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) : 40.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE REMARK 3 COMPLETENESS FOR RANGE (%) : 99.98 REMARK 3 NUMBER OF REFLECTIONS : 30522 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) : 0.20293 REMARK 3 R VALUE (WORKING SET) : 0.19992 REMARK 3 FREE R VALUE : 0.25944 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1 REMARK 3 FREE R VALUE TEST SET COUNT : 1629 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) : 2.700 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.770 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2194 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.79 REMARK 3 BIN R VALUE (WORKING SET) : 0.320 REMARK 3 BIN FREE R VALUE SET COUNT : 136 REMARK 3 BIN FREE R VALUE : 0.394 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 5896 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 1 REMARK 3 SOLVENT ATOMS : 199 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.080 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.70 REMARK 3 B22 (A**2) : -1.15 REMARK 3 B33 (A**2) : 0.46 REMARK 3 B12 (A**2) : 0.00 REMARK 3 B13 (A**2) : 0.00 REMARK 3 B23 (A**2) : 0.00 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.547 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.319 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.236 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.580 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.926 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.877 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6019 ; 0.010 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8178 ; 1.413 ; 1.957 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 780 ; 7.414 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 239 ;38.930 ;24.059 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 971 ;18.365 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;20.378 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 939 ; 0.104 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4516 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2633 ; 0.222 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4006 ; 0.306 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 286 ; 0.134 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.133 ; 0.200 REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 50 ; 0.207 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.070 ; 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): 3969 ; 0.581 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6253 ; 1.051 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2300 ; 1.323 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1924 ; 2.353 ; 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 : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS. THE FINAL MODEL CONTAINS RESIDUES 61-152 FROM THE REMARK 3 PCSK9 PRODOMAIN (CHAIN P) AND RESIDUES 155-157 AND 178-422 FROM REMARK 3 THE PCSK9 CATALYTIC DOMAIN (CHAIN A) THE FINAL MODEL CONTAINS REMARK 3 RESIDUES 1-212 FROM THE FAB LIGHT CHAIN (CHAINS B AND C)AND REMARK 3 RESIDUES 1-236 FROM THE FAB HEAVY CHAIN (CHAINS D AND E). THERE REMARK 3 WAS NO ELECTRON DENSITY PRESENT FOR PCSK9 RESIDUES 53-60, 153-154, REMARK 3 158-177 AND 423-451, NOR FOR 1D05 FAB RESIDUES 237-255 OF THE REMARK 3 CONSTANT DOMAIN OF THE HEAVY CHAIN (CHAIN E) AND RESIDUE 213 OF REMARK 3 THE CONSTANT DOMAIN OF THE LIGHT CHAIN (CHAIN C). THESE RESIDUES REMARK 3 WERE THEREFORE EXCLUDED FROM THE REFINEMENT. ALL OVER THE REMARK 3 STRUCTURE, WHEN POOR DENSITY FOR SIDE CHAINS WAS PRESENT, THE REMARK 3 CORRESPONDING RESIDUE WAS MODELED AS ALA. ALL OVER THE STRUCTURE, REMARK 3 WHEN POOR DENSITY FOR SIDE CHAINS WAS PRESENT, THE CORRESPONDING REMARK 3 RESIDUE WAS MODELED AS ALA. REMARK 4 REMARK 4 2XTJ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-OCT-10. REMARK 100 THE PDBE ID CODE IS EBI-45730. 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 : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.933 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD (QUANTUM 4) REMARK 200 DETECTOR MANUFACTURER : ADSC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32238 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.70 REMARK 200 RESOLUTION RANGE LOW (A) : 40.00 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 5.1 REMARK 200 R MERGE (I) : 0.13 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.50 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 4.7 REMARK 200 R MERGE FOR SHELL (I) : 0.51 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.60 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 2W2M REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.34 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZATION EXPERIMENTS REMARK 280 WERE PERFORMED AT ROOM TEMPERATURE BY THE HANGING-DROP AND REMARK 280 SITTING-DROP METHODS. THIN PLATE-LIKE CRYSTALS WERE REMARK 280 OBTAINED IN 100 MM NA CITRATE PH 6.5, 13% PEG 6000. FOR DATA REMARK 280 COLLECTION CRYSTALS WERE TRANSFERRED TO A STABILIZING REMARK 280 SOLUTION (20 MM TRIS PH 8.0, 50 MM NACITRATE PH 6.5, 100 REMARK 280 MM NACL, 5% GLYCEROL, 1 MM TCEP, 1 MICROM CACL2, 25% REMARK 280 PEG6000), THEN TRANSFERRED FOR 2 MIN TO A CRYOPROTECTANT REMARK 280 SOLUTION (20 MM TRIS PH 8.0, 50 MM NACITRATE PH 6.5, 100 REMARK 280 MM NACL, 20% GLYCEROL, 1 MM TCEP, 1 MICROM CACL2, 35% REMARK 280 PEG6000) AND FINALLY PLACED DIRECTLY INTO LIQUID NITROGEN. 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 33.29450 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 125.43000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.91700 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 125.43000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.29450 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.91700 REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 10210 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 40980 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.9 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P, B, D, C, 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 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 153 REMARK 465 ILE A 154 REMARK 465 LEU A 158 REMARK 465 GLU A 159 REMARK 465 ARG A 160 REMARK 465 ILE A 161 REMARK 465 THR A 162 REMARK 465 PRO A 163 REMARK 465 PRO A 164 REMARK 465 ARG A 165 REMARK 465 TYR A 166 REMARK 465 ARG A 167 REMARK 465 ALA A 168 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 GLY A 176 REMARK 465 GLY A 177 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 VAL A 423 REMARK 465 ILE A 424 REMARK 465 ASN A 425 REMARK 465 GLU A 426 REMARK 465 ALA A 427 REMARK 465 TRP A 428 REMARK 465 PHE A 429 REMARK 465 PRO A 430 REMARK 465 GLU A 431 REMARK 465 ASP A 432 REMARK 465 GLN A 433 REMARK 465 ARG A 434 REMARK 465 VAL A 435 REMARK 465 LEU A 436 REMARK 465 THR A 437 REMARK 465 PRO A 438 REMARK 465 ASN A 439 REMARK 465 LEU A 440 REMARK 465 VAL A 441 REMARK 465 ALA A 442 REMARK 465 ALA A 443 REMARK 465 LEU A 444 REMARK 465 PRO A 445 REMARK 465 PRO A 446 REMARK 465 SER A 447 REMARK 465 THR A 448 REMARK 465 HIS A 449 REMARK 465 GLY A 450 REMARK 465 ALA A 451 REMARK 465 ALA A 452 REMARK 465 GLY A 453 REMARK 465 THR A 454 REMARK 465 ALA A 455 REMARK 465 ALA A 456 REMARK 465 ALA A 457 REMARK 465 SER A 458 REMARK 465 HIS A 459 REMARK 465 HIS A 460 REMARK 465 HIS A 461 REMARK 465 HIS A 462 REMARK 465 HIS A 463 REMARK 465 HIS A 464 REMARK 465 ALA C 213 REMARK 465 GLN E 237 REMARK 465 LYS E 238 REMARK 465 LEU E 239 REMARK 465 ILE E 240 REMARK 465 SER E 241 REMARK 465 GLU E 242 REMARK 465 GLU E 243 REMARK 465 ASP E 244 REMARK 465 LEU E 245 REMARK 465 ASN E 246 REMARK 465 GLY E 247 REMARK 465 ALA E 248 REMARK 465 PRO E 249 REMARK 465 HIS E 250 REMARK 465 HIS E 251 REMARK 465 HIS E 252 REMARK 465 HIS E 253 REMARK 465 HIS E 254 REMARK 465 HIS E 255 REMARK 465 MET P 39 REMARK 465 LYS P 40 REMARK 465 GLY P 41 REMARK 465 SER P 42 REMARK 465 LYS P 43 REMARK 465 GLY P 44 REMARK 465 SER P 45 REMARK 465 LYS P 46 REMARK 465 GLY P 47 REMARK 465 SER P 48 REMARK 465 LYS P 49 REMARK 465 PRO P 50 REMARK 465 MET P 51 REMARK 465 SER 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 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 ASP A 212 CG OD1 OD2 REMARK 470 GLN A 278 CG CD OE1 NE2 REMARK 470 LYS C 168 CG CD CE NZ REMARK 470 GLU C 212 CG CD OE1 OE2 REMARK 470 LYS E 232 CG CD CE NZ REMARK 470 GLU E 234 CG CD OE1 OE2 REMARK 470 GLU E 236 CG CD OE1 OE2 REMARK 470 THR P 61 OG1 CG2 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 -160.24 -167.49 REMARK 500 VAL A 234 -74.42 89.40 REMARK 500 VAL A 280 168.10 80.94 REMARK 500 LEU A 287 78.61 -118.20 REMARK 500 PRO A 288 49.26 -79.83 REMARK 500 ARG A 319 53.70 39.75 REMARK 500 GLU A 332 -5.63 66.87 REMARK 500 ASN A 340 -157.98 -96.59 REMARK 500 LEU A 348 -127.85 -109.93 REMARK 500 LEU A 351 -133.36 -126.60 REMARK 500 PRO A 404 14.69 -68.55 REMARK 500 SER A 419 13.60 -65.31 REMARK 500 LYS A 421 78.22 -169.65 REMARK 500 ARG B 30 -111.74 45.78 REMARK 500 THR B 69 -38.95 -137.65 REMARK 500 ALA B 84 -176.99 -171.33 REMARK 500 ASP B 94 98.23 84.76 REMARK 500 TYR D 107 -14.64 86.60 REMARK 500 MET D 109 104.45 56.11 REMARK 500 ASN D 110 28.62 86.01 REMARK 500 SER E 145 -153.17 -166.72 REMARK 500 LYS E 147 -49.98 118.89 REMARK 500 SER E 174 27.90 45.27 REMARK 500 LYS E 232 -89.78 -85.47 REMARK 500 GLU E 234 -43.87 90.12 REMARK 500 PHE E 235 -94.48 -9.67 REMARK 500 LEU P 74 66.48 -118.87 REMARK 500 HIS P 116 -102.95 -85.52 REMARK 500 HIS P 139 -5.59 83.80 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 GLY A 244 ALA A 245 -35.37 REMARK 500 GLY B 93 ASP B 94 -148.73 REMARK 500 TYR D 107 GLY D 108 -37.24 REMARK 500 TRP D 121 GLY D 122 42.27 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 280 18.1 L L OUTSIDE RANGE REMARK 500 TYR D 107 21.3 L L OUTSIDE RANGE REMARK 500 ASN D 110 11.9 L L OUTSIDE RANGE REMARK 500 SER E 146 24.9 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A1423 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA A 330 O REMARK 620 2 THR A 335 OG1 91.7 REMARK 620 3 VAL A 333 O 78.6 80.6 REMARK 620 4 ASP A 360 OD2 169.2 78.3 95.7 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1423 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2W2N RELATED DB: PDB REMARK 900 WT PCSK9-DELTAC BOUND TO EGF-A H306Y REMARK 900 MUTANT OF LDLR REMARK 900 RELATED ID: 2W2P RELATED DB: PDB REMARK 900 PCSK9-DELTAC D374A MUTANT BOUND TO WT EGF REMARK 900 -A OF LDLR REMARK 900 RELATED ID: 2W2M RELATED DB: PDB REMARK 900 WT PCSK9-DELTAC BOUND TO WT EGF-A OF REMARK 900 LDLR REMARK 900 RELATED ID: 2W2O RELATED DB: PDB REMARK 900 PCSK9-DELTAC D374Y MUTANT BOUND TO WT EGF REMARK 900 -A OF LDLR REMARK 900 RELATED ID: 2W2Q RELATED DB: PDB REMARK 900 PCSK9-DELTAC D374H MUTANT BOUND TO WT EGF REMARK 900 -A OF LDLR REMARK 999 REMARK 999 SEQUENCE REMARK 999 LEUCINE PRESENT AT A417 IN ORIGINAL CONSTRUCT. POSSIBLE REMARK 999 NATURAL VARIANT