HEADER HYDROLASE/HYDROLASE INHIBITOR 22-JUN-11 3SKG
TITLE CRYSTAL STRUCTURE OF BETA-SITE APP-CLEAVING ENZYME 1 (BACE-WT) COMPLEX
TITLE 2 WITH (2S)-2-((3R)-3-ACETAMIDO-3-ISOBUTYL-2-OXO-1-PYRROLIDINYL)-N-
TITLE 3 ((1S,2R)-1-(3,5-DIFLUOROBENZYL)-2-HYDROXY-2-(1,2,3,4-TETRAHYDRO-3-
TITLE 4 ISOQUINOLINYL)ETHYL)-4-PHENYLBUTANAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-SECRETASE 1;
COMPND 3 CHAIN: A, B, D, E;
COMPND 4 FRAGMENT: UNP RESIDUES 14-454;
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
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: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS ALZHEIMER'S DISEASE, BACE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.K.MUCKELBAUER
REVDAT 4 05-DEC-12 3SKG 1 DBREF SEQADV
REVDAT 3 02-NOV-11 3SKG 1 JRNL
REVDAT 2 19-OCT-11 3SKG 1 JRNL
REVDAT 1 07-SEP-11 3SKG 0
JRNL AUTH L.A.THOMPSON,J.SHI,C.P.DECICCO,A.J.TEBBEN,R.E.OLSON,K.M.BOY,
JRNL AUTH 2 J.M.GUERNON,A.C.GOOD,A.LIAUW,C.ZHENG,R.A.COPELAND,A.P.COMBS,
JRNL AUTH 3 G.L.TRAINOR,D.M.CAMAC,J.K.MUCKELBAUER,K.A.LENTZ,J.E.GRACE,
JRNL AUTH 4 C.R.BURTON,J.H.TOYN,D.M.BARTEN,J.MARCINKEVICIENE,
JRNL AUTH 5 J.E.MEREDITH,C.F.ALBRIGHT,J.E.MACOR
JRNL TITL SYNTHESIS AND IN VIVO EVALUATION OF CYCLIC DIAMINOPROPANE
JRNL TITL 2 BACE-1 INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 21 6909 2011
JRNL REFN ISSN 0960-894X
JRNL PMID 21974952
JRNL DOI 10.1016/J.BMCL.2011.06.116
REMARK 2
REMARK 2 RESOLUTION. 2.88 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.88
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 40650
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) : 0.259
REMARK 3 R VALUE (WORKING SET) : 0.255
REMARK 3 FREE R VALUE : 0.348
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2159
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.88
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2615
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.24
REMARK 3 BIN R VALUE (WORKING SET) : 0.2940
REMARK 3 BIN FREE R VALUE SET COUNT : 142
REMARK 3 BIN FREE R VALUE : 0.4950
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12136
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 192
REMARK 3 SOLVENT ATOMS : 106
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.42000
REMARK 3 B22 (A**2) : -3.10000
REMARK 3 B33 (A**2) : 5.57000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.24000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.566
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.462
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.461
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.868
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.757
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12667 ; 0.029 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17246 ; 2.504 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1540 ; 8.835 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 572 ;37.118 ;23.916
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1980 ;21.663 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 68 ;19.529 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1900 ; 0.151 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9744 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 6494 ; 0.274 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 8319 ; 0.333 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 568 ; 0.226 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 94 ; 0.304 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.182 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 8020 ; 1.454 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12396 ; 2.269 ; 2.500
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5534 ; 2.484 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4850 ; 3.641 ; 4.500
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3SKG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUN-11.
REMARK 100 THE RCSB ID CODE IS RCSB066312.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
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+ DW
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.541
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MICROMAX CONFOCAL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 92
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42876
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.878
REMARK 200 RESOLUTION RANGE LOW (A) : 30.628
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.17200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.53200
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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.2, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 65.22550
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, 3, 4
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 350
REMARK 350 BIOMOLECULE: 3
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: D
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: 4
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: E
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 -61
REMARK 465 ALA A -60
REMARK 465 SER A -59
REMARK 465 MET A -58
REMARK 465 THR A -57
REMARK 465 GLY A -56
REMARK 465 GLY A -55
REMARK 465 GLN A -54
REMARK 465 GLN A -53
REMARK 465 MET A -52
REMARK 465 GLY A -51
REMARK 465 ARG A -50
REMARK 465 GLY A -49
REMARK 465 SER A -48
REMARK 465 ALA A -47
REMARK 465 GLY A -46
REMARK 465 VAL A -45
REMARK 465 LEU A -44
REMARK 465 PRO A -43
REMARK 465 ALA A -42
REMARK 465 HIS A -41
REMARK 465 GLY A -40
REMARK 465 THR A -39
REMARK 465 GLN A -38
REMARK 465 HIS A -37
REMARK 465 GLY A -36
REMARK 465 ILE A -35
REMARK 465 ARG A -34
REMARK 465 LEU A -33
REMARK 465 PRO A -32
REMARK 465 LEU A -31
REMARK 465 ARG A -30
REMARK 465 SER A -29
REMARK 465 GLY A -28
REMARK 465 LEU A -27
REMARK 465 GLY A -26
REMARK 465 GLY A -25
REMARK 465 ALA A -24
REMARK 465 PRO A -23
REMARK 465 LEU A -22
REMARK 465 GLY A -21
REMARK 465 LEU A -20
REMARK 465 ARG A -19
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 ARG A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 ASN A 385
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 465 THR A 393
REMARK 465 MET B -61
REMARK 465 ALA B -60
REMARK 465 SER B -59
REMARK 465 MET B -58
REMARK 465 THR B -57
REMARK 465 GLY B -56
REMARK 465 GLY B -55
REMARK 465 GLN B -54
REMARK 465 GLN B -53
REMARK 465 MET B -52
REMARK 465 GLY B -51
REMARK 465 ARG B -50
REMARK 465 GLY B -49
REMARK 465 SER B -48
REMARK 465 ALA B -47
REMARK 465 GLY B -46
REMARK 465 VAL B -45
REMARK 465 LEU B -44
REMARK 465 PRO B -43
REMARK 465 ALA B -42
REMARK 465 HIS B -41
REMARK 465 GLY B -40
REMARK 465 THR B -39
REMARK 465 GLN B -38
REMARK 465 HIS B -37
REMARK 465 GLY B -36
REMARK 465 ILE B -35
REMARK 465 ARG B -34
REMARK 465 LEU B -33
REMARK 465 PRO B -32
REMARK 465 LEU B -31
REMARK 465 ARG B -30
REMARK 465 SER B -29
REMARK 465 GLY B -28
REMARK 465 LEU B -27
REMARK 465 GLY B -26
REMARK 465 GLY B -25
REMARK 465 ALA B -24
REMARK 465 PRO B -23
REMARK 465 LEU B -22
REMARK 465 GLY B -21
REMARK 465 LEU B -20
REMARK 465 ARG B -19
REMARK 465 LEU B -18
REMARK 465 PRO B -17
REMARK 465 ARG B -16
REMARK 465 GLU B -15
REMARK 465 THR B -14
REMARK 465 ASP B -13
REMARK 465 GLU B -12
REMARK 465 GLU B -11
REMARK 465 PRO B -10
REMARK 465 GLU B -9
REMARK 465 GLU B -8
REMARK 465 PRO B -7
REMARK 465 GLY B -6
REMARK 465 ARG B -5
REMARK 465 ARG B -4
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 ASN B 385
REMARK 465 ILE B 386
REMARK 465 PRO B 387
REMARK 465 GLN B 388
REMARK 465 THR B 389
REMARK 465 ASP B 390
REMARK 465 GLU B 391
REMARK 465 SER B 392
REMARK 465 THR B 393
REMARK 465 MET D -61
REMARK 465 ALA D -60
REMARK 465 SER D -59
REMARK 465 MET D -58
REMARK 465 THR D -57
REMARK 465 GLY D -56
REMARK 465 GLY D -55
REMARK 465 GLN D -54
REMARK 465 GLN D -53
REMARK 465 MET D -52
REMARK 465 GLY D -51
REMARK 465 ARG D -50
REMARK 465 GLY D -49
REMARK 465 SER D -48
REMARK 465 ALA D -47
REMARK 465 GLY D -46
REMARK 465 VAL D -45
REMARK 465 LEU D -44
REMARK 465 PRO D -43
REMARK 465 ALA D -42
REMARK 465 HIS D -41
REMARK 465 GLY D -40
REMARK 465 THR D -39
REMARK 465 GLN D -38
REMARK 465 HIS D -37
REMARK 465 GLY D -36
REMARK 465 ILE D -35
REMARK 465 ARG D -34
REMARK 465 LEU D -33
REMARK 465 PRO D -32
REMARK 465 LEU D -31
REMARK 465 ARG D -30
REMARK 465 SER D -29
REMARK 465 GLY D -28
REMARK 465 LEU D -27
REMARK 465 GLY D -26
REMARK 465 GLY D -25
REMARK 465 ALA D -24
REMARK 465 PRO D -23
REMARK 465 LEU D -22
REMARK 465 GLY D -21
REMARK 465 LEU D -20
REMARK 465 ARG D -19
REMARK 465 LEU D -18
REMARK 465 PRO D -17
REMARK 465 ARG D -16
REMARK 465 GLU D -15
REMARK 465 THR D -14
REMARK 465 ASP D -13
REMARK 465 GLU D -12
REMARK 465 GLU D -11
REMARK 465 PRO D -10
REMARK 465 GLU D -9
REMARK 465 GLU D -8
REMARK 465 PRO D -7
REMARK 465 GLY D -6
REMARK 465 ARG D -5
REMARK 465 ARG D -4
REMARK 465 GLY D -3
REMARK 465 SER D -2
REMARK 465 ASN D 385
REMARK 465 ILE D 386
REMARK 465 PRO D 387
REMARK 465 GLN D 388
REMARK 465 THR D 389
REMARK 465 ASP D 390
REMARK 465 GLU D 391
REMARK 465 SER D 392
REMARK 465 THR D 393
REMARK 465 MET E -61
REMARK 465 ALA E -60
REMARK 465 SER E -59
REMARK 465 MET E -58
REMARK 465 THR E -57
REMARK 465 GLY E -56
REMARK 465 GLY E -55
REMARK 465 GLN E -54
REMARK 465 GLN E -53
REMARK 465 MET E -52
REMARK 465 GLY E -51
REMARK 465 ARG E -50
REMARK 465 GLY E -49
REMARK 465 SER E -48
REMARK 465 ALA E -47
REMARK 465 GLY E -46
REMARK 465 VAL E -45
REMARK 465 LEU E -44
REMARK 465 PRO E -43
REMARK 465 ALA E -42
REMARK 465 HIS E -41
REMARK 465 GLY E -40
REMARK 465 THR E -39
REMARK 465 GLN E -38
REMARK 465 HIS E -37
REMARK 465 GLY E -36
REMARK 465 ILE E -35
REMARK 465 ARG E -34
REMARK 465 LEU E -33
REMARK 465 PRO E -32
REMARK 465 LEU E -31
REMARK 465 ARG E -30
REMARK 465 SER E -29
REMARK 465 GLY E -28
REMARK 465 LEU E -27
REMARK 465 GLY E -26
REMARK 465 GLY E -25
REMARK 465 ALA E -24
REMARK 465 PRO E -23
REMARK 465 LEU E -22
REMARK 465 GLY E -21
REMARK 465 LEU E -20
REMARK 465 ARG E -19
REMARK 465 LEU E -18
REMARK 465 PRO E -17
REMARK 465 ARG E -16
REMARK 465 GLU E -15
REMARK 465 THR E -14
REMARK 465 ASP E -13
REMARK 465 GLU E -12
REMARK 465 GLU E -11
REMARK 465 PRO E -10
REMARK 465 GLU E -9
REMARK 465 GLU E -8
REMARK 465 PRO E -7
REMARK 465 GLY E -6
REMARK 465 ARG E -5
REMARK 465 ARG E -4
REMARK 465 GLY E -3
REMARK 465 SER E -2
REMARK 465 ASN E 385
REMARK 465 ILE E 386
REMARK 465 PRO E 387
REMARK 465 GLN E 388
REMARK 465 THR E 389
REMARK 465 ASP E 390
REMARK 465 GLU E 391
REMARK 465 SER E 392
REMARK 465 THR E 393
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 OD2 ASP A 228 N39 PB8 A 394 2.03
REMARK 500 N ILE E 87 O HOH E 396 2.12
REMARK 500 NH1 ARG A 349 O HOH A 417 2.16
REMARK 500 OH TYR D 15 OD1 ASN D 114 2.16
REMARK 500 OG SER A 327 O GLY A 330 2.16
REMARK 500 OD2 ASP A 318 O HOH A 418 2.16
REMARK 500 O LEU B 140 OG1 THR B 144 2.17
REMARK 500 O LYS D 238 CG GLU D 242 2.19
REMARK 500 ND2 ASN A 98 O HOH A 399 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TYR A 190 CE2 TYR A 190 CD2 0.123
REMARK 500 CYS A 217 CB CYS A 217 SG -0.105
REMARK 500 CYS A 359 CB CYS A 359 SG -0.245
REMARK 500 GLU A 364 CG GLU A 364 CD 0.136
REMARK 500 VAL B 93 CB VAL B 93 CG2 0.136
REMARK 500 GLU B 196 CG GLU B 196 CD -0.104
REMARK 500 CYS B 217 CB CYS B 217 SG -0.132
REMARK 500 VAL B 344 CB VAL B 344 CG2 -0.131
REMARK 500 CYS B 359 CB CYS B 359 SG -0.187
REMARK 500 GLU B 364 CG GLU B 364 CD 0.137
REMARK 500 GLU B 364 CD GLU B 364 OE2 0.076
REMARK 500 GLU D 200 CD GLU D 200 OE1 0.068
REMARK 500 TYR E 14 CE1 TYR E 14 CZ 0.078
REMARK 500 ASP E 62 CB ASP E 62 CG 0.131
REMARK 500 CYS E 217 CB CYS E 217 SG -0.187
REMARK 500 ASP E 311 CB ASP E 311 CG 0.126
REMARK 500 GLU E 364 CG GLU E 364 CD 0.112
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 63 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500 ARG A 96 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 96 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 LEU A 167 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500 ASP A 212 CB - CG - OD1 ANGL. DEV. = 7.8 DEGREES
REMARK 500 CYS A 359 CA - CB - SG ANGL. DEV. = -13.7 DEGREES
REMARK 500 ARG B 96 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 96 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 CYS B 217 CA - CB - SG ANGL. DEV. = -18.0 DEGREES
REMARK 500 VAL B 227 CB - CA - C ANGL. DEV. = -12.1 DEGREES
REMARK 500 LEU B 267 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 ASP B 318 CB - CG - OD1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ASP D 4 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP D 131 CB - CG - OD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 LEU D 154 CB - CG - CD1 ANGL. DEV. = 11.6 DEGREES
REMARK 500 PRO D 192 C - N - CA ANGL. DEV. = 9.0 DEGREES
REMARK 500 ARG D 297 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 PRO D 302 C - N - CA ANGL. DEV. = 10.2 DEGREES
REMARK 500 LEU D 306 CB - CG - CD1 ANGL. DEV. = -11.3 DEGREES
REMARK 500 LEU D 377 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500 ARG E 7 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 VAL E 40 CB - CA - C ANGL. DEV. = -12.2 DEGREES
REMARK 500 ASP E 62 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ARG E 64 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 LEU E 84 CB - CG - CD1 ANGL. DEV. = -10.4 DEGREES
REMARK 500 ARG E 96 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP E 138 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 CYS E 217 CA - CB - SG ANGL. DEV. = -16.1 DEGREES
REMARK 500 ARG E 235 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG E 235 NE - CZ - NH2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG E 349 NE - CZ - NH2 ANGL. DEV. = -4.3 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 VAL A 3 131.43 -35.74
REMARK 500 ASP A 4 15.33 83.74
REMARK 500 SER A 10 -62.76 -24.78
REMARK 500 SER A 36 -0.12 -142.69
REMARK 500 PRO A 44 136.05 -37.63
REMARK 500 GLN A 55 -24.71 -29.68
REMARK 500 TYR A 60 146.49 -31.77
REMARK 500 LYS A 75 139.90 -173.79
REMARK 500 HIS A 89 71.49 -101.01
REMARK 500 LYS A 107 38.54 26.93
REMARK 500 PHE A 108 -63.48 -93.32
REMARK 500 ASN A 111 117.73 -39.47
REMARK 500 ALA A 122 -156.56 -75.26
REMARK 500 ASP A 131 -9.16 -55.88
REMARK 500 THR A 144 -154.74 -148.63
REMARK 500 ARG A 195 138.20 177.96
REMARK 500 TRP A 197 -87.01 -125.52
REMARK 500 ASP A 216 109.05 -42.71
REMARK 500 CYS A 217 -65.78 -17.23
REMARK 500 ASP A 223 -74.37 65.96
REMARK 500 ALA A 272 120.53 -39.57
REMARK 500 TRP A 277 -38.68 -32.45
REMARK 500 ASN A 293 27.04 48.75
REMARK 500 ALA A 313 46.12 -145.39
REMARK 500 LYS A 350 53.51 36.12
REMARK 500 ALA A 358 21.94 -68.96
REMARK 500 VAL A 375 61.87 -109.80
REMARK 500 ASP A 378 23.30 49.48
REMARK 500 GLU A 380 -17.71 -46.28
REMARK 500 GLN B 55 -38.67 -33.60
REMARK 500 ARG B 64 61.97 37.59
REMARK 500 TYR B 71 -158.88 -98.80
REMARK 500 LYS B 75 155.20 176.40
REMARK 500 HIS B 89 68.95 -102.77
REMARK 500 LYS B 107 48.38 38.94
REMARK 500 ASN B 114 -8.61 76.62
REMARK 500 ALA B 122 -153.85 -86.25
REMARK 500 GLU B 125 -38.55 -39.65
REMARK 500 TRP B 197 -79.80 -132.10
REMARK 500 CYS B 217 -63.39 -14.94
REMARK 500 ASP B 223 -63.95 91.20
REMARK 500 THR B 254 -3.15 -59.56
REMARK 500 GLN B 303 -1.91 -57.00
REMARK 500 THR B 314 11.99 48.77
REMARK 500 SER B 315 -168.37 -77.26
REMARK 500 ALA B 358 13.47 -58.03
REMARK 500 VAL B 375 74.08 -109.04
REMARK 500 LEU B 377 -158.50 -84.53
REMARK 500 ASP B 378 46.38 37.12
REMARK 500 VAL D 0 -39.93 -32.78
REMARK 500
REMARK 500 THIS ENTRY HAS 104 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TRP D 197 TYR D 198 147.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 HIS A 181 24.9 L L OUTSIDE RANGE
REMARK 500 LEU A 263 24.4 L L OUTSIDE RANGE
REMARK 500 ILE A 352 24.3 L L OUTSIDE RANGE
REMARK 500 ASP A 381 16.2 L L OUTSIDE RANGE
REMARK 500 ILE B 279 21.0 L L OUTSIDE RANGE
REMARK 500 ASN B 293 24.6 L L OUTSIDE RANGE
REMARK 500 VAL B 312 24.3 L L OUTSIDE RANGE
REMARK 500 PHE B 365 24.4 L L OUTSIDE RANGE
REMARK 500 ASN D 293 24.2 L L OUTSIDE RANGE
REMARK 500 SER E 169 24.8 L L OUTSIDE RANGE
REMARK 500 SER E 325 21.3 L L OUTSIDE RANGE
REMARK 500 GLU E 364 24.6 L L OUTSIDE RANGE
REMARK 500 PHE E 365 23.0 L L OUTSIDE RANGE
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 PB8 A 394
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB8 B 394
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB8 D 394
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB8 E 394
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3R2F RELATED DB: PDB
REMARK 900 RELATED ID: 3SKF RELATED DB: PDB
DBREF 3SKG A -47 393 UNP P56817 BACE1_HUMAN 14 454
DBREF 3SKG B -47 393 UNP P56817 BACE1_HUMAN 14 454
DBREF 3SKG D -47 393 UNP P56817 BACE1_HUMAN 14 454
DBREF 3SKG E -47 393 UNP P56817 BACE1_HUMAN 14 454
SEQADV 3SKG MET A -61 UNP P56817 EXPRESSION TAG
SEQADV 3SKG ALA A -60 UNP P56817 EXPRESSION TAG
SEQADV 3SKG SER A -59 UNP P56817 EXPRESSION TAG
SEQADV 3SKG MET A -58 UNP P56817 EXPRESSION TAG
SEQADV 3SKG THR A -57 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLY A -56 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLY A -55 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLN A -54 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLN A -53 UNP P56817 EXPRESSION TAG
SEQADV 3SKG MET A -52 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLY A -51 UNP P56817 EXPRESSION TAG
SEQADV 3SKG ARG A -50 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLY A -49 UNP P56817 EXPRESSION TAG
SEQADV 3SKG SER A -48 UNP P56817 EXPRESSION TAG
SEQADV 3SKG MET B -61 UNP P56817 EXPRESSION TAG
SEQADV 3SKG ALA B -60 UNP P56817 EXPRESSION TAG
SEQADV 3SKG SER B -59 UNP P56817 EXPRESSION TAG
SEQADV 3SKG MET B -58 UNP P56817 EXPRESSION TAG
SEQADV 3SKG THR B -57 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLY B -56 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLY B -55 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLN B -54 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLN B -53 UNP P56817 EXPRESSION TAG
SEQADV 3SKG MET B -52 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLY B -51 UNP P56817 EXPRESSION TAG
SEQADV 3SKG ARG B -50 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLY B -49 UNP P56817 EXPRESSION TAG
SEQADV 3SKG SER B -48 UNP P56817 EXPRESSION TAG
SEQADV 3SKG MET D -61 UNP P56817 EXPRESSION TAG
SEQADV 3SKG ALA D -60 UNP P56817 EXPRESSION TAG
SEQADV 3SKG SER D -59 UNP P56817 EXPRESSION TAG
SEQADV 3SKG MET D -58 UNP P56817 EXPRESSION TAG
SEQADV 3SKG THR D -57 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLY D -56 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLY D -55 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLN D -54 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLN D -53 UNP P56817 EXPRESSION TAG
SEQADV 3SKG MET D -52 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLY D -51 UNP P56817 EXPRESSION TAG
SEQADV 3SKG ARG D -50 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLY D -49 UNP P56817 EXPRESSION TAG
SEQADV 3SKG SER D -48 UNP P56817 EXPRESSION TAG
SEQADV 3SKG MET E -61 UNP P56817 EXPRESSION TAG
SEQADV 3SKG ALA E -60 UNP P56817 EXPRESSION TAG
SEQADV 3SKG SER E -59 UNP P56817 EXPRESSION TAG
SEQADV 3SKG MET E -58 UNP P56817 EXPRESSION TAG
SEQADV 3SKG THR E -57 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLY E -56 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLY E -55 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLN E -54 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLN E -53 UNP P56817 EXPRESSION TAG
SEQADV 3SKG MET E -52 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLY E -51 UNP P56817 EXPRESSION TAG
SEQADV 3SKG ARG E -50 UNP P56817 EXPRESSION TAG
SEQADV 3SKG GLY E -49 UNP P56817 EXPRESSION TAG
SEQADV 3SKG SER E -48 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
SEQRES 1 D 455 MET ALA SER MET THR GLY GLY GLN GLN MET GLY ARG GLY
SEQRES 2 D 455 SER ALA GLY VAL LEU PRO ALA HIS GLY THR GLN HIS GLY
SEQRES 3 D 455 ILE ARG LEU PRO LEU ARG SER GLY LEU GLY GLY ALA PRO
SEQRES 4 D 455 LEU GLY LEU ARG LEU PRO ARG GLU THR ASP GLU GLU PRO
SEQRES 5 D 455 GLU GLU PRO GLY ARG ARG GLY SER PHE VAL GLU MET VAL
SEQRES 6 D 455 ASP ASN LEU ARG GLY LYS SER GLY GLN GLY TYR TYR VAL
SEQRES 7 D 455 GLU MET THR VAL GLY SER PRO PRO GLN THR LEU ASN ILE
SEQRES 8 D 455 LEU VAL ASP THR GLY SER SER ASN PHE ALA VAL GLY ALA
SEQRES 9 D 455 ALA PRO HIS PRO PHE LEU HIS ARG TYR TYR GLN ARG GLN
SEQRES 10 D 455 LEU SER SER THR TYR ARG ASP LEU ARG LYS GLY VAL TYR
SEQRES 11 D 455 VAL PRO TYR THR GLN GLY LYS TRP GLU GLY GLU LEU GLY
SEQRES 12 D 455 THR ASP LEU VAL SER ILE PRO HIS GLY PRO ASN VAL THR
SEQRES 13 D 455 VAL ARG ALA ASN ILE ALA ALA ILE THR GLU SER ASP LYS
SEQRES 14 D 455 PHE PHE ILE ASN GLY SER ASN TRP GLU GLY ILE LEU GLY
SEQRES 15 D 455 LEU ALA TYR ALA GLU ILE ALA ARG PRO ASP ASP SER LEU
SEQRES 16 D 455 GLU PRO PHE PHE ASP SER LEU VAL LYS GLN THR HIS VAL
SEQRES 17 D 455 PRO ASN LEU PHE SER LEU GLN LEU CYS GLY ALA GLY PHE
SEQRES 18 D 455 PRO LEU ASN GLN SER GLU VAL LEU ALA SER VAL GLY GLY
SEQRES 19 D 455 SER MET ILE ILE GLY GLY ILE ASP HIS SER LEU TYR THR
SEQRES 20 D 455 GLY SER LEU TRP TYR THR PRO ILE ARG ARG GLU TRP TYR
SEQRES 21 D 455 TYR GLU VAL ILE ILE VAL ARG VAL GLU ILE ASN GLY GLN
SEQRES 22 D 455 ASP LEU LYS MET ASP CYS LYS GLU TYR ASN TYR ASP LYS
SEQRES 23 D 455 SER ILE VAL ASP SER GLY THR THR ASN LEU ARG LEU PRO
SEQRES 24 D 455 LYS LYS VAL PHE GLU ALA ALA VAL LYS SER ILE LYS ALA
SEQRES 25 D 455 ALA SER SER THR GLU LYS PHE PRO ASP GLY PHE TRP LEU
SEQRES 26 D 455 GLY GLU GLN LEU VAL CYS TRP GLN ALA GLY THR THR PRO
SEQRES 27 D 455 TRP ASN ILE PHE PRO VAL ILE SER LEU TYR LEU MET GLY
SEQRES 28 D 455 GLU VAL THR ASN GLN SER PHE ARG ILE THR ILE LEU PRO
SEQRES 29 D 455 GLN GLN TYR LEU ARG PRO VAL GLU ASP VAL ALA THR SER
SEQRES 30 D 455 GLN ASP ASP CYS TYR LYS PHE ALA ILE SER GLN SER SER
SEQRES 31 D 455 THR GLY THR VAL MET GLY ALA VAL ILE MET GLU GLY PHE
SEQRES 32 D 455 TYR VAL VAL PHE ASP ARG ALA ARG LYS ARG ILE GLY PHE
SEQRES 33 D 455 ALA VAL SER ALA CYS HIS VAL HIS ASP GLU PHE ARG THR
SEQRES 34 D 455 ALA ALA VAL GLU GLY PRO PHE VAL THR LEU ASP MET GLU
SEQRES 35 D 455 ASP CYS GLY TYR ASN ILE PRO GLN THR ASP GLU SER THR
SEQRES 1 E 455 MET ALA SER MET THR GLY GLY GLN GLN MET GLY ARG GLY
SEQRES 2 E 455 SER ALA GLY VAL LEU PRO ALA HIS GLY THR GLN HIS GLY
SEQRES 3 E 455 ILE ARG LEU PRO LEU ARG SER GLY LEU GLY GLY ALA PRO
SEQRES 4 E 455 LEU GLY LEU ARG LEU PRO ARG GLU THR ASP GLU GLU PRO
SEQRES 5 E 455 GLU GLU PRO GLY ARG ARG GLY SER PHE VAL GLU MET VAL
SEQRES 6 E 455 ASP ASN LEU ARG GLY LYS SER GLY GLN GLY TYR TYR VAL
SEQRES 7 E 455 GLU MET THR VAL GLY SER PRO PRO GLN THR LEU ASN ILE
SEQRES 8 E 455 LEU VAL ASP THR GLY SER SER ASN PHE ALA VAL GLY ALA
SEQRES 9 E 455 ALA PRO HIS PRO PHE LEU HIS ARG TYR TYR GLN ARG GLN
SEQRES 10 E 455 LEU SER SER THR TYR ARG ASP LEU ARG LYS GLY VAL TYR
SEQRES 11 E 455 VAL PRO TYR THR GLN GLY LYS TRP GLU GLY GLU LEU GLY
SEQRES 12 E 455 THR ASP LEU VAL SER ILE PRO HIS GLY PRO ASN VAL THR
SEQRES 13 E 455 VAL ARG ALA ASN ILE ALA ALA ILE THR GLU SER ASP LYS
SEQRES 14 E 455 PHE PHE ILE ASN GLY SER ASN TRP GLU GLY ILE LEU GLY
SEQRES 15 E 455 LEU ALA TYR ALA GLU ILE ALA ARG PRO ASP ASP SER LEU
SEQRES 16 E 455 GLU PRO PHE PHE ASP SER LEU VAL LYS GLN THR HIS VAL
SEQRES 17 E 455 PRO ASN LEU PHE SER LEU GLN LEU CYS GLY ALA GLY PHE
SEQRES 18 E 455 PRO LEU ASN GLN SER GLU VAL LEU ALA SER VAL GLY GLY
SEQRES 19 E 455 SER MET ILE ILE GLY GLY ILE ASP HIS SER LEU TYR THR
SEQRES 20 E 455 GLY SER LEU TRP TYR THR PRO ILE ARG ARG GLU TRP TYR
SEQRES 21 E 455 TYR GLU VAL ILE ILE VAL ARG VAL GLU ILE ASN GLY GLN
SEQRES 22 E 455 ASP LEU LYS MET ASP CYS LYS GLU TYR ASN TYR ASP LYS
SEQRES 23 E 455 SER ILE VAL ASP SER GLY THR THR ASN LEU ARG LEU PRO
SEQRES 24 E 455 LYS LYS VAL PHE GLU ALA ALA VAL LYS SER ILE LYS ALA
SEQRES 25 E 455 ALA SER SER THR GLU LYS PHE PRO ASP GLY PHE TRP LEU
SEQRES 26 E 455 GLY GLU GLN LEU VAL CYS TRP GLN ALA GLY THR THR PRO
SEQRES 27 E 455 TRP ASN ILE PHE PRO VAL ILE SER LEU TYR LEU MET GLY
SEQRES 28 E 455 GLU VAL THR ASN GLN SER PHE ARG ILE THR ILE LEU PRO
SEQRES 29 E 455 GLN GLN TYR LEU ARG PRO VAL GLU ASP VAL ALA THR SER
SEQRES 30 E 455 GLN ASP ASP CYS TYR LYS PHE ALA ILE SER GLN SER SER
SEQRES 31 E 455 THR GLY THR VAL MET GLY ALA VAL ILE MET GLU GLY PHE
SEQRES 32 E 455 TYR VAL VAL PHE ASP ARG ALA ARG LYS ARG ILE GLY PHE
SEQRES 33 E 455 ALA VAL SER ALA CYS HIS VAL HIS ASP GLU PHE ARG THR
SEQRES 34 E 455 ALA ALA VAL GLU GLY PRO PHE VAL THR LEU ASP MET GLU
SEQRES 35 E 455 ASP CYS GLY TYR ASN ILE PRO GLN THR ASP GLU SER THR
HET PB8 A 394 48
HET PB8 B 394 48
HET PB8 D 394 48
HET PB8 E 394 48
HETNAM PB8 (2S)-2-[(3R)-3-(ACETYLAMINO)-3-(2-METHYLPROPYL)-2-
HETNAM 2 PB8 OXOPYRROLIDIN-1-YL]-N-{(1R,2S)-3-(3,5-DIFLUOROPHENYL)-
HETNAM 3 PB8 1-HYDROXY-1-[(3R)-1,2,3,4-TETRAHYDROISOQUINOLIN-3-
HETNAM 4 PB8 YL]PROPAN-2-YL}-4-PHENYLBUTANAMIDE
FORMUL 5 PB8 4(C38 H46 F2 N4 O4)
FORMUL 9 HOH *106(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 ASN A 162 SER A 169 1 8
HELIX 5 5 ASP A 180 SER A 182 5 3
HELIX 6 6 ASP A 216 ASN A 221 1 6
HELIX 7 7 LYS A 238 SER A 252 1 15
HELIX 8 8 SER A 253 GLU A 255 5 3
HELIX 9 9 PRO A 258 LEU A 263 1 6
HELIX 10 10 PRO A 276 PHE A 280 5 5
HELIX 11 11 LEU A 301 TYR A 305 1 5
HELIX 12 12 GLY A 334 GLU A 339 1 6
HELIX 13 13 ARG A 347 ARG A 349 5 3
HELIX 14 14 PHE B -1 VAL B 3 5 5
HELIX 15 15 GLN B 53 SER B 57 5 5
HELIX 16 16 TYR B 123 ALA B 127 5 5
HELIX 17 17 PRO B 135 THR B 144 1 10
HELIX 18 18 ASN B 162 SER B 169 1 8
HELIX 19 19 ASP B 180 SER B 182 5 3
HELIX 20 20 ASP B 216 ASN B 221 1 6
HELIX 21 21 LYS B 238 SER B 252 1 15
HELIX 22 22 PRO B 258 LEU B 263 1 6
HELIX 23 23 PRO B 276 PHE B 280 5 5
HELIX 24 24 LEU B 301 TYR B 305 1 5
HELIX 25 25 GLY B 334 GLU B 339 1 6
HELIX 26 26 ARG B 347 ARG B 349 5 3
HELIX 27 27 GLN D 53 SER D 57 5 5
HELIX 28 28 TYR D 123 ALA D 127 5 5
HELIX 29 29 PRO D 135 GLN D 143 1 9
HELIX 30 30 ASN D 162 SER D 169 1 8
HELIX 31 31 ASP D 180 SER D 182 5 3
HELIX 32 32 ASP D 216 ASN D 221 1 6
HELIX 33 33 LYS D 238 SER D 252 1 15
HELIX 34 34 PRO D 276 PHE D 280 5 5
HELIX 35 35 LEU D 301 TYR D 305 1 5
HELIX 36 36 ALA D 335 GLU D 339 1 5
HELIX 37 37 ARG D 347 ARG D 349 5 3
HELIX 38 38 GLN E 53 SER E 57 5 5
HELIX 39 39 TYR E 123 ALA E 127 5 5
HELIX 40 40 PRO E 135 THR E 144 1 10
HELIX 41 41 ASN E 162 SER E 169 1 8
HELIX 42 42 ASP E 180 SER E 182 5 3
HELIX 43 43 ASP E 216 TYR E 222 5 7
HELIX 44 44 LYS E 238 SER E 252 1 15
HELIX 45 45 PRO E 276 PHE E 280 5 5
HELIX 46 46 LEU E 301 TYR E 305 1 5
HELIX 47 47 GLY E 334 GLU E 339 1 6
SHEET 1 A 8 LEU A 6 LYS A 9 0
SHEET 2 A 8 GLY A 13 VAL A 20 -1 N GLY A 13 O LYS A 9
SHEET 3 A 8 GLN A 25 ASP A 32 -1 O LEU A 27 N MET A 18
SHEET 4 A 8 GLY A 117 GLY A 120 1 O LEU A 119 N LEU A 30
SHEET 5 A 8 PHE A 38 GLY A 41 -1 N ALA A 39 O ILE A 118
SHEET 6 A 8 VAL A 95 ASP A 106 1 O ILE A 102 N VAL A 40
SHEET 7 A 8 LYS A 75 SER A 86 -1 N GLU A 77 O GLU A 104
SHEET 8 A 8 ARG A 61 PRO A 70 -1 N VAL A 67 O GLY A 78
SHEET 1 B 4 LEU A 6 LYS A 9 0
SHEET 2 B 4 GLY A 13 VAL A 20 -1 N GLY A 13 O LYS A 9
SHEET 3 B 4 LYS A 75 SER A 86 -1 O SER A 86 N THR A 19
SHEET 4 B 4 ARG A 61 PRO A 70 -1 N VAL A 67 O GLY A 78
SHEET 1 C 5 GLY A 172 ILE A 176 0
SHEET 2 C 5 PHE A 150 LEU A 154 -1 N GLN A 153 O SER A 173
SHEET 3 C 5 PHE A 341 ASP A 346 -1 O VAL A 343 N LEU A 152
SHEET 4 C 5 ARG A 351 SER A 357 -1 O GLY A 353 N VAL A 344
SHEET 5 C 5 TYR A 184 PRO A 192 -1 N THR A 191 O ILE A 352
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 VAL A 204
SHEET 4 D 5 SER A 295 ILE A 300 -1 O PHE A 296 N LEU A 287
SHEET 5 D 5 ALA A 369 PHE A 374 -1 O PHE A 374 N SER A 295
SHEET 1 E 2 SER A 225 VAL A 227 0
SHEET 2 E 2 THR A 331 MET A 333 1 O MET A 333 N ILE A 226
SHEET 1 F 2 LEU A 234 PRO A 237 0
SHEET 2 F 2 ILE A 324 SER A 327 1 O SER A 325 N LEU A 236
SHEET 1 G 3 VAL A 268 TRP A 270 0
SHEET 2 G 3 ASP A 318 PHE A 322 -1 O ASP A 318 N TRP A 270
SHEET 3 G 3 LEU A 306 PRO A 308 -1 N ARG A 307 O LYS A 321
SHEET 1 H 8 LEU B 6 LYS B 9 0
SHEET 2 H 8 GLY B 13 VAL B 20 -1 O GLY B 13 N LYS B 9
SHEET 3 H 8 GLN B 25 ASP B 32 -1 O VAL B 31 N TYR B 14
SHEET 4 H 8 GLY B 117 GLY B 120 1 O LEU B 119 N LEU B 30
SHEET 5 H 8 PHE B 38 GLY B 41 -1 N ALA B 39 O ILE B 118
SHEET 6 H 8 VAL B 95 ASP B 106 1 O ILE B 102 N VAL B 40
SHEET 7 H 8 LYS B 75 SER B 86 -1 N GLY B 81 O ILE B 99
SHEET 8 H 8 ARG B 61 PRO B 70 -1 N ARG B 61 O THR B 82
SHEET 1 I 4 LEU B 6 LYS B 9 0
SHEET 2 I 4 GLY B 13 VAL B 20 -1 O GLY B 13 N LYS B 9
SHEET 3 I 4 LYS B 75 SER B 86 -1 O SER B 86 N THR B 19
SHEET 4 I 4 ARG B 61 PRO B 70 -1 N ARG B 61 O THR B 82
SHEET 1 J 5 GLY B 172 ILE B 176 0
SHEET 2 J 5 PHE B 150 LEU B 154 -1 N GLN B 153 O SER B 173
SHEET 3 J 5 PHE B 341 ASP B 346 -1 O VAL B 343 N LEU B 152
SHEET 4 J 5 ARG B 351 SER B 357 -1 O GLY B 353 N VAL B 344
SHEET 5 J 5 TYR B 184 PRO B 192 -1 N THR B 191 O ILE B 352
SHEET 1 K 5 GLN B 211 ASP B 212 0
SHEET 2 K 5 ILE B 203 ILE B 208 -1 N ILE B 208 O GLN B 211
SHEET 3 K 5 ILE B 283 MET B 288 -1 O SER B 284 N GLU B 207
SHEET 4 K 5 SER B 295 ILE B 300 -1 O PHE B 296 N LEU B 287
SHEET 5 K 5 ALA B 369 PHE B 374 -1 O GLU B 371 N ARG B 297
SHEET 1 L 4 SER B 225 VAL B 227 0
SHEET 2 L 4 THR B 331 MET B 333 1 O MET B 333 N ILE B 226
SHEET 3 L 4 LEU B 234 PRO B 237 -1 N ARG B 235 O VAL B 332
SHEET 4 L 4 ILE B 324 SER B 327 1 O SER B 325 N LEU B 234
SHEET 1 M 3 VAL B 268 TRP B 270 0
SHEET 2 M 3 ASP B 318 PHE B 322 -1 O ASP B 318 N TRP B 270
SHEET 3 M 3 LEU B 306 PRO B 308 -1 N ARG B 307 O LYS B 321
SHEET 1 N 8 LEU D 6 LYS D 9 0
SHEET 2 N 8 GLY D 13 VAL D 20 -1 O TYR D 15 N ARG D 7
SHEET 3 N 8 GLN D 25 ASP D 32 -1 O GLN D 25 N VAL D 20
SHEET 4 N 8 GLY D 117 GLY D 120 1 O GLY D 117 N LEU D 30
SHEET 5 N 8 ALA D 39 GLY D 41 -1 N ALA D 39 O ILE D 118
SHEET 6 N 8 ALA D 100 ASP D 106 1 O ILE D 102 N VAL D 40
SHEET 7 N 8 LYS D 75 SER D 86 -1 N GLU D 79 O ALA D 101
SHEET 8 N 8 ARG D 61 PRO D 70 -1 N LYS D 65 O LEU D 80
SHEET 1 O 3 ARG D 61 PRO D 70 0
SHEET 2 O 3 LYS D 75 SER D 86 -1 O LEU D 80 N LYS D 65
SHEET 3 O 3 THR D 94 ASN D 98 -1 O VAL D 95 N VAL D 85
SHEET 1 P 4 THR D 94 ASN D 98 0
SHEET 2 P 4 LYS D 75 SER D 86 -1 N VAL D 85 O VAL D 95
SHEET 3 P 4 GLY D 13 VAL D 20 -1 N THR D 19 O SER D 86
SHEET 4 P 4 LEU D 6 LYS D 9 -1 N ARG D 7 O TYR D 15
SHEET 1 Q 5 GLY D 172 ILE D 176 0
SHEET 2 Q 5 PHE D 150 LEU D 154 -1 N GLN D 153 O SER D 173
SHEET 3 Q 5 PHE D 341 ASP D 346 -1 O VAL D 343 N LEU D 152
SHEET 4 Q 5 ARG D 351 SER D 357 -1 O GLY D 353 N VAL D 344
SHEET 5 Q 5 TYR D 184 PRO D 192 -1 N THR D 191 O ILE D 352
SHEET 1 R 5 GLN D 211 ASP D 212 0
SHEET 2 R 5 ILE D 203 ILE D 208 -1 N ILE D 208 O GLN D 211
SHEET 3 R 5 ILE D 283 MET D 288 -1 O TYR D 286 N VAL D 204
SHEET 4 R 5 SER D 295 ILE D 300 -1 O PHE D 296 N LEU D 287
SHEET 5 R 5 ALA D 369 PHE D 374 -1 O GLU D 371 N ARG D 297
SHEET 1 S 2 SER D 225 ASP D 228 0
SHEET 2 S 2 THR D 331 GLY D 334 1 O MET D 333 N ILE D 226
SHEET 1 T 2 LEU D 234 PRO D 237 0
SHEET 2 T 2 ILE D 324 SER D 327 1 O SER D 325 N LEU D 236
SHEET 1 U 3 VAL D 268 TRP D 270 0
SHEET 2 U 3 ASP D 318 PHE D 322 -1 O TYR D 320 N VAL D 268
SHEET 3 U 3 LEU D 306 VAL D 309 -1 N ARG D 307 O LYS D 321
SHEET 1 V 8 LEU E 6 LYS E 9 0
SHEET 2 V 8 GLY E 13 VAL E 20 -1 O GLY E 13 N LYS E 9
SHEET 3 V 8 GLN E 25 ASP E 32 -1 O VAL E 31 N TYR E 14
SHEET 4 V 8 GLY E 117 GLY E 120 1 O LEU E 119 N LEU E 30
SHEET 5 V 8 ALA E 39 GLY E 41 -1 N ALA E 39 O ILE E 118
SHEET 6 V 8 THR E 94 ASP E 106 1 O ALA E 100 N VAL E 40
SHEET 7 V 8 LYS E 75 SER E 86 -1 N VAL E 85 O VAL E 95
SHEET 8 V 8 ARG E 61 PRO E 70 -1 N VAL E 67 O GLY E 78
SHEET 1 W 4 LEU E 6 LYS E 9 0
SHEET 2 W 4 GLY E 13 VAL E 20 -1 O GLY E 13 N LYS E 9
SHEET 3 W 4 LYS E 75 SER E 86 -1 O SER E 86 N THR E 19
SHEET 4 W 4 ARG E 61 PRO E 70 -1 N VAL E 67 O GLY E 78
SHEET 1 X 5 GLY E 172 ILE E 176 0
SHEET 2 X 5 LEU E 149 LEU E 154 -1 N GLN E 153 O SER E 173
SHEET 3 X 5 PHE E 341 ASP E 346 -1 O PHE E 345 N PHE E 150
SHEET 4 X 5 ARG E 351 SER E 357 -1 O ALA E 355 N TYR E 342
SHEET 5 X 5 TYR E 184 PRO E 192 -1 N THR E 191 O ILE E 352
SHEET 1 Y 5 GLN E 211 ASP E 212 0
SHEET 2 Y 5 ILE E 203 ILE E 208 -1 N ILE E 208 O GLN E 211
SHEET 3 Y 5 ILE E 283 MET E 288 -1 O TYR E 286 N ARG E 205
SHEET 4 Y 5 SER E 295 ILE E 300 -1 O ILE E 298 N LEU E 285
SHEET 5 Y 5 ALA E 369 PHE E 374 -1 O GLU E 371 N ARG E 297
SHEET 1 Z 4 SER E 225 VAL E 227 0
SHEET 2 Z 4 THR E 331 MET E 333 1 O THR E 331 N ILE E 226
SHEET 3 Z 4 LEU E 234 PRO E 237 -1 N ARG E 235 O VAL E 332
SHEET 4 Z 4 ILE E 324 SER E 327 1 O SER E 325 N LEU E 234
SHEET 1 AA 3 VAL E 268 TRP E 270 0
SHEET 2 AA 3 ASP E 318 PHE E 322 -1 O TYR E 320 N VAL E 268
SHEET 3 AA 3 LEU E 306 VAL E 309 -1 N ARG E 307 O LYS E 321
SSBOND 1 CYS A 155 CYS A 359 1555 1555 2.05
SSBOND 2 CYS A 217 CYS A 382 1555 1555 2.04
SSBOND 3 CYS A 269 CYS A 319 1555 1555 2.00
SSBOND 4 CYS B 155 CYS B 359 1555 1555 2.01
SSBOND 5 CYS B 217 CYS B 382 1555 1555 2.04
SSBOND 6 CYS B 269 CYS B 319 1555 1555 2.05
SSBOND 7 CYS D 155 CYS D 359 1555 1555 2.06
SSBOND 8 CYS D 269 CYS D 319 1555 1555 2.13
SSBOND 9 CYS E 155 CYS E 359 1555 1555 2.04
SSBOND 10 CYS E 217 CYS E 382 1555 1555 2.10
SSBOND 11 CYS E 269 CYS E 319 1555 1555 2.19
CISPEP 1 SER A 22 PRO A 23 0 -6.67
CISPEP 2 ARG A 128 PRO A 129 0 25.22
CISPEP 3 GLY A 372 PRO A 373 0 6.36
CISPEP 4 SER B 22 PRO B 23 0 -6.21
CISPEP 5 ARG B 128 PRO B 129 0 0.65
CISPEP 6 GLY B 372 PRO B 373 0 6.53
CISPEP 7 SER D 22 PRO D 23 0 -10.14
CISPEP 8 ARG D 128 PRO D 129 0 11.98
CISPEP 9 GLY D 372 PRO D 373 0 14.11
CISPEP 10 SER E 22 PRO E 23 0 -6.30
CISPEP 11 ARG E 128 PRO E 129 0 -8.91
CISPEP 12 GLY E 372 PRO E 373 0 7.55
SITE 1 AC1 17 GLY A 11 GLN A 12 LEU A 30 ASP A 32
SITE 2 AC1 17 GLY A 34 TYR A 71 THR A 72 GLN A 73
SITE 3 AC1 17 PHE A 108 ILE A 110 TRP A 115 TYR A 198
SITE 4 AC1 17 ASP A 228 GLY A 230 THR A 231 THR A 232
SITE 5 AC1 17 ARG A 235
SITE 1 AC2 18 GLY B 11 GLY B 13 ASP B 32 GLY B 34
SITE 2 AC2 18 SER B 35 TYR B 71 THR B 72 GLN B 73
SITE 3 AC2 18 PHE B 108 ILE B 110 TRP B 115 TYR B 198
SITE 4 AC2 18 ASP B 228 GLY B 230 THR B 231 THR B 232
SITE 5 AC2 18 ARG B 235 HOH B 430
SITE 1 AC3 18 GLY D 11 LEU D 30 ASP D 32 GLY D 34
SITE 2 AC3 18 SER D 35 TYR D 71 THR D 72 GLN D 73
SITE 3 AC3 18 PHE D 108 ILE D 110 TRP D 115 TYR D 198
SITE 4 AC3 18 ILE D 226 ASP D 228 GLY D 230 THR D 231
SITE 5 AC3 18 THR D 232 ARG D 235
SITE 1 AC4 19 GLN E 12 GLY E 13 LEU E 30 ASP E 32
SITE 2 AC4 19 GLY E 34 TYR E 71 THR E 72 GLN E 73
SITE 3 AC4 19 LYS E 107 PHE E 108 ILE E 110 TRP E 115
SITE 4 AC4 19 TYR E 198 ASP E 228 GLY E 230 THR E 231
SITE 5 AC4 19 THR E 232 ARG E 235 HOH E 402
CRYST1 86.240 130.451 86.872 90.00 96.65 90.00 P 1 21 1 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 0.011596 0.000000 0.001352 0.00000
SCALE2 0.000000 0.007666 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011589 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
