HEADER HYDROLASE/RECEPTOR 03-NOV-08 2W2O
TITLE PCSK9-DELTAC D374Y MUTANT BOUND TO WT EGF-A OF LDLR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROPROTEIN CONVERTASE SUBTILISIN/KEXIN TYPE 9;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 153-451;
COMPND 5 SYNONYM: PCSK9, PROPROTEIN CONVERTASE PC9, SUBTILISIN/KEXIN-LIKE
COMPND 6 PROTEASE PC9, NEURAL APOPTOSIS-REGULATED CONVERTASE 1, NARC-1;
COMPND 7 EC: 3.4.21.-;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: LOW-DENSITY LIPOPROTEIN RECEPTOR;
COMPND 12 CHAIN: E;
COMPND 13 FRAGMENT: EGF-A DOMAIN, RESIDUES 314-393;
COMPND 14 SYNONYM: LDL RECEPTOR;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 3;
COMPND 17 MOLECULE: PROPROTEIN CONVERTASE SUBTILISIN/KEXIN TYPE 9;
COMPND 18 CHAIN: P;
COMPND 19 FRAGMENT: PROPEPTIDE, RESIDUES 53-152;
COMPND 20 SYNONYM: PCSK9, PROPROTEIN CONVERTASE PC9, SUBTILISIN/KEXIN-LIKE
COMPND 21 PROTEASE PC9, NEURAL APOPTOSIS-REGULATED CONVERTASE 1, NARC-1;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PETM-10;
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: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PETM-11;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 19 ORGANISM_COMMON: HUMAN;
SOURCE 20 ORGANISM_TAXID: 9606;
SOURCE 21 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 22 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 23 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 24 EXPRESSION_SYSTEM_PLASMID: PETM-10
KEYWDS HYDROLASE-RECEPTOR COMPLEX, PCSK9, LDLR, PROPROTEIN CONVERTASE, LOW-
KEYWDS 2 DENSITY LIPOPROTEIN RECEPTOR, EGF, CARDIOVASCULAR DISEASE, FAMILIAL
KEYWDS 3 HYPERCHOLESTEROLEMIA, LIPID METABOLISM, SERINE PROTEASE, HYDROLASE,
KEYWDS 4 LIPID TRANSPORT, STEROID METABOLISM, RECEPTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR M.J.BOTTOMLEY,A.CIRILLO,L.ORSATTI,L.RUGGERI,T.S.FISHER,J.C.SANTORO,
AUTHOR 2 R.T.CUMMINGS,R.M.CUBBON,P.LO SURDO,A.CALZETTA,A.NOTO,J.BAYSAROWICH,
AUTHOR 3 M.MATTU,F.TALAMO,R.DE FRANCESCO,C.P.SPARROW,A.SITLANI,A.CARFI
REVDAT 6 13-DEC-23 2W2O 1 LINK
REVDAT 5 13-JUL-11 2W2O 1 VERSN
REVDAT 4 27-OCT-09 2W2O 1 REMARK
REVDAT 3 13-JAN-09 2W2O 1 JRNL
REVDAT 2 23-DEC-08 2W2O 1 VERSN JRNL
REVDAT 1 18-NOV-08 2W2O 0
JRNL AUTH M.J.BOTTOMLEY,A.CIRILLO,L.ORSATTI,L.RUGGERI,T.S.FISHER,
JRNL AUTH 2 J.C.SANTORO,R.T.CUMMINGS,R.M.CUBBON,P.LO SURDO,A.CALZETTA,
JRNL AUTH 3 A.NOTO,J.BAYSAROWICH,M.MATTU,F.TALAMO,R.DE FRANCESCO,
JRNL AUTH 4 C.P.SPARROW,A.SITLANI,A.CARFI
JRNL TITL STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF THE WILD TYPE
JRNL TITL 2 PCSK9/EGF-AB COMPLEX AND NATURAL FH MUTANTS.
JRNL REF J.BIOL.CHEM. V. 284 1313 2009
JRNL REFN ISSN 0021-9258
JRNL PMID 19001363
JRNL DOI 10.1074/JBC.M808363200
REMARK 2
REMARK 2 RESOLUTION. 2.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 23984
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) : 0.228
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1287
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) : 2.62
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1741
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3720
REMARK 3 BIN FREE R VALUE SET COUNT : 92
REMARK 3 BIN FREE R VALUE : 0.3730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3125
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 19
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.13000
REMARK 3 B22 (A**2) : 4.13000
REMARK 3 B33 (A**2) : -8.25000
REMARK 3 B12 (A**2) : 0.00000
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): 0.320
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.256
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.244
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.361
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.895
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3212 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4369 ; 1.238 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 414 ; 5.969 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 137 ;35.504 ;23.723
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 518 ;18.119 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;21.141 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 506 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2428 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1413 ; 0.202 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2158 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 110 ; 0.109 ; 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 ; 0.200 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.179 ; 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): 2107 ; 0.401 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3313 ; 0.734 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1215 ; 0.892 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1054 ; 1.492 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 3
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 446
REMARK 3 ORIGIN FOR THE GROUP (A): -15.9634 -3.1974 30.0060
REMARK 3 T TENSOR
REMARK 3 T11: 0.0176 T22: 0.5248
REMARK 3 T33: 0.1424 T12: -0.1374
REMARK 3 T13: -0.0536 T23: 0.1182
REMARK 3 L TENSOR
REMARK 3 L11: 1.8564 L22: 2.4408
REMARK 3 L33: 6.4553 L12: -0.4178
REMARK 3 L13: -0.3211 L23: -1.8262
REMARK 3 S TENSOR
REMARK 3 S11: 0.0664 S12: -0.0575 S13: 0.0374
REMARK 3 S21: 0.2475 S22: -0.3446 S23: -0.0690
REMARK 3 S31: -0.5782 S32: 0.9384 S33: 0.2783
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 : E 285 E 332
REMARK 3 ORIGIN FOR THE GROUP (A): -0.1491 -15.2142 9.5934
REMARK 3 T TENSOR
REMARK 3 T11: -0.1936 T22: 0.9449
REMARK 3 T33: 0.1428 T12: 0.1375
REMARK 3 T13: -0.0258 T23: 0.1733
REMARK 3 L TENSOR
REMARK 3 L11: 6.3963 L22: 4.5218
REMARK 3 L33: 6.9332 L12: -0.1454
REMARK 3 L13: -5.7404 L23: 0.0711
REMARK 3 S TENSOR
REMARK 3 S11: -0.4772 S12: -0.2810 S13: -0.5934
REMARK 3 S21: 0.1560 S22: 0.2488 S23: 0.1184
REMARK 3 S31: -0.0153 S32: -0.1151 S33: 0.2284
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 60 P 152
REMARK 3 ORIGIN FOR THE GROUP (A): -30.2104 -15.3918 52.3589
REMARK 3 T TENSOR
REMARK 3 T11: 0.0980 T22: 0.3207
REMARK 3 T33: 0.1544 T12: -0.0276
REMARK 3 T13: 0.0113 T23: 0.0535
REMARK 3 L TENSOR
REMARK 3 L11: 2.5660 L22: 2.4724
REMARK 3 L33: 9.3209 L12: 0.4558
REMARK 3 L13: -2.4288 L23: -2.0577
REMARK 3 S TENSOR
REMARK 3 S11: -0.0106 S12: -0.0027 S13: -0.0033
REMARK 3 S21: 0.4345 S22: -0.1193 S23: 0.1445
REMARK 3 S31: -0.3374 S32: 0.5156 S33: 0.1299
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.
REMARK 4
REMARK 4 2W2O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-NOV-08.
REMARK 100 THE DEPOSITION ID IS D_1290037852.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.072
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25321
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.620
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.62
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.70000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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 2QTW
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.5, 10% (W/V) PEG 8000
REMARK 280 AND 8% (V/V) ETHYLENE GLYCOL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 109.16450
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 42.97400
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 42.97400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 163.74675
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 42.97400
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 42.97400
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 54.58225
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 42.97400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.97400
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 163.74675
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 42.97400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.97400
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 54.58225
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 109.16450
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, 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 ENGINEERED RESIDUE IN CHAIN A, ASP 374 TO TYR
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 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 GLN A 219
REMARK 465 ALA A 220
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 MET E 266
REMARK 465 LYS E 267
REMARK 465 HIS E 268
REMARK 465 HIS E 269
REMARK 465 HIS E 270
REMARK 465 HIS E 271
REMARK 465 HIS E 272
REMARK 465 HIS E 273
REMARK 465 PRO E 274
REMARK 465 MET E 275
REMARK 465 SER E 276
REMARK 465 ASP E 277
REMARK 465 TYR E 278
REMARK 465 ASP E 279
REMARK 465 ILE E 280
REMARK 465 PRO E 281
REMARK 465 THR E 282
REMARK 465 THR E 283
REMARK 465 GLU E 284
REMARK 465 ASN E 285
REMARK 465 ASP E 333
REMARK 465 ILE E 334
REMARK 465 ASP E 335
REMARK 465 GLU E 336
REMARK 465 CYS E 337
REMARK 465 GLN E 338
REMARK 465 ASP E 339
REMARK 465 PRO E 340
REMARK 465 ASP E 341
REMARK 465 THR E 342
REMARK 465 CYS E 343
REMARK 465 SER E 344
REMARK 465 GLN E 345
REMARK 465 LEU E 346
REMARK 465 CYS E 347
REMARK 465 VAL E 348
REMARK 465 ASN E 349
REMARK 465 LEU E 350
REMARK 465 GLU E 351
REMARK 465 GLY E 352
REMARK 465 GLY E 353
REMARK 465 TYR E 354
REMARK 465 LYS E 355
REMARK 465 CYS E 356
REMARK 465 GLN E 357
REMARK 465 CYS E 358
REMARK 465 GLU E 359
REMARK 465 GLU E 360
REMARK 465 GLY E 361
REMARK 465 PHE E 362
REMARK 465 GLN E 363
REMARK 465 LEU E 364
REMARK 465 ASP E 365
REMARK 465 PRO E 366
REMARK 465 HIS E 367
REMARK 465 THR E 368
REMARK 465 LYS E 369
REMARK 465 ALA E 370
REMARK 465 CYS E 371
REMARK 465 LYS E 372
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 ARG A 165 CG CD NE CZ NH1 NH2
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 PRO A 331 C - N - CD ANGL. DEV. = -17.6 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 ASP A 186 -153.34 -164.38
REMARK 500 GLU A 197 109.28 -39.58
REMARK 500 VAL A 241 -72.21 -68.03
REMARK 500 ALA A 245 112.75 72.93
REMARK 500 ASN A 254 -158.36 -81.58
REMARK 500 GLN A 278 67.76 -116.87
REMARK 500 PRO A 288 58.97 -91.76
REMARK 500 ASN A 317 40.91 -109.86
REMARK 500 GLU A 332 -21.33 85.37
REMARK 500 LEU A 351 -155.94 -101.58
REMARK 500 ASP A 432 -37.46 -34.24
REMARK 500 PHE E 288 -92.59 -108.85
REMARK 500 LEU E 298 6.42 -56.23
REMARK 500 ASN E 300 48.76 27.34
REMARK 500 HIS E 306 -71.76 -120.72
REMARK 500 PRO E 320 -151.05 -79.98
REMARK 500 ARG E 329 -50.88 -137.74
REMARK 500 GLU P 85 54.50 -95.22
REMARK 500 HIS P 113 141.44 -172.62
REMARK 500 HIS P 139 -2.26 75.11
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 E1333 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR E 294 O
REMARK 620 2 GLU E 296 OE1 69.8
REMARK 620 3 ASP E 310 OD2 78.1 93.9
REMARK 620 4 LEU E 311 O 141.2 147.8 87.0
REMARK 620 5 GLY E 314 O 144.1 74.5 102.0 73.8
REMARK 620 N 1 2 3 4
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E1333
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1F5Y RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF A CONCATEMER OF THE FIRST AND SECOND LIGAND-
REMARK 900 BINDING MODULES OF THE HUMAN LDL RECEPTOR
REMARK 900 RELATED ID: 1HJ7 RELATED DB: PDB
REMARK 900 NMR STUDY OF A PAIR OF LDL RECEPTOR CA ==2+== BINDING EPIDERMAL
REMARK 900 GROWTH FACTOR-LIKE DOMAINS, 20 STRUCTURES
REMARK 900 RELATED ID: 1N7D RELATED DB: PDB
REMARK 900 EXTRACELLULAR DOMAIN OF THE LDL RECEPTOR
REMARK 900 RELATED ID: 2FCW RELATED DB: PDB
REMARK 900 STRUCTURE OF A COMPLEX BETWEEN THE PAIR OF THE LDL RECEPTORLIGAND-
REMARK 900 BINDING MODULES 3-4 AND THE RECEPTOR ASSOCIATEDPROTEIN (RAP).
REMARK 900 RELATED ID: 1I0U RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF A CONCATEMER OFEGF-
REMARK 900 HOMOLOGY MODULES OF THE HUMAN LOW DENSITY LIPOPROTEINRECEPTOR
REMARK 900 RELATED ID: 1D2J RELATED DB: PDB
REMARK 900 LDL RECEPTOR LIGAND-BINDING MODULE 6
REMARK 900 RELATED ID: 1LRX RELATED DB: PDB
REMARK 900 THEORETIC MODEL OF THE HUMAN LOW-DENSITY LIPOPROTEINRECEPTOR YWTD
REMARK 900 BETA-PROPELLER DOMAIN
REMARK 900 RELATED ID: 1HZ8 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF A CONCATEMER OFEGF-
REMARK 900 HOMOLOGY MODULES OF THE HUMAN LOW DENSITY LIPOPROTEINRECEPTOR
REMARK 900 RELATED ID: 1F8Z RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE SIXTH LIGAND-BINDING MODULE OF THE LDLRECEPTOR
REMARK 900 RELATED ID: 1XFE RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE LA7-EGFA PAIR FROM THE LDLRECEPTOR
REMARK 900 RELATED ID: 1AJJ RELATED DB: PDB
REMARK 900 LDL RECEPTOR LIGAND-BINDING MODULE 5, CALCIUM-COORDINATING
REMARK 900 RELATED ID: 1LDL RELATED DB: PDB
REMARK 900 RELATED ID: 1LDR RELATED DB: PDB
REMARK 900 SECOND REPEAT OF THE LDL RECEPTOR LIGAND- BINDING DOMAIN
REMARK 900 RELATED ID: 1IJQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LDL RECEPTOR YWTD- EGF DOMAIN PAIR
REMARK 900 RELATED ID: 2W2M RELATED DB: PDB
REMARK 900 WT PCSK9-DELTAC BOUND TO WT EGF-A OF LDLR
REMARK 900 RELATED ID: 2W2N RELATED DB: PDB
REMARK 900 WT PCSK9-DELTAC BOUND TO EGF-A H306Y MUTANT OF LDLR
REMARK 900 RELATED ID: 2W2P RELATED DB: PDB
REMARK 900 PCSK9-DELTAC D374A MUTANT BOUND TO WT EGF -A OF LDLR
REMARK 900 RELATED ID: 2W2Q RELATED DB: PDB
REMARK 900 PCSK9-DELTAC D374H MUTANT BOUND TO WT EGF -A OF LDLR
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 HUMAN PCSK9 PRODOMAIN. THE FIRST 14 RESIDUES IN THE
REMARK 999 SEQUENCE ARE A RESULT OF THE CLONING PROCEDURE. THE 15TH
REMARK 999 RESIDUE CORRESPONDS TO ALA53 OF WT PCSK9.
REMARK 999 HUMAN PCSK9 CATALYTIC DOMAIN. THE LAST 13 RESIDUES ARE A
REMARK 999 LINKER AND A 6HIS TAG, RESULTING FROM THE CLONING
REMARK 999 PROCEDURE. THE FIRST RESIDUE CORRESPONDS TO SER153 OF WT
REMARK 999 PCSK9.
REMARK 999 HUMAN LDLR EGF-AB DOMAINS. THE FIRST 27 RESIDUES IN THE
REMARK 999 SEQUENCE ARE A 6HIS TAG AND A LINKER FROM THE CLONING
REMARK 999 PROCEDURE. THE 28TH RESIDUE CORRESPONDS TO GLY293 OF WT
REMARK 999 LDLR.
DBREF 2W2O P 39 52 PDB 2W2O 2W2O 39 52
DBREF 2W2O P 53 152 UNP Q8NBP7 PCSK9_HUMAN 53 152
DBREF 2W2O A 153 451 UNP Q8NBP7 PCSK9_HUMAN 153 451
DBREF 2W2O A 452 464 PDB 2W2O 2W2O 452 464
DBREF 2W2O E 266 292 PDB 2W2O 2W2O 266 292
DBREF 2W2O E 293 372 UNP P01130 LDLR_HUMAN 314 393
SEQADV 2W2O TYR A 374 UNP Q8NBP7 ASP 374 ENGINEERED MUTATION
SEQRES 1 A 312 SER ILE PRO TRP ASN LEU GLU ARG ILE THR PRO PRO ARG
SEQRES 2 A 312 TYR ARG ALA ASP GLU TYR GLN PRO PRO ASP GLY GLY SER
SEQRES 3 A 312 LEU VAL GLU VAL TYR LEU LEU ASP THR SER ILE GLN SER
SEQRES 4 A 312 ASP HIS ARG GLU ILE GLU GLY ARG VAL MET VAL THR ASP
SEQRES 5 A 312 PHE GLU ASN VAL PRO GLU GLU ASP GLY THR ARG PHE HIS
SEQRES 6 A 312 ARG GLN ALA SER LYS CYS ASP SER HIS GLY THR HIS LEU
SEQRES 7 A 312 ALA GLY VAL VAL SER GLY ARG ASP ALA GLY VAL ALA LYS
SEQRES 8 A 312 GLY ALA SER MET ARG SER LEU ARG VAL LEU ASN CYS GLN
SEQRES 9 A 312 GLY LYS GLY THR VAL SER GLY THR LEU ILE GLY LEU GLU
SEQRES 10 A 312 PHE ILE ARG LYS SER GLN LEU VAL GLN PRO VAL GLY PRO
SEQRES 11 A 312 LEU VAL VAL LEU LEU PRO LEU ALA GLY GLY TYR SER ARG
SEQRES 12 A 312 VAL LEU ASN ALA ALA CYS GLN ARG LEU ALA ARG ALA GLY
SEQRES 13 A 312 VAL VAL LEU VAL THR ALA ALA GLY ASN PHE ARG ASP ASP
SEQRES 14 A 312 ALA CYS LEU TYR SER PRO ALA SER ALA PRO GLU VAL ILE
SEQRES 15 A 312 THR VAL GLY ALA THR ASN ALA GLN ASP GLN PRO VAL THR
SEQRES 16 A 312 LEU GLY THR LEU GLY THR ASN PHE GLY ARG CYS VAL ASP
SEQRES 17 A 312 LEU PHE ALA PRO GLY GLU ASP ILE ILE GLY ALA SER SER
SEQRES 18 A 312 TYR CYS SER THR CYS PHE VAL SER GLN SER GLY THR SER
SEQRES 19 A 312 GLN ALA ALA ALA HIS VAL ALA GLY ILE ALA ALA MET MET
SEQRES 20 A 312 LEU SER ALA GLU PRO GLU LEU THR LEU ALA GLU LEU ARG
SEQRES 21 A 312 GLN ARG LEU ILE HIS PHE SER ALA LYS ASP VAL ILE ASN
SEQRES 22 A 312 GLU ALA TRP PHE PRO GLU ASP GLN ARG VAL LEU THR PRO
SEQRES 23 A 312 ASN LEU VAL ALA ALA LEU PRO PRO SER THR HIS GLY ALA
SEQRES 24 A 312 ALA GLY THR ALA ALA ALA SER HIS HIS HIS HIS HIS HIS
SEQRES 1 E 107 MET LYS HIS HIS HIS HIS HIS HIS PRO MET SER ASP TYR
SEQRES 2 E 107 ASP ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA
SEQRES 3 E 107 MET GLY THR ASN GLU CYS LEU ASP ASN ASN GLY GLY CYS
SEQRES 4 E 107 SER HIS VAL CYS ASN ASP LEU LYS ILE GLY TYR GLU CYS
SEQRES 5 E 107 LEU CYS PRO ASP GLY PHE GLN LEU VAL ALA GLN ARG ARG
SEQRES 6 E 107 CYS GLU ASP ILE ASP GLU CYS GLN ASP PRO ASP THR CYS
SEQRES 7 E 107 SER GLN LEU CYS VAL ASN LEU GLU GLY GLY TYR LYS CYS
SEQRES 8 E 107 GLN CYS GLU GLU GLY PHE GLN LEU ASP PRO HIS THR LYS
SEQRES 9 E 107 ALA CYS LYS
SEQRES 1 P 114 MET LYS GLY SER LYS GLY SER LYS GLY SER LYS PRO MET
SEQRES 2 P 114 SER ALA GLU ALA PRO GLU HIS GLY THR THR ALA THR PHE
SEQRES 3 P 114 HIS ARG CYS ALA LYS ASP PRO TRP ARG LEU PRO GLY THR
SEQRES 4 P 114 TYR VAL VAL VAL LEU LYS GLU GLU THR HIS LEU SER GLN
SEQRES 5 P 114 SER GLU ARG THR ALA ARG ARG LEU GLN ALA GLN ALA ALA
SEQRES 6 P 114 ARG ARG GLY TYR LEU THR LYS ILE LEU HIS VAL PHE HIS
SEQRES 7 P 114 GLY LEU LEU PRO GLY PHE LEU VAL LYS MET SER GLY ASP
SEQRES 8 P 114 LEU LEU GLU LEU ALA LEU LYS LEU PRO HIS VAL ASP TYR
SEQRES 9 P 114 ILE GLU GLU ASP SER SER VAL PHE ALA GLN
HET CA E1333 1
HETNAM CA CALCIUM ION
FORMUL 4 CA CA 2+
FORMUL 5 HOH *19(H2 O)
HELIX 1 1 PRO A 155 ILE A 161 1 7
HELIX 2 2 ASP A 224 GLY A 236 1 13
HELIX 3 3 VAL A 261 GLN A 278 1 18
HELIX 4 4 SER A 294 ALA A 307 1 14
HELIX 5 5 GLY A 384 GLU A 403 1 20
HELIX 6 6 THR A 407 SER A 419 1 13
HELIX 7 7 ASN A 425 PHE A 429 5 5
HELIX 8 8 PRO A 430 ARG A 434 5 5
HELIX 9 9 ASP E 299 CYS E 304 5 6
HELIX 10 10 LYS P 69 PRO P 71 5 3
HELIX 11 11 HIS P 87 ARG P 104 1 18
HELIX 12 12 SER P 127 ASP P 129 5 3
HELIX 13 13 LEU P 130 LYS P 136 1 7
SHEET 1 AA 7 VAL A 200 GLU A 206 0
SHEET 2 AA 7 SER A 246 ARG A 251 1 O MET A 247 N MET A 201
SHEET 3 AA 7 GLU A 181 ASP A 186 1 O VAL A 182 N ARG A 248
SHEET 4 AA 7 LEU A 283 LEU A 287 1 O VAL A 284 N TYR A 183
SHEET 5 AA 7 VAL A 310 ALA A 314 1 O VAL A 310 N VAL A 285
SHEET 6 AA 7 ILE A 334 THR A 339 1 O ILE A 334 N THR A 313
SHEET 7 AA 7 LEU A 361 PRO A 364 1 O LEU A 361 N GLY A 337
SHEET 1 AB 4 LYS A 258 THR A 260 0
SHEET 2 AB 4 VAL P 140 ALA P 151 -1 O VAL P 149 N GLY A 259
SHEET 3 AB 4 LEU A 289 GLY A 292 -1 O ALA A 290 N PHE P 150
SHEET 4 AB 4 TYR A 325 SER A 326 -1 O SER A 326 N GLY A 291
SHEET 1 AC 3 LYS A 258 THR A 260 0
SHEET 2 AC 3 VAL P 140 ALA P 151 -1 O VAL P 149 N GLY A 259
SHEET 3 AC 3 THR P 63 HIS P 65 1 O THR P 63 N ILE P 143
SHEET 1 AD 4 ILE A 368 ALA A 371 0
SHEET 2 AD 4 CYS A 378 GLN A 382 -1 O VAL A 380 N GLY A 370
SHEET 3 AD 4 VAL E 307 ASP E 310 -1 O CYS E 308 N PHE A 379
SHEET 4 AD 4 TYR E 315 LEU E 318 -1 O GLU E 316 N ASN E 309
SHEET 1 AE 2 ALA A 420 LYS A 421 0
SHEET 2 AE 2 LEU A 440 VAL A 441 -1 O VAL A 441 N ALA A 420
SHEET 1 EA 2 LEU E 325 VAL E 326 0
SHEET 2 EA 2 ARG E 330 CYS E 331 -1 O ARG E 330 N VAL E 326
SSBOND 1 CYS A 223 CYS A 255 1555 1555 2.06
SSBOND 2 CYS A 323 CYS A 358 1555 1555 2.07
SSBOND 3 CYS A 375 CYS A 378 1555 1555 2.04
SSBOND 4 CYS E 297 CYS E 308 1555 1555 2.05
SSBOND 5 CYS E 304 CYS E 317 1555 1555 2.05
SSBOND 6 CYS E 319 CYS E 331 1555 1555 2.04
LINK O THR E 294 CA CA E1333 1555 1555 2.35
LINK OE1 GLU E 296 CA CA E1333 1555 1555 2.49
LINK OD2 ASP E 310 CA CA E1333 1555 1555 2.38
LINK O LEU E 311 CA CA E1333 1555 1555 2.54
LINK O GLY E 314 CA CA E1333 1555 1555 2.50
CISPEP 1 PRO A 279 VAL A 280 0 -2.71
CISPEP 2 SER A 326 PRO A 327 0 -1.76
SITE 1 AC1 5 THR E 294 GLU E 296 ASP E 310 LEU E 311
SITE 2 AC1 5 GLY E 314
CRYST1 85.948 85.948 218.329 90.00 90.00 90.00 P 43 21 2 8
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 0.011635 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011635 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004580 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
