REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 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) : 3.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.99 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) (%) : 93.1 REMARK 3 NUMBER OF REFLECTIONS : 52105 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) : 0.296 REMARK 3 FREE R VALUE : 0.338 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 2556 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.19 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 76.80 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6760 REMARK 3 BIN R VALUE (WORKING SET) : 0.5450 REMARK 3 BIN FREE R VALUE : 0.5340 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 353 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.028 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 13215 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 6 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 71.20 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 79.80 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -11.55000 REMARK 3 B22 (A**2) : 20.94000 REMARK 3 B33 (A**2) : -9.39000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 12.76000 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) : 0.69 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.94 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 1.40 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.50 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.02 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.620 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.720 ; 2.500 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.070 ; 2.500 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.340 ; 3.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.26 REMARK 3 BSOL : 20.87 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 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : ION.TOP REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1OTT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-03. REMARK 100 THE RCSB ID CODE IS RCSB018661. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-OCT-02 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 9.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS REMARK 200 BEAMLINE : X25 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL 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 : SDMS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52212 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 REMARK 200 RESOLUTION RANGE LOW (A) : 35.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.07200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11 REMARK 200 COMPLETENESS FOR SHELL (%) : 76.2 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.49200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE, DM REMARK 200 STARTING MODEL: PDB ENTRY 1OTS REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 67.48 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 300, SODIUM CHLORIDE, GLYCINE, REMARK 280 PH 9.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298.0K 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 115.80700 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.85950 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 115.80700 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 47.85950 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 300 REMARK: THE BIOLOGICAL ASSEMBLY FOR REMARK 300 THE CLC CHANNEL IS A DIMER FORMED BY CHAIN A AND B 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F 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 MET A 1 REMARK 465 LYS A 2 REMARK 465 THR A 3 REMARK 465 ASP A 4 REMARK 465 THR A 5 REMARK 465 PRO A 6 REMARK 465 SER A 7 REMARK 465 LEU A 8 REMARK 465 GLU A 9 REMARK 465 THR A 10 REMARK 465 PRO A 11 REMARK 465 GLN A 12 REMARK 465 ALA A 13 REMARK 465 ALA A 14 REMARK 465 ARG A 15 REMARK 465 LEU A 16 REMARK 465 LEU A 461 REMARK 465 ALA A 462 REMARK 465 ARG A 463 REMARK 465 SER A 464 REMARK 465 LYS A 465 REMARK 465 MET B 1 REMARK 465 LYS B 2 REMARK 465 THR B 3 REMARK 465 ASP B 4 REMARK 465 THR B 5 REMARK 465 PRO B 6 REMARK 465 SER B 7 REMARK 465 LEU B 8 REMARK 465 GLU B 9 REMARK 465 THR B 10 REMARK 465 PRO B 11 REMARK 465 GLN B 12 REMARK 465 ALA B 13 REMARK 465 ALA B 14 REMARK 465 ARG B 15 REMARK 465 LEU B 16 REMARK 465 ARG B 17 REMARK 465 GLU B 459 REMARK 465 GLN B 460 REMARK 465 LEU B 461 REMARK 465 ALA B 462 REMARK 465 ARG B 463 REMARK 465 SER B 464 REMARK 465 LYS B 465 REMARK 465 GLU C 1 REMARK 465 GLU E 1 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 ARG A 18 -19.13 -49.12 REMARK 500 ASP A 29 70.10 49.21 REMARK 500 TRP A 59 -39.62 -39.58 REMARK 500 ARG A 64 10.81 -59.43 REMARK 500 LEU A 78 -78.90 -66.18 REMARK 500 LEU A 79 -16.66 -37.87 REMARK 500 LEU A 96 -6.80 -55.23 REMARK 500 TYR A 100 -16.91 -144.01 REMARK 500 ALA A 101 75.84 -170.43 REMARK 500 ALA A 104 -80.20 -67.89 REMARK 500 SER A 107 -71.21 -34.56 REMARK 500 GLU A 111 -70.00 -56.14 REMARK 500 VAL A 122 76.78 -108.88 REMARK 500 LEU A 128 -70.11 -43.65 REMARK 500 VAL A 130 -71.92 -63.07 REMARK 500 PHE A 132 -78.40 -60.96 REMARK 500 ALA A 148 -92.40 -52.60 REMARK 500 ARG A 167 58.61 30.88 REMARK 500 ASP A 171 -41.74 -17.90 REMARK 500 ILE A 201 39.29 -88.23 REMARK 500 GLU A 202 -13.61 -156.69 REMARK 500 GLU A 203 -66.11 -142.92 REMARK 500 TYR A 210 148.37 -35.33 REMARK 500 LEU A 212 38.08 -88.96 REMARK 500 LYS A 216 -30.15 -36.45 REMARK 500 VAL A 236 100.38 -164.25 REMARK 500 VAL A 241 -2.87 -142.44 REMARK 500 TRP A 272 -71.64 -46.91 REMARK 500 ARG A 282 -72.13 -59.30 REMARK 500 VAL A 283 -45.67 -19.79 REMARK 500 TRP A 291 -75.45 -88.38 REMARK 500 PHE A 307 -4.25 -175.36 REMARK 500 ALA A 309 69.61 166.96 REMARK 500 SER A 313 -160.65 -101.62 REMARK 500 PHE A 317 -71.69 -41.14 REMARK 500 ASN A 318 -30.76 -35.08 REMARK 500 PHE A 337 -74.13 -54.28 REMARK 500 LEU A 345 -71.29 -45.71 REMARK 500 LEU A 346 -34.22 -39.19 REMARK 500 PRO A 353 86.98 -68.55 REMARK 500 ALA A 386 -24.90 -34.53 REMARK 500 ALA A 404 54.83 -119.63 REMARK 500 ILE A 409 -48.66 -27.81 REMARK 500 VAL A 412 -74.76 -56.39 REMARK 500 ASP A 417 49.29 34.68 REMARK 500 TYR A 419 -30.65 -36.67 REMARK 500 GLN A 437 -75.85 -83.67 REMARK 500 PHE A 438 4.95 -45.22 REMARK 500 THR A 439 53.46 -141.33 REMARK 500 PRO A 443 98.52 -45.90 REMARK 500 GLU A 457 -150.50 -87.21 REMARK 500 ALA A 458 25.22 48.11 REMARK 500 GLU A 459 43.21 -157.29 REMARK 500 LEU B 26 -7.83 -55.34 REMARK 500 THR B 71 30.43 -96.34 REMARK 500 LEU B 96 -1.32 -51.13 REMARK 500 TYR B 100 -14.68 -145.88 REMARK 500 ALA B 101 79.27 -175.31 REMARK 500 ALA B 104 -89.52 -72.25 REMARK 500 SER B 107 -72.23 -39.25 REMARK 500 GLU B 111 -77.48 -57.18 REMARK 500 VAL B 122 76.28 -105.03 REMARK 500 PHE B 132 -83.38 -55.66 REMARK 500 ARG B 147 -4.95 -147.81 REMARK 500 ALA B 148 -94.58 -60.02 REMARK 500 PRO B 150 -52.15 -29.95 REMARK 500 ARG B 167 33.30 31.18 REMARK 500 ALA B 188 4.74 -67.68 REMARK 500 GLU B 202 -22.49 -143.69 REMARK 500 GLU B 203 -76.40 -131.63 REMARK 500 TYR B 210 146.93 -39.69 REMARK 500 LEU B 212 38.32 -96.38 REMARK 500 LYS B 216 -28.84 -38.58 REMARK 500 PHE B 219 -72.07 -40.39 REMARK 500 ILE B 220 -36.29 -37.81 REMARK 500 HIS B 234 161.06 -38.20 REMARK 500 SER B 245 -176.57 -60.56 REMARK 500 ASP B 246 -158.84 -103.36 REMARK 500 LEU B 274 -75.80 -66.56 REMARK 500 LEU B 279 -11.10 -48.31 REMARK 500 ARG B 282 -76.96 -51.74 REMARK 500 VAL B 283 -41.25 -17.60 REMARK 500 TRP B 291 -75.44 -87.49 REMARK 500 VAL B 292 -37.02 -34.22 REMARK 500 PHE B 307 0.16 -169.12 REMARK 500 ALA B 309 67.03 163.59 REMARK 500 SER B 313 -156.58 -88.36 REMARK 500 ASN B 318 -25.84 -36.60 REMARK 500 PHE B 337 -74.36 -59.75 REMARK 500 ILE B 342 -74.71 -85.36 REMARK 500 THR B 343 -33.49 -38.41 REMARK 500 SER B 350 31.89 -81.43 REMARK 500 ALA B 362 -38.21 -35.26 REMARK 500 THR B 365 -72.26 -55.27 REMARK 500 VAL B 376 -72.09 -50.18 REMARK 500 SER B 401 -83.69 -73.25 REMARK 500 ARG B 403 47.51 39.58 REMARK 500 PRO B 405 -71.74 -46.56 REMARK 500 LEU B 413 -71.60 -35.96 REMARK 500 GLU B 414 -19.29 -34.62 REMARK 500 GLN B 437 -75.61 -80.29 REMARK 500 PHE B 438 -2.98 -46.71 REMARK 500 PRO B 443 93.95 -47.08 REMARK 500 SER C 7 -151.62 -106.27 REMARK 500 SER C 30 -169.42 -63.33 REMARK 500 ARG C 31 -10.43 55.68 REMARK 500 ILE C 48 -70.88 -95.58 REMARK 500 PRO C 53 -77.05 -50.90 REMARK 500 VAL C 54 11.70 -66.11 REMARK 500 PRO C 62 97.20 -63.00 REMARK 500 LYS C 65 -88.04 26.43 REMARK 500 TRP C 106 146.40 -14.11 REMARK 500 ASP C 109 -78.55 -58.19 REMARK 500 ALA C 122 149.57 -38.70 REMARK 500 THR C 124 168.68 -48.83 REMARK 500 THR C 125 124.32 -174.15 REMARK 500 LEU C 132 77.48 -104.37 REMARK 500 ALA C 137 38.03 -89.17 REMARK 500 ALA C 140 86.80 -42.06 REMARK 500 LEU C 146 -156.75 -110.85 REMARK 500 PHE C 154 139.13 -172.53 REMARK 500 ASN C 163 22.68 48.73 REMARK 500 SER C 164 24.71 83.50 REMARK 500 GLN C 179 119.02 -169.17 REMARK 500 TRP C 196 -83.99 -81.82 REMARK 500 GLU C 199 -169.83 -115.69 REMARK 500 SER C 210 -7.29 -58.80 REMARK 500 VAL D 3 76.09 -101.19 REMARK 500 SER D 7 -98.51 -52.06 REMARK 500 PRO D 15 165.95 -42.94 REMARK 500 CYS D 23 87.40 -160.50 REMARK 500 SER D 27 -139.55 -119.64 REMARK 500 TRP D 46 -81.03 -92.82 REMARK 500 THR D 50 -27.96 75.01 REMARK 500 SER D 51 26.90 -164.99 REMARK 500 SER D 55 90.62 -39.64 REMARK 500 SER D 64 176.42 169.26 REMARK 500 THR D 76 86.96 60.32 REMARK 500 GLU D 78 -165.15 -100.54 REMARK 500 GLU D 80 30.47 -69.39 REMARK 500 ALA D 83 -171.84 169.41 REMARK 500 TRP D 90 36.20 -169.69 REMARK 500 ILE D 105 78.69 -58.90 REMARK 500 SER D 126 15.53 174.06 REMARK 500 ALA D 129 89.68 -155.56 REMARK 500 ASN D 137 88.53 53.72 REMARK 500 PRO D 140 -174.53 -66.42 REMARK 500 ASP D 150 42.36 39.99 REMARK 500 GLU D 153 -178.04 -47.95 REMARK 500 ARG D 154 122.07 162.13 REMARK 500 GLN D 165 128.59 -29.81 REMARK 500 LYS D 168 -95.78 -78.75 REMARK 500 ASP D 169 -1.43 -55.01 REMARK 500 ASN D 189 -67.75 -123.91 REMARK 500 THR D 199 -10.78 -42.30 REMARK 500 SER E 7 -144.57 -101.62 REMARK 500 SER E 30 -169.35 -59.34 REMARK 500 ARG E 31 -3.28 51.34 REMARK 500 PRO E 41 114.92 -38.53 REMARK 500 ILE E 48 -76.27 -94.86 REMARK 500 ASN E 52 169.84 -48.95 REMARK 500 PRO E 53 -73.34 -48.27 REMARK 500 VAL E 54 10.32 -67.49 REMARK 500 SER E 55 27.41 47.88 REMARK 500 ILE E 58 106.30 -160.55 REMARK 500 PRO E 62 83.05 -56.87 REMARK 500 SER E 63 -156.30 -105.96 REMARK 500 LEU E 64 -135.79 -103.32 REMARK 500 LYS E 65 -83.68 -78.26 REMARK 500 ILE E 69 80.67 -154.11 REMARK 500 ASP E 77 37.65 37.86 REMARK 500 LEU E 81 119.30 -162.75 REMARK 500 TRP E 106 145.37 -12.58 REMARK 500 ASP E 109 -74.69 -57.85 REMARK 500 ALA E 113 -81.93 -65.97 REMARK 500 THR E 115 135.89 -175.12 REMARK 500 ALA E 122 -168.34 -57.35 REMARK 500 LEU E 132 79.48 -106.23 REMARK 500 ALA E 137 38.13 -86.40 REMARK 500 ALA E 140 87.17 -35.52 REMARK 500 LEU E 146 -153.44 -109.09 REMARK 500 SER E 164 34.79 75.69 REMARK 500 SER E 166 -18.64 -47.38 REMARK 500 GLN E 179 118.63 -169.27 REMARK 500 TRP E 196 -80.57 -81.90 REMARK 500 ARG E 221 81.50 -69.65 REMARK 500 SER F 7 -100.03 -47.20 REMARK 500 PRO F 15 140.64 -34.91 REMARK 500 SER F 27 -131.97 -112.35 REMARK 500 TRP F 46 -91.89 -86.92 REMARK 500 THR F 50 -28.13 74.75 REMARK 500 SER F 51 35.29 -165.90 REMARK 500 SER F 55 106.15 -42.23 REMARK 500 SER F 64 -173.79 -174.34 REMARK 500 SER F 66 109.94 167.76 REMARK 500 THR F 76 98.14 64.03 REMARK 500 ALA F 83 -174.28 178.64 REMARK 500 TRP F 90 30.30 -157.76 REMARK 500 ASP F 109 146.58 -37.70 REMARK 500 ALA F 110 68.94 -161.13 REMARK 500 ALA F 111 133.76 -31.59 REMARK 500 PRO F 112 -162.72 -48.72 REMARK 500 THR F 113 89.02 -169.40 REMARK 500 SER F 115 110.55 -160.80 REMARK 500 PRO F 119 135.38 -35.95 REMARK 500 SER F 126 12.22 175.07 REMARK 500 ALA F 129 87.96 -155.11 REMARK 500 LEU F 135 79.61 -157.32 REMARK 500 ASN F 137 70.66 54.15 REMARK 500 TYR F 139 128.19 178.03 REMARK 500 PRO F 140 -179.98 -60.92 REMARK 500 ASP F 150 41.56 38.80 REMARK 500 GLU F 153 175.63 -49.22 REMARK 500 ARG F 154 126.53 168.78 REMARK 500 GLN F 165 149.12 -32.37 REMARK 500 ARG F 187 35.08 -84.59 REMARK 500 ASN F 189 -62.53 -131.79 REMARK 500 PRO F 203 162.62 -46.36 REMARK 500 LYS F 206 94.09 -160.72 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 F 139 0.07 SIDE_CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 466 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 467 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 468 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 466 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 467 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 468 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1OTS RELATED DB: PDB REMARK 900 ECCLC FAB COMPLEX WT REMARK 900 RELATED ID: 1OTU RELATED DB: PDB REMARK 900 ECCLC FAB COMPLEX E148Q MUTANT