REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.54 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 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) : 3.54 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.92 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 4326688.230 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.1 REMARK 3 NUMBER OF REFLECTIONS : 33480 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : OTHER REMARK 3 R VALUE (WORKING SET) : 0.258 REMARK 3 FREE R VALUE : 0.296 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1680 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) : 3.50 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.72 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 60.00 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3760 REMARK 3 BIN R VALUE (WORKING SET) : 0.3960 REMARK 3 BIN FREE R VALUE : 0.4280 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 204 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.030 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 13207 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 2 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 72.60 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 91.00 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -7.50000 REMARK 3 B22 (A**2) : 24.12000 REMARK 3 B33 (A**2) : -16.62000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 4.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.52 REMARK 3 ESD FROM SIGMAA (A) : 0.80 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.59 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.97 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.015 REMARK 3 BOND ANGLES (DEGREES) : 1.60 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.80 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.18 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) : 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 : FLAT MODEL REMARK 3 KSOL : 0.22 REMARK 3 BSOL : 14.37 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 2EZ0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-DEC-05. REMARK 100 THE RCSB ID CODE IS RCSB035267. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-FEB-05 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 : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.91931 REMARK 200 MONOCHROMATOR : LN2 COOLED FIXED-EXIT SI(111) REMARK 200 MONOCHROMATOR REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33492 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 89.1 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.62 REMARK 200 COMPLETENESS FOR SHELL (%) : 90.6 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: PDB ENTRY 1OTU REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 70.22 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.13 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 36% PEG200/300 1:2, 100MM NABR, 50 REMARK 280 MM NAKTART, 50 MM GLYCINE, PH 9.5, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 293K 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 110.07750 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.01600 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 110.07750 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 62.01600 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: 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 ALA A 466 REMARK 465 ALA A 467 REMARK 465 SER A 468 REMARK 465 ALA A 469 REMARK 465 SER A 470 REMARK 465 GLU A 471 REMARK 465 ASN A 472 REMARK 465 THR A 473 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 ALA B 466 REMARK 465 ALA B 467 REMARK 465 SER B 468 REMARK 465 ALA B 469 REMARK 465 SER B 470 REMARK 465 GLU B 471 REMARK 465 ASN B 472 REMARK 465 THR B 473 REMARK 465 GLU C 1 REMARK 465 GLU E 1 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 THR C 61 CB THR C 61 CG2 -0.217 REMARK 500 SER C 121 CA SER C 121 CB 0.115 REMARK 500 SER C 121 C ALA C 122 N -0.157 REMARK 500 ARG D 107 C ARG D 107 O -0.224 REMARK 500 ALA D 108 CA ALA D 108 CB 0.173 REMARK 500 SER E 121 CA SER E 121 C -0.169 REMARK 500 ALA E 122 CA ALA E 122 CB 0.168 REMARK 500 LYS F 102 CE LYS F 102 NZ -0.152 REMARK 500 ARG F 107 C ALA F 108 N 0.285 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 CYS C 22 CA - CB - SG ANGL. DEV. = 7.6 DEGREES REMARK 500 THR D 50 O - C - N ANGL. DEV. = -15.0 DEGREES REMARK 500 ARG D 107 CA - C - O ANGL. DEV. = 23.1 DEGREES REMARK 500 ARG D 107 CA - C - N ANGL. DEV. = -19.4 DEGREES REMARK 500 CYS E 22 CA - CB - SG ANGL. DEV. = 6.9 DEGREES REMARK 500 SER E 121 N - CA - C ANGL. DEV. = 19.5 DEGREES REMARK 500 SER E 121 CA - C - O ANGL. DEV. = 14.8 DEGREES REMARK 500 SER E 121 CA - C - N ANGL. DEV. = -24.1 DEGREES REMARK 500 ALA E 122 C - N - CA ANGL. DEV. = -18.2 DEGREES REMARK 500 THR F 50 O - C - N ANGL. DEV. = -13.1 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 ALA A 49 -75.72 -60.87 REMARK 500 ARG A 64 12.75 -69.50 REMARK 500 ASP A 73 -67.06 -99.07 REMARK 500 TYR A 75 -73.84 -62.66 REMARK 500 LEU A 78 -77.87 -54.34 REMARK 500 LEU A 79 -47.80 -26.88 REMARK 500 ALA A 82 28.63 -76.73 REMARK 500 PHE A 83 -47.29 -137.99 REMARK 500 LEU A 96 -4.25 -56.33 REMARK 500 VAL A 97 -66.26 -100.07 REMARK 500 TYR A 100 -25.55 -143.43 REMARK 500 ALA A 101 68.86 -161.88 REMARK 500 PRO A 102 -34.11 -39.54 REMARK 500 ARG A 123 52.04 -69.99 REMARK 500 ARG A 126 -64.83 -120.58 REMARK 500 LEU A 128 -76.16 -52.10 REMARK 500 PHE A 132 -79.54 -54.97 REMARK 500 GLN A 148 -75.02 -78.45 REMARK 500 ARG A 167 -7.18 43.53 REMARK 500 LEU A 168 127.30 -37.67 REMARK 500 LEU A 186 -14.10 -49.99 REMARK 500 ALA A 189 -76.80 -66.71 REMARK 500 ASN A 191 37.60 38.61 REMARK 500 LEU A 194 -70.50 -51.97 REMARK 500 LEU A 198 -16.76 -43.99 REMARK 500 ILE A 200 -9.80 -53.23 REMARK 500 ARG A 205 117.22 -38.03 REMARK 500 PRO A 206 101.60 -46.25 REMARK 500 LEU A 212 48.08 -91.26 REMARK 500 ILE A 215 -56.38 -29.68 REMARK 500 ILE A 223 -74.13 -43.68 REMARK 500 ASN A 233 3.07 -152.80 REMARK 500 HIS A 234 174.57 -39.81 REMARK 500 GLU A 235 -27.70 58.49 REMARK 500 LEU A 274 -81.17 -65.10 REMARK 500 PHE A 307 19.09 -146.61 REMARK 500 VAL A 308 13.25 -147.85 REMARK 500 ALA A 309 59.32 150.87 REMARK 500 PRO A 310 -20.83 -39.99 REMARK 500 SER A 313 -169.85 -109.16 REMARK 500 ASN A 318 -7.11 -49.30 REMARK 500 MET A 332 -34.54 -34.38 REMARK 500 PHE A 337 -82.04 -66.68 REMARK 500 LEU A 346 -32.49 -39.50 REMARK 500 SER A 350 4.55 -64.10 REMARK 500 PRO A 359 -11.18 -45.89 REMARK 500 VAL A 366 -70.66 -59.67 REMARK 500 ALA A 400 -36.66 -144.44 REMARK 500 ARG A 403 53.27 33.47 REMARK 500 THR A 416 -3.73 -155.40 REMARK 500 ASN A 418 51.75 -111.22 REMARK 500 TYR A 419 0.57 -49.49 REMARK 500 ALA A 432 -81.42 -50.67 REMARK 500 GLN A 437 -63.42 -99.19 REMARK 500 PHE A 438 7.74 -61.47 REMARK 500 PRO A 443 95.36 -54.81 REMARK 500 GLU A 457 -157.99 -82.25 REMARK 500 ALA A 458 11.33 48.13 REMARK 500 ASP B 29 47.63 37.52 REMARK 500 ALA B 49 -75.59 -61.34 REMARK 500 ARG B 64 15.21 -68.87 REMARK 500 ASP B 73 -65.53 -100.57 REMARK 500 TYR B 75 -72.74 -65.07 REMARK 500 LEU B 78 -78.13 -53.46 REMARK 500 LEU B 79 -44.56 -27.71 REMARK 500 ALA B 82 25.58 -73.95 REMARK 500 PHE B 83 -48.21 -136.21 REMARK 500 LEU B 96 -5.02 -51.80 REMARK 500 VAL B 97 -60.78 -100.33 REMARK 500 TYR B 100 -25.76 -145.65 REMARK 500 ALA B 101 69.19 -160.14 REMARK 500 ARG B 123 57.67 -69.09 REMARK 500 ARG B 126 -64.98 -121.10 REMARK 500 LEU B 128 -78.25 -48.21 REMARK 500 VAL B 130 -71.82 -58.71 REMARK 500 PHE B 132 -80.85 -53.33 REMARK 500 LEU B 136 -35.66 -38.97 REMARK 500 GLN B 148 -73.68 -81.41 REMARK 500 ARG B 167 -8.33 45.86 REMARK 500 LEU B 168 128.91 -36.22 REMARK 500 ASP B 171 -28.65 -39.03 REMARK 500 ALA B 189 -73.74 -68.03 REMARK 500 PHE B 190 33.75 -86.79 REMARK 500 ASN B 191 37.38 29.60 REMARK 500 ILE B 200 -8.10 -53.86 REMARK 500 GLU B 203 -91.12 -107.64 REMARK 500 MET B 204 -61.33 -22.14 REMARK 500 ARG B 205 117.32 -36.56 REMARK 500 PRO B 206 96.23 -46.05 REMARK 500 LEU B 212 50.60 -91.10 REMARK 500 ILE B 223 -73.59 -42.15 REMARK 500 HIS B 234 172.00 -41.61 REMARK 500 GLU B 235 -30.17 61.96 REMARK 500 LEU B 274 -81.71 -63.87 REMARK 500 PHE B 307 20.19 -145.41 REMARK 500 VAL B 308 11.71 -147.84 REMARK 500 ALA B 309 61.93 152.07 REMARK 500 PRO B 310 -17.88 -44.43 REMARK 500 SER B 313 -168.30 -109.78 REMARK 500 ASN B 318 -5.97 -50.33 REMARK 500 MET B 332 -33.16 -32.38 REMARK 500 PHE B 337 -76.97 -72.11 REMARK 500 ILE B 342 -72.48 -83.01 REMARK 500 THR B 343 -15.95 -42.96 REMARK 500 SER B 350 10.00 -64.46 REMARK 500 ALA B 358 -71.05 -57.09 REMARK 500 PRO B 359 -12.95 -46.68 REMARK 500 VAL B 366 -72.14 -57.78 REMARK 500 ALA B 400 -42.85 -140.15 REMARK 500 ARG B 403 50.79 29.39 REMARK 500 THR B 416 -13.37 -143.02 REMARK 500 TYR B 419 -0.36 -47.76 REMARK 500 ALA B 432 -82.96 -49.71 REMARK 500 GLN B 437 -60.48 -103.59 REMARK 500 PHE B 438 6.48 -64.80 REMARK 500 PRO B 443 91.65 -52.04 REMARK 500 LEU B 444 -19.12 -43.44 REMARK 500 GLN B 456 -75.98 -64.08 REMARK 500 SER C 7 -156.32 -108.83 REMARK 500 PRO C 14 141.00 -36.29 REMARK 500 SER C 30 -171.59 -64.23 REMARK 500 ARG C 31 -5.83 55.15 REMARK 500 ILE C 48 -72.42 -98.87 REMARK 500 ASN C 52 170.15 -58.27 REMARK 500 PRO C 53 -77.90 -45.21 REMARK 500 VAL C 54 11.97 -65.24 REMARK 500 PRO C 62 92.02 -58.10 REMARK 500 LEU C 64 -167.16 -73.70 REMARK 500 LYS C 65 -85.92 -31.53 REMARK 500 TRP C 106 144.43 -23.93 REMARK 500 ASP C 109 -78.41 -55.18 REMARK 500 ALA C 122 158.48 -37.12 REMARK 500 THR C 124 171.64 -51.38 REMARK 500 THR C 125 119.81 -177.03 REMARK 500 ALA C 137 35.80 -90.38 REMARK 500 ALA C 140 87.52 -43.40 REMARK 500 LEU C 146 -157.45 -110.09 REMARK 500 PHE C 154 139.90 -171.90 REMARK 500 ASN C 163 23.66 49.36 REMARK 500 SER C 164 29.84 81.09 REMARK 500 SER C 166 -12.96 -48.86 REMARK 500 TRP C 196 -84.57 -84.13 REMARK 500 GLU C 199 -165.47 -111.54 REMARK 500 SER D 7 -92.12 -52.62 REMARK 500 PRO D 15 152.82 -37.55 REMARK 500 SER D 27 -133.56 -110.80 REMARK 500 TRP D 46 -76.09 -93.60 REMARK 500 THR D 50 7.90 57.61 REMARK 500 SER D 51 28.61 175.79 REMARK 500 SER D 55 99.62 -40.94 REMARK 500 VAL D 59 7.83 -69.79 REMARK 500 SER D 64 -175.14 -172.97 REMARK 500 SER D 66 134.20 -179.65 REMARK 500 THR D 76 88.02 62.67 REMARK 500 GLU D 80 20.29 -70.65 REMARK 500 ALA D 83 -170.05 177.19 REMARK 500 TRP D 90 34.02 -161.47 REMARK 500 ILE D 105 83.60 -55.70 REMARK 500 SER D 126 33.87 170.82 REMARK 500 ALA D 129 91.38 -160.88 REMARK 500 ASN D 137 84.33 54.65 REMARK 500 PRO D 140 -178.14 -65.00 REMARK 500 GLU D 153 173.53 -46.04 REMARK 500 ARG D 154 125.63 171.16 REMARK 500 GLN D 165 129.60 -32.74 REMARK 500 LYS D 168 -73.33 -90.92 REMARK 500 ARG D 187 31.94 -88.93 REMARK 500 ASN D 189 -63.97 -129.62 REMARK 500 THR D 199 -5.08 -52.15 REMARK 500 LYS D 206 97.21 -161.50 REMARK 500 SER E 7 -153.62 -104.88 REMARK 500 PRO E 14 141.88 -34.72 REMARK 500 SER E 30 -172.81 -63.78 REMARK 500 ARG E 31 -5.96 56.73 REMARK 500 PRO E 41 120.47 -38.89 REMARK 500 ILE E 48 -74.70 -93.75 REMARK 500 PRO E 53 -77.55 -43.02 REMARK 500 VAL E 54 9.23 -65.32 REMARK 500 PRO E 62 96.71 -66.24 REMARK 500 LEU E 64 -172.07 -60.88 REMARK 500 LYS E 65 -89.45 -24.23 REMARK 500 ALA E 92 -177.05 -170.50 REMARK 500 TRP E 106 143.65 -19.15 REMARK 500 ASP E 109 -74.98 -59.14 REMARK 500 ALA E 113 -80.32 -65.41 REMARK 500 ALA E 122 -149.57 -55.39 REMARK 500 ALA E 137 34.09 -87.02 REMARK 500 ALA E 140 88.79 -41.40 REMARK 500 LEU E 146 -154.18 -114.65 REMARK 500 SER E 164 32.26 77.26 REMARK 500 SER E 166 -15.74 -49.92 REMARK 500 GLN E 179 117.07 -168.65 REMARK 500 TRP E 196 -80.86 -86.17 REMARK 500 GLU E 199 -163.38 -106.45 REMARK 500 ARG E 221 77.69 -69.10 REMARK 500 SER F 7 -98.02 -48.71 REMARK 500 PRO F 15 153.27 -35.48 REMARK 500 SER F 27 -128.73 -109.75 REMARK 500 TRP F 46 -79.62 -89.18 REMARK 500 THR F 50 -4.14 59.72 REMARK 500 SER F 51 35.25 -176.17 REMARK 500 SER F 55 102.29 -51.87 REMARK 500 SER F 64 -172.71 -170.37 REMARK 500 SER F 66 126.40 175.84 REMARK 500 THR F 76 90.20 64.71 REMARK 500 GLU F 80 14.75 -67.84 REMARK 500 ALA F 83 -171.39 178.42 REMARK 500 TRP F 90 30.73 -155.09 REMARK 500 ASP F 109 153.65 -48.02 REMARK 500 ALA F 110 75.12 -168.74 REMARK 500 ALA F 111 134.75 -38.13 REMARK 500 PRO F 112 -160.21 -38.60 REMARK 500 THR F 113 78.09 -177.81 REMARK 500 PRO F 119 121.99 -31.00 REMARK 500 SER F 120 151.90 -46.11 REMARK 500 SER F 126 32.95 172.38 REMARK 500 ALA F 129 89.57 -158.88 REMARK 500 ASN F 137 79.58 53.33 REMARK 500 PRO F 140 -176.66 -62.72 REMARK 500 GLU F 153 172.14 -48.03 REMARK 500 ARG F 154 128.43 173.34 REMARK 500 GLN F 165 129.34 -31.47 REMARK 500 LYS F 168 -65.80 -96.12 REMARK 500 ARG F 187 37.38 -88.50 REMARK 500 ASN F 189 -60.85 -132.97 REMARK 500 THR F 199 -6.59 -54.59 REMARK 500 PRO F 203 161.24 -47.06 REMARK 500 LYS F 206 100.22 -160.59 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 31 0.07 SIDE_CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 THR D 50 -21.11 REMARK 500 THR F 50 -17.69 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 BR B 474 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 474 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1OTS RELATED DB: PDB REMARK 900 RELATED ID: 2EXW RELATED DB: PDB REMARK 900 RELATED ID: 2EXY RELATED DB: PDB