REMARK 2 REMARK 2 RESOLUTION. 3.42 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.0 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.42 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.26 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.3 REMARK 3 NUMBER OF REFLECTIONS : 44127 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 + TEST SET) : 0.236 REMARK 3 R VALUE (WORKING SET) : 0.234 REMARK 3 FREE R VALUE : 0.272 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050 REMARK 3 FREE R VALUE TEST SET COUNT : 2230 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 (ANGSTROMS) : 3.42 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.51 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.26 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3203 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2593 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3020 REMARK 3 BIN R VALUE (WORKING SET) : 0.2574 REMARK 3 BIN FREE R VALUE : 0.2919 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.71 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 183 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 : 15819 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 73.77 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 112.38 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -64.26760 REMARK 3 B22 (A**2) : 34.44400 REMARK 3 B33 (A**2) : 29.82360 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) : 0.86 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.831 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.784 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 16230 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 22070 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 5460 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 398 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 2345 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 16230 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : NULL ; NULL ; NULL REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : NULL ; NULL ; NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 1.16 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL REMARK 3 OTHER TORSION ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|1 - A|224 } REMARK 3 ORIGIN FOR THE GROUP (A): -17.3345 17.6231 30.2094 REMARK 3 T TENSOR REMARK 3 T11: 0.1130 T22: -0.1826 REMARK 3 T33: -0.0800 T12: 0.0157 REMARK 3 T13: -0.0093 T23: 0.0113 REMARK 3 L TENSOR REMARK 3 L11: 0.1561 L22: 2.6187 REMARK 3 L33: 2.8439 L12: -0.2999 REMARK 3 L13: 0.1903 L23: 0.9089 REMARK 3 S TENSOR REMARK 3 S11: -0.0130 S12: -0.0479 S13: 0.1494 REMARK 3 S21: -0.1979 S22: 0.0156 S23: 0.0342 REMARK 3 S31: 0.0547 S32: -0.0172 S33: -0.0026 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { B|1 - B|219 } REMARK 3 ORIGIN FOR THE GROUP (A): -28.8387 7.8407 39.6063 REMARK 3 T TENSOR REMARK 3 T11: 0.0801 T22: -0.1676 REMARK 3 T33: 0.0724 T12: -0.0034 REMARK 3 T13: -0.1073 T23: 0.0096 REMARK 3 L TENSOR REMARK 3 L11: 0.4738 L22: 2.7855 REMARK 3 L33: 0.9583 L12: -1.0522 REMARK 3 L13: -0.8306 L23: 1.3719 REMARK 3 S TENSOR REMARK 3 S11: 0.0048 S12: -0.0242 S13: 0.1260 REMARK 3 S21: -0.0381 S22: 0.0228 S23: 0.1931 REMARK 3 S31: 0.1433 S32: -0.0399 S33: -0.0275 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { C|1 - C|220 } REMARK 3 ORIGIN FOR THE GROUP (A): -18.2832 -38.3750 42.5255 REMARK 3 T TENSOR REMARK 3 T11: 0.0176 T22: -0.0857 REMARK 3 T33: 0.0061 T12: 0.0325 REMARK 3 T13: -0.0588 T23: -0.0201 REMARK 3 L TENSOR REMARK 3 L11: 0.2524 L22: 3.1046 REMARK 3 L33: 0.6276 L12: 0.2030 REMARK 3 L13: 0.1047 L23: -1.2792 REMARK 3 S TENSOR REMARK 3 S11: -0.0215 S12: -0.0318 S13: 0.0356 REMARK 3 S21: -0.0593 S22: 0.0260 S23: 0.1017 REMARK 3 S31: -0.0511 S32: 0.0347 S33: -0.0045 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: { D|1 - D|219 } REMARK 3 ORIGIN FOR THE GROUP (A): -6.2572 -47.6004 32.8577 REMARK 3 T TENSOR REMARK 3 T11: 0.1297 T22: -0.1150 REMARK 3 T33: -0.0491 T12: 0.0498 REMARK 3 T13: -0.0177 T23: -0.0068 REMARK 3 L TENSOR REMARK 3 L11: 0.5932 L22: 1.0546 REMARK 3 L33: 2.0638 L12: 0.6586 REMARK 3 L13: -1.2114 L23: -1.5938 REMARK 3 S TENSOR REMARK 3 S11: 0.0116 S12: 0.0087 S13: 0.0048 REMARK 3 S21: -0.1333 S22: 0.0590 S23: -0.1218 REMARK 3 S31: 0.0694 S32: 0.1023 S33: -0.0706 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: { E|2 - E|612 } REMARK 3 ORIGIN FOR THE GROUP (A): 21.2652 -20.6000 77.1798 REMARK 3 T TENSOR REMARK 3 T11: -0.1548 T22: 0.0584 REMARK 3 T33: 0.0011 T12: 0.1469 REMARK 3 T13: -0.0057 T23: -0.0822 REMARK 3 L TENSOR REMARK 3 L11: 0.0000 L22: 0.9155 REMARK 3 L33: 0.2400 L12: 0.2844 REMARK 3 L13: -0.0982 L23: 1.0306 REMARK 3 S TENSOR REMARK 3 S11: 0.0819 S12: 0.0382 S13: -0.1279 REMARK 3 S21: 0.1495 S22: -0.0013 S23: -0.0680 REMARK 3 S31: 0.0955 S32: -0.0713 S33: -0.0806 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: { F|2 - F|611 } REMARK 3 ORIGIN FOR THE GROUP (A): -18.6180 -19.8800 -31.9436 REMARK 3 T TENSOR REMARK 3 T11: 0.0514 T22: -0.0119 REMARK 3 T33: -0.1343 T12: 0.0234 REMARK 3 T13: -0.0071 T23: -0.1085 REMARK 3 L TENSOR REMARK 3 L11: 0.2341 L22: 1.3479 REMARK 3 L33: 0.6544 L12: -0.1901 REMARK 3 L13: 0.4943 L23: -1.1670 REMARK 3 S TENSOR REMARK 3 S11: -0.0259 S12: 0.2634 S13: -0.0770 REMARK 3 S21: 0.2582 S22: 0.0291 S23: 0.0536 REMARK 3 S31: 0.0319 S32: -0.0686 S33: -0.0032 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3U9U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-11. REMARK 100 THE RCSB ID CODE IS RCSB068487. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-FEB-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0331 REMARK 200 MONOCHROMATOR : DOULBE CRYSTAL CRYO-COOLED REMARK 200 SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44255 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2 REMARK 200 DATA REDUNDANCY : 2.900 REMARK 200 R MERGE (I) : 0.15000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.52 REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8 REMARK 200 DATA REDUNDANCY IN SHELL : 2.30 REMARK 200 R MERGE FOR SHELL (I) : 0.61200 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: PHASER REMARK 200 STARTING MODEL: 2AHX, 1N8Z REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 65.13 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG4000, 0.2 M SODIUM ACETATE, 0.1 REMARK 280 M SODIUM CITRATE PH 5.5, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K 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 41.56050 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 181.02550 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.45700 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 181.02550 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.56050 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.45700 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3960 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19720 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3770 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19320 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: E 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: 4 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLY A 135 REMARK 465 ASP A 136 REMARK 465 THR A 137 REMARK 465 THR A 138 REMARK 465 GLY A 139 REMARK 465 GLY C 135 REMARK 465 ASP C 136 REMARK 465 THR C 137 REMARK 465 THR C 138 REMARK 465 GLY C 139 REMARK 465 PRO C 221 REMARK 465 THR C 222 REMARK 465 ILE C 223 REMARK 465 LYS C 224 REMARK 465 GLN E 1 REMARK 465 PRO E 145 REMARK 465 TRP E 146 REMARK 465 PRO E 147 REMARK 465 SER E 148 REMARK 465 ASN E 149 REMARK 465 LEU E 150 REMARK 465 THR E 151 REMARK 465 LEU E 152 REMARK 465 VAL E 153 REMARK 465 SER E 154 REMARK 465 THR E 155 REMARK 465 ASN E 156 REMARK 465 GLY E 157 REMARK 465 SER E 158 REMARK 465 SER E 159 REMARK 465 GLY E 160 REMARK 465 CYS E 161 REMARK 465 GLY E 162 REMARK 465 ARG E 163 REMARK 465 CYS E 188 REMARK 465 ALA E 189 REMARK 465 GLU E 190 REMARK 465 GLN E 191 REMARK 465 CYS E 301 REMARK 465 THR E 302 REMARK 465 ASP E 303 REMARK 465 TRP E 613 REMARK 465 THR E 614 REMARK 465 GLY E 615 REMARK 465 HIS E 616 REMARK 465 SER E 617 REMARK 465 THR E 618 REMARK 465 LEU E 619 REMARK 465 PRO E 620 REMARK 465 GLN E 621 REMARK 465 HIS E 622 REMARK 465 ALA E 623 REMARK 465 ARG E 624 REMARK 465 THR E 625 REMARK 465 GLN F 1 REMARK 465 ASN F 103 REMARK 465 PHE F 104 REMARK 465 GLY F 105 REMARK 465 SER F 148 REMARK 465 ASN F 149 REMARK 465 LEU F 150 REMARK 465 SER F 154 REMARK 465 THR F 155 REMARK 465 ASN F 156 REMARK 465 GLY F 157 REMARK 465 SER F 158 REMARK 465 SER F 159 REMARK 465 GLY F 160 REMARK 465 CYS F 161 REMARK 465 GLY F 162 REMARK 465 ARG F 163 REMARK 465 CYS F 164 REMARK 465 HIS F 165 REMARK 465 LYS F 166 REMARK 465 SER F 167 REMARK 465 CYS F 168 REMARK 465 THR F 169 REMARK 465 ASP F 193 REMARK 465 GLY F 194 REMARK 465 ARG F 195 REMARK 465 GLU F 292 REMARK 465 ASN F 293 REMARK 465 CYS F 301 REMARK 465 THR F 302 REMARK 465 ASP F 303 REMARK 465 PRO F 612 REMARK 465 TRP F 613 REMARK 465 THR F 614 REMARK 465 GLY F 615 REMARK 465 HIS F 616 REMARK 465 SER F 617 REMARK 465 THR F 618 REMARK 465 LEU F 619 REMARK 465 PRO F 620 REMARK 465 GLN F 621 REMARK 465 HIS F 622 REMARK 465 ALA F 623 REMARK 465 ARG F 624 REMARK 465 THR F 625 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 TYR E 353 CG CD1 CD2 CE1 CE2 CZ OH 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 VAL A 2 99.32 9.44 REMARK 500 SER A 43 58.96 6.52 REMARK 500 LEU A 50 -63.48 -101.71 REMARK 500 ARG A 66 -74.30 39.29 REMARK 500 ASP A 102 -109.98 66.34 REMARK 500 ASP A 103 148.49 -24.88 REMARK 500 HIS A 104 86.76 -69.00 REMARK 500 TYR A 105 165.76 173.14 REMARK 500 ASN A 161 43.16 35.84 REMARK 500 SER A 166 -30.49 -135.20 REMARK 500 SER A 178 -83.44 -140.54 REMARK 500 SER A 196 -46.99 -21.46 REMARK 500 SER B 32 -39.46 -37.27 REMARK 500 TYR B 37 64.71 -103.30 REMARK 500 VAL B 56 -40.52 61.64 REMARK 500 THR B 74 -61.25 -122.01 REMARK 500 VAL B 83 121.92 -29.84 REMARK 500 ALA B 135 77.58 -157.22 REMARK 500 ASN B 143 82.69 46.72 REMARK 500 LYS B 174 -78.23 -89.98 REMARK 500 SER C 43 57.84 7.46 REMARK 500 LEU C 50 -61.28 -98.26 REMARK 500 ARG C 66 -131.94 -55.74 REMARK 500 THR C 70 98.87 -162.47 REMARK 500 ASP C 102 -108.37 67.55 REMARK 500 ASP C 103 146.98 -26.31 REMARK 500 HIS C 104 88.20 -69.59 REMARK 500 TYR C 105 165.88 171.90 REMARK 500 SER C 178 -83.77 -140.13 REMARK 500 SER C 196 -47.12 -21.56 REMARK 500 SER D 32 -38.14 -38.50 REMARK 500 VAL D 56 -39.58 60.51 REMARK 500 THR D 74 -61.40 -121.65 REMARK 500 VAL D 83 121.90 -29.82 REMARK 500 ALA D 135 80.78 -158.29 REMARK 500 ASN D 143 83.01 46.68 REMARK 500 LYS D 174 -78.22 -90.15 REMARK 500 ASN D 195 -64.05 -103.07 REMARK 500 ASN D 217 -77.09 -43.93 REMARK 500 LYS E 10 -124.69 64.56 REMARK 500 GLU E 29 -72.06 -38.28 REMARK 500 LEU E 74 48.32 -109.90 REMARK 500 ASN E 97 55.81 -96.60 REMARK 500 LYS E 100 104.20 -56.44 REMARK 500 ASN E 103 -46.16 -154.00 REMARK 500 LEU E 111 60.72 -117.37 REMARK 500 LEU E 114 99.47 -56.46 REMARK 500 TYR E 132 -20.21 65.86 REMARK 500 THR E 169 83.30 37.12 REMARK 500 HIS E 179 51.84 -90.22 REMARK 500 REMARK 500 THIS ENTRY HAS 113 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 VAL A 2 23.7 L L OUTSIDE RANGE REMARK 500 ASP B 175 24.7 L L OUTSIDE RANGE REMARK 500 ASN C 202 22.8 L L OUTSIDE RANGE REMARK 500 VAL D 56 22.4 L L OUTSIDE RANGE REMARK 500 ASP D 175 24.6 L L OUTSIDE RANGE REMARK 500 GLU E 116 24.7 L L OUTSIDE RANGE REMARK 500 ILE E 136 24.3 L L OUTSIDE RANGE REMARK 500 ILE E 417 24.5 L L OUTSIDE RANGE REMARK 500 GLN E 423 22.6 L L OUTSIDE RANGE REMARK 500 LYS E 536 24.2 L L OUTSIDE RANGE REMARK 500 LEU F 14 24.6 L L OUTSIDE RANGE REMARK 500 GLU F 116 24.5 L L OUTSIDE RANGE REMARK 500 GLN F 423 22.7 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL