HEADER HYDROLASE/INHIBITOR 26-JUN-12 4FRJ
TITLE CRYSTAL STRUCTURE OF BACE1 IN COMPLEX WITH AMINOOXAZOLINE XANTHENE 9L
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-SECRETASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 43-453;
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;
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: BACE, BACE1, KIAA1149;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MEMBRANE PROTEIN, ALZHEIMER'S DISEASE, ASPARTIC PROTEASE, HYDROLASE-
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.WHITTINGTON,A.M.LONG
REVDAT 2 12-DEC-12 4FRJ 1 JRNL
REVDAT 1 12-SEP-12 4FRJ 0
JRNL AUTH H.HUANG,D.S.LA,A.C.CHENG,D.A.WHITTINGTON,V.F.PATEL,K.CHEN,
JRNL AUTH 2 T.A.DINEEN,O.EPSTEIN,R.GRACEFFA,D.HICKMAN,Y.H.KIANG,S.LOUIE,
JRNL AUTH 3 Y.LUO,R.C.WAHL,P.H.WEN,S.WOOD,R.T.FREMEAU
JRNL TITL STRUCTURE- AND PROPERTY-BASED DESIGN OF AMINOOXAZOLINE
JRNL TITL 2 XANTHENES AS SELECTIVE, ORALLY EFFICACIOUS, AND CNS
JRNL TITL 3 PENETRABLE BACE INHIBITORS FOR THE TREATMENT OF ALZHEIMER'S
JRNL TITL 4 DISEASE.
JRNL REF J.MED.CHEM. V. 55 9156 2012
JRNL REFN ISSN 0022-2623
JRNL PMID 22928914
JRNL DOI 10.1021/JM300598E
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 36318
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1808
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1695
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 67.96
REMARK 3 BIN R VALUE (WORKING SET) : 0.4270
REMARK 3 BIN FREE R VALUE SET COUNT : 74
REMARK 3 BIN FREE R VALUE : 0.4440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2938
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 330
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.31000
REMARK 3 B22 (A**2) : 0.31000
REMARK 3 B33 (A**2) : -0.46000
REMARK 3 B12 (A**2) : 0.15000
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): 0.148
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.137
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.088
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.109
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3056 ; 0.008 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 2045 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4156 ; 1.288 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4938 ; 0.827 ; 3.004
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 370 ; 6.555 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 138 ;32.578 ;23.768
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 481 ;13.344 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;18.479 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 450 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3398 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 650 ; 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 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4FRJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUL-12.
REMARK 100 THE RCSB ID CODE IS RCSB073265.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-08
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 FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : VARIMAX HR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36345
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 200 DATA REDUNDANCY : 8.300
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.80200
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 5000 MONOMETHYL ETHER, 200 MM
REMARK 280 AMMONIUM IODIDE, 180 MM SODIUM CITRATE (PH 6.6), VAPOR DIFFUSION,
REMARK 280 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 56.15233
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 112.30467
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 84.22850
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 140.38083
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 28.07617
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 56.15233
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 112.30467
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 140.38083
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 84.22850
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 28.07617
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 656 LIES ON A SPECIAL POSITION.
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 LEU A -18
REMARK 465 PRO A -17
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 ASP A 311
REMARK 465 VAL A 312
REMARK 465 ALA A 313
REMARK 465 THR A 314
REMARK 465 SER A 315
REMARK 465 GLN A 316
REMARK 465 ILE A 386
REMARK 465 PRO A 387
REMARK 465 GLN A 388
REMARK 465 THR A 389
REMARK 465 ASP A 390
REMARK 465 GLU A 391
REMARK 465 SER A 392
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 49.09 -106.61
REMARK 500 TRP A 197 -88.11 -141.55
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DWB A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 405
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FRI RELATED DB: PDB
REMARK 900 RELATED ID: 4FRK RELATED DB: PDB
DBREF 4FRJ A -18 392 UNP P56817 BACE1_HUMAN 43 453
SEQADV 4FRJ LYS A -5 UNP P56817 ARG 56 ENGINEERED MUTATION
SEQADV 4FRJ LYS A -4 UNP P56817 ARG 57 ENGINEERED MUTATION
SEQRES 1 A 411 LEU PRO ARG GLU THR ASP GLU GLU PRO GLU GLU PRO GLY
SEQRES 2 A 411 LYS LYS GLY SER PHE VAL GLU MET VAL ASP ASN LEU ARG
SEQRES 3 A 411 GLY LYS SER GLY GLN GLY TYR TYR VAL GLU MET THR VAL
SEQRES 4 A 411 GLY SER PRO PRO GLN THR LEU ASN ILE LEU VAL ASP THR
SEQRES 5 A 411 GLY SER SER ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO
SEQRES 6 A 411 PHE LEU HIS ARG TYR TYR GLN ARG GLN LEU SER SER THR
SEQRES 7 A 411 TYR ARG ASP LEU ARG LYS GLY VAL TYR VAL PRO TYR THR
SEQRES 8 A 411 GLN GLY LYS TRP GLU GLY GLU LEU GLY THR ASP LEU VAL
SEQRES 9 A 411 SER ILE PRO HIS GLY PRO ASN VAL THR VAL ARG ALA ASN
SEQRES 10 A 411 ILE ALA ALA ILE THR GLU SER ASP LYS PHE PHE ILE ASN
SEQRES 11 A 411 GLY SER ASN TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA
SEQRES 12 A 411 GLU ILE ALA ARG PRO ASP ASP SER LEU GLU PRO PHE PHE
SEQRES 13 A 411 ASP SER LEU VAL LYS GLN THR HIS VAL PRO ASN LEU PHE
SEQRES 14 A 411 SER LEU GLN LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN
SEQRES 15 A 411 SER GLU VAL LEU ALA SER VAL GLY GLY SER MET ILE ILE
SEQRES 16 A 411 GLY GLY ILE ASP HIS SER LEU TYR THR GLY SER LEU TRP
SEQRES 17 A 411 TYR THR PRO ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE
SEQRES 18 A 411 ILE VAL ARG VAL GLU ILE ASN GLY GLN ASP LEU LYS MET
SEQRES 19 A 411 ASP CYS LYS GLU TYR ASN TYR ASP LYS SER ILE VAL ASP
SEQRES 20 A 411 SER GLY THR THR ASN LEU ARG LEU PRO LYS LYS VAL PHE
SEQRES 21 A 411 GLU ALA ALA VAL LYS SER ILE LYS ALA ALA SER SER THR
SEQRES 22 A 411 GLU LYS PHE PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU
SEQRES 23 A 411 VAL CYS TRP GLN ALA GLY THR THR PRO TRP ASN ILE PHE
SEQRES 24 A 411 PRO VAL ILE SER LEU TYR LEU MET GLY GLU VAL THR ASN
SEQRES 25 A 411 GLN SER PHE ARG ILE THR ILE LEU PRO GLN GLN TYR LEU
SEQRES 26 A 411 ARG PRO VAL GLU ASP VAL ALA THR SER GLN ASP ASP CYS
SEQRES 27 A 411 TYR LYS PHE ALA ILE SER GLN SER SER THR GLY THR VAL
SEQRES 28 A 411 MET GLY ALA VAL ILE MET GLU GLY PHE TYR VAL VAL PHE
SEQRES 29 A 411 ASP ARG ALA ARG LYS ARG ILE GLY PHE ALA VAL SER ALA
SEQRES 30 A 411 CYS HIS VAL HIS ASP GLU PHE ARG THR ALA ALA VAL GLU
SEQRES 31 A 411 GLY PRO PHE VAL THR LEU ASP MET GLU ASP CYS GLY TYR
SEQRES 32 A 411 ASN ILE PRO GLN THR ASP GLU SER
HET IOD A 401 1
HET IOD A 402 1
HET DWB A 403 29
HET GOL A 404 6
HET DMS A 405 4
HETNAM IOD IODIDE ION
HETNAM DWB (4S)-2'-(5-CHLORO-2-FLUOROPHENYL)-7'-METHOXYSPIRO[1,3-
HETNAM 2 DWB OXAZOLE-4,9'-XANTHEN]-2-AMINE
HETNAM GOL GLYCEROL
HETNAM DMS DIMETHYL SULFOXIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 IOD 2(I 1-)
FORMUL 4 DWB C22 H16 CL F N2 O3
FORMUL 5 GOL C3 H8 O3
FORMUL 6 DMS C2 H6 O S
FORMUL 7 HOH *330(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 THR A 144 1 10
HELIX 4 4 ASP A 180 SER A 182 5 3
HELIX 5 5 ASP A 216 TYR A 222 5 7
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 ASP A 378 GLY A 383 5 6
SHEET 1 A 9 ARG A 61 TYR A 71 0
SHEET 2 A 9 GLY A 74 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 LYS A 9 -1 N ARG A 7 O TYR A 15
SHEET 5 A 9 SER A 169 ILE A 176 -1 O VAL A 170 N GLY A 8
SHEET 6 A 9 PHE A 150 GLY A 156 -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 ALA A 355 N TYR A 342
SHEET 9 A 9 TYR A 184 PRO A 192 -1 N THR A 191 O ILE A 352
SHEET 1 B13 ARG A 61 TYR A 71 0
SHEET 2 B13 GLY A 74 SER A 86 -1 O LEU A 80 N LYS A 65
SHEET 3 B13 THR A 94 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 VAL A 170 N GLY A 8
SHEET 10 B13 PHE A 150 GLY A 156 -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 ALA A 355 N TYR A 342
SHEET 13 B13 TYR A 184 PRO A 192 -1 N THR A 191 O ILE A 352
SHEET 1 C 5 GLU A 200 VAL A 201 0
SHEET 2 C 5 SER A 225 VAL A 227 -1 O SER A 225 N VAL A 201
SHEET 3 C 5 THR A 331 MET A 333 1 O MET A 333 N ILE A 226
SHEET 4 C 5 LEU A 234 PRO A 237 -1 N ARG A 235 O VAL A 332
SHEET 5 C 5 ILE A 324 SER A 327 1 O SER A 325 N LEU A 236
SHEET 1 D 5 GLN A 211 ASP A 212 0
SHEET 2 D 5 ILE A 203 ILE A 208 -1 N ILE A 208 O GLN A 211
SHEET 3 D 5 ILE A 283 MET A 288 -1 O TYR A 286 N ARG A 205
SHEET 4 D 5 GLN A 294 ILE A 300 -1 O ILE A 298 N LEU A 285
SHEET 5 D 5 ALA A 369 VAL A 375 -1 O GLU A 371 N ARG A 297
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 2.07
SSBOND 2 CYS A 217 CYS A 382 1555 1555 2.02
SSBOND 3 CYS A 269 CYS A 319 1555 1555 2.03
CISPEP 1 SER A 22 PRO A 23 0 -4.07
CISPEP 2 ARG A 128 PRO A 129 0 2.41
CISPEP 3 TYR A 222 ASP A 223 0 5.61
CISPEP 4 GLY A 372 PRO A 373 0 -2.67
SITE 1 AC1 1 SER A 105
SITE 1 AC2 1 LYS A 107
SITE 1 AC3 14 GLY A 11 GLY A 13 LEU A 30 ASP A 32
SITE 2 AC3 14 TYR A 71 PHE A 108 ILE A 110 ARG A 128
SITE 3 AC3 14 ASP A 228 SER A 229 GLY A 230 GOL A 404
SITE 4 AC3 14 HOH A 537 HOH A 598
SITE 1 AC4 11 SER A 10 GLY A 11 GLN A 12 GLY A 13
SITE 2 AC4 11 TYR A 14 VAL A 170 THR A 232 ARG A 307
SITE 3 AC4 11 ALA A 335 DWB A 403 HOH A 639
SITE 1 AC5 3 ARG A 96 ASN A 98 GLU A 134
CRYST1 101.544 101.544 168.457 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 0.009848 0.005686 0.000000 0.00000
SCALE2 0.000000 0.011371 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005936 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
