HEADER HYDROLASE 23-JAN-13 3ZKG
TITLE BACE2 MUTANT APO STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-SECRETASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: EXTRACELLULAR, RESIDUES 75-460;
COMPND 5 SYNONYM: ASPARTIC-LIKE PROTEASE 56 KDA, ASPARTYL PROTEASE 1, ASP1,
COMPND 6 ASP 1, BETA-SITE AMYLOID PRECURSOR PROTEIN CLEAVING ENZYME 2, BETA-
COMPND 7 SITE APP CLEAVING ENZYME 2, DOWN REGION ASPARTIC PROTEASE, DRAP,
COMPND 8 MEMAPSIN-1, MEMBRANE-ASSOCIATED ASPARTIC PROTEASE 1, THETA-SECRETASE,
COMPND 9 BACE2;
COMPND 10 EC: 3.4.23.45;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: 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)
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.W.BANNER,A.KUGLSTATTER,J.BENZ,M.STIHLE,A.RUF
REVDAT 3 20-DEC-23 3ZKG 1 REMARK
REVDAT 2 05-JUN-13 3ZKG 1 JRNL
REVDAT 1 29-MAY-13 3ZKG 0
JRNL AUTH D.W.BANNER,B.GSELL,J.BENZ,J.BERTSCHINGER,D.BURGER,S.BRACK,
JRNL AUTH 2 S.CUPPULERI,M.DEBULPAEP,A.GAST,D.GRABULOVSKI,M.HENNIG,
JRNL AUTH 3 H.HILPERT,W.HUBER,A.KUGLSTATTER,E.KUSZNIR,T.LAEREMANS,
JRNL AUTH 4 H.MATILE,C.MISCENIC,A.RUFER,D.SCHLATTER,J.STEYEART,M.STIHLE,
JRNL AUTH 5 R.THOMA,M.WEBER,A.RUF
JRNL TITL MAPPING THE CONFORMATIONAL SPACE ACCESSIBLE TO BACE2 USING
JRNL TITL 2 SURFACE MUTANTS AND CO-CRYSTALS WITH FAB-FRAGMENTS,
JRNL TITL 3 FYNOMERS, AND XAPERONES
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 69 1124 2013
JRNL REFN ISSN 0907-4449
JRNL PMID 23695257
JRNL DOI 10.1107/S0907444913006574
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 58113
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) : 0.231
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3101
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4217
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.88
REMARK 3 BIN R VALUE (WORKING SET) : 0.2920
REMARK 3 BIN FREE R VALUE SET COUNT : 226
REMARK 3 BIN FREE R VALUE : 0.3570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5600
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 302
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.73000
REMARK 3 B22 (A**2) : 1.18000
REMARK 3 B33 (A**2) : 0.61000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.65000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.186
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.170
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.134
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.517
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.910
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.880
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5794 ; 0.010 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 5382 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7878 ; 1.381 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12381 ; 0.773 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 720 ; 6.648 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 246 ;36.990 ;24.228
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 909 ;15.047 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;20.640 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 874 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6558 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1342 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 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. U VALUES REFINED INDIVIDUALLY.
REMARK 4
REMARK 4 3ZKG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-JAN-13.
REMARK 100 THE DEPOSITION ID IS D_1290055535.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAY-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SADABS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61792
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 32.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 2.570
REMARK 200 R MERGE (I) : 0.01000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.99
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.61
REMARK 200 R MERGE FOR SHELL (I) : 0.35000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
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 2EWY
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH8, 25% PEG3350, PH 8.0
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 44.23300
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
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 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 ALA A 13
REMARK 465 LEU A 175
REMARK 465 PRO A 176
REMARK 465 VAL A 177
REMARK 465 ALA A 178
REMARK 465 GLY A 179
REMARK 465 SER A 180
REMARK 465 GLY A 181
REMARK 465 THR A 182
REMARK 465 PRO A 268
REMARK 465 ALA A 269
REMARK 465 THR A 284
REMARK 465 ASN A 285
REMARK 465 SER A 286
REMARK 465 GLU A 287
REMARK 465 GLY A 324
REMARK 465 ALA A 325
REMARK 465 GLY A 326
REMARK 465 LEU A 327
REMARK 465 ASN A 328
REMARK 465 TYR A 329
REMARK 465 ALA A 398
REMARK 465 ALA B 13
REMARK 465 ASN B 14
REMARK 465 PHE B 15
REMARK 465 GLY B 174
REMARK 465 LEU B 175
REMARK 465 PRO B 176
REMARK 465 VAL B 177
REMARK 465 ALA B 178
REMARK 465 GLY B 179
REMARK 465 SER B 180
REMARK 465 GLY B 181
REMARK 465 THR B 182
REMARK 465 LEU B 266
REMARK 465 ILE B 267
REMARK 465 PRO B 268
REMARK 465 ALA B 269
REMARK 465 PHE B 270
REMARK 465 THR B 284
REMARK 465 ASN B 285
REMARK 465 SER B 286
REMARK 465 GLU B 287
REMARK 465 ALA B 325
REMARK 465 GLY B 326
REMARK 465 LEU B 327
REMARK 465 ASN B 328
REMARK 465 TYR B 329
REMARK 465 ALA B 398
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 2032 O HOH B 2080 2.19
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 210 -82.89 -145.81
REMARK 500 ASP A 236 -71.11 75.32
REMARK 500 SER A 265 -108.63 -102.65
REMARK 500 LEU A 266 44.73 120.69
REMARK 500 ALA B 138 -164.09 -78.99
REMARK 500 TRP B 210 -83.41 -140.53
REMARK 500 LYS B 218 136.16 -178.96
REMARK 500 ASN B 227 12.40 53.42
REMARK 500 ARG B 263 3.15 -69.22
REMARK 500 ASP B 272 -69.02 79.27
REMARK 500 PRO B 315 -39.79 -36.17
REMARK 500 MET B 323 -160.60 -111.60
REMARK 500 ASN B 341 -55.02 -166.57
REMARK 500
REMARK 500 REMARK: NULL
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 B3P A 1000
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ZKI RELATED DB: PDB
REMARK 900 BACE2 MUTANT STRUCTURE WITH LIGAND
REMARK 900 RELATED ID: 3ZKM RELATED DB: PDB
REMARK 900 BACE2 FAB COMPLEX
REMARK 900 RELATED ID: 3ZKN RELATED DB: PDB
REMARK 900 BACE2 FAB INHIBITOR COMPLEX
REMARK 900 RELATED ID: 3ZKQ RELATED DB: PDB
REMARK 900 BACE2 XAPERONE COMPLEX
REMARK 900 RELATED ID: 3ZKS RELATED DB: PDB
REMARK 900 BACE2 XAPERONE COMPLEX WITH INHIBITOR
REMARK 900 RELATED ID: 3ZKX RELATED DB: PDB
REMARK 900 TERNARY BACE2 XAPERONE COMPLEX
REMARK 900 RELATED ID: 3ZL7 RELATED DB: PDB
REMARK 900 BACE2 FYNOMER COMPLEX
REMARK 900 RELATED ID: 3ZOV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BACE-1 IN COMPLEX WITH CHEMICAL LIGAND
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE PDB FILE IS NUMBERED AFTER PDB-ENTRY 2EWY WHICH HAS
REMARK 999 NUMBERS 62 LESS THAN THE DATA BANK SEQUENCE. THE MUTATION
REMARK 999 HERE IS E269A IN THE PDB FILE AND E331A IN THE DATA BANK
REMARK 999 SEQUENCE.
DBREF 3ZKG A 13 398 UNP Q9Y5Z0 BACE2_HUMAN 75 460
DBREF 3ZKG B 13 398 UNP Q9Y5Z0 BACE2_HUMAN 75 460
SEQADV 3ZKG ALA A 269 UNP Q9Y5Z0 GLU 331 ENGINEERED MUTATION
SEQADV 3ZKG ALA B 269 UNP Q9Y5Z0 GLU 331 ENGINEERED MUTATION
SEQRES 1 A 386 ALA ASN PHE LEU ALA MET VAL ASP ASN LEU GLN GLY ASP
SEQRES 2 A 386 SER GLY ARG GLY TYR TYR LEU GLU MET LEU ILE GLY THR
SEQRES 3 A 386 PRO PRO GLN LYS LEU GLN ILE LEU VAL ASP THR GLY SER
SEQRES 4 A 386 SER ASN PHE ALA VAL ALA GLY THR PRO HIS SER TYR ILE
SEQRES 5 A 386 ASP THR TYR PHE ASP THR GLU ARG SER SER THR TYR ARG
SEQRES 6 A 386 SER LYS GLY PHE ASP VAL THR VAL LYS TYR THR GLN GLY
SEQRES 7 A 386 SER TRP THR GLY PHE VAL GLY GLU ASP LEU VAL THR ILE
SEQRES 8 A 386 PRO LYS GLY PHE ASN THR SER PHE LEU VAL ASN ILE ALA
SEQRES 9 A 386 THR ILE PHE GLU SER GLU ASN PHE PHE LEU PRO GLY ILE
SEQRES 10 A 386 LYS TRP ASN GLY ILE LEU GLY LEU ALA TYR ALA THR LEU
SEQRES 11 A 386 ALA LYS PRO SER SER SER LEU GLU THR PHE PHE ASP SER
SEQRES 12 A 386 LEU VAL THR GLN ALA ASN ILE PRO ASN VAL PHE SER MET
SEQRES 13 A 386 GLN MET CYS GLY ALA GLY LEU PRO VAL ALA GLY SER GLY
SEQRES 14 A 386 THR ASN GLY GLY SER LEU VAL LEU GLY GLY ILE GLU PRO
SEQRES 15 A 386 SER LEU TYR LYS GLY ASP ILE TRP TYR THR PRO ILE LYS
SEQRES 16 A 386 GLU GLU TRP TYR TYR GLN ILE GLU ILE LEU LYS LEU GLU
SEQRES 17 A 386 ILE GLY GLY GLN SER LEU ASN LEU ASP CYS ARG GLU TYR
SEQRES 18 A 386 ASN ALA ASP LYS ALA ILE VAL ASP SER GLY THR THR LEU
SEQRES 19 A 386 LEU ARG LEU PRO GLN LYS VAL PHE ASP ALA VAL VAL GLU
SEQRES 20 A 386 ALA VAL ALA ARG ALA SER LEU ILE PRO ALA PHE SER ASP
SEQRES 21 A 386 GLY PHE TRP THR GLY SER GLN LEU ALA CYS TRP THR ASN
SEQRES 22 A 386 SER GLU THR PRO TRP SER TYR PHE PRO LYS ILE SER ILE
SEQRES 23 A 386 TYR LEU ARG ASP GLU ASN SER SER ARG SER PHE ARG ILE
SEQRES 24 A 386 THR ILE LEU PRO GLN LEU TYR ILE GLN PRO MET MET GLY
SEQRES 25 A 386 ALA GLY LEU ASN TYR GLU CYS TYR ARG PHE GLY ILE SER
SEQRES 26 A 386 PRO SER THR ASN ALA LEU VAL ILE GLY ALA THR VAL MET
SEQRES 27 A 386 GLU GLY PHE TYR VAL ILE PHE ASP ARG ALA GLN LYS ARG
SEQRES 28 A 386 VAL GLY PHE ALA ALA SER PRO CYS ALA GLU ILE ALA GLY
SEQRES 29 A 386 ALA ALA VAL SER GLU ILE SER GLY PRO PHE SER THR GLU
SEQRES 30 A 386 ASP VAL ALA SER ASN CYS VAL PRO ALA
SEQRES 1 B 386 ALA ASN PHE LEU ALA MET VAL ASP ASN LEU GLN GLY ASP
SEQRES 2 B 386 SER GLY ARG GLY TYR TYR LEU GLU MET LEU ILE GLY THR
SEQRES 3 B 386 PRO PRO GLN LYS LEU GLN ILE LEU VAL ASP THR GLY SER
SEQRES 4 B 386 SER ASN PHE ALA VAL ALA GLY THR PRO HIS SER TYR ILE
SEQRES 5 B 386 ASP THR TYR PHE ASP THR GLU ARG SER SER THR TYR ARG
SEQRES 6 B 386 SER LYS GLY PHE ASP VAL THR VAL LYS TYR THR GLN GLY
SEQRES 7 B 386 SER TRP THR GLY PHE VAL GLY GLU ASP LEU VAL THR ILE
SEQRES 8 B 386 PRO LYS GLY PHE ASN THR SER PHE LEU VAL ASN ILE ALA
SEQRES 9 B 386 THR ILE PHE GLU SER GLU ASN PHE PHE LEU PRO GLY ILE
SEQRES 10 B 386 LYS TRP ASN GLY ILE LEU GLY LEU ALA TYR ALA THR LEU
SEQRES 11 B 386 ALA LYS PRO SER SER SER LEU GLU THR PHE PHE ASP SER
SEQRES 12 B 386 LEU VAL THR GLN ALA ASN ILE PRO ASN VAL PHE SER MET
SEQRES 13 B 386 GLN MET CYS GLY ALA GLY LEU PRO VAL ALA GLY SER GLY
SEQRES 14 B 386 THR ASN GLY GLY SER LEU VAL LEU GLY GLY ILE GLU PRO
SEQRES 15 B 386 SER LEU TYR LYS GLY ASP ILE TRP TYR THR PRO ILE LYS
SEQRES 16 B 386 GLU GLU TRP TYR TYR GLN ILE GLU ILE LEU LYS LEU GLU
SEQRES 17 B 386 ILE GLY GLY GLN SER LEU ASN LEU ASP CYS ARG GLU TYR
SEQRES 18 B 386 ASN ALA ASP LYS ALA ILE VAL ASP SER GLY THR THR LEU
SEQRES 19 B 386 LEU ARG LEU PRO GLN LYS VAL PHE ASP ALA VAL VAL GLU
SEQRES 20 B 386 ALA VAL ALA ARG ALA SER LEU ILE PRO ALA PHE SER ASP
SEQRES 21 B 386 GLY PHE TRP THR GLY SER GLN LEU ALA CYS TRP THR ASN
SEQRES 22 B 386 SER GLU THR PRO TRP SER TYR PHE PRO LYS ILE SER ILE
SEQRES 23 B 386 TYR LEU ARG ASP GLU ASN SER SER ARG SER PHE ARG ILE
SEQRES 24 B 386 THR ILE LEU PRO GLN LEU TYR ILE GLN PRO MET MET GLY
SEQRES 25 B 386 ALA GLY LEU ASN TYR GLU CYS TYR ARG PHE GLY ILE SER
SEQRES 26 B 386 PRO SER THR ASN ALA LEU VAL ILE GLY ALA THR VAL MET
SEQRES 27 B 386 GLU GLY PHE TYR VAL ILE PHE ASP ARG ALA GLN LYS ARG
SEQRES 28 B 386 VAL GLY PHE ALA ALA SER PRO CYS ALA GLU ILE ALA GLY
SEQRES 29 B 386 ALA ALA VAL SER GLU ILE SER GLY PRO PHE SER THR GLU
SEQRES 30 B 386 ASP VAL ALA SER ASN CYS VAL PRO ALA
HET B3P A1000 19
HETNAM B3P 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-
HETNAM 2 B3P PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
FORMUL 3 B3P C11 H26 N2 O6
FORMUL 4 HOH *302(H2 O)
HELIX 1 1 ASN A 14 MET A 18 5 5
HELIX 2 2 ASP A 69 SER A 73 5 5
HELIX 3 3 TYR A 139 ALA A 143 5 5
HELIX 4 4 THR A 151 ASN A 161 1 11
HELIX 5 5 GLU A 193 TYR A 197 5 5
HELIX 6 6 ASP A 229 ALA A 235 5 7
HELIX 7 7 GLN A 251 SER A 265 1 15
HELIX 8 8 SER A 271 THR A 276 1 6
HELIX 9 9 THR A 288 PHE A 293 5 6
HELIX 10 10 LEU A 314 TYR A 318 1 5
HELIX 11 11 GLY A 346 GLU A 351 1 6
HELIX 12 12 ASP B 69 SER B 73 5 5
HELIX 13 13 TYR B 139 ALA B 143 5 5
HELIX 14 14 THR B 151 ASN B 161 1 11
HELIX 15 15 GLU B 193 TYR B 197 5 5
HELIX 16 16 ASP B 229 TYR B 233 5 5
HELIX 17 17 GLN B 251 ARG B 263 1 13
HELIX 18 18 THR B 288 PHE B 293 5 6
HELIX 19 19 LEU B 314 TYR B 318 1 5
HELIX 20 20 GLY B 346 GLU B 351 1 6
SHEET 1 AA 3 ARG A 77 LYS A 86 0
SHEET 2 AA 3 SER A 91 ILE A 103 -1 O TRP A 92 N VAL A 85
SHEET 3 AA 3 GLY A 29 ILE A 36 -1 O LEU A 35 N THR A 102
SHEET 1 AB 2 ARG A 77 LYS A 86 0
SHEET 2 AB 2 SER A 91 ILE A 103 -1 O TRP A 92 N VAL A 85
SHEET 1 AC 5 GLN A 224 SER A 225 0
SHEET 2 AC 5 ILE A 216 ILE A 221 -1 O ILE A 221 N GLN A 224
SHEET 3 AC 5 ILE A 296 ARG A 301 -1 O SER A 297 N GLU A 220
SHEET 4 AC 5 ARG A 307 ILE A 313 -1 O PHE A 309 N LEU A 300
SHEET 5 AC 5 SER A 380 SER A 387 -1 O GLU A 381 N THR A 312
SHEET 1 AD 2 LYS A 237 VAL A 240 0
SHEET 2 AD 2 ALA A 342 ILE A 345 1 O LEU A 343 N ILE A 239
SHEET 1 AE 2 LEU A 247 PRO A 250 0
SHEET 2 AE 2 ILE A 336 SER A 339 1 O SER A 337 N LEU A 249
SHEET 1 AF 6 ILE A 319 PRO A 321 0
SHEET 2 AF 6 CYS A 331 PHE A 334 -1 O ARG A 333 N GLN A 320
SHEET 3 AF 6 GLN A 279 CYS A 282 -1 O ALA A 281 N TYR A 332
SHEET 4 AF 6 GLN B 279 CYS B 282 -1 O LEU B 280 N LEU A 280
SHEET 5 AF 6 CYS B 331 PHE B 334 -1 O TYR B 332 N ALA B 281
SHEET 6 AF 6 ILE B 319 PRO B 321 -1 O GLN B 320 N ARG B 333
SHEET 1 AG 2 GLU A 373 ILE A 374 0
SHEET 2 AG 2 ALA A 377 ALA A 378 -1 O ALA A 377 N ILE A 374
SHEET 1 BA 7 LEU B 22 ASP B 25 0
SHEET 2 BA 7 GLY B 29 ILE B 36 -1 O GLY B 29 N ASP B 25
SHEET 3 BA 7 GLN B 41 ASP B 48 -1 O GLN B 41 N ILE B 36
SHEET 4 BA 7 GLY B 133 GLY B 136 1 O GLY B 133 N LEU B 46
SHEET 5 BA 7 PHE B 54 ALA B 57 -1 O ALA B 55 N ILE B 134
SHEET 6 BA 7 PHE B 111 GLU B 122 1 O ALA B 116 N VAL B 56
SHEET 7 BA 7 SER B 91 THR B 102 -1 O SER B 91 N GLU B 122
SHEET 1 BB 2 LEU B 22 ASP B 25 0
SHEET 2 BB 2 GLY B 29 ILE B 36 -1 O GLY B 29 N ASP B 25
SHEET 1 BC 5 GLY B 185 LEU B 189 0
SHEET 2 BC 5 VAL B 165 MET B 170 -1 O SER B 167 N VAL B 188
SHEET 3 BC 5 PHE B 353 ASP B 358 -1 O PHE B 353 N MET B 170
SHEET 4 BC 5 ARG B 363 ALA B 368 -1 O ARG B 363 N ASP B 358
SHEET 5 BC 5 LYS B 198 PRO B 205 -1 O LYS B 198 N ALA B 368
SHEET 1 BD 3 GLN B 213 ILE B 214 0
SHEET 2 BD 3 LYS B 237 VAL B 240 -1 O ALA B 238 N ILE B 214
SHEET 3 BD 3 ALA B 342 ILE B 345 1 O LEU B 343 N ILE B 239
SHEET 1 BE 4 ILE B 216 ILE B 221 0
SHEET 2 BE 4 ILE B 296 ARG B 301 -1 O SER B 297 N GLU B 220
SHEET 3 BE 4 ARG B 307 ILE B 313 -1 O PHE B 309 N LEU B 300
SHEET 4 BE 4 SER B 380 SER B 387 -1 O GLU B 381 N THR B 312
SHEET 1 BF 2 LEU B 247 PRO B 250 0
SHEET 2 BF 2 ILE B 336 SER B 339 1 O SER B 337 N LEU B 249
SHEET 1 BG 2 GLU B 373 ILE B 374 0
SHEET 2 BG 2 ALA B 377 ALA B 378 -1 O ALA B 377 N ILE B 374
SSBOND 1 CYS A 171 CYS A 371 1555 1555 2.08
SSBOND 2 CYS A 230 CYS A 395 1555 1555 2.09
SSBOND 3 CYS A 282 CYS A 331 1555 1555 2.08
SSBOND 4 CYS B 171 CYS B 371 1555 1555 2.05
SSBOND 5 CYS B 230 CYS B 395 1555 1555 2.04
SSBOND 6 CYS B 282 CYS B 331 1555 1555 2.05
CISPEP 1 THR A 38 PRO A 39 0 -0.60
CISPEP 2 LYS A 144 PRO A 145 0 6.13
CISPEP 3 GLY A 384 PRO A 385 0 2.13
CISPEP 4 THR B 38 PRO B 39 0 -4.46
CISPEP 5 LYS B 144 PRO B 145 0 11.00
CISPEP 6 GLY B 384 PRO B 385 0 4.51
SITE 1 AC1 14 LEU A 46 ASP A 48 PHE A 124 ILE A 134
SITE 2 AC1 14 TYR A 211 GLY A 243 ARG A 248 ALA A 342
SITE 3 AC1 14 HOH A2021 HOH A2023 HOH A2073 HOH A2093
SITE 4 AC1 14 HOH A2156 HOH A2157
CRYST1 46.887 88.466 98.572 90.00 96.58 90.00 P 1 21 1 4
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 0.021328 0.000000 0.002460 0.00000
SCALE2 0.000000 0.011304 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010212 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
