HEADER HYDROLASE 02-JAN-07 2OF0
TITLE X-RAY CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH COMPOUND 5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-SECRETASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PROTEASE DOMAIN;
COMPND 5 SYNONYM: BETA-SITE APP CLEAVING ENZYME 1, BETA-SITE AMYLOID PRECURSOR
COMPND 6 PROTEIN CLEAVING ENZYME 1, MEMBRANE-ASSOCIATED ASPARTIC PROTEASE 2,
COMPND 7 MEMAPSIN-2, ASPARTYL PROTEASE 2, ASP 2, ASP2;
COMPND 8 EC: 3.4.23.46;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: 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;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
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: PET
KEYWDS ALTERNATIVE SPLICING, ALZHEIMER'S DISEASE, ASPARTIC PROTEASE,
KEYWDS 2 ASPARTYL PROTEASE, BASE, BETA-SECRETASE, GLYCOPROTEIN, HYDROLASE,
KEYWDS 3 MEMAPSIN 2, TRANSMEMBRANE, ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.PATEL
REVDAT 6 30-AUG-23 2OF0 1 REMARK
REVDAT 5 20-OCT-21 2OF0 1 REMARK SEQADV
REVDAT 4 18-OCT-17 2OF0 1 REMARK
REVDAT 3 24-FEB-09 2OF0 1 VERSN
REVDAT 2 01-MAY-07 2OF0 1 JRNL
REVDAT 1 13-MAR-07 2OF0 0
JRNL AUTH C.W.MURRAY,O.CALLAGHAN,G.CHESSARI,A.CLEASBY,M.CONGREVE,
JRNL AUTH 2 M.FREDERICKSON,M.J.HARTSHORN,R.MCMENAMIN,S.PATEL,N.WALLIS
JRNL TITL APPLICATION OF FRAGMENT SCREENING BY X-RAY CRYSTALLOGRAPHY
JRNL TITL 2 TO BETA-SECRETASE.
JRNL REF J.MED.CHEM. V. 50 1116 2007
JRNL REFN ISSN 0022-2623
JRNL PMID 17315856
JRNL DOI 10.1021/JM0611962
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019C
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 23631
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) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1278
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1420
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.15
REMARK 3 BIN R VALUE (WORKING SET) : 0.2830
REMARK 3 BIN FREE R VALUE SET COUNT : 90
REMARK 3 BIN FREE R VALUE : 0.3320
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2966
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 179
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.37000
REMARK 3 B22 (A**2) : -0.37000
REMARK 3 B33 (A**2) : 0.56000
REMARK 3 B12 (A**2) : -0.19000
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): 0.272
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.236
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.174
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.964
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3052 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2027 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4150 ; 1.407 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4915 ; 0.890 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 375 ; 6.986 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 137 ;36.126 ;24.015
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 488 ;14.774 ;15.092
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;12.739 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 453 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3404 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 637 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 634 ; 0.193 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2118 ; 0.204 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1496 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1566 ; 0.089 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 46 ; 0.147 ; 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 ; 0.188 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 66 ; 0.251 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.113 ; 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): 1871 ; 0.055 ; 5.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 767 ; 0.021 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3025 ; 0.076 ; 6.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1181 ; 0.073 ; 6.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1125 ; 0.089 ; 7.500
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2OF0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-07.
REMARK 100 THE DEPOSITION ID IS D_1000041052.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-OCT-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.6
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 RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54180
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24904
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 38.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: C-SEARCH (IN-HOUSE MR PROGRAM
REMARK 200 STARTING MODEL: PDB ENTRY 1W50
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-22.5% (W/V) PEG 5000
REMARK 280 MONOMETHYLETHER (MME), 200 MM SODIUM CITRATE (PH 6.6), 200 MM
REMARK 280 AMMONIUM IODIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.41233
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 112.82467
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 84.61850
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 141.03083
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 28.20617
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 56.41233
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 112.82467
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 141.03083
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 84.61850
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 28.20617
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER
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 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 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 ARG A -16
REMARK 465 GLU A -15
REMARK 465 THR 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 LYS A -5
REMARK 465 LYS A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 GLY A 158
REMARK 465 PHE A 159
REMARK 465 PRO A 160
REMARK 465 LEU A 161
REMARK 465 ASN A 162
REMARK 465 GLN A 163
REMARK 465 SER A 164
REMARK 465 GLU A 165
REMARK 465 VAL A 166
REMARK 465 LEU A 167
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 7 NE CZ NH1 NH2
REMARK 480 ARG A 64 NE CZ NH1 NH2
REMARK 480 GLN A 271 CG CD OE1 NE2
REMARK 480 ASP A 381 CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG A 64 CD ARG A 64 NE -0.265
REMARK 500
REMARK 500 REMARK: NULL
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 A 64 CG - CD - NE ANGL. DEV. = 18.7 DEGREES
REMARK 500 ARG A 64 CD - NE - CZ ANGL. DEV. = 9.2 DEGREES
REMARK 500 GLN A 271 CA - CB - CG ANGL. DEV. = 14.7 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 HIS A 89 44.62 -103.82
REMARK 500 TRP A 197 -84.66 -142.88
REMARK 500 ASN A 209 -2.10 71.45
REMARK 500 ASP A 216 103.85 -48.99
REMARK 500 ASN A 293 11.56 59.45
REMARK 500 ALA A 358 -8.87 -56.83
REMARK 500 ASP A 363 -142.04 -123.22
REMARK 500 PHE A 365 -92.70 -88.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 7 0.08 SIDE CHAIN
REMARK 500 ARG A 64 0.08 SIDE CHAIN
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 IOD A 386
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 387
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 388
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 389
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMZ A 390
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2OHK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH 1-AMINO-
REMARK 900 ISOQUINOLINE
REMARK 900 RELATED ID: 2OHL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH 2-AMINOQUINOLINE
REMARK 900 RELATED ID: 2OHM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH 2,3-
REMARK 900 DIAMINOPYRIDINE
REMARK 900 RELATED ID: 2OHN RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH COMPOUND 4
REMARK 900 RELATED ID: 2OHP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH COMPOUND 3
REMARK 900 RELATED ID: 2OHQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH COMPOUND 4
REMARK 900 RELATED ID: 2OHR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH COMPOUND 6A
REMARK 900 RELATED ID: 2OHS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH COMPOUND 6B
REMARK 900 RELATED ID: 2OHT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH COMPOUND 7
REMARK 900 RELATED ID: 2OHU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH COMPOUND 8B
DBREF 2OF0 A -16 385 UNP P56817 BACE1_HUMAN 45 446
SEQADV 2OF0 LYS A -5 UNP P56817 ARG 56 ENGINEERED MUTATION
SEQADV 2OF0 LYS A -4 UNP P56817 ARG 57 ENGINEERED MUTATION
SEQRES 1 A 402 ARG GLU THR ASP GLU GLU PRO GLU GLU PRO GLY LYS LYS
SEQRES 2 A 402 GLY SER PHE VAL GLU MET VAL ASP ASN LEU ARG GLY LYS
SEQRES 3 A 402 SER GLY GLN GLY TYR TYR VAL GLU MET THR VAL GLY SER
SEQRES 4 A 402 PRO PRO GLN THR LEU ASN ILE LEU VAL ASP THR GLY SER
SEQRES 5 A 402 SER ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO PHE LEU
SEQRES 6 A 402 HIS ARG TYR TYR GLN ARG GLN LEU SER SER THR TYR ARG
SEQRES 7 A 402 ASP LEU ARG LYS GLY VAL TYR VAL PRO TYR THR GLN GLY
SEQRES 8 A 402 LYS TRP GLU GLY GLU LEU GLY THR ASP LEU VAL SER ILE
SEQRES 9 A 402 PRO HIS GLY PRO ASN VAL THR VAL ARG ALA ASN ILE ALA
SEQRES 10 A 402 ALA ILE THR GLU SER ASP LYS PHE PHE ILE ASN GLY SER
SEQRES 11 A 402 ASN TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA GLU ILE
SEQRES 12 A 402 ALA ARG PRO ASP ASP SER LEU GLU PRO PHE PHE ASP SER
SEQRES 13 A 402 LEU VAL LYS GLN THR HIS VAL PRO ASN LEU PHE SER LEU
SEQRES 14 A 402 GLN LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN SER GLU
SEQRES 15 A 402 VAL LEU ALA SER VAL GLY GLY SER MET ILE ILE GLY GLY
SEQRES 16 A 402 ILE ASP HIS SER LEU TYR THR GLY SER LEU TRP TYR THR
SEQRES 17 A 402 PRO ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE ILE VAL
SEQRES 18 A 402 ARG VAL GLU ILE ASN GLY GLN ASP LEU LYS MET ASP CYS
SEQRES 19 A 402 LYS GLU TYR ASN TYR ASP LYS SER ILE VAL ASP SER GLY
SEQRES 20 A 402 THR THR ASN LEU ARG LEU PRO LYS LYS VAL PHE GLU ALA
SEQRES 21 A 402 ALA VAL LYS SER ILE LYS ALA ALA SER SER THR GLU LYS
SEQRES 22 A 402 PHE PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU VAL CYS
SEQRES 23 A 402 TRP GLN ALA GLY THR THR PRO TRP ASN ILE PHE PRO VAL
SEQRES 24 A 402 ILE SER LEU TYR LEU MET GLY GLU VAL THR ASN GLN SER
SEQRES 25 A 402 PHE ARG ILE THR ILE LEU PRO GLN GLN TYR LEU ARG PRO
SEQRES 26 A 402 VAL GLU ASP VAL ALA THR SER GLN ASP ASP CYS TYR LYS
SEQRES 27 A 402 PHE ALA ILE SER GLN SER SER THR GLY THR VAL MET GLY
SEQRES 28 A 402 ALA VAL ILE MET GLU GLY PHE TYR VAL VAL PHE ASP ARG
SEQRES 29 A 402 ALA ARG LYS ARG ILE GLY PHE ALA VAL SER ALA CYS HIS
SEQRES 30 A 402 VAL HIS ASP GLU PHE ARG THR ALA ALA VAL GLU GLY PRO
SEQRES 31 A 402 PHE VAL THR LEU ASP MET GLU ASP CYS GLY TYR ASN
HET IOD A 386 1
HET IOD A 387 1
HET IOD A 388 1
HET DMS A 389 4
HET CMZ A 390 19
HETNAM IOD IODIDE ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM CMZ (2S)-1-(2,5-DIMETHYLPHENOXY)-3-MORPHOLIN-4-YLPROPAN-2-
HETNAM 2 CMZ OL
HETSYN CMZ (S)-1-(2,5-DIMETHYLPHENOXY)-3-MORPHOLINOPROPAN-2-OL
FORMUL 2 IOD 3(I 1-)
FORMUL 5 DMS C2 H6 O S
FORMUL 6 CMZ C15 H23 N O3
FORMUL 7 HOH *179(H2 O)
HELIX 1 1 GLN A 53 SER A 57 5 5
HELIX 2 2 TYR A 123 ALA A 127 5 5
HELIX 3 3 PRO A 135 GLN A 143 1 9
HELIX 4 4 ASP A 180 SER A 182 5 3
HELIX 5 5 ASP A 216 ASN A 221 1 6
HELIX 6 6 LYS A 238 SER A 252 1 15
HELIX 7 7 PRO A 258 LEU A 263 1 6
HELIX 8 8 PRO A 276 PHE A 280 5 5
HELIX 9 9 LEU A 301 TYR A 305 1 5
HELIX 10 10 GLY A 334 GLU A 339 1 6
HELIX 11 11 ARG A 347 ARG A 349 5 3
HELIX 12 12 MET A 379 GLY A 383 5 5
SHEET 1 A 9 ARG A 61 TYR A 71 0
SHEET 2 A 9 GLY A 74 SER A 86 -1 O TRP A 76 N VAL A 69
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 LYS A 9 -1 N ARG A 7 O TYR A 15
SHEET 5 A 9 SER A 169 ILE A 176 -1 O GLY A 172 N LEU A 6
SHEET 6 A 9 PHE A 150 LEU A 154 -1 N GLN A 153 O SER A 173
SHEET 7 A 9 PHE A 341 ASP A 346 -1 O PHE A 345 N PHE A 150
SHEET 8 A 9 ARG A 351 SER A 357 -1 O GLY A 353 N VAL A 344
SHEET 9 A 9 TYR A 184 PRO A 192 -1 N TRP A 189 O PHE A 354
SHEET 1 B13 ARG A 61 TYR A 71 0
SHEET 2 B13 GLY A 74 SER A 86 -1 O TRP A 76 N VAL A 69
SHEET 3 B13 VAL A 95 ASP A 106 -1 O ASP A 106 N LYS A 75
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 LYS A 9 -1 N ARG A 7 O TYR A 15
SHEET 9 B13 SER A 169 ILE A 176 -1 O GLY A 172 N LEU A 6
SHEET 10 B13 PHE A 150 LEU A 154 -1 N GLN A 153 O SER A 173
SHEET 11 B13 PHE A 341 ASP A 346 -1 O PHE A 345 N PHE A 150
SHEET 12 B13 ARG A 351 SER A 357 -1 O GLY A 353 N VAL A 344
SHEET 13 B13 TYR A 184 PRO A 192 -1 N TRP A 189 O PHE A 354
SHEET 1 C 5 GLN A 211 ASP A 212 0
SHEET 2 C 5 ILE A 203 ILE A 208 -1 N ILE A 208 O GLN A 211
SHEET 3 C 5 ILE A 283 MET A 288 -1 O TYR A 286 N ARG A 205
SHEET 4 C 5 GLN A 294 ILE A 300 -1 O ILE A 298 N LEU A 285
SHEET 5 C 5 ALA A 369 VAL A 375 -1 O ALA A 369 N THR A 299
SHEET 1 D 4 SER A 225 VAL A 227 0
SHEET 2 D 4 THR A 331 MET A 333 1 O MET A 333 N ILE A 226
SHEET 3 D 4 LEU A 234 PRO A 237 -1 N ARG A 235 O VAL A 332
SHEET 4 D 4 ILE A 324 SER A 327 1 O SER A 325 N LEU A 236
SHEET 1 E 3 VAL A 268 TRP A 270 0
SHEET 2 E 3 ASP A 318 PHE A 322 -1 O ASP A 318 N TRP A 270
SHEET 3 E 3 LEU A 306 PRO A 308 -1 N ARG A 307 O LYS A 321
SSBOND 1 CYS A 155 CYS A 359 1555 1555 2.04
SSBOND 2 CYS A 217 CYS A 382 1555 1555 2.06
SSBOND 3 CYS A 269 CYS A 319 1555 1555 2.05
CISPEP 1 SER A 22 PRO A 23 0 -8.15
CISPEP 2 ARG A 128 PRO A 129 0 0.83
CISPEP 3 TYR A 222 ASP A 223 0 -10.32
CISPEP 4 GLY A 372 PRO A 373 0 -2.79
SITE 1 AC1 1 SER A 105
SITE 1 AC2 2 LYS A 107 HOH A 476
SITE 1 AC3 2 GLN A 55 HOH A 550
SITE 1 AC4 5 THR A 82 ARG A 96 ASN A 98 GLN A 143
SITE 2 AC4 5 HOH A 420
SITE 1 AC5 10 LEU A 30 ASP A 32 GLY A 34 TYR A 71
SITE 2 AC5 10 GLN A 73 PHE A 108 TRP A 115 ILE A 226
SITE 3 AC5 10 ASP A 228 THR A 231
CRYST1 102.412 102.412 169.237 90.00 90.00 120.00 P 61 2 2 12
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 0.009764 0.005638 0.000000 0.00000
SCALE2 0.000000 0.011275 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005909 0.00000
(ATOM LINES ARE NOT SHOWN.)
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