REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0109 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) : 3.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 154.30 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 28371 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) : 0.186 REMARK 3 R VALUE (WORKING SET) : 0.183 REMARK 3 FREE R VALUE : 0.238 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1439 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) : 3.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.18 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1961 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.95 REMARK 3 BIN R VALUE (WORKING SET) : 0.2510 REMARK 3 BIN FREE R VALUE SET COUNT : 99 REMARK 3 BIN FREE R VALUE : 0.2930 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 7272 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) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.67 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.390 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.282 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 33.974 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.926 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.875 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7444 ; 0.016 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10086 ; 1.871 ; 1.959 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 939 ; 8.268 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 296 ;37.673 ;23.649 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1241 ;23.120 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;18.743 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1095 ; 0.109 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5584 ; 0.006 ; 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): 4675 ; 0.455 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7524 ; 0.930 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2769 ; 1.344 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2562 ; 2.295 ; 4.500 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 : 4 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : A C REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 1 A 122 4 REMARK 3 1 C 1 C 122 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 1 A (A): 938 ; 0.260 ; 0.500 REMARK 3 MEDIUM THERMAL 1 A (A**2): 938 ; 0.310 ; 2.000 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : D G REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 D 0 D 122 4 REMARK 3 1 G 0 G 122 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 2 D (A): 938 ; 0.270 ; 0.500 REMARK 3 MEDIUM THERMAL 2 D (A**2): 938 ; 0.310 ; 2.000 REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : B E REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 B 1 B 122 4 REMARK 3 1 E 1 E 122 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 3 B (A): 874 ; 0.420 ; 0.500 REMARK 3 MEDIUM THERMAL 3 B (A**2): 874 ; 0.370 ; 2.000 REMARK 3 REMARK 3 NCS GROUP NUMBER : 4 REMARK 3 CHAIN NAMES : F H REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 F 0 F 115 4 REMARK 3 1 H 0 H 115 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 4 F (A): 883 ; 0.490 ; 0.500 REMARK 3 MEDIUM THERMAL 4 F (A**2): 883 ; 0.390 ; 2.000 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 8 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1 A 115 REMARK 3 ORIGIN FOR THE GROUP (A): -22.4820 -51.9010 1.1470 REMARK 3 T TENSOR REMARK 3 T11: 0.0569 T22: 0.0808 REMARK 3 T33: 0.1292 T12: 0.0269 REMARK 3 T13: 0.0110 T23: 0.0025 REMARK 3 L TENSOR REMARK 3 L11: 6.7874 L22: 4.1492 REMARK 3 L33: 6.4684 L12: 1.0153 REMARK 3 L13: 1.7843 L23: 1.4684 REMARK 3 S TENSOR REMARK 3 S11: -0.0358 S12: 0.0904 S13: 0.2327 REMARK 3 S21: 0.0996 S22: 0.0866 S23: -0.3080 REMARK 3 S31: 0.0665 S32: -0.5396 S33: -0.0507 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 1 B 115 REMARK 3 ORIGIN FOR THE GROUP (A): -33.5150 -41.2700 15.4450 REMARK 3 T TENSOR REMARK 3 T11: 0.1823 T22: 0.3591 REMARK 3 T33: 0.1596 T12: 0.1314 REMARK 3 T13: -0.0480 T23: -0.0937 REMARK 3 L TENSOR REMARK 3 L11: 4.7104 L22: 8.1156 REMARK 3 L33: 5.8984 L12: -4.4818 REMARK 3 L13: 0.2341 L23: 0.9207 REMARK 3 S TENSOR REMARK 3 S11: -0.3507 S12: -0.6696 S13: 0.0747 REMARK 3 S21: 0.8045 S22: 0.2307 S23: 0.1012 REMARK 3 S31: 0.0269 S32: -0.6025 S33: 0.1200 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 1 C 115 REMARK 3 ORIGIN FOR THE GROUP (A): -51.8820-110.8130 1.1720 REMARK 3 T TENSOR REMARK 3 T11: 0.0604 T22: 0.0376 REMARK 3 T33: 0.1459 T12: -0.0244 REMARK 3 T13: 0.0113 T23: -0.0250 REMARK 3 L TENSOR REMARK 3 L11: 4.2158 L22: 6.6399 REMARK 3 L33: 7.3893 L12: -0.6866 REMARK 3 L13: 1.3619 L23: -1.3956 REMARK 3 S TENSOR REMARK 3 S11: -0.0056 S12: -0.0836 S13: -0.2449 REMARK 3 S21: -0.0552 S22: 0.0283 S23: -0.3305 REMARK 3 S31: -0.5278 S32: -0.0209 S33: -0.0227 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 1 D 115 REMARK 3 ORIGIN FOR THE GROUP (A): -56.0540 -20.6090 -0.0130 REMARK 3 T TENSOR REMARK 3 T11: 0.0586 T22: 0.1503 REMARK 3 T33: 0.0388 T12: 0.0555 REMARK 3 T13: -0.0257 T23: -0.0527 REMARK 3 L TENSOR REMARK 3 L11: 5.5213 L22: 6.5841 REMARK 3 L33: 6.2420 L12: 0.9093 REMARK 3 L13: 0.5467 L23: -1.7252 REMARK 3 S TENSOR REMARK 3 S11: -0.1449 S12: -0.0407 S13: 0.2302 REMARK 3 S21: 0.0357 S22: 0.1356 S23: -0.1485 REMARK 3 S31: 0.4161 S32: -0.0171 S33: 0.0093 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : E 1 E 115 REMARK 3 ORIGIN FOR THE GROUP (A): -44.2930 -29.8970 -14.5740 REMARK 3 T TENSOR REMARK 3 T11: 0.3666 T22: 0.3527 REMARK 3 T33: 0.0707 T12: 0.2428 REMARK 3 T13: 0.0537 T23: 0.0584 REMARK 3 L TENSOR REMARK 3 L11: 9.0767 L22: 8.1794 REMARK 3 L33: 4.1259 L12: -6.0361 REMARK 3 L13: -0.3206 L23: -0.5857 REMARK 3 S TENSOR REMARK 3 S11: 0.7422 S12: 1.2327 S13: -0.1172 REMARK 3 S21: -0.9724 S22: -0.8427 S23: -0.0974 REMARK 3 S31: 0.2022 S32: 0.0041 S33: 0.1005 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : F 1 F 115 REMARK 3 ORIGIN FOR THE GROUP (A): -41.3050 -99.7860 15.4540 REMARK 3 T TENSOR REMARK 3 T11: 0.3454 T22: 0.2331 REMARK 3 T33: 0.1387 T12: -0.1366 REMARK 3 T13: -0.0802 T23: 0.0591 REMARK 3 L TENSOR REMARK 3 L11: 8.8909 L22: 5.5146 REMARK 3 L33: 5.4765 L12: 4.6573 REMARK 3 L13: 0.6085 L23: -0.5449 REMARK 3 S TENSOR REMARK 3 S11: 0.2867 S12: -0.8142 S13: 0.1119 REMARK 3 S21: 0.6468 S22: -0.4457 S23: -0.0767 REMARK 3 S31: -0.6011 S32: 0.0655 S33: 0.1589 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : G 1 G 115 REMARK 3 ORIGIN FOR THE GROUP (A): -20.6150 -77.2440 -0.0320 REMARK 3 T TENSOR REMARK 3 T11: 0.1276 T22: 0.0729 REMARK 3 T33: 0.0292 T12: -0.0581 REMARK 3 T13: -0.0375 T23: 0.0174 REMARK 3 L TENSOR REMARK 3 L11: 7.3267 L22: 5.3757 REMARK 3 L33: 6.3507 L12: 0.2220 REMARK 3 L13: -2.1617 L23: -0.3020 REMARK 3 S TENSOR REMARK 3 S11: 0.0512 S12: -0.1037 S13: -0.1425 REMARK 3 S21: 0.0518 S22: -0.1829 S23: -0.2921 REMARK 3 S31: 0.0916 S32: -0.4886 S33: 0.1317 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 1 H 115 REMARK 3 ORIGIN FOR THE GROUP (A): -29.9060 -88.9880 -14.5830 REMARK 3 T TENSOR REMARK 3 T11: 0.3103 T22: 0.3481 REMARK 3 T33: 0.0904 T12: -0.2302 REMARK 3 T13: 0.0222 T23: -0.0351 REMARK 3 L TENSOR REMARK 3 L11: 8.0362 L22: 10.0422 REMARK 3 L33: 5.0103 L12: 6.3314 REMARK 3 L13: -1.4450 L23: -0.0849 REMARK 3 S TENSOR REMARK 3 S11: -0.8527 S12: 1.0771 S13: -0.1652 REMARK 3 S21: -1.1237 S22: 0.8125 S23: 0.0284 REMARK 3 S31: 0.0403 S32: -0.2931 S33: 0.0402 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: U VALUES: WITH TLS ADDED REMARK 4 REMARK 4 3NN8 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUN-10. REMARK 100 THE RCSB ID CODE IS RCSB060039. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 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-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28384 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100 REMARK 200 RESOLUTION RANGE LOW (A) : 154.303 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 5.600 REMARK 200 R MERGE (I) : 0.12400 REMARK 200 R SYM (I) : 0.12400 REMARK 200 FOR THE DATA SET : 13.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.27 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 5.60 REMARK 200 R MERGE FOR SHELL (I) : 0.34200 REMARK 200 R SYM FOR SHELL (I) : 0.34200 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: MOLREP REMARK 200 STARTING MODEL: PDB ENTRY 1KTR REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 67.60 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, MAGNESIUM ACETATE, PH 6.5, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 3 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,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 Z,X,Y REMARK 290 6555 Z,-X,-Y REMARK 290 7555 -Z,-X,Y REMARK 290 8555 -Z,X,-Y REMARK 290 9555 Y,Z,X REMARK 290 10555 -Y,Z,-X REMARK 290 11555 Y,-Z,-X REMARK 290 12555 -Y,-Z,X REMARK 290 13555 X,Y+1/2,Z+1/2 REMARK 290 14555 -X,-Y+1/2,Z+1/2 REMARK 290 15555 -X,Y+1/2,-Z+1/2 REMARK 290 16555 X,-Y+1/2,-Z+1/2 REMARK 290 17555 Z,X+1/2,Y+1/2 REMARK 290 18555 Z,-X+1/2,-Y+1/2 REMARK 290 19555 -Z,-X+1/2,Y+1/2 REMARK 290 20555 -Z,X+1/2,-Y+1/2 REMARK 290 21555 Y,Z+1/2,X+1/2 REMARK 290 22555 -Y,Z+1/2,-X+1/2 REMARK 290 23555 Y,-Z+1/2,-X+1/2 REMARK 290 24555 -Y,-Z+1/2,X+1/2 REMARK 290 25555 X+1/2,Y,Z+1/2 REMARK 290 26555 -X+1/2,-Y,Z+1/2 REMARK 290 27555 -X+1/2,Y,-Z+1/2 REMARK 290 28555 X+1/2,-Y,-Z+1/2 REMARK 290 29555 Z+1/2,X,Y+1/2 REMARK 290 30555 Z+1/2,-X,-Y+1/2 REMARK 290 31555 -Z+1/2,-X,Y+1/2 REMARK 290 32555 -Z+1/2,X,-Y+1/2 REMARK 290 33555 Y+1/2,Z,X+1/2 REMARK 290 34555 -Y+1/2,Z,-X+1/2 REMARK 290 35555 Y+1/2,-Z,-X+1/2 REMARK 290 36555 -Y+1/2,-Z,X+1/2 REMARK 290 37555 X+1/2,Y+1/2,Z REMARK 290 38555 -X+1/2,-Y+1/2,Z REMARK 290 39555 -X+1/2,Y+1/2,-Z REMARK 290 40555 X+1/2,-Y+1/2,-Z REMARK 290 41555 Z+1/2,X+1/2,Y REMARK 290 42555 Z+1/2,-X+1/2,-Y REMARK 290 43555 -Z+1/2,-X+1/2,Y REMARK 290 44555 -Z+1/2,X+1/2,-Y REMARK 290 45555 Y+1/2,Z+1/2,X REMARK 290 46555 -Y+1/2,Z+1/2,-X REMARK 290 47555 Y+1/2,-Z+1/2,-X REMARK 290 48555 -Y+1/2,-Z+1/2,X 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 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 133.31850 REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 133.31850 REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 133.31850 REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 133.31850 REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 133.31850 REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 133.31850 REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 133.31850 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 133.31850 REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 133.31850 REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 133.31850 REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 133.31850 REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 133.31850 REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 133.31850 REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 133.31850 REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 133.31850 REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 133.31850 REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY1 25 1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY2 25 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 25 0.000000 0.000000 1.000000 133.31850 REMARK 290 SMTRY1 26 -1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY2 26 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 26 0.000000 0.000000 1.000000 133.31850 REMARK 290 SMTRY1 27 -1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY2 27 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 27 0.000000 0.000000 -1.000000 133.31850 REMARK 290 SMTRY1 28 1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY2 28 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 28 0.000000 0.000000 -1.000000 133.31850 REMARK 290 SMTRY1 29 0.000000 0.000000 1.000000 133.31850 REMARK 290 SMTRY2 29 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 29 0.000000 1.000000 0.000000 133.31850 REMARK 290 SMTRY1 30 0.000000 0.000000 1.000000 133.31850 REMARK 290 SMTRY2 30 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 30 0.000000 -1.000000 0.000000 133.31850 REMARK 290 SMTRY1 31 0.000000 0.000000 -1.000000 133.31850 REMARK 290 SMTRY2 31 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 31 0.000000 1.000000 0.000000 133.31850 REMARK 290 SMTRY1 32 0.000000 0.000000 -1.000000 133.31850 REMARK 290 SMTRY2 32 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 32 0.000000 -1.000000 0.000000 133.31850 REMARK 290 SMTRY1 33 0.000000 1.000000 0.000000 133.31850 REMARK 290 SMTRY2 33 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY3 33 1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY1 34 0.000000 -1.000000 0.000000 133.31850 REMARK 290 SMTRY2 34 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY3 34 -1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY1 35 0.000000 1.000000 0.000000 133.31850 REMARK 290 SMTRY2 35 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY3 35 -1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY1 36 0.000000 -1.000000 0.000000 133.31850 REMARK 290 SMTRY2 36 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY3 36 1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY1 37 1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY2 37 0.000000 1.000000 0.000000 133.31850 REMARK 290 SMTRY3 37 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 38 -1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY2 38 0.000000 -1.000000 0.000000 133.31850 REMARK 290 SMTRY3 38 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 39 -1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY2 39 0.000000 1.000000 0.000000 133.31850 REMARK 290 SMTRY3 39 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 40 1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY2 40 0.000000 -1.000000 0.000000 133.31850 REMARK 290 SMTRY3 40 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 41 0.000000 0.000000 1.000000 133.31850 REMARK 290 SMTRY2 41 1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY3 41 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY1 42 0.000000 0.000000 1.000000 133.31850 REMARK 290 SMTRY2 42 -1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY3 42 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY1 43 0.000000 0.000000 -1.000000 133.31850 REMARK 290 SMTRY2 43 -1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY3 43 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY1 44 0.000000 0.000000 -1.000000 133.31850 REMARK 290 SMTRY2 44 1.000000 0.000000 0.000000 133.31850 REMARK 290 SMTRY3 44 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY1 45 0.000000 1.000000 0.000000 133.31850 REMARK 290 SMTRY2 45 0.000000 0.000000 1.000000 133.31850 REMARK 290 SMTRY3 45 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 46 0.000000 -1.000000 0.000000 133.31850 REMARK 290 SMTRY2 46 0.000000 0.000000 1.000000 133.31850 REMARK 290 SMTRY3 46 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 47 0.000000 1.000000 0.000000 133.31850 REMARK 290 SMTRY2 47 0.000000 0.000000 -1.000000 133.31850 REMARK 290 SMTRY3 47 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 48 0.000000 -1.000000 0.000000 133.31850 REMARK 290 SMTRY2 48 0.000000 0.000000 -1.000000 133.31850 REMARK 290 SMTRY3 48 1.000000 0.000000 0.000000 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 300 REMARK: THERE ARE 4 BIOLOGICAL UNITS IN THE ASYMMETRIC UNIT (CHAINS REMARK 300 A & B, CHAINS C & F, CHAINS D & E, CHAINS G & H) 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1720 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 10340 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1720 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 10430 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1730 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 10390 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1740 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 10440 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H 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 SER A 122 REMARK 465 LYS B 0 REMARK 465 SER D 122 REMARK 465 LYS E 0 REMARK 465 SER G 122 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O SER B 10 O LYS B 108 2.11 REMARK 500 O PRO D 14 O LEU D 87 2.15 REMARK 500 O ASP A 91 OH TYR A 95 2.18 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 B 23 CA - CB - SG ANGL. DEV. = -11.1 DEGREES REMARK 500 SER C 86 N - CA - C ANGL. DEV. = -16.8 DEGREES REMARK 500 CYS E 23 CA - CB - SG ANGL. DEV. = -11.3 DEGREES REMARK 500 CYS F 23 CA - CB - SG ANGL. DEV. = -12.4 DEGREES REMARK 500 GLY F 46 N - CA - C ANGL. DEV. = -17.4 DEGREES REMARK 500 SER G 67 N - CA - C ANGL. DEV. = -16.6 DEGREES REMARK 500 CYS H 23 CA - CB - SG ANGL. DEV. = -12.5 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 CYS A 22 106.77 -160.35 REMARK 500 LEU A 29 5.93 -59.91 REMARK 500 SER A 30 19.23 -146.28 REMARK 500 PRO A 43 108.00 -53.58 REMARK 500 LYS A 45 59.95 -144.58 REMARK 500 ASP A 57 34.39 70.91 REMARK 500 SER A 78 26.23 46.47 REMARK 500 SER A 92 97.29 -66.80 REMARK 500 TYR A 106 49.76 36.18 REMARK 500 SER B 10 -69.23 -93.94 REMARK 500 LEU B 11 71.12 46.68 REMARK 500 PRO B 45 -69.17 -24.62 REMARK 500 LEU B 52 -54.79 -125.22 REMARK 500 LYS B 55 62.29 34.02 REMARK 500 VAL B 56 -49.47 57.46 REMARK 500 SER B 61 117.47 -20.81 REMARK 500 SER B 70 80.87 40.46 REMARK 500 SER C 67 16.68 54.49 REMARK 500 SER C 103 -64.93 65.61 REMARK 500 ASP D 56 -169.10 -39.39 REMARK 500 LYS D 66 49.83 38.76 REMARK 500 SER D 86 62.87 39.36 REMARK 500 SER D 92 28.76 -74.82 REMARK 500 GLN E 27 -155.39 -116.39 REMARK 500 ILE E 29 -29.59 72.66 REMARK 500 SER E 32 -40.93 -22.34 REMARK 500 LYS E 55 55.66 18.73 REMARK 500 VAL E 56 -45.71 67.44 REMARK 500 SER E 68 84.72 -152.36 REMARK 500 ILE F 29 -19.67 64.81 REMARK 500 SER F 32 105.04 53.11 REMARK 500 ASN F 33 134.42 1.30 REMARK 500 VAL F 56 -49.64 61.54 REMARK 500 SER F 72 -178.38 -67.79 REMARK 500 ASP G 57 45.53 -89.77 REMARK 500 SER G 67 78.01 -109.63 REMARK 500 SER G 86 69.85 38.84 REMARK 500 GLU G 90 -16.78 -49.27 REMARK 500 SER G 92 96.55 -67.21 REMARK 500 HIS G 105 -0.51 75.41 REMARK 500 TYR G 106 47.42 38.30 REMARK 500 ILE H 29 -41.06 71.52 REMARK 500 VAL H 30 105.44 -56.85 REMARK 500 SER H 32 -24.39 -36.71 REMARK 500 LEU H 52 -61.01 -95.19 REMARK 500 LYS H 55 40.82 36.99 REMARK 500 VAL H 56 -50.34 62.80 REMARK 500 THR H 74 -21.54 65.52 REMARK 500 ARG H 82 66.52 -166.42 REMARK 500 VAL H 83 130.38 -36.30 REMARK 500 REMARK 500 THIS ENTRY HAS 51 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ARG C 85 SER C 86 -30.93 REMARK 500 GLY D 15 ALA D 16 -144.41 REMARK 500 PRO E 45 GLY E 46 -30.74 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 THR H 74 24.1 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL