REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.6.0117 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5 REMARK 3 NUMBER OF REFLECTIONS : 68494 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) : 0.226 REMARK 3 R VALUE (WORKING SET) : 0.223 REMARK 3 FREE R VALUE : 0.269 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3642 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87 REMARK 3 REFLECTION IN BIN (WORKING SET) : 4088 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.26 REMARK 3 BIN R VALUE (WORKING SET) : 0.3120 REMARK 3 BIN FREE R VALUE SET COUNT : 223 REMARK 3 BIN FREE R VALUE : 0.3700 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 12522 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 32 REMARK 3 SOLVENT ATOMS : 35 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 57.70 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.17 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.68000 REMARK 3 B22 (A**2) : -0.10000 REMARK 3 B33 (A**2) : 0.91000 REMARK 3 B12 (A**2) : -0.23000 REMARK 3 B13 (A**2) : -1.11000 REMARK 3 B23 (A**2) : 1.65000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.540 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.334 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.247 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.544 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.889 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.859 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12889 ; 0.008 ; 0.020 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17560 ; 1.290 ; 1.946 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1646 ; 6.018 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 459 ;37.015 ;23.137 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1921 ;20.783 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;17.516 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2011 ; 0.085 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9620 ; 0.005 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: A STRONG DENSITY ON THE SURFACE OF NARK REMARK 3 IS LIKELY FROM THE SUGAR HEAD GROUP OF THE DECYLMALTOSIDE REMARK 3 DETERGENT USED DURING PROTEIN PURIFICATION AND IS MODELLED IN THE REMARK 3 STRUCTURE AS MALTOSE. REMARK 4 REMARK 4 4JRE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-13. REMARK 100 THE RCSB ID CODE IS RCSB078408. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-AUG-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 3.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 8.2.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.99999 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72283 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.100 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.6 REMARK 200 DATA REDUNDANCY : 3.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.15800 REMARK 200 FOR THE DATA SET : 7.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85 REMARK 200 COMPLETENESS FOR SHELL (%) : 76.3 REMARK 200 DATA REDUNDANCY IN SHELL : 2.90 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.86600 REMARK 200 FOR SHELL : 1.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 2.3.0 REMARK 200 STARTING MODEL: PDB ENTRY 4JR9 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 70.31 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.14 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG400, 0.1 M CITRIC ACID PH 3.5, REMARK 280 0.1M NACL AND 0.1M LI2SO4. THE CRYSTAL WAS SUBSEQUENTLY SOAKED REMARK 280 WITH 50MM NANO2 IN THE ABOVE SOLUTION PRIOR TO FREEZING, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K 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 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, H, L 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 -2 REMARK 465 SER A -1 REMARK 465 HIS A 0 REMARK 465 MET A 1 REMARK 465 SER A 2 REMARK 465 HIS A 3 REMARK 465 SER A 4 REMARK 465 SER A 5 REMARK 465 ALA A 6 REMARK 465 PRO A 7 REMARK 465 GLU A 8 REMARK 465 ARG A 9 REMARK 465 ALA A 10 REMARK 465 THR A 11 REMARK 465 GLY A 12 REMARK 465 LEU A 191 REMARK 465 SER A 192 REMARK 465 ILE A 193 REMARK 465 PHE A 194 REMARK 465 ALA A 195 REMARK 465 VAL A 196 REMARK 465 PHE A 197 REMARK 465 GLY A 198 REMARK 465 SER A 199 REMARK 465 GLN A 200 REMARK 465 GLY A 201 REMARK 465 VAL A 202 REMARK 465 LYS A 203 REMARK 465 GLN A 204 REMARK 465 PRO A 205 REMARK 465 ASP A 206 REMARK 465 GLY A 207 REMARK 465 THR A 208 REMARK 465 GLU A 209 REMARK 465 LEU A 210 REMARK 465 THR A 239 REMARK 465 SER A 240 REMARK 465 LYS A 241 REMARK 465 ALA A 242 REMARK 465 SER A 243 REMARK 465 ILE A 244 REMARK 465 LYS A 245 REMARK 465 GLU A 246 REMARK 465 GLN A 247 REMARK 465 LEU A 248 REMARK 465 PRO A 249 REMARK 465 VAL A 250 REMARK 465 LEU A 251 REMARK 465 LYS A 252 REMARK 465 ARG A 253 REMARK 465 GLY A 254 REMARK 465 HIS A 255 REMARK 465 ARG A 459 REMARK 465 HIS A 460 REMARK 465 SER A 461 REMARK 465 LYS A 462 REMARK 465 LYS A 463 REMARK 465 CYS B 133 REMARK 465 GLY B 134 REMARK 465 ASP B 135 REMARK 465 THR B 136 REMARK 465 GLY D -2 REMARK 465 SER D -1 REMARK 465 HIS D 0 REMARK 465 MET D 1 REMARK 465 SER D 2 REMARK 465 HIS D 3 REMARK 465 SER D 4 REMARK 465 SER D 5 REMARK 465 ALA D 6 REMARK 465 PRO D 7 REMARK 465 GLU D 8 REMARK 465 ARG D 9 REMARK 465 ALA D 10 REMARK 465 THR D 11 REMARK 465 GLY D 12 REMARK 465 SER D 192 REMARK 465 ILE D 193 REMARK 465 PHE D 194 REMARK 465 ALA D 195 REMARK 465 VAL D 196 REMARK 465 PHE D 197 REMARK 465 GLY D 198 REMARK 465 SER D 199 REMARK 465 GLN D 200 REMARK 465 GLY D 201 REMARK 465 VAL D 202 REMARK 465 LYS D 203 REMARK 465 GLN D 204 REMARK 465 PRO D 205 REMARK 465 ASP D 206 REMARK 465 GLY D 207 REMARK 465 THR D 208 REMARK 465 GLU D 209 REMARK 465 LEU D 210 REMARK 465 THR D 239 REMARK 465 SER D 240 REMARK 465 LYS D 241 REMARK 465 ALA D 242 REMARK 465 SER D 243 REMARK 465 ILE D 244 REMARK 465 LYS D 245 REMARK 465 GLU D 246 REMARK 465 GLN D 247 REMARK 465 LEU D 248 REMARK 465 PRO D 249 REMARK 465 VAL D 250 REMARK 465 LEU D 251 REMARK 465 LYS D 252 REMARK 465 ARG D 253 REMARK 465 GLY D 254 REMARK 465 HIS D 255 REMARK 465 PRO D 340 REMARK 465 THR D 341 REMARK 465 ASP D 342 REMARK 465 GLY D 343 REMARK 465 GLN D 344 REMARK 465 GLY D 345 REMARK 465 GLY D 346 REMARK 465 SER D 347 REMARK 465 ARG D 459 REMARK 465 HIS D 460 REMARK 465 SER D 461 REMARK 465 LYS D 462 REMARK 465 LYS D 463 REMARK 465 CYS H 133 REMARK 465 GLY H 134 REMARK 465 ASP H 135 REMARK 465 THR H 136 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 GLN A 161 CG CD OE1 NE2 REMARK 470 TYR A 211 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 VAL A 436 CG1 CG2 REMARK 470 GLN B 1 CG CD OE1 NE2 REMARK 470 ASP B 73 CG OD1 OD2 REMARK 470 ASN B 74 CG OD1 ND2 REMARK 470 VAL B 132 CG1 CG2 REMARK 470 ASP C 1 CG OD1 OD2 REMARK 470 SER C 17 OG REMARK 470 LYS C 102 CG CD CE NZ REMARK 470 ASN C 142 CG OD1 ND2 REMARK 470 ASN C 144 CG OD1 ND2 REMARK 470 LYS C 146 CG CD CE NZ REMARK 470 SER C 152 OG REMARK 470 LYS C 168 CG CD CE NZ REMARK 470 LYS C 182 CG CD CE NZ REMARK 470 ASN C 189 CG OD1 ND2 REMARK 470 GLU C 194 CG CD OE1 OE2 REMARK 470 LYS C 198 CG CD CE NZ REMARK 470 GLN D 161 CG CD OE1 NE2 REMARK 470 VAL D 436 CG1 CG2 REMARK 470 GLN H 1 CG CD OE1 NE2 REMARK 470 ASP H 73 CG OD1 OD2 REMARK 470 ASN H 74 CG OD1 ND2 REMARK 470 VAL H 132 CG1 CG2 REMARK 470 THR H 137 OG1 CG2 REMARK 470 SER L 17 OG REMARK 470 LYS L 102 CG CD CE NZ REMARK 470 ASN L 142 CG OD1 ND2 REMARK 470 ASN L 144 CG OD1 ND2 REMARK 470 LYS L 146 CG CD CE NZ REMARK 470 SER L 152 OG REMARK 470 GLN L 155 CG CD OE1 NE2 REMARK 470 ASN L 156 CG OD1 ND2 REMARK 470 LYS L 168 CG CD CE NZ REMARK 470 LYS L 182 CG CD CE NZ REMARK 470 GLU L 194 CD OE1 OE2 REMARK 470 LYS L 198 CG CD CE NZ 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 TRP C 162 CE2 TRP C 162 CD2 0.078 REMARK 500 TRP L 162 CE2 TRP L 162 CD2 0.083 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 LEU D 315 CA - CB - CG ANGL. DEV. = 13.9 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 29 -49.80 -139.29 REMARK 500 LYS A 64 1.78 -63.40 REMARK 500 THR A 266 -65.25 -93.07 REMARK 500 SER A 281 25.76 -79.46 REMARK 500 LEU A 315 35.91 -142.92 REMARK 500 ASP A 342 101.24 -49.59 REMARK 500 LEU A 431 -88.24 -86.93 REMARK 500 TYR A 457 -96.75 -136.47 REMARK 500 ASN B 55 -9.64 -162.33 REMARK 500 SER B 99 120.29 98.46 REMARK 500 ARG B 103 75.28 -108.65 REMARK 500 ASN C 31 -5.51 81.28 REMARK 500 THR C 51 -48.84 63.98 REMARK 500 SER C 52 1.51 -150.08 REMARK 500 ALA C 84 -176.69 -178.73 REMARK 500 ASN C 92 -78.40 -72.35 REMARK 500 LEU C 94 -156.51 51.69 REMARK 500 ASP C 109 145.11 -38.32 REMARK 500 ARG C 210 -4.81 -52.90 REMARK 500 ARG D 29 -24.62 -157.88 REMARK 500 SER D 127 56.55 -108.53 REMARK 500 LYS D 160 29.19 -75.13 REMARK 500 THR D 266 -64.00 -100.61 REMARK 500 SER D 281 9.83 -67.31 REMARK 500 LEU D 334 2.05 -63.58 REMARK 500 TYR D 457 -55.00 -137.37 REMARK 500 ALA H 62 -58.19 -29.29 REMARK 500 SER H 99 118.18 88.22 REMARK 500 ASN H 102 -70.06 -78.21 REMARK 500 ARG H 103 79.85 -106.94 REMARK 500 SER H 207 13.37 -150.65 REMARK 500 ASN L 31 -2.37 76.72 REMARK 500 GLN L 42 -179.45 -68.87 REMARK 500 THR L 51 -51.72 73.18 REMARK 500 ALA L 84 -179.40 179.64 REMARK 500 ASN L 92 -84.74 -69.76 REMARK 500 LEU L 94 -157.86 55.28 REMARK 500 LYS L 198 34.33 -73.31 REMARK 500 SER L 200 147.02 -173.40 REMARK 500 ARG L 210 3.59 -62.63 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 TYR B 101 24.1 L L OUTSIDE RANGE 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 NO2 A 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GYP A 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO2 D 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GYP D 502 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4JR9 RELATED DB: PDB REMARK 900 SUBSTRATE-FREE