HEADER HYDROLASE/IMMUNE SYSTEM 05-JUL-11 3SQO
TITLE PCSK9 J16 FAB COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROPROTEIN CONVERTASE SUBTILISIN/KEXIN TYPE 9;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NEURAL APOPTOSIS-REGULATED CONVERTASE 1, NARC-1, PROPROTEIN
COMPND 5 CONVERTASE 9, PC9, SUBTILISIN/KEXIN-LIKE PROTEASE PC9;
COMPND 6 EC: 3.4.21.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: J16 HEAVY CHAIN;
COMPND 10 CHAIN: H;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: J16 LIGHT CHAIN;
COMPND 14 CHAIN: L;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: PCSK9 PRODOMAIN;
COMPND 18 CHAIN: P;
COMPND 19 SYNONYM: NEURAL APOPTOSIS-REGULATED CONVERTASE 1, NARC-1, PROPROTEIN
COMPND 20 CONVERTASE 9, PC9, SUBTILISIN/KEXIN-LIKE PROTEASE PC9;
COMPND 21 EC: 3.4.21.-;
COMPND 22 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PCSK9, NARC1, PSEC0052;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: HEK293;
SOURCE 16 MOL_ID: 3;
SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 18 ORGANISM_COMMON: HUMAN;
SOURCE 19 ORGANISM_TAXID: 9606;
SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 22 EXPRESSION_SYSTEM_CELL_LINE: HEK293;
SOURCE 23 MOL_ID: 4;
SOURCE 24 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 25 ORGANISM_COMMON: HUMAN;
SOURCE 26 ORGANISM_TAXID: 9606;
SOURCE 27 GENE: PCSK9, NARC1, PSEC0052;
SOURCE 28 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 29 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 30 EXPRESSION_SYSTEM_CELL_LINE: HEK293
KEYWDS CHOLESTEROL REGULATION, LDLR, HYDROLASE-IMMUNE SYSTEM COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.STROP
REVDAT 1 16-MAY-12 3SQO 0
JRNL AUTH H.LIANG,J.CHAPARRO-RIGGERS,P.STROP,T.GENG,J.E.SUTTON,D.TSAI,
JRNL AUTH 2 L.BAI,Y.ABDICHE,J.DILLEY,J.YU,S.WU,S.M.CHIN,N.A.LEE,A.ROSSI,
JRNL AUTH 3 J.C.LIN,A.RAJPAL,J.PONS,D.L.SHELTON
JRNL TITL PROPROTEIN CONVERTASE SUBSTILISIN/KEXIN TYPE 9 ANTAGONISM
JRNL TITL 2 REDUCES LOW-DENSITY LIPOPROTEIN CHOLESTEROL IN
JRNL TITL 3 STATIN-TREATED HYPERCHOLESTEROLEMIC NONHUMAN PRIMATES.
JRNL REF J.PHARMACOL.EXP.THER. V. 340 228 2012
JRNL REFN ISSN 0022-3565
JRNL PMID 22019884
JRNL DOI 10.1124/JPET.111.187419
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 <I/SIGMA(I)> 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 <I/SIGMA(I)> 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
DBREF 3SQO A 153 692 UNP Q8NBP7 PCSK9_HUMAN 153 692
DBREF 3SQO P 31 152 UNP Q8NBP7 PCSK9_HUMAN 31 152
DBREF 3SQO H 1 218 PDB 3SQO 3SQO 1 218
DBREF 3SQO L 1 214 PDB 3SQO 3SQO 1 214
SEQADV 3SQO ILE A 474 UNP Q8NBP7 VAL 474 CONFLICT
SEQADV 3SQO GLU A 670 UNP Q8NBP7 GLY 670 CONFLICT
SEQRES 1 A 540 SER ILE PRO TRP ASN LEU GLU ARG ILE THR PRO PRO ARG
SEQRES 2 A 540 TYR ARG ALA ASP GLU TYR GLN PRO PRO ASP GLY GLY SER
SEQRES 3 A 540 LEU VAL GLU VAL TYR LEU LEU ASP THR SER ILE GLN SER
SEQRES 4 A 540 ASP HIS ARG GLU ILE GLU GLY ARG VAL MET VAL THR ASP
SEQRES 5 A 540 PHE GLU ASN VAL PRO GLU GLU ASP GLY THR ARG PHE HIS
SEQRES 6 A 540 ARG GLN ALA SER LYS CYS ASP SER HIS GLY THR HIS LEU
SEQRES 7 A 540 ALA GLY VAL VAL SER GLY ARG ASP ALA GLY VAL ALA LYS
SEQRES 8 A 540 GLY ALA SER MET ARG SER LEU ARG VAL LEU ASN CYS GLN
SEQRES 9 A 540 GLY LYS GLY THR VAL SER GLY THR LEU ILE GLY LEU GLU
SEQRES 10 A 540 PHE ILE ARG LYS SER GLN LEU VAL GLN PRO VAL GLY PRO
SEQRES 11 A 540 LEU VAL VAL LEU LEU PRO LEU ALA GLY GLY TYR SER ARG
SEQRES 12 A 540 VAL LEU ASN ALA ALA CYS GLN ARG LEU ALA ARG ALA GLY
SEQRES 13 A 540 VAL VAL LEU VAL THR ALA ALA GLY ASN PHE ARG ASP ASP
SEQRES 14 A 540 ALA CYS LEU TYR SER PRO ALA SER ALA PRO GLU VAL ILE
SEQRES 15 A 540 THR VAL GLY ALA THR ASN ALA GLN ASP GLN PRO VAL THR
SEQRES 16 A 540 LEU GLY THR LEU GLY THR ASN PHE GLY ARG CYS VAL ASP
SEQRES 17 A 540 LEU PHE ALA PRO GLY GLU ASP ILE ILE GLY ALA SER SER
SEQRES 18 A 540 ASP CYS SER THR CYS PHE VAL SER GLN SER GLY THR SER
SEQRES 19 A 540 GLN ALA ALA ALA HIS VAL ALA GLY ILE ALA ALA MET MET
SEQRES 20 A 540 LEU SER ALA GLU PRO GLU LEU THR LEU ALA GLU LEU ARG
SEQRES 21 A 540 GLN ARG LEU ILE HIS PHE SER ALA LYS ASP VAL ILE ASN
SEQRES 22 A 540 GLU ALA TRP PHE PRO GLU ASP GLN ARG VAL LEU THR PRO
SEQRES 23 A 540 ASN LEU VAL ALA ALA LEU PRO PRO SER THR HIS GLY ALA
SEQRES 24 A 540 GLY TRP GLN LEU PHE CYS ARG THR VAL TRP SER ALA HIS
SEQRES 25 A 540 SER GLY PRO THR ARG MET ALA THR ALA ILE ALA ARG CYS
SEQRES 26 A 540 ALA PRO ASP GLU GLU LEU LEU SER CYS SER SER PHE SER
SEQRES 27 A 540 ARG SER GLY LYS ARG ARG GLY GLU ARG MET GLU ALA GLN
SEQRES 28 A 540 GLY GLY LYS LEU VAL CYS ARG ALA HIS ASN ALA PHE GLY
SEQRES 29 A 540 GLY GLU GLY VAL TYR ALA ILE ALA ARG CYS CYS LEU LEU
SEQRES 30 A 540 PRO GLN ALA ASN CYS SER VAL HIS THR ALA PRO PRO ALA
SEQRES 31 A 540 GLU ALA SER MET GLY THR ARG VAL HIS CYS HIS GLN GLN
SEQRES 32 A 540 GLY HIS VAL LEU THR GLY CYS SER SER HIS TRP GLU VAL
SEQRES 33 A 540 GLU ASP LEU GLY THR HIS LYS PRO PRO VAL LEU ARG PRO
SEQRES 34 A 540 ARG GLY GLN PRO ASN GLN CYS VAL GLY HIS ARG GLU ALA
SEQRES 35 A 540 SER ILE HIS ALA SER CYS CYS HIS ALA PRO GLY LEU GLU
SEQRES 36 A 540 CYS LYS VAL LYS GLU HIS GLY ILE PRO ALA PRO GLN GLU
SEQRES 37 A 540 GLN VAL THR VAL ALA CYS GLU GLU GLY TRP THR LEU THR
SEQRES 38 A 540 GLY CYS SER ALA LEU PRO GLY THR SER HIS VAL LEU GLY
SEQRES 39 A 540 ALA TYR ALA VAL ASP ASN THR CYS VAL VAL ARG SER ARG
SEQRES 40 A 540 ASP VAL SER THR THR GLY SER THR SER GLU GLU ALA VAL
SEQRES 41 A 540 THR ALA VAL ALA ILE CYS CYS ARG SER ARG HIS LEU ALA
SEQRES 42 A 540 GLN ALA SER GLN GLU LEU GLN
SEQRES 1 H 219 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 H 219 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY
SEQRES 3 H 219 TYR THR PHE THR SER TYR TYR MET HIS TRP VAL ARG GLN
SEQRES 4 H 219 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLU ILE SER
SEQRES 5 H 219 PRO PHE GLY GLY ARG THR ASN TYR ASN GLU LYS PHE LYS
SEQRES 6 H 219 SER ARG VAL THR MET THR ARG ASP THR SER THR SER THR
SEQRES 7 H 219 VAL TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR
SEQRES 8 H 219 ALA VAL TYR TYR CYS ALA ARG GLU ARG PRO LEU TYR ALA
SEQRES 9 H 219 SER ASP LEU TRP GLY GLN GLY THR THR VAL THR VAL SER
SEQRES 10 H 219 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA
SEQRES 11 H 219 PRO SER SER ARG SER THR SER GLU SER THR ALA ALA LEU
SEQRES 12 H 219 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR
SEQRES 13 H 219 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS
SEQRES 14 H 219 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER
SEQRES 15 H 219 LEU SER SER VAL VAL THR VAL PRO SER SER ASN PHE GLY
SEQRES 16 H 219 THR GLN THR TYR THR CYS ASN VAL ASP HIS LYS PRO SER
SEQRES 17 H 219 ASN THR LYS VAL ASP LYS THR VAL GLU ARG LYS
SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA
SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER
SEQRES 3 L 214 GLN GLY ILE SER SER ALA LEU ALA TRP TYR GLN GLN LYS
SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER
SEQRES 5 L 214 TYR ARG TYR THR GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER LEU
SEQRES 7 L 214 GLN PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN ARG
SEQRES 8 L 214 TYR SER LEU TRP ARG THR PHE GLY GLN GLY THR LYS LEU
SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU
SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 L 214 PHE ASN ARG GLY GLU SER
SEQRES 1 P 122 GLN GLU ASP GLU ASP GLY ASP TYR GLU GLU LEU VAL LEU
SEQRES 2 P 122 ALA LEU ARG SER GLU GLU ASP GLY LEU ALA GLU ALA PRO
SEQRES 3 P 122 GLU HIS GLY THR THR ALA THR PHE HIS ARG CYS ALA LYS
SEQRES 4 P 122 ASP PRO TRP ARG LEU PRO GLY THR TYR VAL VAL VAL LEU
SEQRES 5 P 122 LYS GLU GLU THR HIS LEU SER GLN SER GLU ARG THR ALA
SEQRES 6 P 122 ARG ARG LEU GLN ALA GLN ALA ALA ARG ARG GLY TYR LEU
SEQRES 7 P 122 THR LYS ILE LEU HIS VAL PHE HIS GLY LEU LEU PRO GLY
SEQRES 8 P 122 PHE LEU VAL LYS MET SER GLY ASP LEU LEU GLU LEU ALA
SEQRES 9 P 122 LEU LYS LEU PRO HIS VAL ASP TYR ILE GLU GLU ASP SER
SEQRES 10 P 122 SER VAL PHE ALA GLN
FORMUL 5 HOH *32(H2 O)
HELIX 1 1 PRO A 155 THR A 162 1 8
HELIX 2 2 GLN A 219 GLY A 236 1 18
HELIX 3 3 VAL A 261 GLN A 278 1 18
HELIX 4 4 SER A 294 GLY A 308 1 15
HELIX 5 5 ASP A 321 CYS A 323 5 3
HELIX 6 6 GLY A 384 GLU A 403 1 20
HELIX 7 7 THR A 407 PHE A 418 1 12
HELIX 8 8 ASN A 425 PHE A 429 5 5
HELIX 9 9 PRO A 430 ARG A 434 5 5
HELIX 10 10 THR H 28 TYR H 32 5 5
HELIX 11 11 PRO H 52A GLY H 55 5 4
HELIX 12 12 ARG H 83 THR H 87 5 5
HELIX 13 13 GLN L 79 ILE L 83 5 5
HELIX 14 14 SER L 121 SER L 127 1 7
HELIX 15 15 LYS L 183 LYS L 188 1 6
HELIX 16 16 LYS P 69 PRO P 71 5 3
HELIX 17 17 HIS P 87 ARG P 104 1 18
HELIX 18 18 SER P 127 ASP P 129 5 3
HELIX 19 19 LEU P 130 LEU P 135 1 6
SHEET 1 A 7 VAL A 200 GLU A 206 0
SHEET 2 A 7 SER A 246 ARG A 251 1 O MET A 247 N MET A 201
SHEET 3 A 7 GLU A 181 ASP A 186 1 N LEU A 184 O ARG A 248
SHEET 4 A 7 LEU A 283 LEU A 287 1 O VAL A 284 N TYR A 183
SHEET 5 A 7 VAL A 310 ALA A 314 1 O VAL A 312 N LEU A 287
SHEET 6 A 7 ILE A 334 THR A 339 1 O ILE A 334 N THR A 313
SHEET 7 A 7 LEU A 361 PRO A 364 1 O ALA A 363 N THR A 339
SHEET 1 B 3 LYS A 258 THR A 260 0
SHEET 2 B 3 VAL P 140 ALA P 151 -1 O VAL P 149 N GLY A 259
SHEET 3 B 3 THR P 63 HIS P 65 1 N HIS P 65 O ILE P 143
SHEET 1 C 6 TYR A 325 SER A 326 0
SHEET 2 C 6 LEU A 289 GLY A 292 -1 N GLY A 291 O SER A 326
SHEET 3 C 6 VAL P 140 ALA P 151 -1 O PHE P 150 N ALA A 290
SHEET 4 C 6 ARG P 73 LEU P 82 -1 N VAL P 79 O GLU P 144
SHEET 5 C 6 GLY P 121 LYS P 125 -1 O PHE P 122 N VAL P 80
SHEET 6 C 6 LYS P 110 PHE P 115 -1 N LYS P 110 O LYS P 125
SHEET 1 D 2 ILE A 368 ALA A 371 0
SHEET 2 D 2 PHE A 379 GLN A 382 -1 O GLN A 382 N ILE A 368
SHEET 1 E 2 ALA A 420 LYS A 421 0
SHEET 2 E 2 LEU A 440 VAL A 441 -1 O VAL A 441 N ALA A 420
SHEET 1 F 3 CYS A 457 TRP A 461 0
SHEET 2 F 3 TYR A 521 CYS A 527 -1 O ALA A 524 N VAL A 460
SHEET 3 F 3 GLU A 482 PHE A 489 -1 N GLU A 482 O CYS A 527
SHEET 1 G 3 ALA A 473 ALA A 475 0
SHEET 2 G 3 LEU A 507 ASN A 513 -1 O ALA A 511 N ALA A 473
SHEET 3 G 3 ARG A 495 ALA A 502 -1 N ARG A 499 O ARG A 510
SHEET 1 H 3 ALA A 532 ALA A 539 0
SHEET 2 H 3 SER A 595 HIS A 602 -1 O ALA A 598 N HIS A 537
SHEET 3 H 3 HIS A 557 HIS A 565 -1 N HIS A 565 O SER A 595
SHEET 1 I 2 THR A 548 HIS A 551 0
SHEET 2 I 2 GLN A 587 GLY A 590 -1 O CYS A 588 N VAL A 550
SHEET 1 J 3 GLU A 607 PRO A 616 0
SHEET 2 J 3 ALA A 671 ARG A 680 -1 O ALA A 676 N LYS A 611
SHEET 3 J 3 THR A 631 ALA A 637 -1 N SER A 636 O VAL A 675
SHEET 1 K 3 GLN A 621 ALA A 625 0
SHEET 2 K 3 THR A 653 SER A 658 -1 O CYS A 654 N VAL A 624
SHEET 3 K 3 VAL A 644 VAL A 650 -1 N TYR A 648 O VAL A 655
SHEET 1 L 2 GLN H 3 GLN H 6 0
SHEET 2 L 2 CYS H 22 SER H 25 -1 O LYS H 23 N VAL H 5
SHEET 1 M 6 GLU H 10 LYS H 12 0
SHEET 2 M 6 THR H 107 VAL H 111 1 O THR H 110 N LYS H 12
SHEET 3 M 6 ALA H 88 GLU H 95 -1 N ALA H 88 O VAL H 109
SHEET 4 M 6 TYR H 33 ALA H 40 -1 N HIS H 35 O ALA H 93
SHEET 5 M 6 GLY H 44 ILE H 51 -1 O GLU H 46 N ARG H 38
SHEET 6 M 6 THR H 57 TYR H 59 -1 O ASN H 58 N GLU H 50
SHEET 1 N 4 GLU H 10 LYS H 12 0
SHEET 2 N 4 THR H 107 VAL H 111 1 O THR H 110 N LYS H 12
SHEET 3 N 4 ALA H 88 GLU H 95 -1 N ALA H 88 O VAL H 109
SHEET 4 N 4 LEU H 102 TRP H 103 -1 O LEU H 102 N ARG H 94
SHEET 1 O 3 VAL H 18 VAL H 20 0
SHEET 2 O 3 THR H 77 LEU H 82 -1 O MET H 80 N VAL H 20
SHEET 3 O 3 THR H 68 ASP H 72 -1 N THR H 70 O TYR H 79
SHEET 1 P 4 SER H 124 LEU H 128 0
SHEET 2 P 4 ALA H 141 TYR H 149 -1 O LEU H 145 N PHE H 126
SHEET 3 P 4 TYR H 180 THR H 187 -1 O SER H 184 N CYS H 144
SHEET 4 P 4 VAL H 167 THR H 169 -1 N HIS H 168 O VAL H 185
SHEET 1 Q 4 SER H 124 LEU H 128 0
SHEET 2 Q 4 ALA H 141 TYR H 149 -1 O LEU H 145 N PHE H 126
SHEET 3 Q 4 TYR H 180 THR H 187 -1 O SER H 184 N CYS H 144
SHEET 4 Q 4 VAL H 173 LEU H 174 -1 N VAL H 173 O SER H 181
SHEET 1 R 3 THR H 155 TRP H 158 0
SHEET 2 R 3 TYR H 198 HIS H 204 -1 O ASN H 201 N SER H 157
SHEET 3 R 3 THR H 209 VAL H 215 -1 O VAL H 215 N TYR H 198
SHEET 1 S 4 MET L 4 SER L 7 0
SHEET 2 S 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5
SHEET 3 S 4 ASP L 70 ILE L 75 -1 O PHE L 73 N ILE L 21
SHEET 4 S 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74
SHEET 1 T 6 SER L 10 SER L 14 0
SHEET 2 T 6 THR L 102 LYS L 107 1 O LYS L 107 N ALA L 13
SHEET 3 T 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102
SHEET 4 T 6 LEU L 33 GLN L 38 -1 N ALA L 34 O GLN L 89
SHEET 5 T 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37
SHEET 6 T 6 TYR L 53 ARG L 54 -1 O TYR L 53 N TYR L 49
SHEET 1 U 4 SER L 10 SER L 14 0
SHEET 2 U 4 THR L 102 LYS L 107 1 O LYS L 107 N ALA L 13
SHEET 3 U 4 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102
SHEET 4 U 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90
SHEET 1 V 4 SER L 114 PHE L 118 0
SHEET 2 V 4 THR L 129 PHE L 139 -1 O VAL L 133 N PHE L 118
SHEET 3 V 4 TYR L 173 SER L 182 -1 O LEU L 181 N ALA L 130
SHEET 4 V 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176
SHEET 1 W 4 ALA L 153 LEU L 154 0
SHEET 2 W 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153
SHEET 3 W 4 VAL L 191 THR L 197 -1 O ALA L 193 N LYS L 149
SHEET 4 W 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196
SSBOND 1 CYS A 223 CYS A 255 1555 1555 2.05
SSBOND 2 CYS A 323 CYS A 358 1555 1555 2.10
SSBOND 3 CYS A 375 CYS A 378 1555 1555 2.06
SSBOND 4 CYS A 457 CYS A 527 1555 1555 2.04
SSBOND 5 CYS A 477 CYS A 526 1555 1555 2.05
SSBOND 6 CYS A 486 CYS A 509 1555 1555 2.06
SSBOND 7 CYS A 534 CYS A 601 1555 1555 1.85
SSBOND 8 CYS A 552 CYS A 600 1555 1555 2.03
SSBOND 9 CYS A 562 CYS A 588 1555 1555 2.03
SSBOND 10 CYS A 608 CYS A 679 1555 1555 2.06
SSBOND 11 CYS A 626 CYS A 678 1555 1555 2.06
SSBOND 12 CYS A 635 CYS A 654 1555 1555 2.04
SSBOND 13 CYS H 22 CYS H 92 1555 1555 2.05
SSBOND 14 CYS H 144 CYS H 200 1555 1555 2.05
SSBOND 15 CYS L 23 CYS L 88 1555 1555 2.08
SSBOND 16 CYS L 134 CYS L 194 1555 1555 2.05
CISPEP 1 SER A 326 PRO A 327 0 1.30
CISPEP 2 PHE H 150 PRO H 151 0 2.59
CISPEP 3 GLU H 152 PRO H 153 0 -1.13
CISPEP 4 SER L 7 PRO L 8 0 -4.04
CISPEP 5 TYR L 140 PRO L 141 0 2.65
CRYST1 81.921 70.981 109.156 90.00 95.90 90.00 P 1 21 1 2
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012207 0.000000 0.001261 0.00000
SCALE2 0.000000 0.014088 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009210 0.00000
(ATOM LINES ARE NOT SHOWN.)
END