20 REMARK 500 ASP B 101 -90.67 -124.14 REMARK 500 PRO B 118 161.56 -41.52 REMARK 500 PRO B 126 -102.79 -70.43 REMARK 500 SER B 128 -2.95 -154.06 REMARK 500 ALA B 129 -163.73 -118.47 REMARK 500 ALA B 130 102.37 -47.96 REMARK 500 GLN B 131 153.75 -24.85 REMARK 500 GLU B 150 -29.19 -33.08 REMARK 500 SER B 165 41.95 -89.50 REMARK 500 LEU B 166 83.84 -170.94 REMARK 500 PRO B 175 -174.58 -69.52 REMARK 500 ASP B 183 22.48 83.53 REMARK 500 PRO B 198 -97.83 -54.53 REMARK 500 ALA B 214 5.31 -48.48 REMARK 500 SER B 215 -4.37 -140.35 REMARK 500 LYS B 222 -161.97 -160.45 REMARK 500 ILE B 223 -150.85 -153.60 REMARK 500 LEU C 47 -72.26 -105.77 REMARK 500 VAL C 51 -55.87 69.31 REMARK 500 SER C 56 94.11 -63.38 REMARK 500 ARG C 77 70.83 75.34 REMARK 500 ARG C 108 -159.69 -151.22 REMARK 500 ASP C 110 137.02 -38.81 REMARK 500 TYR C 140 133.80 -178.64 REMARK 500 ASP C 143 77.35 -64.42 REMARK 500 SER C 171 47.27 70.87 REMARK 500 HIS C 198 -164.92 -100.68 REMARK 500 LYS C 199 -70.69 -93.18 REMARK 500 SER C 201 72.63 70.15 REMARK 500 THR C 202 44.90 27.91 REMARK 500 HIS D 41 73.49 61.80 REMARK 500 LYS D 43 -33.88 -132.33 REMARK 500 PRO D 52A -18.56 -32.98 REMARK 500 LYS D 64 -74.08 -41.14 REMARK 500 GLU D 85 -8.81 -58.86 REMARK 500 ALA D 88 -173.60 -174.89 REMARK 500 ASP D 101 -61.94 -100.50 REMARK 500 ALA D 114 150.94 -49.34 REMARK 500 ALA D 130 -76.61 -66.72 REMARK 500 ASN D 133 -78.31 -24.36 REMARK 500 SER D 136 3.93 -153.77 REMARK 500 SER D 163 56.50 39.69 REMARK 500 SER D 165 -81.63 -84.55 REMARK 500 LEU D 178 91.42 -69.20 REMARK 500 SER D 180 74.79 40.60 REMARK 500 PRO D 198 -73.77 -53.91 REMARK 500 SER D 202 -57.91 -23.44 REMARK 500 ILE D 223 91.41 -65.65 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 TYR A 140 0.07 SIDE_CHAIN REMARK 500 TYR A 192 0.07 SIDE_CHAIN REMARK 500 TYR B 50 0.07 SIDE_CHAIN REMARK 500 TYR C 140 0.07 SIDE_CHAIN REMARK 500 TYR D 50 0.07 SIDE_CHAIN REMARK 500 TYR D 90 0.07 SIDE_CHAIN 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 B 233 DISTANCE = 7.07 ANGSTROMS REMARK 525 HOH C 218 DISTANCE = 5.09 ANGSTROMS REMARK 525 HOH C 223 DISTANCE = 7.02 ANGSTROMS REMARK 525 HOH B 242 DISTANCE = 5.37 ANGSTROMS REMARK 525 HOH D 242 DISTANCE = 6.08 ANGSTROMS REMARK 525 HOH A 228 DISTANCE = 5.41 ANGSTROMS REMARK 525 HOH C 231 DISTANCE = 6.74 ANGSTROMS REMARK 525 HOH C 232 DISTANCE = 5.83 ANGSTROMS REMARK 525 HOH D 251 DISTANCE = 7.39 ANGSTROMS REMARK 525 HOH A 238 DISTANCE = 5.46 ANGSTROMS REMARK 525 HOH D 256 DISTANCE = 5.39 ANGSTROMS REMARK 525 HOH B 273 DISTANCE = 5.73 ANGSTROMS REMARK 525 HOH C 262 DISTANCE = 5.06 ANGSTROMS REMARK 525 HOH B 278 DISTANCE = 5.56 ANGSTROMS REMARK 525 HOH C 263 DISTANCE = 6.73 ANGSTROMS REMARK 525 HOH A 269 DISTANCE = 6.40 ANGSTROMS REMARK 525 HOH D 286 DISTANCE = 7.86 ANGSTROMS REMARK 525 HOH A 273 DISTANCE = 5.31 ANGSTROMS REMARK 525 HOH D 289 DISTANCE = 7.16 ANGSTROMS REMARK 525 HOH B 293 DISTANCE = 7.51 ANGSTROMS REMARK 525 HOH D 293 DISTANCE = 8.97 ANGSTROMS REMARK 525 HOH A 280 DISTANCE = 5.29 ANGSTROMS REMARK 525 HOH C 284 DISTANCE = 6.18 ANGSTROMS REMARK 525 HOH B 301 DISTANCE = 6.41 ANGSTROMS REMARK 525 HOH A 289 DISTANCE = 8.40 ANGSTROMS REMARK 525 HOH B 307 DISTANCE = 7.70 ANGSTROMS REMARK 525 HOH A 295 DISTANCE = 5.50 ANGSTROMS REMARK 525 HOH D 310 DISTANCE = 6.18 ANGSTROMS REMARK 525 HOH A 306 DISTANCE = 8.89 ANGSTROMS REMARK 525 HOH D 322 DISTANCE = 7.88 ANGSTROMS REMARK 525 HOH B 325 DISTANCE = 5.34 ANGSTROMS REMARK 525 HOH C 311 DISTANCE = 5.77 ANGSTROMS REMARK 525 HOH A 313 DISTANCE = 5.27 ANGSTROMS REMARK 525 HOH C 316 DISTANCE = 5.58 ANGSTROMS REMARK 525 HOH D 332 DISTANCE = 9.44 ANGSTROMS REMARK 525 HOH A 318 DISTANCE = 6.80 ANGSTROMS REMARK 525 HOH D 338 DISTANCE = 6.36 ANGSTROMS REMARK 525 HOH D 339 DISTANCE = 7.91 ANGSTROMS REMARK 525 HOH D 344 DISTANCE = 7.64 ANGSTROMS REMARK 525 HOH B 347 DISTANCE = 5.95 ANGSTROMS REMARK 525 HOH A 333 DISTANCE = 5.23 ANGSTROMS REMARK 525 HOH D 349 DISTANCE = 6.77 ANGSTROMS REMARK 525 HOH A 337 DISTANCE = 6.62 ANGSTROMS REMARK 525 HOH D 355 DISTANCE = 5.66 ANGSTROMS REMARK 525 HOH D 356 DISTANCE = 5.87 ANGSTROMS REMARK 525 HOH C 348 DISTANCE = 8.47 ANGSTROMS REMARK 525 HOH A 348 DISTANCE = 7.42 ANGSTROMS REMARK 525 HOH B 369 DISTANCE = 7.97 ANGSTROMS REMARK 525 HOH A 354 DISTANCE = 7.44 ANGSTROMS REMARK 525 HOH B 370 DISTANCE = 5.43 ANGSTROMS REMARK 525 HOH B 371 DISTANCE = 8.51 ANGSTROMS REMARK 525 HOH A 356 DISTANCE = 6.17 ANGSTROMS REMARK 525 HOH A 357 DISTANCE = 5.60 ANGSTROMS REMARK 525 HOH C 359 DISTANCE = 5.18 ANGSTROMS REMARK 525 HOH A 361 DISTANCE = 7.42 ANGSTROMS REMARK 525 HOH D 376 DISTANCE = 8.62 ANGSTROMS REMARK 525 HOH B 386 DISTANCE = 7.92 ANGSTROMS REMARK 525 HOH A 372 DISTANCE = 6.66 ANGSTROMS REMARK 525 HOH D 387 DISTANCE = 5.14 ANGSTROMS REMARK 525 HOH A 376 DISTANCE = 7.36 ANGSTROMS REMARK 525 HOH A 378 DISTANCE = 6.74 ANGSTROMS REMARK 525 HOH A 381 DISTANCE = 11.12 ANGSTROMS REMARK 525 HOH D 397 DISTANCE = 6.57 ANGSTROMS REMARK 525 HOH D 405 DISTANCE = 6.38 ANGSTROMS REMARK 525 HOH D 410 DISTANCE = 6.83 ANGSTROMS REMARK 525 HOH D 417 DISTANCE = 12.75 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PC B 227 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PC C 212 REMARK 999 REMARK 999 SEQUENCE REMARK 999 REMARK 999 THE FAB MOLECULES ARE NUMBERED ACCORDING TO KABAT REMARK 999 (E.A.KABAT, T.T.WU, H.M.PERRY, K.S.GOTTESMAN, AND REMARK 999 C.FOELLER, SEQUENCES OF PROTEINS OF IMMUNOLOGICAL REMARK 999 INTEREST, 1991).