HEADER HYDROLASE 05-FEB-10 3LPJ
TITLE STRUCTURE OF BACE BOUND TO SCH743641
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-SECRETASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 14-454;
COMPND 5 SYNONYM: BETA-SITE AMYLOID PRECURSOR PROTEIN CLEAVING ENZYME 1, BETA-
COMPND 6 SITE APP 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
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: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET11A
KEYWDS ALZHEIMER'S, ASPARTYL PROTEASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.STRICKLAND,J.CUMMING
REVDAT 3 01-NOV-17 3LPJ 1 REMARK
REVDAT 2 05-MAY-10 3LPJ 1 JRNL
REVDAT 1 14-APR-10 3LPJ 0
JRNL AUTH J.CUMMING,S.BABU,Y.HUANG,C.CARROL,X.CHEN,L.FAVREAU,
JRNL AUTH 2 W.GREENLEE,T.GUO,M.KENNEDY,R.KUVELKAR,T.LE,G.LI,N.MCHUGH,
JRNL AUTH 3 P.ORTH,L.OZGUR,E.PARKER,K.SAIONZ,A.STAMFORD,C.STRICKLAND,
JRNL AUTH 4 D.TADESSE,J.VOIGT,L.ZHANG,Q.ZHANG
JRNL TITL PIPERAZINE SULFONAMIDE BACE1 INHIBITORS: DESIGN, SYNTHESIS,
JRNL TITL 2 AND IN VIVO CHARACTERIZATION.
JRNL REF BIOORG.MED.CHEM.LETT. V. 20 2837 2010
JRNL REFN ISSN 0960-894X
JRNL PMID 20347593
JRNL DOI 10.1016/J.BMCL.2010.03.050
REMARK 2
REMARK 2 RESOLUTION. 1.79 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) : 1.79
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 93199
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4660
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
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) : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6112
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 108
REMARK 3 SOLVENT ATOMS : 934
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : MSI_CNX_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : MSI_CNX_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : MSI_CNX_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 4 : PARATARTRATE.PRO
REMARK 3 PARAMETER FILE 5 : PARASCH743641.PRO
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : MSI_CNX_TOPPAR:PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : MSI_CNX_TOPPAR:WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : MSI_CNX_TOPPAR:ION.TOP
REMARK 3 TOPOLOGY FILE 4 : TOPTARTRATE.PRO
REMARK 3 TOPOLOGY FILE 5 : TOPSCH743641.PRO
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3LPJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-FEB-10.
REMARK 100 THE DEPOSITION ID IS D_1000057569.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : NULL
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 RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
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 : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93259
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.790
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 43.16650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.44450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.52300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.44450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.16650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.52300
REMARK 290 SMTRY3 4 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 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
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: 3
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 MET A 0
REMARK 465 ALA A 1
REMARK 465 SER A 2
REMARK 465 MET A 3
REMARK 465 THR A 4
REMARK 465 GLY A 5
REMARK 465 GLY A 6
REMARK 465 GLN A 7
REMARK 465 GLN A 8
REMARK 465 MET A 9
REMARK 465 GLY A 10
REMARK 465 ARG A 11
REMARK 465 GLY A 12
REMARK 465 SER A 13
REMARK 465 ALA A 14
REMARK 465 GLY A 15
REMARK 465 VAL A 16
REMARK 465 LEU A 17
REMARK 465 PRO A 18
REMARK 465 ALA A 19
REMARK 465 HIS A 20
REMARK 465 GLY A 21
REMARK 465 THR A 22
REMARK 465 GLN A 23
REMARK 465 HIS A 24
REMARK 465 GLY A 25
REMARK 465 ILE A 26
REMARK 465 ARG A 27
REMARK 465 LEU A 28
REMARK 465 PRO A 29
REMARK 465 LEU A 30
REMARK 465 ARG A 31
REMARK 465 SER A 32
REMARK 465 GLY A 33
REMARK 465 LEU A 34
REMARK 465 GLY A 35
REMARK 465 GLY A 36
REMARK 465 ALA A 37
REMARK 465 PRO A 38
REMARK 465 LEU A 39
REMARK 465 GLY A 40
REMARK 465 LEU A 41
REMARK 465 ARG A 42
REMARK 465 LEU A 43
REMARK 465 PRO A 44
REMARK 465 ARG A 45
REMARK 465 GLU A 46
REMARK 465 THR A 47
REMARK 465 ASP A 48
REMARK 465 GLU A 49
REMARK 465 GLU A 50
REMARK 465 PRO A 51
REMARK 465 GLU A 52
REMARK 465 GLU A 53
REMARK 465 PRO A 54
REMARK 465 GLY A 55
REMARK 465 ARG A 56
REMARK 465 ARG A 57
REMARK 465 PRO A 448
REMARK 465 GLN A 449
REMARK 465 THR A 450
REMARK 465 ASP A 451
REMARK 465 GLU A 452
REMARK 465 SER A 453
REMARK 465 THR A 454
REMARK 465 MET B 0
REMARK 465 ALA B 1
REMARK 465 SER B 2
REMARK 465 MET B 3
REMARK 465 THR B 4
REMARK 465 GLY B 5
REMARK 465 GLY B 6
REMARK 465 GLN B 7
REMARK 465 GLN B 8
REMARK 465 MET B 9
REMARK 465 GLY B 10
REMARK 465 ARG B 11
REMARK 465 GLY B 12
REMARK 465 SER B 13
REMARK 465 ALA B 14
REMARK 465 GLY B 15
REMARK 465 VAL B 16
REMARK 465 LEU B 17
REMARK 465 PRO B 18
REMARK 465 ALA B 19
REMARK 465 HIS B 20
REMARK 465 GLY B 21
REMARK 465 THR B 22
REMARK 465 GLN B 23
REMARK 465 HIS B 24
REMARK 465 GLY B 25
REMARK 465 ILE B 26
REMARK 465 ARG B 27
REMARK 465 LEU B 28
REMARK 465 PRO B 29
REMARK 465 LEU B 30
REMARK 465 ARG B 31
REMARK 465 SER B 32
REMARK 465 GLY B 33
REMARK 465 LEU B 34
REMARK 465 GLY B 35
REMARK 465 GLY B 36
REMARK 465 ALA B 37
REMARK 465 PRO B 38
REMARK 465 LEU B 39
REMARK 465 GLY B 40
REMARK 465 LEU B 41
REMARK 465 ARG B 42
REMARK 465 LEU B 43
REMARK 465 PRO B 44
REMARK 465 ARG B 45
REMARK 465 GLU B 46
REMARK 465 THR B 47
REMARK 465 ASP B 48
REMARK 465 GLU B 49
REMARK 465 GLU B 50
REMARK 465 PRO B 51
REMARK 465 GLU B 52
REMARK 465 GLU B 53
REMARK 465 PRO B 54
REMARK 465 GLY B 55
REMARK 465 ARG B 56
REMARK 465 ARG B 57
REMARK 465 ILE B 447
REMARK 465 PRO B 448
REMARK 465 GLN B 449
REMARK 465 THR B 450
REMARK 465 ASP B 451
REMARK 465 GLU B 452
REMARK 465 SER B 453
REMARK 465 THR B 454
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 473 O HOH B 740 3645 2.17
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 150 62.91 -107.73
REMARK 500 PHE A 169 -64.86 -103.58
REMARK 500 ASP A 192 3.13 -69.00
REMARK 500 TRP A 258 -82.10 -143.63
REMARK 500 ALA A 333 122.14 -39.40
REMARK 500 THR A 375 26.90 41.27
REMARK 500 SER A 376 -167.90 -59.44
REMARK 500 ALA A 384 39.73 -93.64
REMARK 500 HIS B 150 56.01 -107.91
REMARK 500 PHE B 169 -61.63 -104.34
REMARK 500 ASP B 192 2.38 -68.34
REMARK 500 TRP B 258 -81.07 -139.36
REMARK 500 THR B 375 16.78 58.72
REMARK 500 SER B 376 -177.73 -54.60
REMARK 500 ALA B 384 40.25 -94.16
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 TLA A 455
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Z75 A 456
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TLA B 455
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Z75 B 456
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3LPI RELATED DB: PDB
REMARK 900 STRUCTURE OF BACE BOUND TO SCH745132
REMARK 900 RELATED ID: 3LPK RELATED DB: PDB
REMARK 900 STRUCTURE OF BACE BOUND TO SCH747123
DBREF 3LPJ A 14 454 UNP P56817 BACE1_HUMAN 14 454
DBREF 3LPJ B 14 454 UNP P56817 BACE1_HUMAN 14 454
SEQADV 3LPJ MET A 0 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ ALA A 1 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ SER A 2 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ MET A 3 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ THR A 4 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ GLY A 5 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ GLY A 6 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ GLN A 7 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ GLN A 8 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ MET A 9 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ GLY A 10 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ ARG A 11 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ GLY A 12 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ SER A 13 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ MET B 0 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ ALA B 1 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ SER B 2 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ MET B 3 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ THR B 4 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ GLY B 5 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ GLY B 6 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ GLN B 7 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ GLN B 8 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ MET B 9 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ GLY B 10 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ ARG B 11 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ GLY B 12 UNP P56817 EXPRESSION TAG
SEQADV 3LPJ SER B 13 UNP P56817 EXPRESSION TAG
SEQRES 1 A 455 MET ALA SER MET THR GLY GLY GLN GLN MET GLY ARG GLY
SEQRES 2 A 455 SER ALA GLY VAL LEU PRO ALA HIS GLY THR GLN HIS GLY
SEQRES 3 A 455 ILE ARG LEU PRO LEU ARG SER GLY LEU GLY GLY ALA PRO
SEQRES 4 A 455 LEU GLY LEU ARG LEU PRO ARG GLU THR ASP GLU GLU PRO
SEQRES 5 A 455 GLU GLU PRO GLY ARG ARG GLY SER PHE VAL GLU MET VAL
SEQRES 6 A 455 ASP ASN LEU ARG GLY LYS SER GLY GLN GLY TYR TYR VAL
SEQRES 7 A 455 GLU MET THR VAL GLY SER PRO PRO GLN THR LEU ASN ILE
SEQRES 8 A 455 LEU VAL ASP THR GLY SER SER ASN PHE ALA VAL GLY ALA
SEQRES 9 A 455 ALA PRO HIS PRO PHE LEU HIS ARG TYR TYR GLN ARG GLN
SEQRES 10 A 455 LEU SER SER THR TYR ARG ASP LEU ARG LYS GLY VAL TYR
SEQRES 11 A 455 VAL PRO TYR THR GLN GLY LYS TRP GLU GLY GLU LEU GLY
SEQRES 12 A 455 THR ASP LEU VAL SER ILE PRO HIS GLY PRO ASN VAL THR
SEQRES 13 A 455 VAL ARG ALA ASN ILE ALA ALA ILE THR GLU SER ASP LYS
SEQRES 14 A 455 PHE PHE ILE ASN GLY SER ASN TRP GLU GLY ILE LEU GLY
SEQRES 15 A 455 LEU ALA TYR ALA GLU ILE ALA ARG PRO ASP ASP SER LEU
SEQRES 16 A 455 GLU PRO PHE PHE ASP SER LEU VAL LYS GLN THR HIS VAL
SEQRES 17 A 455 PRO ASN LEU PHE SER LEU GLN LEU CYS GLY ALA GLY PHE
SEQRES 18 A 455 PRO LEU ASN GLN SER GLU VAL LEU ALA SER VAL GLY GLY
SEQRES 19 A 455 SER MET ILE ILE GLY GLY ILE ASP HIS SER LEU TYR THR
SEQRES 20 A 455 GLY SER LEU TRP TYR THR PRO ILE ARG ARG GLU TRP TYR
SEQRES 21 A 455 TYR GLU VAL ILE ILE VAL ARG VAL GLU ILE ASN GLY GLN
SEQRES 22 A 455 ASP LEU LYS MET ASP CYS LYS GLU TYR ASN TYR ASP LYS
SEQRES 23 A 455 SER ILE VAL ASP SER GLY THR THR ASN LEU ARG LEU PRO
SEQRES 24 A 455 LYS LYS VAL PHE GLU ALA ALA VAL LYS SER ILE LYS ALA
SEQRES 25 A 455 ALA SER SER THR GLU LYS PHE PRO ASP GLY PHE TRP LEU
SEQRES 26 A 455 GLY GLU GLN LEU VAL CYS TRP GLN ALA GLY THR THR PRO
SEQRES 27 A 455 TRP ASN ILE PHE PRO VAL ILE SER LEU TYR LEU MET GLY
SEQRES 28 A 455 GLU VAL THR ASN GLN SER PHE ARG ILE THR ILE LEU PRO
SEQRES 29 A 455 GLN GLN TYR LEU ARG PRO VAL GLU ASP VAL ALA THR SER
SEQRES 30 A 455 GLN ASP ASP CYS TYR LYS PHE ALA ILE SER GLN SER SER
SEQRES 31 A 455 THR GLY THR VAL MET GLY ALA VAL ILE MET GLU GLY PHE
SEQRES 32 A 455 TYR VAL VAL PHE ASP ARG ALA ARG LYS ARG ILE GLY PHE
SEQRES 33 A 455 ALA VAL SER ALA CYS HIS VAL HIS ASP GLU PHE ARG THR
SEQRES 34 A 455 ALA ALA VAL GLU GLY PRO PHE VAL THR LEU ASP MET GLU
SEQRES 35 A 455 ASP CYS GLY TYR ASN ILE PRO GLN THR ASP GLU SER THR
SEQRES 1 B 455 MET ALA SER MET THR GLY GLY GLN GLN MET GLY ARG GLY
SEQRES 2 B 455 SER ALA GLY VAL LEU PRO ALA HIS GLY THR GLN HIS GLY
SEQRES 3 B 455 ILE ARG LEU PRO LEU ARG SER GLY LEU GLY GLY ALA PRO
SEQRES 4 B 455 LEU GLY LEU ARG LEU PRO ARG GLU THR ASP GLU GLU PRO
SEQRES 5 B 455 GLU GLU PRO GLY ARG ARG GLY SER PHE VAL GLU MET VAL
SEQRES 6 B 455 ASP ASN LEU ARG GLY LYS SER GLY GLN GLY TYR TYR VAL
SEQRES 7 B 455 GLU MET THR VAL GLY SER PRO PRO GLN THR LEU ASN ILE
SEQRES 8 B 455 LEU VAL ASP THR GLY SER SER ASN PHE ALA VAL GLY ALA
SEQRES 9 B 455 ALA PRO HIS PRO PHE LEU HIS ARG TYR TYR GLN ARG GLN
SEQRES 10 B 455 LEU SER SER THR TYR ARG ASP LEU ARG LYS GLY VAL TYR
SEQRES 11 B 455 VAL PRO TYR THR GLN GLY LYS TRP GLU GLY GLU LEU GLY
SEQRES 12 B 455 THR ASP LEU VAL SER ILE PRO HIS GLY PRO ASN VAL THR
SEQRES 13 B 455 VAL ARG ALA ASN ILE ALA ALA ILE THR GLU SER ASP LYS
SEQRES 14 B 455 PHE PHE ILE ASN GLY SER ASN TRP GLU GLY ILE LEU GLY
SEQRES 15 B 455 LEU ALA TYR ALA GLU ILE ALA ARG PRO ASP ASP SER LEU
SEQRES 16 B 455 GLU PRO PHE PHE ASP SER LEU VAL LYS GLN THR HIS VAL
SEQRES 17 B 455 PRO ASN LEU PHE SER LEU GLN LEU CYS GLY ALA GLY PHE
SEQRES 18 B 455 PRO LEU ASN GLN SER GLU VAL LEU ALA SER VAL GLY GLY
SEQRES 19 B 455 SER MET ILE ILE GLY GLY ILE ASP HIS SER LEU TYR THR
SEQRES 20 B 455 GLY SER LEU TRP TYR THR PRO ILE ARG ARG GLU TRP TYR
SEQRES 21 B 455 TYR GLU VAL ILE ILE VAL ARG VAL GLU ILE ASN GLY GLN
SEQRES 22 B 455 ASP LEU LYS MET ASP CYS LYS GLU TYR ASN TYR ASP LYS
SEQRES 23 B 455 SER ILE VAL ASP SER GLY THR THR ASN LEU ARG LEU PRO
SEQRES 24 B 455 LYS LYS VAL PHE GLU ALA ALA VAL LYS SER ILE LYS ALA
SEQRES 25 B 455 ALA SER SER THR GLU LYS PHE PRO ASP GLY PHE TRP LEU
SEQRES 26 B 455 GLY GLU GLN LEU VAL CYS TRP GLN ALA GLY THR THR PRO
SEQRES 27 B 455 TRP ASN ILE PHE PRO VAL ILE SER LEU TYR LEU MET GLY
SEQRES 28 B 455 GLU VAL THR ASN GLN SER PHE ARG ILE THR ILE LEU PRO
SEQRES 29 B 455 GLN GLN TYR LEU ARG PRO VAL GLU ASP VAL ALA THR SER
SEQRES 30 B 455 GLN ASP ASP CYS TYR LYS PHE ALA ILE SER GLN SER SER
SEQRES 31 B 455 THR GLY THR VAL MET GLY ALA VAL ILE MET GLU GLY PHE
SEQRES 32 B 455 TYR VAL VAL PHE ASP ARG ALA ARG LYS ARG ILE GLY PHE
SEQRES 33 B 455 ALA VAL SER ALA CYS HIS VAL HIS ASP GLU PHE ARG THR
SEQRES 34 B 455 ALA ALA VAL GLU GLY PRO PHE VAL THR LEU ASP MET GLU
SEQRES 35 B 455 ASP CYS GLY TYR ASN ILE PRO GLN THR ASP GLU SER THR
HET TLA A 455 10
HET Z75 A 456 44
HET TLA B 455 10
HET Z75 B 456 44
HETNAM TLA L(+)-TARTARIC ACID
HETNAM Z75 N'-[(1S,2S)-2-[(2R)-4-BENZYLPIPERAZIN-2-YL]-1-(3,5-
HETNAM 2 Z75 DIFLUOROBENZYL)-2-HYDROXYETHYL]-5-METHYL-N,N-
HETNAM 3 Z75 DIPROPYLBENZENE-1,3-DICARBOXAMIDE
FORMUL 3 TLA 2(C4 H6 O6)
FORMUL 4 Z75 2(C35 H44 F2 N4 O3)
FORMUL 7 HOH *934(H2 O)
HELIX 1 1 GLN A 114 SER A 118 5 5
HELIX 2 2 TYR A 184 ALA A 188 5 5
HELIX 3 3 PRO A 196 THR A 205 1 10
HELIX 4 4 ASN A 223 SER A 230 1 8
HELIX 5 5 ASP A 241 SER A 243 5 3
HELIX 6 6 ASP A 277 TYR A 283 5 7
HELIX 7 7 LYS A 299 SER A 313 1 15
HELIX 8 8 PRO A 319 LEU A 324 1 6
HELIX 9 9 PRO A 337 PHE A 341 5 5
HELIX 10 10 LEU A 362 TYR A 366 1 5
HELIX 11 11 GLY A 395 GLU A 400 1 6
HELIX 12 12 ASP A 439 GLY A 444 5 6
HELIX 13 13 GLN B 114 SER B 118 5 5
HELIX 14 14 TYR B 184 ALA B 188 5 5
HELIX 15 15 PRO B 196 THR B 205 1 10
HELIX 16 16 ASN B 223 SER B 230 1 8
HELIX 17 17 ASP B 241 SER B 243 5 3
HELIX 18 18 ASP B 277 TYR B 283 5 7
HELIX 19 19 LYS B 299 SER B 313 1 15
HELIX 20 20 PRO B 319 LEU B 324 1 6
HELIX 21 21 PRO B 337 PHE B 341 5 5
HELIX 22 22 LEU B 362 TYR B 366 1 5
HELIX 23 23 GLY B 395 GLU B 400 1 6
HELIX 24 24 ASP B 439 GLY B 444 5 6
SHEET 1 A 8 LEU A 67 LYS A 70 0
SHEET 2 A 8 GLY A 74 VAL A 81 -1 O TYR A 76 N ARG A 68
SHEET 3 A 8 GLN A 86 ASP A 93 -1 O ILE A 90 N VAL A 77
SHEET 4 A 8 GLY A 178 GLY A 181 1 O LEU A 180 N LEU A 91
SHEET 5 A 8 PHE A 99 GLY A 102 -1 N ALA A 100 O ILE A 179
SHEET 6 A 8 THR A 155 ASP A 167 1 O ILE A 163 N VAL A 101
SHEET 7 A 8 LYS A 136 SER A 147 -1 N VAL A 146 O VAL A 156
SHEET 8 A 8 ARG A 122 PRO A 131 -1 N LYS A 126 O LEU A 141
SHEET 1 B 4 LEU A 67 LYS A 70 0
SHEET 2 B 4 GLY A 74 VAL A 81 -1 O TYR A 76 N ARG A 68
SHEET 3 B 4 LYS A 136 SER A 147 -1 O SER A 147 N THR A 80
SHEET 4 B 4 ARG A 122 PRO A 131 -1 N LYS A 126 O LEU A 141
SHEET 1 C 5 GLY A 233 ILE A 237 0
SHEET 2 C 5 PHE A 211 LEU A 215 -1 N GLN A 214 O SER A 234
SHEET 3 C 5 PHE A 402 ASP A 407 -1 O VAL A 404 N LEU A 213
SHEET 4 C 5 ARG A 412 SER A 418 -1 O GLY A 414 N VAL A 405
SHEET 5 C 5 TYR A 245 PRO A 253 -1 N THR A 252 O ILE A 413
SHEET 1 D 5 GLN A 272 ASP A 273 0
SHEET 2 D 5 ILE A 264 ILE A 269 -1 N ILE A 269 O GLN A 272
SHEET 3 D 5 ILE A 344 MET A 349 -1 O TYR A 347 N ARG A 266
SHEET 4 D 5 GLN A 355 ILE A 361 -1 O ILE A 361 N ILE A 344
SHEET 5 D 5 ALA A 430 VAL A 436 -1 O GLU A 432 N ARG A 358
SHEET 1 E 4 SER A 286 VAL A 288 0
SHEET 2 E 4 THR A 392 MET A 394 1 O MET A 394 N ILE A 287
SHEET 3 E 4 LEU A 295 PRO A 298 -1 N ARG A 296 O VAL A 393
SHEET 4 E 4 ILE A 385 SER A 388 1 O SER A 386 N LEU A 297
SHEET 1 F 3 VAL A 329 TRP A 331 0
SHEET 2 F 3 ASP A 379 PHE A 383 -1 O ASP A 379 N TRP A 331
SHEET 3 F 3 LEU A 367 VAL A 370 -1 N ARG A 368 O LYS A 382
SHEET 1 G 8 LEU B 67 LYS B 70 0
SHEET 2 G 8 GLY B 74 VAL B 81 -1 O TYR B 76 N ARG B 68
SHEET 3 G 8 GLN B 86 ASP B 93 -1 O ILE B 90 N VAL B 77
SHEET 4 G 8 GLY B 178 GLY B 181 1 O LEU B 180 N LEU B 91
SHEET 5 G 8 PHE B 99 GLY B 102 -1 N ALA B 100 O ILE B 179
SHEET 6 G 8 THR B 155 ASP B 167 1 O ILE B 163 N VAL B 101
SHEET 7 G 8 LYS B 136 SER B 147 -1 N VAL B 146 O VAL B 156
SHEET 8 G 8 ARG B 122 PRO B 131 -1 N LYS B 126 O LEU B 141
SHEET 1 H 4 LEU B 67 LYS B 70 0
SHEET 2 H 4 GLY B 74 VAL B 81 -1 O TYR B 76 N ARG B 68
SHEET 3 H 4 LYS B 136 SER B 147 -1 O SER B 147 N THR B 80
SHEET 4 H 4 ARG B 122 PRO B 131 -1 N LYS B 126 O LEU B 141
SHEET 1 I 5 GLY B 233 ILE B 237 0
SHEET 2 I 5 PHE B 211 LEU B 215 -1 N GLN B 214 O SER B 234
SHEET 3 I 5 PHE B 402 ASP B 407 -1 O VAL B 404 N LEU B 213
SHEET 4 I 5 ARG B 412 SER B 418 -1 O ALA B 416 N TYR B 403
SHEET 5 I 5 TYR B 245 PRO B 253 -1 N THR B 252 O ILE B 413
SHEET 1 J 5 GLU B 261 VAL B 262 0
SHEET 2 J 5 SER B 286 VAL B 288 -1 O SER B 286 N VAL B 262
SHEET 3 J 5 THR B 392 MET B 394 1 O MET B 394 N ILE B 287
SHEET 4 J 5 LEU B 295 PRO B 298 -1 N ARG B 296 O VAL B 393
SHEET 5 J 5 ILE B 385 SER B 388 1 O SER B 386 N LEU B 297
SHEET 1 K 5 GLN B 272 ASP B 273 0
SHEET 2 K 5 ILE B 264 ILE B 269 -1 N ILE B 269 O GLN B 272
SHEET 3 K 5 ILE B 344 MET B 349 -1 O TYR B 347 N ARG B 266
SHEET 4 K 5 GLN B 355 ILE B 361 -1 O ILE B 361 N ILE B 344
SHEET 5 K 5 ALA B 430 VAL B 436 -1 O GLU B 432 N ARG B 358
SHEET 1 L 3 VAL B 329 TRP B 331 0
SHEET 2 L 3 ASP B 379 PHE B 383 -1 O ASP B 379 N TRP B 331
SHEET 3 L 3 LEU B 367 VAL B 370 -1 N ARG B 368 O LYS B 382
SSBOND 1 CYS A 216 CYS A 420 1555 1555 2.06
SSBOND 2 CYS A 278 CYS A 443 1555 1555 2.04
SSBOND 3 CYS A 330 CYS A 380 1555 1555 2.05
SSBOND 4 CYS B 216 CYS B 420 1555 1555 2.06
SSBOND 5 CYS B 278 CYS B 443 1555 1555 2.04
SSBOND 6 CYS B 330 CYS B 380 1555 1555 2.05
CISPEP 1 SER A 83 PRO A 84 0 -0.45
CISPEP 2 ARG A 189 PRO A 190 0 0.01
CISPEP 3 TYR A 283 ASP A 284 0 8.23
CISPEP 4 GLY A 433 PRO A 434 0 -0.17
CISPEP 5 SER B 83 PRO B 84 0 -0.41
CISPEP 6 ARG B 189 PRO B 190 0 0.13
CISPEP 7 TYR B 283 ASP B 284 0 4.06
CISPEP 8 GLY B 433 PRO B 434 0 -0.08
SITE 1 AC1 9 ARG A 68 ASN A 89 HIS A 110 ARG A 111
SITE 2 AC1 9 ASN A 175 HOH A 599 HOH A 657 HOH A 672
SITE 3 AC1 9 HOH A 854
SITE 1 AC2 18 GLY A 72 LEU A 91 ASP A 93 GLY A 95
SITE 2 AC2 18 SER A 96 TYR A 132 THR A 133 GLN A 134
SITE 3 AC2 18 GLY A 135 PHE A 169 ILE A 171 TRP A 176
SITE 4 AC2 18 ILE A 187 TYR A 259 ASP A 289 GLY A 291
SITE 5 AC2 18 THR A 293 HOH A 909
SITE 1 AC3 9 ARG B 68 ASN B 89 HIS B 110 ARG B 111
SITE 2 AC3 9 ASN B 175 HOH B 557 HOH B 622 HOH B 707
SITE 3 AC3 9 HOH B 713
SITE 1 AC4 21 GLY B 72 LEU B 91 ASP B 93 GLY B 95
SITE 2 AC4 21 SER B 96 TYR B 132 THR B 133 GLN B 134
SITE 3 AC4 21 GLY B 135 LYS B 168 PHE B 169 ILE B 171
SITE 4 AC4 21 TRP B 176 ILE B 187 TYR B 259 ILE B 287
SITE 5 AC4 21 ASP B 289 GLY B 291 THR B 292 THR B 293
SITE 6 AC4 21 HOH B 852
CRYST1 86.333 89.046 130.889 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011583 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011230 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007640 0.00000
(ATOM LINES ARE NOT SHOWN.)
END