HEADER HYDROLASE/HYDROLASE INHIBITOR 10-JAN-12 4D83
TITLE CRYSTAL STRUCTURE OF HUMAN BETA SECRETASE IN COMPLEX WITH NVP-BUR436,
TITLE 2 DERIVED FROM A CO-CRYSTALLIZATION EXPERIMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-SECRETASE 1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: UNP RESIDUES 48-447;
COMPND 5 SYNONYM: ASPARTYL PROTEASE 2, ASP2, ASP 2, BETA-SITE AMYLOID
COMPND 6 PRECURSOR PROTEIN CLEAVING ENZYME 1, BETA-SITE APP CLEAVING ENZYME 1,
COMPND 7 MEMAPSIN-2, MEMBRANE-ASSOCIATED ASPARTIC PROTEASE 2;
COMPND 8 EC: 3.4.23.46;
COMPND 9 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: BACE, BACE1, KIAA1149;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24
KEYWDS BETA-SECRETASE, MEMAPSIN2, BACE1, ASPARTIC PROTEINASE, ALZHEIMER'S
KEYWDS 2 DISEASE, ENZYME INHIBITOR COMPLEX, STRUCTURE-BASED DRUG DESIGN,
KEYWDS 3 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.RONDEAU,E.BOURGIER
REVDAT 2 15-NOV-17 4D83 1 REMARK
REVDAT 1 21-NOV-12 4D83 0
JRNL AUTH H.RUEEGER,R.LUEOEND,O.ROGEL,J.M.RONDEAU,H.MOBITZ,R.MACHAUER,
JRNL AUTH 2 L.JACOBSON,M.STAUFENBIEL,S.DESRAYAUD,U.NEUMANN
JRNL TITL DISCOVERY OF CYCLIC SULFONE HYDROXYETHYLAMINES AS POTENT AND
JRNL TITL 2 SELECTIVE BETA-SITE APP-CLEAVING ENZYME 1 (BACE1)
JRNL TITL 3 INHIBITORS: STRUCTURE BASED DESIGN AND IN VIVO REDUCTION OF
JRNL TITL 4 AMYLOID BETA-PEPTIDES
JRNL REF J.MED.CHEM. V. 55 3364 2012
JRNL REFN ISSN 0022-2623
JRNL PMID 22380629
JRNL DOI 10.1021/JM300069Y
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.RUEEGER,J.M.RONDEAU,C.MCCARTHY,H.MOBITZ,
REMARK 1 AUTH 2 M.TINTELNOT-BLOMLEY,U.NEUMANN,S.DESRAYAUD
REMARK 1 TITL STRUCTURE BASED DESIGN, SYNTHESIS AND SAR OF CYCLIC
REMARK 1 TITL 2 HYDROXYETHYLAMINE (HEA) BACE-1 INHIBITORS.
REMARK 1 REF BIOORG.MED.CHEM.LETT. V. 21 1942 2011
REMARK 1 REFN ISSN 0960-894X
REMARK 1 PMID 21388807
REMARK 1 DOI 10.1016/J.BMCL.2011.02.038
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 14392781.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 61642
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3109
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 61642
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 9555
REMARK 3 BIN R VALUE (WORKING SET) : 0.2700
REMARK 3 BIN FREE R VALUE : 0.3140
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 504
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8898
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 105
REMARK 3 SOLVENT ATOMS : 411
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.98000
REMARK 3 B22 (A**2) : 14.90000
REMARK 3 B33 (A**2) : -7.92000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.39000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.29
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.37
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 0.900
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 28.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.660
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.380 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.340 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.890 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.830 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 44.66
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NVP-BUR436.PARAM
REMARK 3 PARAMETER FILE 4 : CIS_PEPTIDE.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NVP-BUR436.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4D83 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000070000.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61714
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.44200
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNX 2002
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M AMMONIUM SULFATE IN WATER, PH
REMARK 280 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
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 51.44650
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -15
REMARK 465 PRO A -14
REMARK 465 ASP A -13
REMARK 465 GLU A -12
REMARK 465 GLU A -11
REMARK 465 PRO A -10
REMARK 465 GLU A -9
REMARK 465 GLU A -8
REMARK 465 PRO A -7
REMARK 465 GLY A -6
REMARK 465 ARG A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 GLY A 157A
REMARK 465 PHE A 157B
REMARK 465 PRO A 157C
REMARK 465 LEU A 157D
REMARK 465 ASN A 157E
REMARK 465 GLN A 157F
REMARK 465 SER A 157G
REMARK 465 GLU A 157H
REMARK 465 VAL A 157I
REMARK 465 LEU A 157J
REMARK 465 ALA A 157K
REMARK 465 ILE A 375
REMARK 465 GLY B -15
REMARK 465 PRO B -14
REMARK 465 ASP B -13
REMARK 465 GLU B -12
REMARK 465 GLU B -11
REMARK 465 PRO B -10
REMARK 465 GLU B -9
REMARK 465 GLU B -8
REMARK 465 PRO B -7
REMARK 465 GLY B -6
REMARK 465 ARG B -5
REMARK 465 ARG B -4
REMARK 465 GLY B -3
REMARK 465 GLY B 157A
REMARK 465 PHE B 157B
REMARK 465 PRO B 157C
REMARK 465 LEU B 157D
REMARK 465 ASN B 157E
REMARK 465 GLN B 157F
REMARK 465 SER B 157G
REMARK 465 GLU B 157H
REMARK 465 VAL B 157I
REMARK 465 LEU B 157J
REMARK 465 ALA B 157K
REMARK 465 ILE B 375
REMARK 465 GLY C -15
REMARK 465 PRO C -14
REMARK 465 ASP C -13
REMARK 465 GLU C -12
REMARK 465 GLU C -11
REMARK 465 PRO C -10
REMARK 465 GLU C -9
REMARK 465 GLU C -8
REMARK 465 PRO C -7
REMARK 465 GLY C -6
REMARK 465 ARG C -5
REMARK 465 ARG C -4
REMARK 465 GLY C -3
REMARK 465 GLY C 157A
REMARK 465 PHE C 157B
REMARK 465 PRO C 157C
REMARK 465 LEU C 157D
REMARK 465 ASN C 157E
REMARK 465 GLN C 157F
REMARK 465 SER C 157G
REMARK 465 GLU C 157H
REMARK 465 VAL C 157I
REMARK 465 LEU C 157J
REMARK 465 ALA C 157K
REMARK 465 ILE C 375
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 ARG C 54 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG C 54 NE - CZ - NH2 ANGL. DEV. = 3.1 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 LYS A 65 125.74 -175.28
REMARK 500 HIS A 89 51.32 -93.44
REMARK 500 ASN A 114 4.03 80.90
REMARK 500 TRP A 186 -81.46 -134.66
REMARK 500 ALA A 261 122.96 -39.04
REMARK 500 VAL A 301 49.87 -89.55
REMARK 500 THR A 303 33.34 -74.87
REMARK 500 CYS A 348 47.06 -97.70
REMARK 500 HIS B 89 50.23 -94.87
REMARK 500 TRP B 186 -80.80 -134.91
REMARK 500 ALA B 261 123.12 -38.82
REMARK 500 THR B 303 45.13 -84.42
REMARK 500 GLN B 305 53.62 -108.08
REMARK 500 CYS B 348 43.17 -99.11
REMARK 500 HIS B 351 144.97 -172.75
REMARK 500 ASP B 352 -148.10 -103.57
REMARK 500 HIS C 89 46.47 -96.19
REMARK 500 TRP C 186 -81.55 -134.89
REMARK 500 SER C 304 160.33 175.11
REMARK 500 CYS C 348 46.73 -99.20
REMARK 500 ASP C 352 137.41 176.93
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 RESIDUE 0GT A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0GT B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0GT C 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VEU RELATED DB: PDB
REMARK 900 COMPOUND 3 OF PRIMARY CITATION
REMARK 900 RELATED ID: 3VF3 RELATED DB: PDB
REMARK 900 ANALOGUE OF COMPOUND 14B OF PRIMARY CITATION
REMARK 900 RELATED ID: 3VG1 RELATED DB: PDB
REMARK 900 SAME COMPLEX, AT HIGHER RESOLUTION, FROM SOAKING EXPERIMENT USING A
REMARK 900 DIFFERENT CRYSTAL FORM (P212121)
REMARK 900 RELATED ID: 4D85 RELATED DB: PDB
REMARK 900 RELATED ID: 4D88 RELATED DB: PDB
REMARK 900 RELATED ID: 4D89 RELATED DB: PDB
REMARK 900 RELATED ID: 4D8C RELATED DB: PDB
DBREF 4D83 A -13 375 UNP P56817 BACE1_HUMAN 48 447
DBREF 4D83 B -13 375 UNP P56817 BACE1_HUMAN 48 447
DBREF 4D83 C -13 375 UNP P56817 BACE1_HUMAN 48 447
SEQADV 4D83 GLY A -15 UNP P56817 EXPRESSION TAG
SEQADV 4D83 PRO A -14 UNP P56817 EXPRESSION TAG
SEQADV 4D83 GLY B -15 UNP P56817 EXPRESSION TAG
SEQADV 4D83 PRO B -14 UNP P56817 EXPRESSION TAG
SEQADV 4D83 GLY C -15 UNP P56817 EXPRESSION TAG
SEQADV 4D83 PRO C -14 UNP P56817 EXPRESSION TAG
SEQRES 1 A 402 GLY PRO ASP GLU GLU PRO GLU GLU PRO GLY ARG ARG GLY
SEQRES 2 A 402 SER PHE VAL GLU MET VAL ASP ASN LEU ARG GLY LYS SER
SEQRES 3 A 402 GLY GLN GLY TYR TYR VAL GLU MET THR VAL GLY SER PRO
SEQRES 4 A 402 PRO GLN THR LEU ASN ILE LEU VAL ASP THR GLY SER SER
SEQRES 5 A 402 ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO PHE LEU HIS
SEQRES 6 A 402 ARG TYR TYR GLN ARG GLN LEU SER SER THR TYR ARG ASP
SEQRES 7 A 402 LEU ARG LYS GLY VAL TYR VAL PRO TYR THR GLN GLY LYS
SEQRES 8 A 402 TRP GLU GLY GLU LEU GLY THR ASP LEU VAL SER ILE PRO
SEQRES 9 A 402 HIS GLY PRO ASN VAL THR VAL ARG ALA ASN ILE ALA ALA
SEQRES 10 A 402 ILE THR GLU SER ASP LYS PHE PHE ILE ASN GLY SER ASN
SEQRES 11 A 402 TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA GLU ILE ALA
SEQRES 12 A 402 ARG PRO ASP ASP SER LEU GLU PRO PHE PHE ASP SER LEU
SEQRES 13 A 402 VAL LYS GLN THR HIS VAL PRO ASN LEU PHE SER LEU GLN
SEQRES 14 A 402 LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN SER GLU VAL
SEQRES 15 A 402 LEU ALA SER VAL GLY GLY SER MET ILE ILE GLY GLY ILE
SEQRES 16 A 402 ASP HIS SER LEU TYR THR GLY SER LEU TRP TYR THR PRO
SEQRES 17 A 402 ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE ILE VAL ARG
SEQRES 18 A 402 VAL GLU ILE ASN GLY GLN ASP LEU LYS MET ASP CYS LYS
SEQRES 19 A 402 GLU TYR ASN TYR ASP LYS SER ILE VAL ASP SER GLY THR
SEQRES 20 A 402 THR ASN LEU ARG LEU PRO LYS LYS VAL PHE GLU ALA ALA
SEQRES 21 A 402 VAL LYS SER ILE LYS ALA ALA SER SER THR GLU LYS PHE
SEQRES 22 A 402 PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU VAL CYS TRP
SEQRES 23 A 402 GLN ALA GLY THR THR PRO TRP ASN ILE PHE PRO VAL ILE
SEQRES 24 A 402 SER LEU TYR LEU MET GLY GLU VAL THR ASN GLN SER PHE
SEQRES 25 A 402 ARG ILE THR ILE LEU PRO GLN GLN TYR LEU ARG PRO VAL
SEQRES 26 A 402 GLU ASP VAL ALA THR SER GLN ASP ASP CYS TYR LYS PHE
SEQRES 27 A 402 ALA ILE SER GLN SER SER THR GLY THR VAL MET GLY ALA
SEQRES 28 A 402 VAL ILE MET GLU GLY PHE TYR VAL VAL PHE ASP ARG ALA
SEQRES 29 A 402 ARG LYS ARG ILE GLY PHE ALA VAL SER ALA CYS HIS VAL
SEQRES 30 A 402 HIS ASP GLU PHE ARG THR ALA ALA VAL GLU GLY PRO PHE
SEQRES 31 A 402 VAL THR LEU ASP MET GLU ASP CYS GLY TYR ASN ILE
SEQRES 1 B 402 GLY PRO ASP GLU GLU PRO GLU GLU PRO GLY ARG ARG GLY
SEQRES 2 B 402 SER PHE VAL GLU MET VAL ASP ASN LEU ARG GLY LYS SER
SEQRES 3 B 402 GLY GLN GLY TYR TYR VAL GLU MET THR VAL GLY SER PRO
SEQRES 4 B 402 PRO GLN THR LEU ASN ILE LEU VAL ASP THR GLY SER SER
SEQRES 5 B 402 ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO PHE LEU HIS
SEQRES 6 B 402 ARG TYR TYR GLN ARG GLN LEU SER SER THR TYR ARG ASP
SEQRES 7 B 402 LEU ARG LYS GLY VAL TYR VAL PRO TYR THR GLN GLY LYS
SEQRES 8 B 402 TRP GLU GLY GLU LEU GLY THR ASP LEU VAL SER ILE PRO
SEQRES 9 B 402 HIS GLY PRO ASN VAL THR VAL ARG ALA ASN ILE ALA ALA
SEQRES 10 B 402 ILE THR GLU SER ASP LYS PHE PHE ILE ASN GLY SER ASN
SEQRES 11 B 402 TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA GLU ILE ALA
SEQRES 12 B 402 ARG PRO ASP ASP SER LEU GLU PRO PHE PHE ASP SER LEU
SEQRES 13 B 402 VAL LYS GLN THR HIS VAL PRO ASN LEU PHE SER LEU GLN
SEQRES 14 B 402 LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN SER GLU VAL
SEQRES 15 B 402 LEU ALA SER VAL GLY GLY SER MET ILE ILE GLY GLY ILE
SEQRES 16 B 402 ASP HIS SER LEU TYR THR GLY SER LEU TRP TYR THR PRO
SEQRES 17 B 402 ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE ILE VAL ARG
SEQRES 18 B 402 VAL GLU ILE ASN GLY GLN ASP LEU LYS MET ASP CYS LYS
SEQRES 19 B 402 GLU TYR ASN TYR ASP LYS SER ILE VAL ASP SER GLY THR
SEQRES 20 B 402 THR ASN LEU ARG LEU PRO LYS LYS VAL PHE GLU ALA ALA
SEQRES 21 B 402 VAL LYS SER ILE LYS ALA ALA SER SER THR GLU LYS PHE
SEQRES 22 B 402 PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU VAL CYS TRP
SEQRES 23 B 402 GLN ALA GLY THR THR PRO TRP ASN ILE PHE PRO VAL ILE
SEQRES 24 B 402 SER LEU TYR LEU MET GLY GLU VAL THR ASN GLN SER PHE
SEQRES 25 B 402 ARG ILE THR ILE LEU PRO GLN GLN TYR LEU ARG PRO VAL
SEQRES 26 B 402 GLU ASP VAL ALA THR SER GLN ASP ASP CYS TYR LYS PHE
SEQRES 27 B 402 ALA ILE SER GLN SER SER THR GLY THR VAL MET GLY ALA
SEQRES 28 B 402 VAL ILE MET GLU GLY PHE TYR VAL VAL PHE ASP ARG ALA
SEQRES 29 B 402 ARG LYS ARG ILE GLY PHE ALA VAL SER ALA CYS HIS VAL
SEQRES 30 B 402 HIS ASP GLU PHE ARG THR ALA ALA VAL GLU GLY PRO PHE
SEQRES 31 B 402 VAL THR LEU ASP MET GLU ASP CYS GLY TYR ASN ILE
SEQRES 1 C 402 GLY PRO ASP GLU GLU PRO GLU GLU PRO GLY ARG ARG GLY
SEQRES 2 C 402 SER PHE VAL GLU MET VAL ASP ASN LEU ARG GLY LYS SER
SEQRES 3 C 402 GLY GLN GLY TYR TYR VAL GLU MET THR VAL GLY SER PRO
SEQRES 4 C 402 PRO GLN THR LEU ASN ILE LEU VAL ASP THR GLY SER SER
SEQRES 5 C 402 ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO PHE LEU HIS
SEQRES 6 C 402 ARG TYR TYR GLN ARG GLN LEU SER SER THR TYR ARG ASP
SEQRES 7 C 402 LEU ARG LYS GLY VAL TYR VAL PRO TYR THR GLN GLY LYS
SEQRES 8 C 402 TRP GLU GLY GLU LEU GLY THR ASP LEU VAL SER ILE PRO
SEQRES 9 C 402 HIS GLY PRO ASN VAL THR VAL ARG ALA ASN ILE ALA ALA
SEQRES 10 C 402 ILE THR GLU SER ASP LYS PHE PHE ILE ASN GLY SER ASN
SEQRES 11 C 402 TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA GLU ILE ALA
SEQRES 12 C 402 ARG PRO ASP ASP SER LEU GLU PRO PHE PHE ASP SER LEU
SEQRES 13 C 402 VAL LYS GLN THR HIS VAL PRO ASN LEU PHE SER LEU GLN
SEQRES 14 C 402 LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN SER GLU VAL
SEQRES 15 C 402 LEU ALA SER VAL GLY GLY SER MET ILE ILE GLY GLY ILE
SEQRES 16 C 402 ASP HIS SER LEU TYR THR GLY SER LEU TRP TYR THR PRO
SEQRES 17 C 402 ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE ILE VAL ARG
SEQRES 18 C 402 VAL GLU ILE ASN GLY GLN ASP LEU LYS MET ASP CYS LYS
SEQRES 19 C 402 GLU TYR ASN TYR ASP LYS SER ILE VAL ASP SER GLY THR
SEQRES 20 C 402 THR ASN LEU ARG LEU PRO LYS LYS VAL PHE GLU ALA ALA
SEQRES 21 C 402 VAL LYS SER ILE LYS ALA ALA SER SER THR GLU LYS PHE
SEQRES 22 C 402 PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU VAL CYS TRP
SEQRES 23 C 402 GLN ALA GLY THR THR PRO TRP ASN ILE PHE PRO VAL ILE
SEQRES 24 C 402 SER LEU TYR LEU MET GLY GLU VAL THR ASN GLN SER PHE
SEQRES 25 C 402 ARG ILE THR ILE LEU PRO GLN GLN TYR LEU ARG PRO VAL
SEQRES 26 C 402 GLU ASP VAL ALA THR SER GLN ASP ASP CYS TYR LYS PHE
SEQRES 27 C 402 ALA ILE SER GLN SER SER THR GLY THR VAL MET GLY ALA
SEQRES 28 C 402 VAL ILE MET GLU GLY PHE TYR VAL VAL PHE ASP ARG ALA
SEQRES 29 C 402 ARG LYS ARG ILE GLY PHE ALA VAL SER ALA CYS HIS VAL
SEQRES 30 C 402 HIS ASP GLU PHE ARG THR ALA ALA VAL GLU GLY PRO PHE
SEQRES 31 C 402 VAL THR LEU ASP MET GLU ASP CYS GLY TYR ASN ILE
HET 0GT A 401 48
HET 0GT B 501 48
HET 0GT C 501 48
HETNAM 0GT (3R,4S,5S)-3-[(3-TERT-BUTYLBENZYL)AMINO]-5-{[3-(2,2-
HETNAM 2 0GT DIFLUOROETHYL)-1H-INDOL-5-YL]METHYL}TETRAHYDRO-2H-
HETNAM 3 0GT THIOPYRAN-4-OL 1,1-DIOXIDE
FORMUL 4 0GT 3(C27 H34 F2 N2 O3 S)
FORMUL 7 HOH *411(H2 O)
HELIX 1 1 SER A -2 MET A 2 5 5
HELIX 2 2 GLN A 53 SER A 57 5 5
HELIX 3 3 TYR A 123 ALA A 127 5 5
HELIX 4 4 PRO A 135 THR A 144 1 10
HELIX 5 5 ASP A 205 TYR A 211 5 7
HELIX 6 6 LYS A 227 SER A 241 1 15
HELIX 7 7 PRO A 265 PHE A 269 5 5
HELIX 8 8 LEU A 290 TYR A 294 1 5
HELIX 9 9 GLY A 323 GLU A 328 1 6
HELIX 10 10 ARG A 336 ARG A 338 5 3
HELIX 11 11 ASP A 367 GLY A 372 5 6
HELIX 12 12 SER B -2 MET B 2 5 5
HELIX 13 13 GLN B 53 SER B 57 5 5
HELIX 14 14 TYR B 123 ALA B 127 5 5
HELIX 15 15 PRO B 135 THR B 144 1 10
HELIX 16 16 ASP B 169 SER B 171 5 3
HELIX 17 17 ASP B 205 TYR B 211 5 7
HELIX 18 18 LYS B 227 SER B 242 1 16
HELIX 19 19 PRO B 247 LEU B 252 1 6
HELIX 20 20 PRO B 265 PHE B 269 5 5
HELIX 21 21 LEU B 290 TYR B 294 1 5
HELIX 22 22 GLY B 323 GLU B 328 1 6
HELIX 23 23 ASP B 367 GLY B 372 5 6
HELIX 24 24 SER C -2 VAL C 3 5 6
HELIX 25 25 GLN C 53 SER C 57 5 5
HELIX 26 26 TYR C 123 ALA C 127 5 5
HELIX 27 27 PRO C 135 THR C 144 1 10
HELIX 28 28 ASP C 169 SER C 171 5 3
HELIX 29 29 LYS C 207 TYR C 211 5 5
HELIX 30 30 LYS C 227 SER C 242 1 16
HELIX 31 31 PRO C 247 LEU C 252 1 6
HELIX 32 32 PRO C 265 PHE C 269 5 5
HELIX 33 33 LEU C 290 TYR C 294 1 5
HELIX 34 34 GLY C 323 GLU C 328 1 6
HELIX 35 35 ARG C 336 ARG C 338 5 3
HELIX 36 36 ASP C 367 GLY C 372 1 6
SHEET 1 A 9 ARG A 61 PRO A 70 0
SHEET 2 A 9 LYS A 75 SER A 86 -1 O LEU A 80 N LYS A 65
SHEET 3 A 9 TYR A 14 VAL A 20 -1 N THR A 19 O SER A 86
SHEET 4 A 9 LEU A 6 GLY A 8 -1 N ARG A 7 O TYR A 15
SHEET 5 A 9 VAL A 159 ILE A 165 -1 O VAL A 159 N GLY A 8
SHEET 6 A 9 PHE A 150 LEU A 154 -1 N GLN A 153 O SER A 162
SHEET 7 A 9 PHE A 330 ASP A 335 -1 O VAL A 332 N LEU A 152
SHEET 8 A 9 ARG A 340 SER A 346 -1 O ALA A 344 N TYR A 331
SHEET 9 A 9 TYR A 173 PRO A 181 -1 N THR A 180 O ILE A 341
SHEET 1 B13 ARG A 61 PRO A 70 0
SHEET 2 B13 LYS A 75 SER A 86 -1 O LEU A 80 N LYS A 65
SHEET 3 B13 THR A 94 ASP A 106 -1 O ILE A 99 N GLY A 81
SHEET 4 B13 PHE A 38 GLY A 41 1 N VAL A 40 O ILE A 102
SHEET 5 B13 GLY A 117 GLY A 120 -1 O ILE A 118 N ALA A 39
SHEET 6 B13 GLN A 25 ASP A 32 1 N LEU A 30 O LEU A 119
SHEET 7 B13 TYR A 14 VAL A 20 -1 N TYR A 14 O VAL A 31
SHEET 8 B13 LEU A 6 GLY A 8 -1 N ARG A 7 O TYR A 15
SHEET 9 B13 VAL A 159 ILE A 165 -1 O VAL A 159 N GLY A 8
SHEET 10 B13 PHE A 150 LEU A 154 -1 N GLN A 153 O SER A 162
SHEET 11 B13 PHE A 330 ASP A 335 -1 O VAL A 332 N LEU A 152
SHEET 12 B13 ARG A 340 SER A 346 -1 O ALA A 344 N TYR A 331
SHEET 13 B13 TYR A 173 PRO A 181 -1 N THR A 180 O ILE A 341
SHEET 1 C 5 GLU A 189 VAL A 190 0
SHEET 2 C 5 SER A 214 VAL A 216 -1 O SER A 214 N VAL A 190
SHEET 3 C 5 THR A 320 MET A 322 1 O MET A 322 N ILE A 215
SHEET 4 C 5 LEU A 223 PRO A 226 -1 N ARG A 224 O VAL A 321
SHEET 5 C 5 ILE A 313 SER A 316 1 O SER A 316 N LEU A 225
SHEET 1 D 5 GLN A 200 ASP A 201 0
SHEET 2 D 5 ILE A 192 ILE A 197 -1 N ILE A 197 O GLN A 200
SHEET 3 D 5 ILE A 272 MET A 277 -1 O SER A 273 N GLU A 196
SHEET 4 D 5 GLN A 283 ILE A 289 -1 O ILE A 289 N ILE A 272
SHEET 5 D 5 ALA A 358 VAL A 364 -1 O PHE A 363 N SER A 284
SHEET 1 E 3 VAL A 257 GLN A 260 0
SHEET 2 E 3 ASP A 306 PHE A 311 -1 O ASP A 307 N TRP A 259
SHEET 3 E 3 LEU A 295 PRO A 297 -1 N ARG A 296 O LYS A 310
SHEET 1 F 9 ARG B 61 PRO B 70 0
SHEET 2 F 9 LYS B 75 SER B 86 -1 O TRP B 76 N VAL B 69
SHEET 3 F 9 TYR B 14 VAL B 20 -1 N THR B 19 O SER B 86
SHEET 4 F 9 LEU B 6 GLY B 8 -1 N ARG B 7 O TYR B 15
SHEET 5 F 9 VAL B 159 ILE B 165 -1 O GLY B 161 N LEU B 6
SHEET 6 F 9 PHE B 150 LEU B 154 -1 N GLN B 153 O SER B 162
SHEET 7 F 9 PHE B 330 ASP B 335 -1 O VAL B 332 N LEU B 152
SHEET 8 F 9 ARG B 340 SER B 346 -1 O ALA B 344 N TYR B 331
SHEET 9 F 9 TYR B 173 PRO B 181 -1 N THR B 180 O ILE B 341
SHEET 1 G13 ARG B 61 PRO B 70 0
SHEET 2 G13 LYS B 75 SER B 86 -1 O TRP B 76 N VAL B 69
SHEET 3 G13 THR B 94 ASP B 106 -1 O ILE B 99 N GLY B 81
SHEET 4 G13 PHE B 38 GLY B 41 1 N VAL B 40 O ILE B 102
SHEET 5 G13 GLY B 117 GLY B 120 -1 O ILE B 118 N ALA B 39
SHEET 6 G13 GLN B 25 ASP B 32 1 N LEU B 30 O LEU B 119
SHEET 7 G13 TYR B 14 VAL B 20 -1 N VAL B 16 O ILE B 29
SHEET 8 G13 LEU B 6 GLY B 8 -1 N ARG B 7 O TYR B 15
SHEET 9 G13 VAL B 159 ILE B 165 -1 O GLY B 161 N LEU B 6
SHEET 10 G13 PHE B 150 LEU B 154 -1 N GLN B 153 O SER B 162
SHEET 11 G13 PHE B 330 ASP B 335 -1 O VAL B 332 N LEU B 152
SHEET 12 G13 ARG B 340 SER B 346 -1 O ALA B 344 N TYR B 331
SHEET 13 G13 TYR B 173 PRO B 181 -1 N THR B 180 O ILE B 341
SHEET 1 H 5 GLU B 189 VAL B 190 0
SHEET 2 H 5 SER B 214 VAL B 216 -1 O SER B 214 N VAL B 190
SHEET 3 H 5 THR B 320 MET B 322 1 O MET B 322 N ILE B 215
SHEET 4 H 5 LEU B 223 PRO B 226 -1 N ARG B 224 O VAL B 321
SHEET 5 H 5 ILE B 313 SER B 316 1 O SER B 316 N LEU B 225
SHEET 1 I 5 GLN B 200 ASP B 201 0
SHEET 2 I 5 ILE B 192 ILE B 197 -1 N ILE B 197 O GLN B 200
SHEET 3 I 5 ILE B 272 MET B 277 -1 O SER B 273 N GLU B 196
SHEET 4 I 5 GLN B 283 ILE B 289 -1 O ILE B 289 N ILE B 272
SHEET 5 I 5 ALA B 358 VAL B 364 -1 O PHE B 363 N SER B 284
SHEET 1 J 3 VAL B 257 GLN B 260 0
SHEET 2 J 3 ASP B 306 PHE B 311 -1 O ASP B 307 N TRP B 259
SHEET 3 J 3 LEU B 295 PRO B 297 -1 N ARG B 296 O LYS B 310
SHEET 1 K 9 ARG C 61 PRO C 70 0
SHEET 2 K 9 LYS C 75 SER C 86 -1 O LEU C 80 N LYS C 65
SHEET 3 K 9 TYR C 15 VAL C 20 -1 N THR C 19 O SER C 86
SHEET 4 K 9 LEU C 6 GLY C 8 -1 N ARG C 7 O TYR C 15
SHEET 5 K 9 VAL C 159 ILE C 165 -1 O VAL C 159 N GLY C 8
SHEET 6 K 9 PHE C 150 LEU C 154 -1 N GLN C 153 O SER C 162
SHEET 7 K 9 PHE C 330 ASP C 335 -1 O VAL C 332 N LEU C 152
SHEET 8 K 9 ARG C 340 SER C 346 -1 O ALA C 344 N TYR C 331
SHEET 9 K 9 TYR C 173 PRO C 181 -1 N THR C 180 O ILE C 341
SHEET 1 L13 ARG C 61 PRO C 70 0
SHEET 2 L13 LYS C 75 SER C 86 -1 O LEU C 80 N LYS C 65
SHEET 3 L13 VAL C 95 ASP C 106 -1 O ASP C 106 N LYS C 75
SHEET 4 L13 PHE C 38 GLY C 41 1 N VAL C 40 O ILE C 102
SHEET 5 L13 GLY C 117 GLY C 120 -1 O ILE C 118 N ALA C 39
SHEET 6 L13 GLN C 25 ASP C 32 1 N LEU C 30 O LEU C 119
SHEET 7 L13 TYR C 15 VAL C 20 -1 N VAL C 16 O ILE C 29
SHEET 8 L13 LEU C 6 GLY C 8 -1 N ARG C 7 O TYR C 15
SHEET 9 L13 VAL C 159 ILE C 165 -1 O VAL C 159 N GLY C 8
SHEET 10 L13 PHE C 150 LEU C 154 -1 N GLN C 153 O SER C 162
SHEET 11 L13 PHE C 330 ASP C 335 -1 O VAL C 332 N LEU C 152
SHEET 12 L13 ARG C 340 SER C 346 -1 O ALA C 344 N TYR C 331
SHEET 13 L13 TYR C 173 PRO C 181 -1 N THR C 180 O ILE C 341
SHEET 1 M 5 GLU C 189 VAL C 190 0
SHEET 2 M 5 SER C 214 VAL C 216 -1 O SER C 214 N VAL C 190
SHEET 3 M 5 THR C 320 MET C 322 1 O MET C 322 N ILE C 215
SHEET 4 M 5 LEU C 223 PRO C 226 -1 N ARG C 224 O VAL C 321
SHEET 5 M 5 ILE C 313 SER C 316 1 O SER C 316 N LEU C 225
SHEET 1 N 5 GLN C 200 ASP C 201 0
SHEET 2 N 5 ILE C 192 ILE C 197 -1 N ILE C 197 O GLN C 200
SHEET 3 N 5 ILE C 272 LEU C 276 -1 O SER C 273 N GLU C 196
SHEET 4 N 5 SER C 284 ILE C 289 -1 O PHE C 285 N LEU C 276
SHEET 5 N 5 ALA C 358 PHE C 363 -1 O PHE C 363 N SER C 284
SHEET 1 O 3 VAL C 257 TRP C 259 0
SHEET 2 O 3 ASP C 307 PHE C 311 -1 O ASP C 307 N TRP C 259
SHEET 3 O 3 LEU C 295 PRO C 297 -1 N ARG C 296 O LYS C 310
SSBOND 1 CYS A 155 CYS A 348 1555 1555 2.66
SSBOND 2 CYS A 206 CYS A 371 1555 1555 2.61
SSBOND 3 CYS A 258 CYS A 308 1555 1555 2.89
SSBOND 4 CYS B 155 CYS B 348 1555 1555 2.63
SSBOND 5 CYS B 206 CYS B 371 1555 1555 2.60
SSBOND 6 CYS B 258 CYS B 308 1555 1555 2.86
SSBOND 7 CYS C 155 CYS C 348 1555 1555 2.69
SSBOND 8 CYS C 206 CYS C 371 1555 1555 2.66
SSBOND 9 CYS C 258 CYS C 308 1555 1555 2.81
CISPEP 1 SER A 22 PRO A 23 0 -0.49
CISPEP 2 ARG A 128 PRO A 129 0 0.16
CISPEP 3 TYR A 211 ASP A 212 0 0.80
CISPEP 4 GLY A 361 PRO A 362 0 -1.19
CISPEP 5 SER B 22 PRO B 23 0 -0.51
CISPEP 6 ARG B 128 PRO B 129 0 -0.05
CISPEP 7 TYR B 211 ASP B 212 0 0.85
CISPEP 8 GLY B 361 PRO B 362 0 -0.51
CISPEP 9 SER C 22 PRO C 23 0 -0.54
CISPEP 10 ARG C 128 PRO C 129 0 0.02
CISPEP 11 TYR C 211 ASP C 212 0 0.44
CISPEP 12 GLY C 361 PRO C 362 0 0.47
SITE 1 AC1 21 GLY A 11 GLN A 12 GLY A 13 LEU A 30
SITE 2 AC1 21 ASP A 32 GLY A 34 SER A 35 VAL A 69
SITE 3 AC1 21 PRO A 70 TYR A 71 THR A 72 GLN A 73
SITE 4 AC1 21 PHE A 108 ILE A 110 TRP A 115 ASP A 217
SITE 5 AC1 21 GLY A 219 THR A 220 THR A 221 ARG A 224
SITE 6 AC1 21 HOH A 618
SITE 1 AC2 22 GLY B 11 GLN B 12 GLY B 13 LEU B 30
SITE 2 AC2 22 ASP B 32 GLY B 34 SER B 35 VAL B 69
SITE 3 AC2 22 PRO B 70 TYR B 71 THR B 72 GLN B 73
SITE 4 AC2 22 PHE B 108 ILE B 110 TRP B 115 TYR B 187
SITE 5 AC2 22 ASP B 217 GLY B 219 THR B 220 THR B 221
SITE 6 AC2 22 ARG B 224 HOH B 677
SITE 1 AC3 21 GLY C 11 GLN C 12 GLY C 13 LEU C 30
SITE 2 AC3 21 ASP C 32 GLY C 34 SER C 35 VAL C 69
SITE 3 AC3 21 PRO C 70 TYR C 71 THR C 72 GLN C 73
SITE 4 AC3 21 PHE C 108 ILE C 110 TRP C 115 ASP C 217
SITE 5 AC3 21 GLY C 219 THR C 220 THR C 221 ARG C 224
SITE 6 AC3 21 HOH C 694
CRYST1 81.946 102.893 100.200 90.00 103.99 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 0.012203 0.000000 0.003040 0.00000
SCALE2 0.000000 0.009719 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010285 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
