REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.30 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) : 3.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.85 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) (%) : 97.0 REMARK 3 NUMBER OF REFLECTIONS : 41239 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) : 0.294 REMARK 3 FREE R VALUE : 0.325 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 2004 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) : 3.30 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.51 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.60 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6369 REMARK 3 BIN R VALUE (WORKING SET) : 0.4540 REMARK 3 BIN FREE R VALUE : 0.4950 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 345 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.027 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 13223 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) : 76.60 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 79.10 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -14.57000 REMARK 3 B22 (A**2) : 37.03000 REMARK 3 B33 (A**2) : -22.47000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 2.53000 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) : 0.65 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.98 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.50 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.70 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.95 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 : 0.20 REMARK 3 BSOL : 10.00 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 1OTU 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 RCSB018662. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-OCT-01 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 9.5 REMARK 200 NUMBER OF CRYSTALS USED : NULL 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 : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41743 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300 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 (%) : 96.9 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.07500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.2 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.42900 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: 1OTT REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 67.77 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.85 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 116.05650 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.04500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 116.05650 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 48.04500 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 THE CLC CHANNEL IS A DIMER REMARK 300 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: 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 OD1 ASP A 171 NH2 ARG D 210 3545 2.19 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 ASP B 171 CB - CG - OD1 ANGL. DEV. = -7.0 DEGREES REMARK 500 CYS C 22 CA - CB - SG ANGL. DEV. = 6.8 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 ARG A 18 -13.12 -49.92 REMARK 500 LEU A 26 -0.83 -59.77 REMARK 500 TRP A 59 -38.63 -38.13 REMARK 500 ARG A 64 16.32 -64.95 REMARK 500 LEU A 78 -78.20 -69.40 REMARK 500 LEU A 79 -19.22 -36.63 REMARK 500 PHE A 83 -51.14 -129.01 REMARK 500 PHE A 92 -34.12 -38.58 REMARK 500 LEU A 96 0.53 -49.40 REMARK 500 TYR A 100 -16.34 -142.12 REMARK 500 ALA A 101 75.22 -168.94 REMARK 500 SER A 107 -79.57 -47.66 REMARK 500 VAL A 122 71.27 -118.62 REMARK 500 ARG A 123 63.68 -69.96 REMARK 500 TRP A 125 -6.42 -54.10 REMARK 500 LEU A 128 -74.80 -40.98 REMARK 500 PHE A 132 -90.62 -57.17 REMARK 500 GLN A 148 -75.97 -64.91 REMARK 500 PRO A 150 -35.59 -38.69 REMARK 500 ARG A 167 33.86 27.76 REMARK 500 ASP A 171 -58.21 -24.74 REMARK 500 ALA A 187 -70.60 -64.99 REMARK 500 ILE A 197 -65.48 -95.13 REMARK 500 LEU A 198 -31.40 -39.81 REMARK 500 ILE A 201 32.14 -98.62 REMARK 500 GLU A 202 -15.44 -146.26 REMARK 500 GLU A 203 -77.56 -136.74 REMARK 500 TYR A 210 145.14 -36.00 REMARK 500 LEU A 212 36.62 -93.15 REMARK 500 MET A 224 -35.30 -36.41 REMARK 500 HIS A 234 -177.40 -57.10 REMARK 500 GLU A 235 8.10 46.70 REMARK 500 ASP A 240 64.23 -159.82 REMARK 500 SER A 245 -163.71 -67.86 REMARK 500 LEU A 274 -77.15 -62.38 REMARK 500 TRP A 291 -69.77 -93.05 REMARK 500 VAL A 292 -37.28 -39.65 REMARK 500 PHE A 307 34.98 165.64 REMARK 500 VAL A 308 -11.46 -164.53 REMARK 500 ALA A 309 65.82 166.46 REMARK 500 PHE A 317 -71.65 -46.19 REMARK 500 ASN A 318 -30.28 -33.49 REMARK 500 PHE A 337 -73.80 -59.04 REMARK 500 ILE A 342 -61.61 -93.34 REMARK 500 SER A 349 -19.46 -48.20 REMARK 500 ALA A 386 -39.94 -32.66 REMARK 500 ALA A 399 32.02 -86.00 REMARK 500 ALA A 400 -43.97 -155.42 REMARK 500 ILE A 409 -54.08 -24.85 REMARK 500 GLU A 414 -35.71 -38.01 REMARK 500 ASN A 418 52.48 -113.30 REMARK 500 GLN A 437 -69.48 -92.71 REMARK 500 PHE A 438 16.66 -54.08 REMARK 500 THR A 439 50.33 -150.56 REMARK 500 PRO A 443 101.07 -49.44 REMARK 500 LEU A 444 -18.75 -48.14 REMARK 500 GLU A 457 -156.90 -97.33 REMARK 500 ALA A 458 17.30 53.31 REMARK 500 GLU A 459 53.90 -147.60 REMARK 500 LEU B 26 -4.27 -55.55 REMARK 500 LEU B 48 -38.94 -37.21 REMARK 500 ARG B 64 15.50 -63.68 REMARK 500 LEU B 78 -77.05 -67.64 REMARK 500 LEU B 79 -19.73 -38.09 REMARK 500 PHE B 83 -51.01 -126.87 REMARK 500 PHE B 92 -30.21 -39.56 REMARK 500 PHE B 95 -71.63 -53.93 REMARK 500 LEU B 96 0.69 -46.57 REMARK 500 TYR B 100 -17.02 -144.71 REMARK 500 ALA B 101 77.48 -169.35 REMARK 500 ALA B 104 -71.21 -64.75 REMARK 500 SER B 107 -78.58 -51.75 REMARK 500 ASP B 118 45.71 70.02 REMARK 500 VAL B 122 71.50 -112.91 REMARK 500 TRP B 125 -8.68 -52.48 REMARK 500 LEU B 128 -74.68 -39.75 REMARK 500 PHE B 132 -94.77 -55.19 REMARK 500 PHE B 133 -37.48 -39.68 REMARK 500 GLN B 148 -79.24 -69.97 REMARK 500 PRO B 150 -39.02 -37.40 REMARK 500 ARG B 167 40.47 27.27 REMARK 500 ASP B 171 -66.36 -10.90 REMARK 500 ALA B 183 -73.12 -41.06 REMARK 500 ALA B 187 -83.04 -59.08 REMARK 500 ALA B 188 -16.30 -36.24 REMARK 500 GLU B 202 -19.54 -142.63 REMARK 500 GLU B 203 -81.82 -130.73 REMARK 500 PRO B 206 108.85 -47.43 REMARK 500 LEU B 212 36.90 -97.00 REMARK 500 HIS B 234 172.94 -46.63 REMARK 500 GLU B 235 15.28 47.69 REMARK 500 ASP B 240 67.15 -152.40 REMARK 500 SER B 245 -164.30 -65.54 REMARK 500 ASP B 246 -167.34 -114.68 REMARK 500 LEU B 274 -78.76 -61.14 REMARK 500 LEU B 279 -9.95 -54.74 REMARK 500 TRP B 291 -70.05 -94.25 REMARK 500 VAL B 292 -36.69 -39.62 REMARK 500 PHE B 307 34.63 173.78 REMARK 500 VAL B 308 -7.54 -164.50 REMARK 500 ALA B 309 64.65 163.60 REMARK 500 ASN B 318 -30.51 -34.45 REMARK 500 PHE B 337 -71.07 -63.15 REMARK 500 ILE B 342 -70.09 -93.26 REMARK 500 PRO B 359 -19.46 -49.09 REMARK 500 ALA B 390 0.61 -66.82 REMARK 500 ALA B 400 -48.01 -152.82 REMARK 500 ARG B 403 50.58 36.78 REMARK 500 PRO B 405 -72.34 -39.94 REMARK 500 ILE B 409 -56.62 -27.56 REMARK 500 GLU B 414 -36.23 -33.38 REMARK 500 ASN B 418 53.93 -116.53 REMARK 500 THR B 428 -71.66 -84.20 REMARK 500 ALA B 432 -70.39 -62.80 REMARK 500 GLN B 437 -69.50 -90.21 REMARK 500 PHE B 438 12.35 -56.08 REMARK 500 THR B 439 53.47 -144.59 REMARK 500 PRO B 443 98.63 -50.54 REMARK 500 THR B 452 2.13 -66.90 REMARK 500 SER C 7 -157.36 -108.59 REMARK 500 PRO C 14 143.03 -37.41 REMARK 500 SER C 30 -171.20 -63.33 REMARK 500 ARG C 31 -6.12 54.50 REMARK 500 ILE C 48 -73.18 -97.56 REMARK 500 PRO C 53 -78.07 -44.67 REMARK 500 VAL C 54 12.31 -65.48 REMARK 500 PRO C 62 91.57 -58.07 REMARK 500 LEU C 64 -160.12 -73.98 REMARK 500 LYS C 65 -86.23 -33.02 REMARK 500 TRP C 106 145.19 -22.47 REMARK 500 ASP C 109 -77.12 -56.86 REMARK 500 ALA C 122 153.62 -29.89 REMARK 500 THR C 124 173.84 -50.25 REMARK 500 THR C 125 119.99 -178.52 REMARK 500 ALA C 137 36.56 -90.70 REMARK 500 ALA C 140 86.91 -44.16 REMARK 500 LEU C 146 -156.54 -111.55 REMARK 500 PHE C 154 139.65 -170.51 REMARK 500 ASN C 163 23.27 47.94 REMARK 500 SER C 164 29.20 82.35 REMARK 500 SER C 166 -11.54 -48.63 REMARK 500 GLN C 179 119.03 -167.35 REMARK 500 TRP C 196 -86.51 -81.82 REMARK 500 GLU C 199 -165.98 -111.57 REMARK 500 SER D 7 -91.85 -52.09 REMARK 500 PRO D 15 153.14 -36.52 REMARK 500 CYS D 23 89.87 -157.51 REMARK 500 SER D 27 -133.29 -111.10 REMARK 500 TRP D 46 -76.75 -95.43 REMARK 500 THR D 50 -30.63 77.15 REMARK 500 SER D 51 28.85 -164.66 REMARK 500 SER D 55 99.67 -40.72 REMARK 500 VAL D 59 8.29 -69.88 REMARK 500 SER D 64 -175.28 -173.51 REMARK 500 SER D 66 134.57 -179.34 REMARK 500 THR D 76 88.08 61.93 REMARK 500 GLU D 80 19.79 -69.10 REMARK 500 ALA D 83 -171.00 177.55 REMARK 500 TRP D 90 34.67 -161.41 REMARK 500 ILE D 105 80.70 -54.39 REMARK 500 SER D 120 153.71 -49.46 REMARK 500 SER D 126 34.03 168.93 REMARK 500 ASN D 137 81.99 54.85 REMARK 500 PRO D 140 -177.99 -64.54 REMARK 500 GLU D 153 174.43 -46.92 REMARK 500 ARG D 154 125.49 171.12 REMARK 500 GLN D 165 131.27 -33.69 REMARK 500 LYS D 168 -72.79 -90.88 REMARK 500 ARG D 187 31.27 -90.48 REMARK 500 ASN D 189 -64.35 -129.05 REMARK 500 THR D 199 -5.24 -50.00 REMARK 500 SER E 7 -153.26 -105.38 REMARK 500 PRO E 14 141.77 -33.74 REMARK 500 SER E 30 -173.07 -61.85 REMARK 500 ARG E 31 -5.47 54.89 REMARK 500 PRO E 41 119.14 -38.96 REMARK 500 ILE E 48 -75.67 -92.73 REMARK 500 ASN E 52 167.39 -49.47 REMARK 500 PRO E 53 -76.93 -43.33 REMARK 500 VAL E 54 9.88 -66.29 REMARK 500 PRO E 62 97.12 -65.05 REMARK 500 LEU E 64 -173.52 -60.38 REMARK 500 LYS E 65 -93.26 -20.72 REMARK 500 TRP E 106 144.52 -18.81 REMARK 500 ASP E 109 -74.93 -59.83 REMARK 500 ALA E 113 -79.79 -64.50 REMARK 500 ALA E 122 -163.30 -49.11 REMARK 500 LEU E 132 79.98 -104.10 REMARK 500 ALA E 137 33.95 -87.52 REMARK 500 ALA E 140 87.49 -41.50 REMARK 500 LEU E 146 -155.85 -113.66 REMARK 500 SER E 164 30.75 78.54 REMARK 500 GLN E 179 117.89 -168.69 REMARK 500 TRP E 196 -81.56 -86.43 REMARK 500 GLU E 199 -164.56 -107.96 REMARK 500 ARG E 221 77.92 -68.10 REMARK 500 SER F 7 -97.93 -48.24 REMARK 500 PRO F 15 152.59 -34.22 REMARK 500 SER F 27 -128.97 -109.92 REMARK 500 TRP F 46 -82.00 -88.93 REMARK 500 THR F 50 -33.51 76.42 REMARK 500 SER F 51 33.64 -162.34 REMARK 500 SER F 55 101.36 -52.72 REMARK 500 SER F 64 -172.84 -171.03 REMARK 500 SER F 66 126.37 175.07 REMARK 500 THR F 76 91.93 60.97 REMARK 500 GLU F 80 13.64 -66.95 REMARK 500 ALA F 83 -171.19 178.80 REMARK 500 TRP F 90 31.03 -154.69 REMARK 500 ASP F 109 150.97 -47.23 REMARK 500 ALA F 110 75.81 -167.91 REMARK 500 ALA F 111 132.19 -37.76 REMARK 500 PRO F 112 -160.44 -37.18 REMARK 500 THR F 113 80.04 -175.61 REMARK 500 PRO F 119 123.43 -31.02 REMARK 500 SER F 120 152.70 -47.67 REMARK 500 SER F 126 33.18 172.21 REMARK 500 ALA F 129 89.28 -157.94 REMARK 500 LEU F 135 89.18 -150.11 REMARK 500 ASN F 137 80.38 55.01 REMARK 500 PRO F 140 -177.13 -63.94 REMARK 500 ASP F 150 46.61 39.56 REMARK 500 GLU F 153 172.01 -48.88 REMARK 500 ARG F 154 128.80 173.92 REMARK 500 GLN F 155 -6.81 -140.56 REMARK 500 GLN F 165 128.60 -32.15 REMARK 500 LYS F 168 -65.15 -96.51 REMARK 500 ARG F 187 37.58 -88.69 REMARK 500 ASN F 189 -59.63 -133.00 REMARK 500 THR F 199 -5.36 -55.41 REMARK 500 PRO F 203 162.25 -47.16 REMARK 500 LYS F 206 100.02 -160.52 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: 1OTT RELATED DB: PDB REMARK 900 ECCLC FAB COMPLEX E148A MUTANT