REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 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) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 30265 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) : 0.190 REMARK 3 R VALUE (WORKING SET) : 0.188 REMARK 3 FREE R VALUE : 0.232 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1610 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 25 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.16 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1709 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.42 REMARK 3 BIN R VALUE (WORKING SET) : 0.2670 REMARK 3 BIN FREE R VALUE SET COUNT : 94 REMARK 3 BIN FREE R VALUE : 0.3280 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 7740 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 B VALUE TYPE : LIKELY RESIDUAL REMARK 3 FROM WILSON PLOT (A**2) : 102.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 97.09 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.13000 REMARK 3 B22 (A**2) : -2.13000 REMARK 3 B33 (A**2) : 3.20000 REMARK 3 B12 (A**2) : -1.07000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 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): 0.371 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.295 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 37.339 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7954 ; 0.010 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 5414 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10818 ; 1.309 ; 1.948 REMARK 3 BOND ANGLES OTHERS (DEGREES): 13140 ; 0.828 ; 3.003 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 983 ; 7.316 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 352 ;34.682 ;23.835 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1270 ;18.277 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;17.306 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1164 ; 0.073 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8876 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1631 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1594 ; 0.205 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5462 ; 0.191 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3742 ; 0.188 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 4454 ; 0.087 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 160 ; 0.157 ; 0.200 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): 16 ; 0.183 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 44 ; 0.206 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.204 ; 0.200 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): 6292 ; 2.754 ; 2.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1999 ; 0.452 ; 2.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7966 ; 3.850 ; 5.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3634 ; 2.212 ; 2.500 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2852 ; 3.360 ; 5.000 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 : 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 26 A 148 REMARK 3 ORIGIN FOR THE GROUP (A): 40.9844 -66.6712 -21.7118 REMARK 3 T TENSOR REMARK 3 T11: 0.0426 T22: -0.5616 REMARK 3 T33: -0.0781 T12: -0.0938 REMARK 3 T13: 0.5535 T23: -0.0835 REMARK 3 L TENSOR REMARK 3 L11: 5.4856 L22: 3.2562 REMARK 3 L33: 4.3218 L12: 2.4527 REMARK 3 L13: -1.3419 L23: -0.0037 REMARK 3 S TENSOR REMARK 3 S11: 0.6606 S12: -0.4301 S13: 1.2621 REMARK 3 S21: 0.8843 S22: -0.4343 S23: 0.8907 REMARK 3 S31: -0.5291 S32: -0.1925 S33: -0.2262 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 : A 149 A 272 REMARK 3 ORIGIN FOR THE GROUP (A): 70.2656 -49.9567 -19.1061 REMARK 3 T TENSOR REMARK 3 T11: -0.2707 T22: -0.2152 REMARK 3 T33: -0.2174 T12: -0.3338 REMARK 3 T13: 0.2144 T23: -0.0256 REMARK 3 L TENSOR REMARK 3 L11: 2.9563 L22: 7.1990 REMARK 3 L33: 7.5997 L12: -1.7107 REMARK 3 L13: -1.4427 L23: 3.6715 REMARK 3 S TENSOR REMARK 3 S11: -0.0448 S12: 0.3736 S13: 0.0224 REMARK 3 S21: -0.1765 S22: -0.1357 S23: -0.5808 REMARK 3 S31: 0.1111 S32: 0.3166 S33: 0.1805 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 : A 273 A 428 REMARK 3 ORIGIN FOR THE GROUP (A): 59.0804 -22.5032 -21.9708 REMARK 3 T TENSOR REMARK 3 T11: -0.2564 T22: -0.0849 REMARK 3 T33: -0.4491 T12: -0.3213 REMARK 3 T13: -0.0288 T23: 0.1000 REMARK 3 L TENSOR REMARK 3 L11: 4.9272 L22: 6.9575 REMARK 3 L33: 4.7733 L12: 0.2815 REMARK 3 L13: -1.0689 L23: -0.9527 REMARK 3 S TENSOR REMARK 3 S11: -0.0549 S12: 1.0391 S13: 0.7366 REMARK 3 S21: -0.4171 S22: -0.0388 S23: 0.1308 REMARK 3 S31: -0.2721 S32: -0.2378 S33: 0.0937 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 : A 429 A 595 REMARK 3 ORIGIN FOR THE GROUP (A): 47.5403 -41.4692 1.4651 REMARK 3 T TENSOR REMARK 3 T11: -0.0835 T22: -0.5732 REMARK 3 T33: -0.4680 T12: -0.2803 REMARK 3 T13: 0.2763 T23: -0.1714 REMARK 3 L TENSOR REMARK 3 L11: 8.6445 L22: 4.9990 REMARK 3 L33: 5.5272 L12: 0.7939 REMARK 3 L13: -1.7605 L23: 0.0641 REMARK 3 S TENSOR REMARK 3 S11: -0.3989 S12: -0.0218 S13: -0.1158 REMARK 3 S21: 0.5461 S22: -0.0666 S23: 0.6200 REMARK 3 S31: 0.5485 S32: -0.1800 S33: 0.4655 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 : L 1 L 109 REMARK 3 ORIGIN FOR THE GROUP (A): 21.7522 -98.1904 -16.3692 REMARK 3 T TENSOR REMARK 3 T11: -0.2212 T22: -0.4097 REMARK 3 T33: -0.4960 T12: -0.2653 REMARK 3 T13: 0.0939 T23: 0.1126 REMARK 3 L TENSOR REMARK 3 L11: 8.2714 L22: 5.3646 REMARK 3 L33: 2.7094 L12: 3.4176 REMARK 3 L13: -4.4400 L23: -2.3484 REMARK 3 S TENSOR REMARK 3 S11: 0.7525 S12: -0.7261 S13: -0.6398 REMARK 3 S21: 0.7973 S22: -0.4331 S23: -0.1953 REMARK 3 S31: -0.0224 S32: -0.1138 S33: -0.3194 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 : L 110 L 214 REMARK 3 ORIGIN FOR THE GROUP (A): 29.3067-134.2768 -13.6348 REMARK 3 T TENSOR REMARK 3 T11: 0.5898 T22: -0.2676 REMARK 3 T33: 0.4597 T12: -0.1266 REMARK 3 T13: 0.0397 T23: 0.3504 REMARK 3 L TENSOR REMARK 3 L11: 10.6088 L22: 4.2232 REMARK 3 L33: 1.8260 L12: -4.3172 REMARK 3 L13: -0.1026 L23: 0.2556 REMARK 3 S TENSOR REMARK 3 S11: -0.6133 S12: -0.1961 S13: -1.4563 REMARK 3 S21: 0.9515 S22: 0.1814 S23: -0.5841 REMARK 3 S31: 0.9602 S32: 0.4480 S33: 0.4319 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 : H 1 H 114 REMARK 3 ORIGIN FOR THE GROUP (A): 40.7316 -95.6262 -26.3287 REMARK 3 T TENSOR REMARK 3 T11: -0.5203 T22: -0.3963 REMARK 3 T33: -0.3232 T12: -0.2214 REMARK 3 T13: 0.0267 T23: 0.0737 REMARK 3 L TENSOR REMARK 3 L11: 7.7230 L22: 6.8541 REMARK 3 L33: 3.2136 L12: -0.2740 REMARK 3 L13: -1.5145 L23: -1.2728 REMARK 3 S TENSOR REMARK 3 S11: 0.6306 S12: 0.3292 S13: -1.1092 REMARK 3 S21: 0.6364 S22: -0.2150 S23: -0.5909 REMARK 3 S31: 0.0935 S32: 0.5995 S33: -0.4157 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 115 H 216 REMARK 3 ORIGIN FOR THE GROUP (A): 35.0288-129.0442 -27.7922 REMARK 3 T TENSOR REMARK 3 T11: 0.1147 T22: 0.1313 REMARK 3 T33: 0.4291 T12: -0.1129 REMARK 3 T13: -0.0212 T23: 0.0858 REMARK 3 L TENSOR REMARK 3 L11: 6.5796 L22: 3.4182 REMARK 3 L33: 2.2855 L12: -0.8473 REMARK 3 L13: -1.7847 L23: 0.4644 REMARK 3 S TENSOR REMARK 3 S11: -0.0903 S12: 1.4945 S13: -0.8378 REMARK 3 S21: 0.0969 S22: -0.2636 S23: -1.1463 REMARK 3 S31: 1.1225 S32: -0.2394 S33: 0.3540 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 2QQL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-07. REMARK 100 THE RCSB ID CODE IS RCSB043931. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-APR-06 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 5.0.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.00 REMARK 200 MONOCHROMATOR : NULL 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 : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31929 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 3.800 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.06100 REMARK 200 FOR THE DATA SET : 18.3000 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) : 3.21 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9 REMARK 200 DATA REDUNDANCY IN SHELL : 3.60 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.51500 REMARK 200 FOR SHELL : 2.600 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: PDB ENTRY 2QQK REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 67.61 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 1000, 10% PEG 8000, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 297K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+1/3 REMARK 290 6555 -X,-X+Y,-Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 135.14467 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 67.57233 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 67.57233 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 135.14467 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 14540 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -67.57233 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 GLN A 23 REMARK 465 PRO A 24 REMARK 465 ASP A 25 REMARK 465 GLU A 197 REMARK 465 HIS A 198 REMARK 465 ASP A 199 REMARK 465 PRO A 200 REMARK 465 LEU A 201 REMARK 465 GLN A 202 REMARK 465 VAL A 203 REMARK 465 GLY A 204 REMARK 465 GLU A 205 REMARK 465 GLY A 206 REMARK 465 ASP A 207 REMARK 465 GLY A 509 REMARK 465 ASP A 510 REMARK 465 SER A 511 REMARK 465 ILE A 512 REMARK 465 THR A 513 REMARK 465 ALA A 514 REMARK 465 VAL A 515 REMARK 465 GLU A 516 REMARK 465 HIS A 596 REMARK 465 HIS A 597 REMARK 465 HIS A 598 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 REMARK 465 HIS H 220 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 ARG H 100A NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 ARG L 108 NE - CZ - NH1 ANGL. DEV. = 3.2 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 PRO A 43 -58.61 -26.22 REMARK 500 TYR A 45 127.88 -22.40 REMARK 500 ASN A 65 -63.77 -7.72 REMARK 500 LYS A 80 -115.50 -81.28 REMARK 500 HIS A 81 -123.66 58.97 REMARK 500 TYR A 85 -64.91 -102.99 REMARK 500 ASP A 94 127.41 167.79 REMARK 500 SER A 95 164.70 85.26 REMARK 500 ALA A 129 118.03 170.95 REMARK 500 ARG A 130 142.73 52.71 REMARK 500 SER A 146 150.73 -48.30 REMARK 500 LYS A 184 7.75 80.38 REMARK 500 VAL A 222 -49.45 -137.10 REMARK 500 LYS A 233 75.74 -65.22 REMARK 500 ASN A 274 86.55 -59.24 REMARK 500 ASN A 278 13.40 -142.97 REMARK 500 TRP A 304 48.71 -142.09 REMARK 500 ASN A 316 -112.10 41.17 REMARK 500 LYS A 326 41.03 -94.95 REMARK 500 ARG A 334 -56.91 76.03 REMARK 500 ALA A 347 139.65 -174.56 REMARK 500 SER A 349 107.40 -57.13 REMARK 500 HIS A 381 171.01 -56.88 REMARK 500 ALA A 386 -117.45 -94.77 REMARK 500 HIS A 399 -65.56 2.91 REMARK 500 ARG A 405 -51.71 -128.29 REMARK 500 SER A 416 -67.37 65.10 REMARK 500 CYS A 427 -179.56 -178.24 REMARK 500 SER A 435 31.40 -143.24 REMARK 500 VAL A 468 -48.46 63.78 REMARK 500 SER A 472 -72.60 -136.39 REMARK 500 GLN A 544 61.54 69.38 REMARK 500 GLN A 545 142.40 -175.40 REMARK 500 PRO H 41 114.81 -33.03 REMARK 500 ALA H 88 170.30 178.84 REMARK 500 ARG H 100 57.14 -148.34 REMARK 500 PRO H 126 -163.39 -55.38 REMARK 500 ASP H 144 68.33 63.36 REMARK 500 PHE H 146 141.40 -171.87 REMARK 500 THR H 191 20.57 -143.35 REMARK 500 SER L 30 -137.80 49.12 REMARK 500 ALA L 51 -43.93 82.81 REMARK 500 SER L 67 64.01 179.78 REMARK 500 GLU L 81 -19.58 -48.61 REMARK 500 ALA L 84 179.31 177.56 REMARK 500 TRP L 92 -53.29 -127.14 REMARK 500 ASN L 138 100.83 52.24 REMARK 500 LEU L 154 85.15 -36.76 REMARK 500 ASN L 158 36.19 -153.62 REMARK 500 LYS L 190 -63.64 -102.65 REMARK 500 REMARK 500 THIS ENTRY HAS 52 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 PRO A 64 ASN A 65 147.12 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2QQI RELATED DB: PDB REMARK 900 RELATED ID: 2QQJ RELATED DB: PDB REMARK 900 RELATED ID: 2QQK RELATED DB: PDB REMARK 900 RELATED ID: 2QQM RELATED DB: PDB REMARK 900 RELATED ID: 2QQN RELATED DB: PDB REMARK 900 RELATED ID: 2QQO RELATED DB: PDB