REMARK 2 REMARK 2 RESOLUTION. 2.70 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) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5 REMARK 3 NUMBER OF REFLECTIONS : 33325 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 : 0.283 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200 REMARK 3 FREE R VALUE TEST SET COUNT : 1721 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) : 2.70 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1975 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.09 REMARK 3 BIN R VALUE (WORKING SET) : 0.3090 REMARK 3 BIN FREE R VALUE SET COUNT : 98 REMARK 3 BIN FREE R VALUE : 0.3750 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 7624 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 32 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.88 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.26000 REMARK 3 B22 (A**2) : 0.15000 REMARK 3 B33 (A**2) : -0.23000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -1.65000 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): 0.387 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.310 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 32.279 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.925 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.873 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7801 ; 0.008 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 5261 ; 0.007 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10605 ; 1.062 ; 1.952 REMARK 3 BOND ANGLES OTHERS (DEGREES): 12773 ; 0.932 ; 3.005 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 995 ; 6.070 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 317 ;32.606 ;23.281 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1248 ;17.252 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 55 ;14.167 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1202 ; 0.058 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8717 ; 0.002 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1564 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1559 ; 0.189 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5325 ; 0.189 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3686 ; 0.172 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 4429 ; 0.086 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 185 ; 0.131 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.016 ; 0.200 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): 24 ; 0.265 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 59 ; 0.195 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.163 ; 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): 6377 ; 0.556 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2037 ; 0.074 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8047 ; 0.539 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3241 ; 0.939 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2558 ; 1.331 ; 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 : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 7 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 153 A 449 REMARK 3 ORIGIN FOR THE GROUP (A): -8.8370 -20.6930 -13.1480 REMARK 3 T TENSOR REMARK 3 T11: -0.1587 T22: -0.4373 REMARK 3 T33: -0.2207 T12: 0.0357 REMARK 3 T13: -0.0849 T23: 0.0040 REMARK 3 L TENSOR REMARK 3 L11: 2.2951 L22: 2.5116 REMARK 3 L33: 2.8159 L12: 0.6907 REMARK 3 L13: 0.7993 L23: 0.0681 REMARK 3 S TENSOR REMARK 3 S11: -0.1261 S12: 0.2751 S13: 0.1157 REMARK 3 S21: -0.1680 S22: 0.0849 S23: 0.0900 REMARK 3 S31: -0.2561 S32: 0.0341 S33: 0.0412 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 453 A 659 REMARK 3 ORIGIN FOR THE GROUP (A): -28.2130 -31.6730 12.0050 REMARK 3 T TENSOR REMARK 3 T11: -0.0577 T22: -0.1639 REMARK 3 T33: -0.1209 T12: 0.0770 REMARK 3 T13: 0.0288 T23: 0.0445 REMARK 3 L TENSOR REMARK 3 L11: 4.8482 L22: 5.9855 REMARK 3 L33: 5.5415 L12: -1.1627 REMARK 3 L13: -0.6233 L23: -0.3236 REMARK 3 S TENSOR REMARK 3 S11: -0.1474 S12: -0.5405 S13: -0.3143 REMARK 3 S21: 0.8210 S22: 0.1163 S23: 0.5030 REMARK 3 S31: 0.0305 S32: -0.4332 S33: 0.0311 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 : P 61 P 152 REMARK 3 ORIGIN FOR THE GROUP (A): 13.7960 -26.0430 5.2670 REMARK 3 T TENSOR REMARK 3 T11: -0.1335 T22: -0.5249 REMARK 3 T33: -0.1751 T12: -0.0173 REMARK 3 T13: -0.0998 T23: 0.0496 REMARK 3 L TENSOR REMARK 3 L11: 5.9805 L22: 3.3998 REMARK 3 L33: 4.4977 L12: 0.8498 REMARK 3 L13: 2.9643 L23: 1.4566 REMARK 3 S TENSOR REMARK 3 S11: -0.0170 S12: -0.1861 S13: 0.0113 REMARK 3 S21: 0.2546 S22: 0.0004 S23: -0.4128 REMARK 3 S31: -0.0379 S32: 0.1028 S33: 0.0166 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 : L 4 L 105 REMARK 3 ORIGIN FOR THE GROUP (A): -13.5570 -20.6450 -48.6430 REMARK 3 T TENSOR REMARK 3 T11: 0.0202 T22: -0.2390 REMARK 3 T33: -0.2773 T12: 0.0470 REMARK 3 T13: -0.0133 T23: 0.0369 REMARK 3 L TENSOR REMARK 3 L11: 3.6967 L22: 4.6140 REMARK 3 L33: 8.2790 L12: 1.1251 REMARK 3 L13: 3.1457 L23: 0.7441 REMARK 3 S TENSOR REMARK 3 S11: 0.0153 S12: 0.3699 S13: -0.0137 REMARK 3 S21: -0.2475 S22: -0.0795 S23: -0.0398 REMARK 3 S31: 0.3515 S32: 0.3109 S33: 0.0641 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 106 L 214 REMARK 3 ORIGIN FOR THE GROUP (A): -31.6630 -9.0980 -78.6240 REMARK 3 T TENSOR REMARK 3 T11: 0.1927 T22: 0.0115 REMARK 3 T33: -0.1782 T12: 0.2156 REMARK 3 T13: 0.0083 T23: -0.0283 REMARK 3 L TENSOR REMARK 3 L11: 3.7147 L22: 6.6438 REMARK 3 L33: 8.2002 L12: -1.1702 REMARK 3 L13: 2.3891 L23: -3.1581 REMARK 3 S TENSOR REMARK 3 S11: 0.1281 S12: 0.2234 S13: 0.3364 REMARK 3 S21: -0.5348 S22: -0.2853 S23: -0.3786 REMARK 3 S31: -0.3573 S32: -0.5924 S33: 0.1572 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 : H 4 H 110 REMARK 3 ORIGIN FOR THE GROUP (A): -9.1970 0.7270 -46.0660 REMARK 3 T TENSOR REMARK 3 T11: 0.2310 T22: -0.1808 REMARK 3 T33: 0.0197 T12: -0.1304 REMARK 3 T13: -0.1504 T23: 0.0623 REMARK 3 L TENSOR REMARK 3 L11: 4.1729 L22: 6.0379 REMARK 3 L33: 7.2765 L12: 1.1876 REMARK 3 L13: 1.3011 L23: -3.7084 REMARK 3 S TENSOR REMARK 3 S11: -0.3405 S12: 0.0416 S13: 0.4442 REMARK 3 S21: 0.1597 S22: 0.0133 S23: -0.5247 REMARK 3 S31: -1.1534 S32: 0.5318 S33: 0.3272 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 111 H 212 REMARK 3 ORIGIN FOR THE GROUP (A): -32.9730 1.9550 -66.3910 REMARK 3 T TENSOR REMARK 3 T11: 0.4011 T22: 0.0148 REMARK 3 T33: -0.0806 T12: 0.3154 REMARK 3 T13: -0.1406 T23: -0.0649 REMARK 3 L TENSOR REMARK 3 L11: 9.2187 L22: 8.1739 REMARK 3 L33: 6.3897 L12: 5.1981 REMARK 3 L13: 4.3506 L23: 0.1609 REMARK 3 S TENSOR REMARK 3 S11: -0.4303 S12: -0.4611 S13: 0.5589 REMARK 3 S21: -0.0921 S22: -0.3394 S23: 0.5178 REMARK 3 S31: -0.8667 S32: -1.1647 S33: 0.7697 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3SQO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUL-11. REMARK 100 THE RCSB ID CODE IS RCSB066532. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-NOV-08 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.2 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) : 1.0 REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL, SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35342 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7 REMARK 200 DATA REDUNDANCY : 2.900 REMARK 200 R MERGE (I) : 0.11900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74 REMARK 200 COMPLETENESS FOR SHELL (%) : 73.5 REMARK 200 DATA REDUNDANCY IN SHELL : 1.90 REMARK 200 R MERGE FOR SHELL (I) : 0.47200 REMARK 200 R SYM FOR SHELL (I) : 0.47200 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.82 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 7% PEG 10000, 100 MM HEPES PH 7.2, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 35.49050 REMARK 290 SMTRY3 2 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L, P 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 400 REMARK 400 COMPOUND REMARK 400 CHAINS A AND P ARE EXPRESSED AS A SINGLE CHAIN. THERE IS AN AUTO- REMARK 400 PROTEOLYSIS THAT CUTS THE CHAIN INTO TWO, BUT THE SECOND CHAIN REMARK 400 STAYS VERY TIGHTLY ASSOCIATED. IT HAS BEEN THE NOMENCLATURE OF THE REMARK 400 PREVIOUSLY PUBLISHED PCSK9 STRUCTURES TO HAVE CHAIN P AS THE PRO- REMARK 400 DOMAIN AND CHAIN A AS THE CATALYTIC DOMAIN 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 ASP A 169 REMARK 465 GLU A 170 REMARK 465 TYR A 171 REMARK 465 GLN A 172 REMARK 465 PRO A 173 REMARK 465 PRO A 174 REMARK 465 ASP A 175 REMARK 465 ASP A 212 REMARK 465 GLY A 213 REMARK 465 THR A 214 REMARK 465 ARG A 215 REMARK 465 PHE A 216 REMARK 465 HIS A 217 REMARK 465 ARG A 218 REMARK 465 ALA A 451 REMARK 465 GLY A 452 REMARK 465 THR A 573 REMARK 465 HIS A 574 REMARK 465 LYS A 575 REMARK 465 PRO A 576 REMARK 465 PRO A 577 REMARK 465 VAL A 578 REMARK 465 LEU A 579 REMARK 465 ARG A 580 REMARK 465 PRO A 581 REMARK 465 ARG A 582 REMARK 465 GLY A 583 REMARK 465 GLN A 584 REMARK 465 ASP A 660 REMARK 465 VAL A 661 REMARK 465 SER A 662 REMARK 465 THR A 663 REMARK 465 THR A 664 REMARK 465 GLY A 665 REMARK 465 SER A 666 REMARK 465 THR A 667 REMARK 465 SER A 668 REMARK 465 GLU A 669 REMARK 465 ARG A 682 REMARK 465 HIS A 683 REMARK 465 LEU A 684 REMARK 465 ALA A 685 REMARK 465 GLN A 686 REMARK 465 ALA A 687 REMARK 465 SER A 688 REMARK 465 GLN A 689 REMARK 465 GLU A 690 REMARK 465 LEU A 691 REMARK 465 GLN A 692 REMARK 465 SER H 119 REMARK 465 ARG H 133 REMARK 465 SER H 134 REMARK 465 THR H 135 REMARK 465 SER H 136 REMARK 465 GLU H 137 REMARK 465 SER H 138 REMARK 465 LYS H 218 REMARK 465 ASP L 1 REMARK 465 GLN P 31 REMARK 465 GLU P 32 REMARK 465 ASP P 33 REMARK 465 GLU P 34 REMARK 465 ASP P 35 REMARK 465 GLY P 36 REMARK 465 ASP P 37 REMARK 465 TYR P 38 REMARK 465 GLU P 39 REMARK 465 GLU P 40 REMARK 465 LEU P 41 REMARK 465 VAL P 42 REMARK 465 LEU P 43 REMARK 465 ALA P 44 REMARK 465 LEU P 45 REMARK 465 ARG P 46 REMARK 465 SER P 47 REMARK 465 GLU P 48 REMARK 465 GLU P 49 REMARK 465 ASP P 50 REMARK 465 GLY P 51 REMARK 465 LEU P 52 REMARK 465 ALA P 53 REMARK 465 GLU P 54 REMARK 465 ALA P 55 REMARK 465 PRO P 56 REMARK 465 GLU P 57 REMARK 465 HIS P 58 REMARK 465 GLY P 59 REMARK 465 THR P 60 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 ASP A 186 -139.35 -159.38 REMARK 500 ASN A 207 87.77 -159.03 REMARK 500 VAL A 280 -141.00 -114.20 REMARK 500 ASN A 317 43.45 -106.14 REMARK 500 PRO A 446 -175.00 -68.92 REMARK 500 SER A 447 -101.72 -57.71 REMARK 500 GLN A 531 -119.60 -63.49 REMARK 500 ALA A 532 -168.89 176.44 REMARK 500 ASN A 533 91.16 34.68 REMARK 500 ALA A 542 -127.58 -102.72 REMARK 500 ALA A 544 -81.29 -54.98 REMARK 500 SER A 564 117.66 -163.47 REMARK 500 PRO A 616 174.68 -48.42 REMARK 500 ALA A 617 -74.74 -48.46 REMARK 500 THR A 641 -166.59 -71.59 REMARK 500 SER A 642 -62.43 -140.20 REMARK 500 ASP A 651 -121.88 53.94 REMARK 500 CYS H 22 113.83 -162.43 REMARK 500 GLN H 43 -64.81 -164.20 REMARK 500 ALA H 100 79.53 -10.75 REMARK 500 SER H 100A 80.56 52.90 REMARK 500 SER H 131 38.46 -145.91 REMARK 500 ASP H 148 83.43 46.39 REMARK 500 THR H 164 -46.85 -139.77 REMARK 500 THR H 195 50.52 -144.87 REMARK 500 ASN H 208 68.49 65.44 REMARK 500 GLU H 216 -84.68 -113.70 REMARK 500 CYS L 23 115.84 -164.30 REMARK 500 SER L 30 -131.10 49.80 REMARK 500 ALA L 51 -22.96 83.03 REMARK 500 ASN L 138 62.75 64.03 REMARK 500 LYS L 169 -65.40 -101.20 REMARK 500 LYS L 188 20.63 -77.85 REMARK 500 LYS L 190 -63.23 -97.59 REMARK 500 GLU P 84 -66.39 -17.55 REMARK 500 HIS P 139 -9.95 87.00 REMARK 500 REMARK 500 REMARK: NULL