HEADER HYDROLASE 24-FEB-16 5IE1
TITLE CRYSTAL STRUCTURE OF BACE1 IN COMPLEX WITH 3-(2-AMINO-6-(O-TOLYL)
TITLE 2 QUINOLIN-3-YL)-N-(3,3-DIMETHYLBUTYL)PROPANAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-SECRETASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 43-453;
COMPND 5 SYNONYM: ASPARTYL PROTEASE 2,ASP 2,BETA-SITE AMYLOID PRECURSOR
COMPND 6 PROTEIN CLEAVING ENZYME 1,BETA-SITE APP CLEAVING ENZYME 1,MEMAPSIN-2,
COMPND 7 MEMBRANE-ASSOCIATED ASPARTIC PROTEASE 2;
COMPND 8 EC: 3.4.23.46;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BACE1, BACE, KIAA1149;
SOURCE 6 EXPRESSION_SYSTEM: ENTEROBACTERIA PHAGE L1;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 268588
KEYWDS ASPARTIC PROTEASE, ALZHEIMER'S DISEASE, APP, AMYLOID PRECURSOR
KEYWDS 2 PROTEIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.B.JORDAN,D.A.WHITTINGTON,M.D.BARTBERGER,E.A.SICKMIER,K.CHEN,
AUTHOR 2 Y.CHENG,T.JUDD
REVDAT 3 11-MAY-16 5IE1 1 JRNL
REVDAT 2 20-APR-16 5IE1 1 JRNL
REVDAT 1 30-MAR-16 5IE1 0
JRNL AUTH J.B.JORDAN,D.A.WHITTINGTON,M.D.BARTBERGER,E.A.SICKMIER,
JRNL AUTH 2 K.CHEN,Y.CHENG,T.JUDD
JRNL TITL FRAGMENT-LINKING APPROACH USING (19)F NMR SPECTROSCOPY TO
JRNL TITL 2 OBTAIN HIGHLY POTENT AND SELECTIVE INHIBITORS OF
JRNL TITL 3 BETA-SECRETASE.
JRNL REF J.MED.CHEM. V. 59 3732 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 26978477
JRNL DOI 10.1021/ACS.JMEDCHEM.5B01917
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.59
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 23543
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 1205
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 29.5899 - 4.7731 1.00 2728 174 0.2060 0.2250
REMARK 3 2 4.7731 - 3.7911 1.00 2587 143 0.1761 0.2223
REMARK 3 3 3.7911 - 3.3126 1.00 2552 133 0.2033 0.2541
REMARK 3 4 3.3126 - 3.0100 1.00 2546 114 0.2174 0.2488
REMARK 3 5 3.0100 - 2.7945 1.00 2538 117 0.2351 0.2640
REMARK 3 6 2.7945 - 2.6298 1.00 2513 115 0.2465 0.3036
REMARK 3 7 2.6298 - 2.4982 1.00 2476 150 0.2478 0.3302
REMARK 3 8 2.4982 - 2.3895 0.98 2421 131 0.2521 0.2855
REMARK 3 9 2.3895 - 2.2975 0.80 1977 128 0.2571 0.3198
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.580
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.08
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.01
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 2963
REMARK 3 ANGLE : 0.821 4020
REMARK 3 CHIRALITY : 0.050 433
REMARK 3 PLANARITY : 0.004 511
REMARK 3 DIHEDRAL : 15.808 1730
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5IE1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000218598.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
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 : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23699
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.298
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 11.20
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.26100
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: PHASER
REMARK 200 STARTING MODEL: IN-HOUSE MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% POLYETHYLENE GLYCOL 5000 MME, 200
REMARK 280 MM AMMONIUM IODIDE, 170 MM SODIUM CITRATE (PH 6.6), VAPOR
REMARK 280 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 56.44933
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 112.89867
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 84.67400
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 141.12333
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 28.22467
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 56.44933
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 112.89867
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 141.12333
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 84.67400
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 28.22467
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 675 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 706 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 ALA A 157
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 465 ALA A 272
REMARK 465 GLY A 273
REMARK 465 THR A 274
REMARK 465 THR A 275
REMARK 465 PRO A 276
REMARK 465 TRP A 277
REMARK 465 ASN A 278
REMARK 465 GLU A 310
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 ASP A 317
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: 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 SER A 328 O HOH A 501 2.17
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 LEU A 267 CA - CB - CG ANGL. DEV. = 19.2 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 THR A 72 93.28 -67.72
REMARK 500 GLN A 73 -7.65 71.50
REMARK 500 HIS A 89 42.25 -98.11
REMARK 500 TRP A 197 -79.13 -137.33
REMARK 500 ARG A 205 143.08 -170.62
REMARK 500 ASP A 223 -70.59 75.58
REMARK 500 SER A 252 51.46 -110.64
REMARK 500 ALA A 323 35.12 -99.58
REMARK 500 ASP A 363 -167.75 -79.42
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 IOD A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6BS A 407
DBREF 5IE1 A -18 392 UNP P56817 BACE1_HUMAN 43 453
SEQADV 5IE1 LYS A -5 UNP P56817 ARG 56 CONFLICT
SEQADV 5IE1 LYS A -4 UNP P56817 ARG 57 CONFLICT
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 IOD A 403 1
HET IOD A 404 1
HET GOL A 405 6
HET GOL A 406 6
HET 6BS A 407 29
HETNAM IOD IODIDE ION
HETNAM GOL GLYCEROL
HETNAM 6BS 3-[2-AMINO-6-(2-METHYLPHENYL)QUINOLIN-3-YL]-N-(3,3-
HETNAM 2 6BS DIMETHYLBUTYL)PROPANAMIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 IOD 4(I 1-)
FORMUL 6 GOL 2(C3 H8 O3)
FORMUL 8 6BS C25 H31 N3 O
FORMUL 9 HOH *215(H2 O)
HELIX 1 AA1 PHE A -1 VAL A 3 5 5
HELIX 2 AA2 GLN A 53 SER A 57 5 5
HELIX 3 AA3 TYR A 123 ALA A 127 5 5
HELIX 4 AA4 PRO A 135 THR A 144 1 10
HELIX 5 AA5 ASP A 180 SER A 182 5 3
HELIX 6 AA6 ASP A 216 ASN A 221 1 6
HELIX 7 AA7 LYS A 238 SER A 252 1 15
HELIX 8 AA8 ASP A 259 GLY A 264 5 6
HELIX 9 AA9 LEU A 301 LEU A 306 1 6
HELIX 10 AB1 GLY A 334 GLU A 339 1 6
HELIX 11 AB2 MET A 379 GLY A 383 5 5
SHEET 1 AA1 9 ARG A 61 PRO A 70 0
SHEET 2 AA1 9 LYS A 75 SER A 86 -1 O LEU A 80 N LYS A 65
SHEET 3 AA1 9 TYR A 14 VAL A 20 -1 N THR A 19 O SER A 86
SHEET 4 AA1 9 LEU A 6 LYS A 9 -1 N ARG A 7 O TYR A 15
SHEET 5 AA1 9 SER A 169 ILE A 176 -1 O VAL A 170 N GLY A 8
SHEET 6 AA1 9 PHE A 150 CYS A 155 -1 N CYS A 155 O GLY A 171
SHEET 7 AA1 9 PHE A 341 ASP A 346 -1 O PHE A 345 N PHE A 150
SHEET 8 AA1 9 ARG A 351 SER A 357 -1 O ALA A 355 N TYR A 342
SHEET 9 AA1 9 TYR A 184 PRO A 192 -1 N THR A 191 O ILE A 352
SHEET 1 AA213 ARG A 61 PRO A 70 0
SHEET 2 AA213 LYS A 75 SER A 86 -1 O LEU A 80 N LYS A 65
SHEET 3 AA213 VAL A 95 ASP A 106 -1 O ILE A 99 N GLY A 81
SHEET 4 AA213 PHE A 38 GLY A 41 1 N VAL A 40 O ILE A 102
SHEET 5 AA213 GLY A 117 GLY A 120 -1 O ILE A 118 N ALA A 39
SHEET 6 AA213 GLN A 25 ASP A 32 1 N LEU A 30 O LEU A 119
SHEET 7 AA213 TYR A 14 VAL A 20 -1 N TYR A 14 O VAL A 31
SHEET 8 AA213 LEU A 6 LYS A 9 -1 N ARG A 7 O TYR A 15
SHEET 9 AA213 SER A 169 ILE A 176 -1 O VAL A 170 N GLY A 8
SHEET 10 AA213 PHE A 150 CYS A 155 -1 N CYS A 155 O GLY A 171
SHEET 11 AA213 PHE A 341 ASP A 346 -1 O PHE A 345 N PHE A 150
SHEET 12 AA213 ARG A 351 SER A 357 -1 O ALA A 355 N TYR A 342
SHEET 13 AA213 TYR A 184 PRO A 192 -1 N THR A 191 O ILE A 352
SHEET 1 AA3 5 GLN A 211 ASP A 212 0
SHEET 2 AA3 5 ILE A 203 ILE A 208 -1 N ILE A 208 O GLN A 211
SHEET 3 AA3 5 ILE A 283 MET A 288 -1 O TYR A 286 N ARG A 205
SHEET 4 AA3 5 GLN A 294 ILE A 300 -1 O ILE A 298 N LEU A 285
SHEET 5 AA3 5 ALA A 369 VAL A 375 -1 O GLU A 371 N ARG A 297
SHEET 1 AA4 4 SER A 225 VAL A 227 0
SHEET 2 AA4 4 THR A 331 MET A 333 1 O MET A 333 N ILE A 226
SHEET 3 AA4 4 LEU A 234 PRO A 237 -1 N ARG A 235 O VAL A 332
SHEET 4 AA4 4 ILE A 324 SER A 327 1 O SER A 325 N LEU A 236
SSBOND 1 CYS A 155 CYS A 359 1555 1555 2.04
SSBOND 2 CYS A 217 CYS A 382 1555 1555 2.03
SSBOND 3 CYS A 269 CYS A 319 1555 1555 2.03
CISPEP 1 SER A 22 PRO A 23 0 -1.63
CISPEP 2 ARG A 128 PRO A 129 0 3.08
CISPEP 3 GLY A 372 PRO A 373 0 -3.03
SITE 1 AC1 1 SER A 105
SITE 1 AC2 1 LYS A 107
SITE 1 AC3 1 ARG A 96
SITE 1 AC4 1 ARG A 349
SITE 1 AC5 8 LYS A 9 GLY A 11 GLY A 13 VAL A 170
SITE 2 AC5 8 SER A 229 THR A 231 THR A 232 ALA A 335
SITE 1 AC6 7 ARG A 50 TYR A 51 GLN A 53 SER A 187
SITE 2 AC6 7 HOH A 518 HOH A 544 HOH A 596
SITE 1 AC7 11 ASP A 32 GLY A 34 SER A 35 TYR A 71
SITE 2 AC7 11 LYS A 75 TRP A 76 PHE A 108 ILE A 118
SITE 3 AC7 11 ARG A 128 TYR A 198 ASP A 228
CRYST1 102.494 102.494 169.348 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 0.009757 0.005633 0.000000 0.00000
SCALE2 0.000000 0.011266 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005905 0.00000
(ATOM LINES ARE NOT SHOWN.)
END