HEADER HYDROLASE/HYDROLASE INHIBITOR 18-JUN-14 4TRW
TITLE STRUCTURE OF BACE1 COMPLEX WITH A SYN-HEA-TYPE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-SECRETASE 1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: UNP RESIDUES 58-447;
COMPND 5 SYNONYM: ASPARTYL PROTEASE 2,ASP 2,BETA-SITE AMYLOID PRECURSOR
COMPND 6 PROTEIN CLEAVING ENZYME 1,BETA-SITE APP CLEAVING ENZYME 1,MEMAPSIN-2,
COMPND 7 MEMBRANE-ASSOCIATED ASPARTIC PROTEASE 2;
COMPND 8 EC: 3.4.23.46;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: L-ALPHA-GLUTAMYL-L-ISOLEUCYL-N-[(2R,3S)-1-{[(1S)-1-
COMPND 12 CARBOXYBUTYL]AMINO}-2-HYDROXY-5-METHYLHEXAN-3-YL]-3-THIOPHEN-2-YL-L-
COMPND 13 ALANINAMIDE;
COMPND 14 CHAIN: D, E, F;
COMPND 15 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: BACE1, BACE, KIAA1149;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 13 ORGANISM_TAXID: 32630;
SOURCE 14 OTHER_DETAILS: DESIGNED AND CHEMICALLY SYNTHESIZED
KEYWDS HYDRASE PROTEINASE CONVERTING, DESIGNED INHIBITOR, HYDRASE-INHIBITOR
KEYWDS 2 COMPLEX, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.AKAJI,K.TERUYA,T.AKIYAMA,A.SANJHO,E.YAMASHITA,A.NAKAGAWA
REVDAT 7 15-NOV-23 4TRW 1 LINK ATOM
REVDAT 6 08-NOV-23 4TRW 1 REMARK
REVDAT 5 29-JAN-20 4TRW 1 JRNL REMARK
REVDAT 4 09-SEP-15 4TRW 1 JRNL
REVDAT 3 02-SEP-15 4TRW 1 JRNL
REVDAT 2 08-JUL-15 4TRW 1 REMARK
REVDAT 1 01-JUL-15 4TRW 0
JRNL AUTH Y.HATTORI,K.KOBAYASHI,A.DEGUCHI,Y.NOHARA,T.AKIYAMA,K.TERUYA,
JRNL AUTH 2 A.SANJOH,A.NAKAGAWA,E.YAMASHITA,K.AKAJI
JRNL TITL EVALUATION OF TRANSITION-STATE MIMICS IN A SUPERIOR BACE1
JRNL TITL 2 CLEAVAGE SEQUENCE AS PEPTIDE-MIMETIC BACE1 INHIBITORS
JRNL REF BIOORG.MED.CHEM. V. 23 5626 2015
JRNL REFN ESSN 1464-3391
JRNL PMID 26264846
JRNL DOI 10.1016/J.BMC.2015.07.023
REMARK 2
REMARK 2 RESOLUTION. 2.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 2.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 38827
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1950
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) : 2.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.92
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2404
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.54
REMARK 3 BIN R VALUE (WORKING SET) : 0.2730
REMARK 3 BIN FREE R VALUE SET COUNT : 129
REMARK 3 BIN FREE R VALUE : 0.3580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9304
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 49
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.03000
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): 0.349
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.263
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.704
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.914
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9547 ; 0.013 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 8886 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12983 ; 1.665 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 20422 ; 0.978 ; 3.008
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1165 ; 7.982 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 432 ;33.658 ;23.958
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1497 ;15.592 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 51 ;19.129 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1422 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10840 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2254 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 4678 ; 4.072 ; 5.504
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4676 ; 4.072 ; 5.504
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5837 ; 6.598 ; 8.248
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 59 A 447
REMARK 3 ORIGIN FOR THE GROUP (A): -7.5355 0.8656 20.7330
REMARK 3 T TENSOR
REMARK 3 T11: 0.1146 T22: 0.0856
REMARK 3 T33: 0.0457 T12: -0.0074
REMARK 3 T13: -0.0395 T23: 0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 0.7630 L22: 1.2745
REMARK 3 L33: 0.3591 L12: -0.0499
REMARK 3 L13: 0.0807 L23: -0.4584
REMARK 3 S TENSOR
REMARK 3 S11: -0.1679 S12: 0.0098 S13: 0.0652
REMARK 3 S21: 0.0511 S22: 0.1471 S23: 0.0951
REMARK 3 S31: -0.1131 S32: 0.0329 S33: 0.0208
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 : B 59 B 447
REMARK 3 ORIGIN FOR THE GROUP (A): -30.1619 -38.9160 42.8189
REMARK 3 T TENSOR
REMARK 3 T11: 0.0401 T22: 0.0997
REMARK 3 T33: 0.0676 T12: 0.0050
REMARK 3 T13: -0.0043 T23: 0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 0.5347 L22: 1.0072
REMARK 3 L33: 0.8564 L12: 0.3373
REMARK 3 L13: -0.2359 L23: -0.3638
REMARK 3 S TENSOR
REMARK 3 S11: 0.1246 S12: -0.0609 S13: -0.0205
REMARK 3 S21: 0.0066 S22: -0.0727 S23: -0.0078
REMARK 3 S31: -0.0210 S32: -0.0789 S33: -0.0520
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 : C 58 C 447
REMARK 3 ORIGIN FOR THE GROUP (A): 18.0009 -41.9600 18.2096
REMARK 3 T TENSOR
REMARK 3 T11: 0.0715 T22: 0.0268
REMARK 3 T33: 0.1238 T12: -0.0053
REMARK 3 T13: -0.0147 T23: -0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 1.9755 L22: 0.2537
REMARK 3 L33: 0.9610 L12: -0.4982
REMARK 3 L13: -0.2344 L23: 0.1013
REMARK 3 S TENSOR
REMARK 3 S11: 0.0324 S12: -0.0296 S13: -0.3903
REMARK 3 S21: -0.0450 S22: -0.0049 S23: 0.1545
REMARK 3 S31: 0.0326 S32: 0.1188 S33: -0.0276
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: NULL
REMARK 4
REMARK 4 4TRW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000202076.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.90000
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL
REMARK 200 OPTICS : HORIZONTAL FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SCALEPACK, HKL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38857
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.66900
REMARK 200 R SYM FOR SHELL (I) : NULL
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: MOLREP
REMARK 200 STARTING MODEL: 2QP8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM CITRATE, 200MM AMMONIUM
REMARK 280 SULFATE, 14%(V/V) PEG 10000, PH 5.0, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
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 51.83050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F
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
REMARK 400 THE BETA-SECRETASE1 INHIBITOR IS PEPTIDE-LIKE, A MEMBER OF ENZYME
REMARK 400 INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: BETA-SECRETASE1 INHIBITOR
REMARK 400 CHAIN: D, E, F
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
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 GLY A 58
REMARK 465 GLY B 58
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 C 221 C - N - CD ANGL. DEV. = -29.2 DEGREES
REMARK 500 LHE D 4 C - N - CA ANGL. DEV. = -45.9 DEGREES
REMARK 500 LHE E 4 C - N - CA ANGL. DEV. = -32.7 DEGREES
REMARK 500 LHE F 4 C - N - CA ANGL. DEV. = -46.4 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 TRP A 258 -84.41 -124.34
REMARK 500 TRP B 258 -84.21 -116.59
REMARK 500 MET B 440 -179.34 81.14
REMARK 500 TRP C 258 -85.44 -118.29
REMARK 500 TIH D 3 54.60 -140.25
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 TIH D 3 LHE D 4 135.09
REMARK 500 TIH E 3 LHE E 4 128.63
REMARK 500 TIH F 3 LHE F 4 121.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF L-ALPHA-GLUTAMYL-L
REMARK 800 -ISOLEUCYL-N-[(2R,3S)-1-{[(1S)-1- CARBOXYBUTYL]AMINO}-2-HYDROXY-
REMARK 800 5-METHYLHEXAN-3-YL]-3-THIOPHEN-2-YL-L- ALANINAMIDE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN E OF L-ALPHA-GLUTAMYL-L
REMARK 800 -ISOLEUCYL-N-[(2R,3S)-1-{[(1S)-1- CARBOXYBUTYL]AMINO}-2-HYDROXY-
REMARK 800 5-METHYLHEXAN-3-YL]-3-THIOPHEN-2-YL-L- ALANINAMIDE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN F OF L-ALPHA-GLUTAMYL-L
REMARK 800 -ISOLEUCYL-N-[(2R,3S)-1-{[(1S)-1- CARBOXYBUTYL]AMINO}-2-HYDROXY-
REMARK 800 5-METHYLHEXAN-3-YL]-3-THIOPHEN-2-YL-L- ALANINAMIDE
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4TRZ RELATED DB: PDB
REMARK 900 RELATED ID: 4TRY RELATED DB: PDB
DBREF 4TRW A 58 447 UNP P56817 BACE1_HUMAN 58 447
DBREF 4TRW B 58 447 UNP P56817 BACE1_HUMAN 58 447
DBREF 4TRW C 58 447 UNP P56817 BACE1_HUMAN 58 447
DBREF 4TRW D 1 4 PDB 4TRW 4TRW 1 4
DBREF 4TRW E 1 4 PDB 4TRW 4TRW 1 4
DBREF 4TRW F 1 4 PDB 4TRW 4TRW 1 4
SEQRES 1 A 390 GLY SER PHE VAL GLU MET VAL ASP ASN LEU ARG GLY LYS
SEQRES 2 A 390 SER GLY GLN GLY TYR TYR VAL GLU MET THR VAL GLY SER
SEQRES 3 A 390 PRO PRO GLN THR LEU ASN ILE LEU VAL ASP THR GLY SER
SEQRES 4 A 390 SER ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO PHE LEU
SEQRES 5 A 390 HIS ARG TYR TYR GLN ARG GLN LEU SER SER THR TYR ARG
SEQRES 6 A 390 ASP LEU ARG LYS GLY VAL TYR VAL PRO TYR THR GLN GLY
SEQRES 7 A 390 LYS TRP GLU GLY GLU LEU GLY THR ASP LEU VAL SER ILE
SEQRES 8 A 390 PRO HIS GLY PRO ASN VAL THR VAL ARG ALA ASN ILE ALA
SEQRES 9 A 390 ALA ILE THR GLU SER ASP LYS PHE PHE ILE ASN GLY SER
SEQRES 10 A 390 ASN TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA GLU ILE
SEQRES 11 A 390 ALA ARG PRO ASP ASP SER LEU GLU PRO PHE PHE ASP SER
SEQRES 12 A 390 LEU VAL LYS GLN THR HIS VAL PRO ASN LEU PHE SER LEU
SEQRES 13 A 390 GLN LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN SER GLU
SEQRES 14 A 390 VAL LEU ALA SER VAL GLY GLY SER MET ILE ILE GLY GLY
SEQRES 15 A 390 ILE ASP HIS SER LEU TYR THR GLY SER LEU TRP TYR THR
SEQRES 16 A 390 PRO ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE ILE VAL
SEQRES 17 A 390 ARG VAL GLU ILE ASN GLY GLN ASP LEU LYS MET ASP CYS
SEQRES 18 A 390 LYS GLU TYR ASN TYR ASP LYS SER ILE VAL ASP SER GLY
SEQRES 19 A 390 THR THR ASN LEU ARG LEU PRO LYS LYS VAL PHE GLU ALA
SEQRES 20 A 390 ALA VAL LYS SER ILE LYS ALA ALA SER SER THR GLU LYS
SEQRES 21 A 390 PHE PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU VAL CYS
SEQRES 22 A 390 TRP GLN ALA GLY THR THR PRO TRP ASN ILE PHE PRO VAL
SEQRES 23 A 390 ILE SER LEU TYR LEU MET GLY GLU VAL THR ASN GLN SER
SEQRES 24 A 390 PHE ARG ILE THR ILE LEU PRO GLN GLN TYR LEU ARG PRO
SEQRES 25 A 390 VAL GLU ASP VAL ALA THR SER GLN ASP ASP CYS TYR LYS
SEQRES 26 A 390 PHE ALA ILE SER GLN SER SER THR GLY THR VAL MET GLY
SEQRES 27 A 390 ALA VAL ILE MET GLU GLY PHE TYR VAL VAL PHE ASP ARG
SEQRES 28 A 390 ALA ARG LYS ARG ILE GLY PHE ALA VAL SER ALA CYS HIS
SEQRES 29 A 390 VAL HIS ASP GLU PHE ARG THR ALA ALA VAL GLU GLY PRO
SEQRES 30 A 390 PHE VAL THR LEU ASP MET GLU ASP CYS GLY TYR ASN ILE
SEQRES 1 B 390 GLY SER PHE VAL GLU MET VAL ASP ASN LEU ARG GLY LYS
SEQRES 2 B 390 SER GLY GLN GLY TYR TYR VAL GLU MET THR VAL GLY SER
SEQRES 3 B 390 PRO PRO GLN THR LEU ASN ILE LEU VAL ASP THR GLY SER
SEQRES 4 B 390 SER ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO PHE LEU
SEQRES 5 B 390 HIS ARG TYR TYR GLN ARG GLN LEU SER SER THR TYR ARG
SEQRES 6 B 390 ASP LEU ARG LYS GLY VAL TYR VAL PRO TYR THR GLN GLY
SEQRES 7 B 390 LYS TRP GLU GLY GLU LEU GLY THR ASP LEU VAL SER ILE
SEQRES 8 B 390 PRO HIS GLY PRO ASN VAL THR VAL ARG ALA ASN ILE ALA
SEQRES 9 B 390 ALA ILE THR GLU SER ASP LYS PHE PHE ILE ASN GLY SER
SEQRES 10 B 390 ASN TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA GLU ILE
SEQRES 11 B 390 ALA ARG PRO ASP ASP SER LEU GLU PRO PHE PHE ASP SER
SEQRES 12 B 390 LEU VAL LYS GLN THR HIS VAL PRO ASN LEU PHE SER LEU
SEQRES 13 B 390 GLN LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN SER GLU
SEQRES 14 B 390 VAL LEU ALA SER VAL GLY GLY SER MET ILE ILE GLY GLY
SEQRES 15 B 390 ILE ASP HIS SER LEU TYR THR GLY SER LEU TRP TYR THR
SEQRES 16 B 390 PRO ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE ILE VAL
SEQRES 17 B 390 ARG VAL GLU ILE ASN GLY GLN ASP LEU LYS MET ASP CYS
SEQRES 18 B 390 LYS GLU TYR ASN TYR ASP LYS SER ILE VAL ASP SER GLY
SEQRES 19 B 390 THR THR ASN LEU ARG LEU PRO LYS LYS VAL PHE GLU ALA
SEQRES 20 B 390 ALA VAL LYS SER ILE LYS ALA ALA SER SER THR GLU LYS
SEQRES 21 B 390 PHE PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU VAL CYS
SEQRES 22 B 390 TRP GLN ALA GLY THR THR PRO TRP ASN ILE PHE PRO VAL
SEQRES 23 B 390 ILE SER LEU TYR LEU MET GLY GLU VAL THR ASN GLN SER
SEQRES 24 B 390 PHE ARG ILE THR ILE LEU PRO GLN GLN TYR LEU ARG PRO
SEQRES 25 B 390 VAL GLU ASP VAL ALA THR SER GLN ASP ASP CYS TYR LYS
SEQRES 26 B 390 PHE ALA ILE SER GLN SER SER THR GLY THR VAL MET GLY
SEQRES 27 B 390 ALA VAL ILE MET GLU GLY PHE TYR VAL VAL PHE ASP ARG
SEQRES 28 B 390 ALA ARG LYS ARG ILE GLY PHE ALA VAL SER ALA CYS HIS
SEQRES 29 B 390 VAL HIS ASP GLU PHE ARG THR ALA ALA VAL GLU GLY PRO
SEQRES 30 B 390 PHE VAL THR LEU ASP MET GLU ASP CYS GLY TYR ASN ILE
SEQRES 1 C 390 GLY SER PHE VAL GLU MET VAL ASP ASN LEU ARG GLY LYS
SEQRES 2 C 390 SER GLY GLN GLY TYR TYR VAL GLU MET THR VAL GLY SER
SEQRES 3 C 390 PRO PRO GLN THR LEU ASN ILE LEU VAL ASP THR GLY SER
SEQRES 4 C 390 SER ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO PHE LEU
SEQRES 5 C 390 HIS ARG TYR TYR GLN ARG GLN LEU SER SER THR TYR ARG
SEQRES 6 C 390 ASP LEU ARG LYS GLY VAL TYR VAL PRO TYR THR GLN GLY
SEQRES 7 C 390 LYS TRP GLU GLY GLU LEU GLY THR ASP LEU VAL SER ILE
SEQRES 8 C 390 PRO HIS GLY PRO ASN VAL THR VAL ARG ALA ASN ILE ALA
SEQRES 9 C 390 ALA ILE THR GLU SER ASP LYS PHE PHE ILE ASN GLY SER
SEQRES 10 C 390 ASN TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA GLU ILE
SEQRES 11 C 390 ALA ARG PRO ASP ASP SER LEU GLU PRO PHE PHE ASP SER
SEQRES 12 C 390 LEU VAL LYS GLN THR HIS VAL PRO ASN LEU PHE SER LEU
SEQRES 13 C 390 GLN LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN SER GLU
SEQRES 14 C 390 VAL LEU ALA SER VAL GLY GLY SER MET ILE ILE GLY GLY
SEQRES 15 C 390 ILE ASP HIS SER LEU TYR THR GLY SER LEU TRP TYR THR
SEQRES 16 C 390 PRO ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE ILE VAL
SEQRES 17 C 390 ARG VAL GLU ILE ASN GLY GLN ASP LEU LYS MET ASP CYS
SEQRES 18 C 390 LYS GLU TYR ASN TYR ASP LYS SER ILE VAL ASP SER GLY
SEQRES 19 C 390 THR THR ASN LEU ARG LEU PRO LYS LYS VAL PHE GLU ALA
SEQRES 20 C 390 ALA VAL LYS SER ILE LYS ALA ALA SER SER THR GLU LYS
SEQRES 21 C 390 PHE PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU VAL CYS
SEQRES 22 C 390 TRP GLN ALA GLY THR THR PRO TRP ASN ILE PHE PRO VAL
SEQRES 23 C 390 ILE SER LEU TYR LEU MET GLY GLU VAL THR ASN GLN SER
SEQRES 24 C 390 PHE ARG ILE THR ILE LEU PRO GLN GLN TYR LEU ARG PRO
SEQRES 25 C 390 VAL GLU ASP VAL ALA THR SER GLN ASP ASP CYS TYR LYS
SEQRES 26 C 390 PHE ALA ILE SER GLN SER SER THR GLY THR VAL MET GLY
SEQRES 27 C 390 ALA VAL ILE MET GLU GLY PHE TYR VAL VAL PHE ASP ARG
SEQRES 28 C 390 ALA ARG LYS ARG ILE GLY PHE ALA VAL SER ALA CYS HIS
SEQRES 29 C 390 VAL HIS ASP GLU PHE ARG THR ALA ALA VAL GLU GLY PRO
SEQRES 30 C 390 PHE VAL THR LEU ASP MET GLU ASP CYS GLY TYR ASN ILE
SEQRES 1 D 4 GLU ILE TIH LHE
SEQRES 1 E 4 GLU ILE TIH LHE
SEQRES 1 F 4 GLU ILE TIH LHE
HET TIH D 3 10
HET LHE D 4 17
HET TIH E 3 10
HET LHE E 4 17
HET TIH F 3 10
HET LHE F 4 17
HETNAM TIH BETA(2-THIENYL)ALANINE
HETNAM LHE N-[(2R,3S)-3-AMINO-2-HYDROXY-5-METHYLHEXYL]-L-NORVALINE
FORMUL 4 TIH 3(C7 H9 N O2 S)
FORMUL 4 LHE 3(C12 H26 N2 O3)
FORMUL 7 HOH *49(H2 O)
HELIX 1 AA1 PHE A 60 VAL A 64 5 5
HELIX 2 AA2 GLN A 114 SER A 118 5 5
HELIX 3 AA3 TYR A 184 ALA A 188 5 5
HELIX 4 AA4 PRO A 196 THR A 205 1 10
HELIX 5 AA5 ASN A 223 SER A 230 1 8
HELIX 6 AA6 ASP A 241 SER A 243 5 3
HELIX 7 AA7 ASP A 277 TYR A 283 5 7
HELIX 8 AA8 LYS A 299 SER A 313 1 15
HELIX 9 AA9 PRO A 337 PHE A 341 5 5
HELIX 10 AB1 LEU A 362 TYR A 366 1 5
HELIX 11 AB2 GLY A 395 GLY A 401 1 7
HELIX 12 AB3 ASP A 439 GLY A 444 5 6
HELIX 13 AB4 SER B 59 VAL B 64 5 6
HELIX 14 AB5 GLN B 114 SER B 118 5 5
HELIX 15 AB6 TYR B 184 ALA B 188 5 5
HELIX 16 AB7 PRO B 196 THR B 205 1 10
HELIX 17 AB8 SER B 225 SER B 230 1 6
HELIX 18 AB9 ASP B 241 SER B 243 5 3
HELIX 19 AC1 ASP B 277 TYR B 283 5 7
HELIX 20 AC2 LYS B 299 SER B 313 1 15
HELIX 21 AC3 PRO B 319 LEU B 324 1 6
HELIX 22 AC4 PRO B 337 PHE B 341 5 5
HELIX 23 AC5 LEU B 362 TYR B 366 1 5
HELIX 24 AC6 GLY B 395 GLU B 400 1 6
HELIX 25 AC7 PHE C 60 VAL C 64 5 5
HELIX 26 AC8 GLN C 114 SER C 118 5 5
HELIX 27 AC9 TYR C 184 ALA C 188 5 5
HELIX 28 AD1 PRO C 196 THR C 205 1 10
HELIX 29 AD2 ASP C 241 SER C 243 5 3
HELIX 30 AD3 ASP C 277 TYR C 283 5 7
HELIX 31 AD4 LYS C 299 SER C 313 1 15
HELIX 32 AD5 PRO C 319 LEU C 324 1 6
HELIX 33 AD6 LEU C 362 TYR C 366 1 5
HELIX 34 AD7 GLY C 395 GLU C 400 1 6
HELIX 35 AD8 ASP C 439 GLY C 444 5 6
SHEET 1 AA1 8 LEU A 67 LYS A 70 0
SHEET 2 AA1 8 GLY A 74 VAL A 81 -1 O TYR A 76 N ARG A 68
SHEET 3 AA1 8 GLN A 86 ASP A 93 -1 O ILE A 90 N VAL A 77
SHEET 4 AA1 8 GLY A 178 GLY A 181 1 O LEU A 180 N LEU A 91
SHEET 5 AA1 8 PHE A 99 GLY A 102 -1 N ALA A 100 O ILE A 179
SHEET 6 AA1 8 THR A 155 ASP A 167 1 O ILE A 163 N VAL A 101
SHEET 7 AA1 8 LYS A 136 SER A 147 -1 N GLU A 140 O ALA A 162
SHEET 8 AA1 8 ARG A 122 PRO A 131 -1 N LYS A 126 O LEU A 141
SHEET 1 AA2 4 LEU A 67 LYS A 70 0
SHEET 2 AA2 4 GLY A 74 VAL A 81 -1 O TYR A 76 N ARG A 68
SHEET 3 AA2 4 LYS A 136 SER A 147 -1 O SER A 147 N THR A 80
SHEET 4 AA2 4 ARG A 122 PRO A 131 -1 N LYS A 126 O LEU A 141
SHEET 1 AA3 5 GLY A 233 ILE A 237 0
SHEET 2 AA3 5 PHE A 211 LEU A 215 -1 N GLN A 214 O SER A 234
SHEET 3 AA3 5 PHE A 402 ASP A 407 -1 O PHE A 406 N PHE A 211
SHEET 4 AA3 5 ARG A 412 SER A 418 -1 O ALA A 416 N TYR A 403
SHEET 5 AA3 5 TYR A 245 PRO A 253 -1 N TRP A 250 O PHE A 415
SHEET 1 AA4 3 GLU A 261 VAL A 262 0
SHEET 2 AA4 3 SER A 286 VAL A 288 -1 O SER A 286 N VAL A 262
SHEET 3 AA4 3 THR A 392 MET A 394 1 O MET A 394 N ILE A 287
SHEET 1 AA5 5 GLN A 272 ASP A 273 0
SHEET 2 AA5 5 ILE A 264 ILE A 269 -1 N ILE A 269 O GLN A 272
SHEET 3 AA5 5 ILE A 344 MET A 349 -1 O SER A 345 N GLU A 268
SHEET 4 AA5 5 GLN A 355 ILE A 361 -1 O ILE A 361 N ILE A 344
SHEET 5 AA5 5 ALA A 430 VAL A 436 -1 O PHE A 435 N SER A 356
SHEET 1 AA6 2 LEU A 295 PRO A 298 0
SHEET 2 AA6 2 ILE A 385 SER A 388 1 O SER A 386 N LEU A 297
SHEET 1 AA7 3 VAL A 329 TRP A 331 0
SHEET 2 AA7 3 ASP A 379 PHE A 383 -1 O TYR A 381 N VAL A 329
SHEET 3 AA7 3 LEU A 367 PRO A 369 -1 N ARG A 368 O LYS A 382
SHEET 1 AA8 8 ARG B 68 LYS B 70 0
SHEET 2 AA8 8 GLY B 74 VAL B 81 -1 O TYR B 76 N ARG B 68
SHEET 3 AA8 8 GLN B 86 ASP B 93 -1 O ILE B 90 N VAL B 77
SHEET 4 AA8 8 GLY B 178 GLY B 181 1 O LEU B 180 N LEU B 91
SHEET 5 AA8 8 PHE B 99 GLY B 102 -1 N ALA B 100 O ILE B 179
SHEET 6 AA8 8 THR B 155 ASP B 167 1 O ILE B 163 N VAL B 101
SHEET 7 AA8 8 LYS B 136 SER B 147 -1 N GLY B 142 O ILE B 160
SHEET 8 AA8 8 ARG B 122 TYR B 129 -1 N VAL B 128 O GLY B 139
SHEET 1 AA9 4 ARG B 68 LYS B 70 0
SHEET 2 AA9 4 GLY B 74 VAL B 81 -1 O TYR B 76 N ARG B 68
SHEET 3 AA9 4 LYS B 136 SER B 147 -1 O SER B 147 N THR B 80
SHEET 4 AA9 4 ARG B 122 TYR B 129 -1 N VAL B 128 O GLY B 139
SHEET 1 AB1 5 GLY B 233 ILE B 237 0
SHEET 2 AB1 5 PHE B 211 LEU B 215 -1 N GLN B 214 O SER B 234
SHEET 3 AB1 5 PHE B 402 ASP B 407 -1 O VAL B 404 N LEU B 213
SHEET 4 AB1 5 ARG B 412 SER B 418 -1 O ALA B 416 N TYR B 403
SHEET 5 AB1 5 TYR B 245 PRO B 253 -1 N THR B 252 O ILE B 413
SHEET 1 AB2 5 GLN B 272 ASP B 273 0
SHEET 2 AB2 5 ILE B 264 ILE B 269 -1 N ILE B 269 O GLN B 272
SHEET 3 AB2 5 ILE B 344 LEU B 348 -1 O SER B 345 N GLU B 268
SHEET 4 AB2 5 PHE B 357 ILE B 361 -1 O ILE B 359 N LEU B 346
SHEET 5 AB2 5 ALA B 430 GLU B 432 -1 O ALA B 430 N THR B 360
SHEET 1 AB3 4 SER B 286 VAL B 288 0
SHEET 2 AB3 4 THR B 392 MET B 394 1 O THR B 392 N ILE B 287
SHEET 3 AB3 4 LEU B 295 PRO B 298 -1 N ARG B 296 O VAL B 393
SHEET 4 AB3 4 ILE B 385 SER B 388 1 O SER B 388 N LEU B 297
SHEET 1 AB4 3 VAL B 329 GLN B 332 0
SHEET 2 AB4 3 ASP B 378 PHE B 383 -1 O TYR B 381 N VAL B 329
SHEET 3 AB4 3 LEU B 367 PRO B 369 -1 N ARG B 368 O LYS B 382
SHEET 1 AB5 8 LEU C 67 LYS C 70 0
SHEET 2 AB5 8 GLY C 74 VAL C 81 -1 O TYR C 76 N ARG C 68
SHEET 3 AB5 8 GLN C 86 ASP C 93 -1 O ILE C 90 N VAL C 77
SHEET 4 AB5 8 GLY C 178 GLY C 181 1 O LEU C 180 N LEU C 91
SHEET 5 AB5 8 ALA C 100 GLY C 102 -1 N ALA C 100 O ILE C 179
SHEET 6 AB5 8 THR C 155 ASP C 167 1 O ILE C 163 N VAL C 101
SHEET 7 AB5 8 LYS C 136 SER C 147 -1 N GLY C 142 O ILE C 160
SHEET 8 AB5 8 ARG C 122 PRO C 131 -1 N LYS C 126 O LEU C 141
SHEET 1 AB6 4 LEU C 67 LYS C 70 0
SHEET 2 AB6 4 GLY C 74 VAL C 81 -1 O TYR C 76 N ARG C 68
SHEET 3 AB6 4 LYS C 136 SER C 147 -1 O SER C 147 N THR C 80
SHEET 4 AB6 4 ARG C 122 PRO C 131 -1 N LYS C 126 O LEU C 141
SHEET 1 AB7 5 SER C 234 ILE C 237 0
SHEET 2 AB7 5 PHE C 211 GLN C 214 -1 N GLN C 214 O SER C 234
SHEET 3 AB7 5 PHE C 402 ASP C 407 -1 O PHE C 406 N PHE C 211
SHEET 4 AB7 5 ARG C 412 SER C 418 -1 O GLY C 414 N VAL C 405
SHEET 5 AB7 5 TYR C 245 PRO C 253 -1 N THR C 252 O ILE C 413
SHEET 1 AB8 5 GLN C 272 ASP C 273 0
SHEET 2 AB8 5 ILE C 264 ILE C 269 -1 N ILE C 269 O GLN C 272
SHEET 3 AB8 5 ILE C 344 MET C 349 -1 O TYR C 347 N VAL C 265
SHEET 4 AB8 5 GLN C 355 ILE C 361 -1 O ILE C 361 N ILE C 344
SHEET 5 AB8 5 ALA C 430 VAL C 436 -1 O GLU C 432 N ARG C 358
SHEET 1 AB9 4 SER C 286 VAL C 288 0
SHEET 2 AB9 4 THR C 392 MET C 394 1 O MET C 394 N ILE C 287
SHEET 3 AB9 4 LEU C 295 PRO C 298 -1 N ARG C 296 O VAL C 393
SHEET 4 AB9 4 ILE C 385 SER C 388 1 O SER C 388 N LEU C 297
SHEET 1 AC1 2 LEU C 367 VAL C 370 0
SHEET 2 AC1 2 CYS C 380 PHE C 383 -1 O CYS C 380 N VAL C 370
SSBOND 1 CYS A 216 CYS A 420 1555 1555 2.05
SSBOND 2 CYS A 278 CYS A 443 1555 1555 2.83
SSBOND 3 CYS A 330 CYS A 380 1555 1555 2.06
SSBOND 4 CYS B 216 CYS B 420 1555 1555 2.60
SSBOND 5 CYS B 278 CYS B 443 1555 1555 2.32
SSBOND 6 CYS B 330 CYS B 380 1555 1555 2.05
SSBOND 7 CYS C 216 CYS C 420 1555 1555 2.05
SSBOND 8 CYS C 278 CYS C 443 1555 1555 2.02
SSBOND 9 CYS C 330 CYS C 380 1555 1555 2.04
LINK C ILE D 2 N TIH D 3 1555 1555 1.32
LINK C TIH D 3 N LHE D 4 1555 1555 1.33
LINK C ILE E 2 N TIH E 3 1555 1555 1.33
LINK C TIH E 3 N LHE E 4 1555 1555 1.30
LINK C ILE F 2 N TIH F 3 1555 1555 1.33
LINK C TIH F 3 N LHE F 4 1555 1555 1.34
CISPEP 1 SER A 83 PRO A 84 0 -1.70
CISPEP 2 ARG A 189 PRO A 190 0 -6.17
CISPEP 3 TYR A 283 ASP A 284 0 4.88
CISPEP 4 GLY A 433 PRO A 434 0 4.76
CISPEP 5 SER B 83 PRO B 84 0 -2.38
CISPEP 6 ARG B 189 PRO B 190 0 -0.47
CISPEP 7 TYR B 283 ASP B 284 0 2.63
CISPEP 8 GLY B 433 PRO B 434 0 2.44
CISPEP 9 MET B 440 GLU B 441 0 -4.10
CISPEP 10 SER C 83 PRO C 84 0 -1.53
CISPEP 11 ARG C 189 PRO C 190 0 -3.44
CISPEP 12 GLY C 219 PHE C 220 0 -24.54
CISPEP 13 PHE C 220 PRO C 221 0 -0.20
CISPEP 14 SER C 230 VAL C 231 0 -1.58
CISPEP 15 VAL C 231 GLY C 232 0 3.26
CISPEP 16 TYR C 283 ASP C 284 0 2.22
CISPEP 17 GLY C 433 PRO C 434 0 -2.08
SITE 1 AC1 14 GLY A 72 GLY A 74 ASP A 93 GLY A 95
SITE 2 AC1 14 TYR A 132 THR A 133 GLN A 134 ILE A 171
SITE 3 AC1 14 TYR A 259 ASP A 289 GLY A 291 THR A 292
SITE 4 AC1 14 THR A 293 ASN A 294
SITE 1 AC2 14 GLY B 72 ASP B 93 GLY B 95 PRO B 131
SITE 2 AC2 14 TYR B 132 THR B 133 GLN B 134 PHE B 169
SITE 3 AC2 14 TYR B 259 ASP B 289 GLY B 291 THR B 292
SITE 4 AC2 14 THR B 293 ASN B 294
SITE 1 AC3 18 GLY C 72 LEU C 91 ASP C 93 GLY C 95
SITE 2 AC3 18 SER C 96 PRO C 131 TYR C 132 THR C 133
SITE 3 AC3 18 GLN C 134 TYR C 259 ASP C 289 GLY C 291
SITE 4 AC3 18 THR C 292 THR C 293 ASN C 294 ARG C 296
SITE 5 AC3 18 ARG C 368 LYS C 382
CRYST1 82.285 103.661 102.000 90.00 102.73 90.00 P 1 21 1 6
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 0.012153 0.000000 0.002746 0.00000
SCALE2 0.000000 0.009647 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010051 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
