HEADER HYDROLASE/HYDROLASE INHIBITOR 07-DEC-09 3KYR
TITLE BACE-1 IN COMPLEX WITH A NORSTATINE TYPE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-SECRETASE 1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: UNP RESIDUES 42-446;
COMPND 5 SYNONYM: BETA-SITE AMYLOID PRECURSOR PROTEIN CLEAVING ENZYME 1, BETA-
COMPND 6 SITE APP CLEAVING ENZYME 1, MEMBRANE-ASSOCIATED ASPARTIC PROTEASE 2,
COMPND 7 MEMAPSIN-2, ASPARTYL PROTEASE 2, ASP 2, ASP2;
COMPND 8 EC: 3.4.23.46;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BACE1, BACE, KIAA1149;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS BACE, BETA-SECRETASE, MEMAPSIN-2, ASPARTYL PROTEASE, INHIBITOR,
KEYWDS 2 NORSTATINE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.D.LINDBERG,N.BORKAKOTI,D.DERBYSHIRE,S.NYSTROM
REVDAT 2 06-SEP-23 3KYR 1 REMARK
REVDAT 1 29-DEC-10 3KYR 0
JRNL AUTH F.WANGSELL,P.NORDEMAN,J.SAVMARKER,R.EMANUELSSON,K.JANSSON,
JRNL AUTH 2 J.LINDBERG,A.ROSENQVIST,B.SAMUELSSON,M.LARHED
JRNL TITL INVESTIGATION OF A-PHENYLNORSTATINE AND A-BENZYLNORSTATINE
JRNL TITL 2 AS TRANSITION STATE ISOSTERE MOTIFS IN THE SEARCH FOR NEW
JRNL TITL 3 BACE-1 INHIBIOTRS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 99.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 45951
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) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2320
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3227
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3090
REMARK 3 BIN FREE R VALUE SET COUNT : 180
REMARK 3 BIN FREE R VALUE : 0.4030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8570
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 156
REMARK 3 SOLVENT ATOMS : 76
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.66
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : 0.11000
REMARK 3 B33 (A**2) : -0.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.561
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.320
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.209
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.650
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.919
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.860
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8952 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12163 ; 1.659 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1076 ; 7.294 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 401 ;34.073 ;23.666
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1404 ;18.383 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 51 ;19.848 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1322 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6859 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3625 ; 0.225 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5981 ; 0.322 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 320 ; 0.154 ; 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): 71 ; 0.264 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.150 ; 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): 5519 ; 0.957 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8704 ; 1.621 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4033 ; 2.059 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3459 ; 3.298 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 3KYR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-10.
REMARK 100 THE DEPOSITION ID IS D_1000056615.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.07225
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.2.25
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46304
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 99.015
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.9
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.11400
REMARK 200 R SYM (I) : 0.11400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.38600
REMARK 200 R SYM FOR SHELL (I) : 0.38600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 1.3.3
REMARK 200 STARTING MODEL: PDB ENTRY 3DM6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG8000, 0.1M CITRATE, 0.3M
REMARK 280 LITHIUM SULPHATE, 0.1M SODIUM CHLORIDE, PH 5.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 299K
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 51.38700
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
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: C
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 ARG A 29P
REMARK 465 LEU A 30P
REMARK 465 PRO A 31P
REMARK 465 ARG A 32P
REMARK 465 GLU A 33P
REMARK 465 THR A 34P
REMARK 465 ASP A 35P
REMARK 465 GLU A 36P
REMARK 465 GLU A 37P
REMARK 465 PRO A 38P
REMARK 465 GLU A 39P
REMARK 465 GLU A 40P
REMARK 465 PRO A 41P
REMARK 465 GLY A 42P
REMARK 465 ARG A 43P
REMARK 465 ARG A 44P
REMARK 465 GLY A 45P
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 168
REMARK 465 LYS A 256
REMARK 465 PHE A 257
REMARK 465 PRO A 258
REMARK 465 ASP A 259
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 ASN A 385
REMARK 465 ARG B 29P
REMARK 465 LEU B 30P
REMARK 465 PRO B 31P
REMARK 465 ARG B 32P
REMARK 465 GLU B 33P
REMARK 465 THR B 34P
REMARK 465 ASP B 35P
REMARK 465 GLU B 36P
REMARK 465 GLU B 37P
REMARK 465 PRO B 38P
REMARK 465 GLU B 39P
REMARK 465 GLU B 40P
REMARK 465 PRO B 41P
REMARK 465 GLY B 42P
REMARK 465 ARG B 43P
REMARK 465 ARG B 44P
REMARK 465 GLY B 45P
REMARK 465 GLY B 158
REMARK 465 PHE B 159
REMARK 465 PRO B 160
REMARK 465 LEU B 161
REMARK 465 ASN B 162
REMARK 465 GLN B 163
REMARK 465 SER B 164
REMARK 465 GLU B 165
REMARK 465 VAL B 166
REMARK 465 LEU B 167
REMARK 465 ALA B 168
REMARK 465 LYS B 256
REMARK 465 PHE B 257
REMARK 465 PRO B 258
REMARK 465 VAL B 309
REMARK 465 GLU B 310
REMARK 465 ASP B 311
REMARK 465 VAL B 312
REMARK 465 ALA B 313
REMARK 465 THR B 314
REMARK 465 SER B 315
REMARK 465 GLN B 316
REMARK 465 GLY B 383
REMARK 465 TYR B 384
REMARK 465 ASN B 385
REMARK 465 ARG C 29P
REMARK 465 LEU C 30P
REMARK 465 PRO C 31P
REMARK 465 ARG C 32P
REMARK 465 GLU C 33P
REMARK 465 THR C 34P
REMARK 465 ASP C 35P
REMARK 465 GLU C 36P
REMARK 465 GLU C 37P
REMARK 465 PRO C 38P
REMARK 465 GLU C 39P
REMARK 465 GLU C 40P
REMARK 465 PRO C 41P
REMARK 465 GLY C 42P
REMARK 465 ARG C 43P
REMARK 465 ARG C 44P
REMARK 465 GLY C 45P
REMARK 465 GLY C 158
REMARK 465 PHE C 159
REMARK 465 PRO C 160
REMARK 465 LEU C 161
REMARK 465 ASN C 162
REMARK 465 GLN C 163
REMARK 465 SER C 164
REMARK 465 GLU C 165
REMARK 465 VAL C 166
REMARK 465 LEU C 167
REMARK 465 ALA C 168
REMARK 465 SER C 252
REMARK 465 SER C 253
REMARK 465 THR C 254
REMARK 465 GLU C 255
REMARK 465 LYS C 256
REMARK 465 PHE C 257
REMARK 465 PRO C 258
REMARK 465 ASP C 259
REMARK 465 GLY C 260
REMARK 465 GLU C 310
REMARK 465 ASP C 311
REMARK 465 VAL C 312
REMARK 465 ALA C 313
REMARK 465 THR C 314
REMARK 465 SER C 315
REMARK 465 GLN C 316
REMARK 465 ASP C 317
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 B 149 CA - CB - CG ANGL. DEV. = 16.6 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 SER A 36 12.31 -150.95
REMARK 500 HIS A 89 46.92 -106.12
REMARK 500 ASN A 114 -0.95 82.13
REMARK 500 ALA A 122 -151.10 -85.32
REMARK 500 TRP A 197 -84.45 -136.70
REMARK 500 LYS A 214 -6.39 74.67
REMARK 500 TYR A 222 94.19 -43.40
REMARK 500 ASP A 223 -74.88 106.36
REMARK 500 LYS A 238 -60.49 -23.25
REMARK 500 THR A 254 -6.28 -55.09
REMARK 500 ALA A 272 125.87 -27.16
REMARK 500 THR A 329 -146.99 -121.14
REMARK 500 CYS A 359 44.24 -85.66
REMARK 500 SER B 36 12.19 -141.18
REMARK 500 ALA B 43 148.34 -175.34
REMARK 500 HIS B 89 48.78 -93.66
REMARK 500 PHE B 108 -62.83 -91.71
REMARK 500 ASP B 131 -7.81 -53.42
REMARK 500 LEU B 149 136.18 -172.38
REMARK 500 TRP B 197 -89.41 -142.15
REMARK 500 ARG B 205 143.30 -175.62
REMARK 500 ASN B 209 50.96 37.84
REMARK 500 TYR B 222 -99.11 1.58
REMARK 500 LYS B 224 143.06 177.19
REMARK 500 SER B 253 9.57 -69.23
REMARK 500 ALA B 272 119.39 -30.39
REMARK 500 ALA B 323 42.53 -102.22
REMARK 500 THR B 329 -145.83 -103.23
REMARK 500 CYS B 359 51.12 -113.69
REMARK 500 SER C 36 12.21 -146.92
REMARK 500 HIS C 89 53.21 -114.84
REMARK 500 PHE C 108 -65.11 -101.08
REMARK 500 ALA C 122 -169.32 -77.09
REMARK 500 GLU C 125 -36.81 -39.62
REMARK 500 LEU C 133 96.30 -68.93
REMARK 500 TRP C 197 -92.51 -142.67
REMARK 500 ASP C 223 -67.41 87.31
REMARK 500 LYS C 224 142.16 -177.50
REMARK 500 ALA C 272 132.48 -32.49
REMARK 500 PRO C 276 33.66 -71.69
REMARK 500 TRP C 277 -40.50 -28.97
REMARK 500 ALA C 323 42.91 -102.01
REMARK 500 THR C 329 -161.58 -122.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE ENZYME INHIBITOR
REMARK 630 MOLECULE NAME: 3-[[(2S)-2-[[[(2S)-2-[[(2S)-2-[[(2S)-2-AZANYL-3-(1H-
REMARK 630 1,2,3,4-TETRAZOL-5-YLCARBONYLAMINO)PROPANOYL]AMINO]-3-METHYL-
REMARK 630 BUTANOYL]AMINO]-4-METHYL-PENTANOYL]AMINO]METHYL]-2-HYDROXY-4-
REMARK 630 PHENYL-BUTANOYL]AMINO]BENZOIC ACID
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 038 A 500
REMARK 630 038 B 500
REMARK 630 038 C 500
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: 35Y VAL LEU 22P GAB
REMARK 630 DETAILS: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 038 A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 038 B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 038 C 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DM6 RELATED DB: PDB
REMARK 900 RELATED ID: 3IXK RELATED DB: PDB
REMARK 900 RELATED ID: 3IXJ RELATED DB: PDB
DBREF 3KYR A 29P 385 UNP P56817 BACE1_HUMAN 42 446
DBREF 3KYR B 29P 385 UNP P56817 BACE1_HUMAN 42 446
DBREF 3KYR C 29P 385 UNP P56817 BACE1_HUMAN 42 446
SEQRES 1 A 405 ARG LEU PRO ARG GLU THR ASP GLU GLU PRO GLU GLU PRO
SEQRES 2 A 405 GLY ARG ARG GLY SER PHE VAL GLU MET VAL ASP ASN LEU
SEQRES 3 A 405 ARG GLY LYS SER GLY GLN GLY TYR TYR VAL GLU MET THR
SEQRES 4 A 405 VAL GLY SER PRO PRO GLN THR LEU ASN ILE LEU VAL ASP
SEQRES 5 A 405 THR GLY SER SER ASN PHE ALA VAL GLY ALA ALA PRO HIS
SEQRES 6 A 405 PRO PHE LEU HIS ARG TYR TYR GLN ARG GLN LEU SER SER
SEQRES 7 A 405 THR TYR ARG ASP LEU ARG LYS GLY VAL TYR VAL PRO TYR
SEQRES 8 A 405 THR GLN GLY LYS TRP GLU GLY GLU LEU GLY THR ASP LEU
SEQRES 9 A 405 VAL SER ILE PRO HIS GLY PRO ASN VAL THR VAL ARG ALA
SEQRES 10 A 405 ASN ILE ALA ALA ILE THR GLU SER ASP LYS PHE PHE ILE
SEQRES 11 A 405 ASN GLY SER ASN TRP GLU GLY ILE LEU GLY LEU ALA TYR
SEQRES 12 A 405 ALA GLU ILE ALA ARG PRO ASP ASP SER LEU GLU PRO PHE
SEQRES 13 A 405 PHE ASP SER LEU VAL LYS GLN THR HIS VAL PRO ASN LEU
SEQRES 14 A 405 PHE SER LEU GLN LEU CYS GLY ALA GLY PHE PRO LEU ASN
SEQRES 15 A 405 GLN SER GLU VAL LEU ALA SER VAL GLY GLY SER MET ILE
SEQRES 16 A 405 ILE GLY GLY ILE ASP HIS SER LEU TYR THR GLY SER LEU
SEQRES 17 A 405 TRP TYR THR PRO ILE ARG ARG GLU TRP TYR TYR GLU VAL
SEQRES 18 A 405 ILE ILE VAL ARG VAL GLU ILE ASN GLY GLN ASP LEU LYS
SEQRES 19 A 405 MET ASP CYS LYS GLU TYR ASN TYR ASP LYS SER ILE VAL
SEQRES 20 A 405 ASP SER GLY THR THR ASN LEU ARG LEU PRO LYS LYS VAL
SEQRES 21 A 405 PHE GLU ALA ALA VAL LYS SER ILE LYS ALA ALA SER SER
SEQRES 22 A 405 THR GLU LYS PHE PRO ASP GLY PHE TRP LEU GLY GLU GLN
SEQRES 23 A 405 LEU VAL CYS TRP GLN ALA GLY THR THR PRO TRP ASN ILE
SEQRES 24 A 405 PHE PRO VAL ILE SER LEU TYR LEU MET GLY GLU VAL THR
SEQRES 25 A 405 ASN GLN SER PHE ARG ILE THR ILE LEU PRO GLN GLN TYR
SEQRES 26 A 405 LEU ARG PRO VAL GLU ASP VAL ALA THR SER GLN ASP ASP
SEQRES 27 A 405 CYS TYR LYS PHE ALA ILE SER GLN SER SER THR GLY THR
SEQRES 28 A 405 VAL MET GLY ALA VAL ILE MET GLU GLY PHE TYR VAL VAL
SEQRES 29 A 405 PHE ASP ARG ALA ARG LYS ARG ILE GLY PHE ALA VAL SER
SEQRES 30 A 405 ALA CYS HIS VAL HIS ASP GLU PHE ARG THR ALA ALA VAL
SEQRES 31 A 405 GLU GLY PRO PHE VAL THR LEU ASP MET GLU ASP CYS GLY
SEQRES 32 A 405 TYR ASN
SEQRES 1 B 405 ARG LEU PRO ARG GLU THR ASP GLU GLU PRO GLU GLU PRO
SEQRES 2 B 405 GLY ARG ARG GLY SER PHE VAL GLU MET VAL ASP ASN LEU
SEQRES 3 B 405 ARG GLY LYS SER GLY GLN GLY TYR TYR VAL GLU MET THR
SEQRES 4 B 405 VAL GLY SER PRO PRO GLN THR LEU ASN ILE LEU VAL ASP
SEQRES 5 B 405 THR GLY SER SER ASN PHE ALA VAL GLY ALA ALA PRO HIS
SEQRES 6 B 405 PRO PHE LEU HIS ARG TYR TYR GLN ARG GLN LEU SER SER
SEQRES 7 B 405 THR TYR ARG ASP LEU ARG LYS GLY VAL TYR VAL PRO TYR
SEQRES 8 B 405 THR GLN GLY LYS TRP GLU GLY GLU LEU GLY THR ASP LEU
SEQRES 9 B 405 VAL SER ILE PRO HIS GLY PRO ASN VAL THR VAL ARG ALA
SEQRES 10 B 405 ASN ILE ALA ALA ILE THR GLU SER ASP LYS PHE PHE ILE
SEQRES 11 B 405 ASN GLY SER ASN TRP GLU GLY ILE LEU GLY LEU ALA TYR
SEQRES 12 B 405 ALA GLU ILE ALA ARG PRO ASP ASP SER LEU GLU PRO PHE
SEQRES 13 B 405 PHE ASP SER LEU VAL LYS GLN THR HIS VAL PRO ASN LEU
SEQRES 14 B 405 PHE SER LEU GLN LEU CYS GLY ALA GLY PHE PRO LEU ASN
SEQRES 15 B 405 GLN SER GLU VAL LEU ALA SER VAL GLY GLY SER MET ILE
SEQRES 16 B 405 ILE GLY GLY ILE ASP HIS SER LEU TYR THR GLY SER LEU
SEQRES 17 B 405 TRP TYR THR PRO ILE ARG ARG GLU TRP TYR TYR GLU VAL
SEQRES 18 B 405 ILE ILE VAL ARG VAL GLU ILE ASN GLY GLN ASP LEU LYS
SEQRES 19 B 405 MET ASP CYS LYS GLU TYR ASN TYR ASP LYS SER ILE VAL
SEQRES 20 B 405 ASP SER GLY THR THR ASN LEU ARG LEU PRO LYS LYS VAL
SEQRES 21 B 405 PHE GLU ALA ALA VAL LYS SER ILE LYS ALA ALA SER SER
SEQRES 22 B 405 THR GLU LYS PHE PRO ASP GLY PHE TRP LEU GLY GLU GLN
SEQRES 23 B 405 LEU VAL CYS TRP GLN ALA GLY THR THR PRO TRP ASN ILE
SEQRES 24 B 405 PHE PRO VAL ILE SER LEU TYR LEU MET GLY GLU VAL THR
SEQRES 25 B 405 ASN GLN SER PHE ARG ILE THR ILE LEU PRO GLN GLN TYR
SEQRES 26 B 405 LEU ARG PRO VAL GLU ASP VAL ALA THR SER GLN ASP ASP
SEQRES 27 B 405 CYS TYR LYS PHE ALA ILE SER GLN SER SER THR GLY THR
SEQRES 28 B 405 VAL MET GLY ALA VAL ILE MET GLU GLY PHE TYR VAL VAL
SEQRES 29 B 405 PHE ASP ARG ALA ARG LYS ARG ILE GLY PHE ALA VAL SER
SEQRES 30 B 405 ALA CYS HIS VAL HIS ASP GLU PHE ARG THR ALA ALA VAL
SEQRES 31 B 405 GLU GLY PRO PHE VAL THR LEU ASP MET GLU ASP CYS GLY
SEQRES 32 B 405 TYR ASN
SEQRES 1 C 405 ARG LEU PRO ARG GLU THR ASP GLU GLU PRO GLU GLU PRO
SEQRES 2 C 405 GLY ARG ARG GLY SER PHE VAL GLU MET VAL ASP ASN LEU
SEQRES 3 C 405 ARG GLY LYS SER GLY GLN GLY TYR TYR VAL GLU MET THR
SEQRES 4 C 405 VAL GLY SER PRO PRO GLN THR LEU ASN ILE LEU VAL ASP
SEQRES 5 C 405 THR GLY SER SER ASN PHE ALA VAL GLY ALA ALA PRO HIS
SEQRES 6 C 405 PRO PHE LEU HIS ARG TYR TYR GLN ARG GLN LEU SER SER
SEQRES 7 C 405 THR TYR ARG ASP LEU ARG LYS GLY VAL TYR VAL PRO TYR
SEQRES 8 C 405 THR GLN GLY LYS TRP GLU GLY GLU LEU GLY THR ASP LEU
SEQRES 9 C 405 VAL SER ILE PRO HIS GLY PRO ASN VAL THR VAL ARG ALA
SEQRES 10 C 405 ASN ILE ALA ALA ILE THR GLU SER ASP LYS PHE PHE ILE
SEQRES 11 C 405 ASN GLY SER ASN TRP GLU GLY ILE LEU GLY LEU ALA TYR
SEQRES 12 C 405 ALA GLU ILE ALA ARG PRO ASP ASP SER LEU GLU PRO PHE
SEQRES 13 C 405 PHE ASP SER LEU VAL LYS GLN THR HIS VAL PRO ASN LEU
SEQRES 14 C 405 PHE SER LEU GLN LEU CYS GLY ALA GLY PHE PRO LEU ASN
SEQRES 15 C 405 GLN SER GLU VAL LEU ALA SER VAL GLY GLY SER MET ILE
SEQRES 16 C 405 ILE GLY GLY ILE ASP HIS SER LEU TYR THR GLY SER LEU
SEQRES 17 C 405 TRP TYR THR PRO ILE ARG ARG GLU TRP TYR TYR GLU VAL
SEQRES 18 C 405 ILE ILE VAL ARG VAL GLU ILE ASN GLY GLN ASP LEU LYS
SEQRES 19 C 405 MET ASP CYS LYS GLU TYR ASN TYR ASP LYS SER ILE VAL
SEQRES 20 C 405 ASP SER GLY THR THR ASN LEU ARG LEU PRO LYS LYS VAL
SEQRES 21 C 405 PHE GLU ALA ALA VAL LYS SER ILE LYS ALA ALA SER SER
SEQRES 22 C 405 THR GLU LYS PHE PRO ASP GLY PHE TRP LEU GLY GLU GLN
SEQRES 23 C 405 LEU VAL CYS TRP GLN ALA GLY THR THR PRO TRP ASN ILE
SEQRES 24 C 405 PHE PRO VAL ILE SER LEU TYR LEU MET GLY GLU VAL THR
SEQRES 25 C 405 ASN GLN SER PHE ARG ILE THR ILE LEU PRO GLN GLN TYR
SEQRES 26 C 405 LEU ARG PRO VAL GLU ASP VAL ALA THR SER GLN ASP ASP
SEQRES 27 C 405 CYS TYR LYS PHE ALA ILE SER GLN SER SER THR GLY THR
SEQRES 28 C 405 VAL MET GLY ALA VAL ILE MET GLU GLY PHE TYR VAL VAL
SEQRES 29 C 405 PHE ASP ARG ALA ARG LYS ARG ILE GLY PHE ALA VAL SER
SEQRES 30 C 405 ALA CYS HIS VAL HIS ASP GLU PHE ARG THR ALA ALA VAL
SEQRES 31 C 405 GLU GLY PRO PHE VAL THR LEU ASP MET GLU ASP CYS GLY
SEQRES 32 C 405 TYR ASN
HET 038 A 500 52
HET 038 B 500 52
HET 038 C 500 52
HETNAM 038 3-[[(2S)-2-[[[(2S)-2-[[(2S)-2-[[(2S)-2-AZANYL-3-(1H-1,
HETNAM 2 038 2,3,4-TETRAZOL-5-YLCARBONYLAMINO)PROPANOYL]AMINO]-3-
HETNAM 3 038 METHYL-BUTANOYL]AMINO]-4-METHYL-
HETNAM 4 038 PENTANOYL]AMINO]METHYL]-2-HYDROXY-4-PHENYL-
HETNAM 5 038 BUTANOYL]AMINO]BENZOIC ACID
FORMUL 4 038 3(C34 H46 N10 O8)
FORMUL 7 HOH *76(H2 O)
HELIX 1 1 SER A 46P VAL A 3 5 6
HELIX 2 2 GLN A 53 SER A 57 5 5
HELIX 3 3 TYR A 123 ALA A 127 5 5
HELIX 4 4 PRO A 135 THR A 144 1 10
HELIX 5 5 ASP A 180 TYR A 184 5 5
HELIX 6 6 ASP A 216 TYR A 220 5 5
HELIX 7 7 LYS A 238 SER A 253 1 16
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
HELIX 13 13 SER B 46P VAL B 3 5 6
HELIX 14 14 GLN B 53 SER B 57 5 5
HELIX 15 15 TYR B 123 ALA B 127 5 5
HELIX 16 16 PRO B 135 THR B 144 1 10
HELIX 17 17 ASP B 180 SER B 182 5 3
HELIX 18 18 CYS B 217 TYR B 222 1 6
HELIX 19 19 LYS B 238 SER B 253 1 16
HELIX 20 20 PRO B 276 PHE B 280 5 5
HELIX 21 21 LEU B 301 TYR B 305 1 5
HELIX 22 22 GLY B 334 GLY B 340 1 7
HELIX 23 23 ARG B 347 ARG B 349 5 3
HELIX 24 24 PHE C 47P VAL C 3 5 5
HELIX 25 25 GLN C 53 SER C 57 5 5
HELIX 26 26 TYR C 123 ALA C 127 5 5
HELIX 27 27 PRO C 135 THR C 144 1 10
HELIX 28 28 ASP C 180 SER C 182 5 3
HELIX 29 29 ASP C 216 TYR C 222 5 7
HELIX 30 30 LYS C 238 ALA C 250 1 13
HELIX 31 31 PRO C 276 PHE C 280 5 5
HELIX 32 32 LEU C 301 TYR C 305 1 5
HELIX 33 33 GLY C 334 GLU C 339 1 6
HELIX 34 34 MET C 379 GLY C 383 5 5
SHEET 1 A 9 ARG A 61 PRO A 70 0
SHEET 2 A 9 LYS A 75 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 GLY A 8 -1 N ARG A 7 O TYR A 15
SHEET 5 A 9 VAL A 170 ILE A 176 -1 O GLY A 172 N LEU A 6
SHEET 6 A 9 PHE A 150 CYS A 155 -1 N CYS A 155 O GLY A 171
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 VAL A 356 -1 O ALA A 355 N TYR A 342
SHEET 9 A 9 TRP A 189 PRO A 192 -1 N TRP A 189 O PHE A 354
SHEET 1 B13 ARG A 61 PRO A 70 0
SHEET 2 B13 LYS A 75 SER A 86 -1 O LEU A 80 N LYS A 65
SHEET 3 B13 THR A 94 ASP A 106 -1 O ILE A 99 N GLY A 81
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 GLY A 8 -1 N ARG A 7 O TYR A 15
SHEET 9 B13 VAL A 170 ILE A 176 -1 O GLY A 172 N LEU A 6
SHEET 10 B13 PHE A 150 CYS A 155 -1 N CYS A 155 O GLY A 171
SHEET 11 B13 PHE A 341 ASP A 346 -1 O PHE A 345 N PHE A 150
SHEET 12 B13 ARG A 351 VAL A 356 -1 O ALA A 355 N TYR A 342
SHEET 13 B13 TRP A 189 PRO A 192 -1 N TRP A 189 O PHE A 354
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 VAL A 332 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 327 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 SER A 284 N GLU A 207
SHEET 4 D 5 GLN A 294 ILE A 300 -1 O ILE A 300 N ILE A 283
SHEET 5 D 5 ALA A 369 VAL A 375 -1 O PHE A 374 N SER A 295
SHEET 1 E 3 VAL A 268 TRP A 270 0
SHEET 2 E 3 ASP A 318 PHE A 322 -1 O TYR A 320 N VAL A 268
SHEET 3 E 3 LEU A 306 VAL A 309 -1 N VAL A 309 O CYS A 319
SHEET 1 F 9 ARG B 61 PRO B 70 0
SHEET 2 F 9 LYS B 75 SER B 86 -1 O TRP B 76 N VAL B 69
SHEET 3 F 9 TYR B 14 VAL B 20 -1 N THR B 19 O SER B 86
SHEET 4 F 9 LEU B 6 GLY B 8 -1 N ARG B 7 O TYR B 15
SHEET 5 F 9 VAL B 170 ILE B 176 -1 O VAL B 170 N GLY B 8
SHEET 6 F 9 PHE B 150 LEU B 154 -1 N GLN B 153 O SER B 173
SHEET 7 F 9 PHE B 341 ASP B 346 -1 O VAL B 343 N LEU B 152
SHEET 8 F 9 ARG B 351 SER B 357 -1 O ALA B 355 N TYR B 342
SHEET 9 F 9 TYR B 184 PRO B 192 -1 N TRP B 189 O PHE B 354
SHEET 1 G13 ARG B 61 PRO B 70 0
SHEET 2 G13 LYS B 75 SER B 86 -1 O TRP B 76 N VAL B 69
SHEET 3 G13 VAL B 95 ASP B 106 -1 O ILE B 99 N GLY B 81
SHEET 4 G13 PHE B 38 GLY B 41 1 N VAL B 40 O ILE B 102
SHEET 5 G13 GLY B 117 GLY B 120 -1 O ILE B 118 N ALA B 39
SHEET 6 G13 GLN B 25 ASP B 32 1 N LEU B 30 O GLY B 117
SHEET 7 G13 TYR B 14 VAL B 20 -1 N VAL B 16 O ILE B 29
SHEET 8 G13 LEU B 6 GLY B 8 -1 N ARG B 7 O TYR B 15
SHEET 9 G13 VAL B 170 ILE B 176 -1 O VAL B 170 N GLY B 8
SHEET 10 G13 PHE B 150 LEU B 154 -1 N GLN B 153 O SER B 173
SHEET 11 G13 PHE B 341 ASP B 346 -1 O VAL B 343 N LEU B 152
SHEET 12 G13 ARG B 351 SER B 357 -1 O ALA B 355 N TYR B 342
SHEET 13 G13 TYR B 184 PRO B 192 -1 N TRP B 189 O PHE B 354
SHEET 1 H 5 GLU B 200 VAL B 201 0
SHEET 2 H 5 SER B 225 VAL B 227 -1 O SER B 225 N VAL B 201
SHEET 3 H 5 VAL B 332 MET B 333 1 O MET B 333 N ILE B 226
SHEET 4 H 5 LEU B 234 PRO B 237 -1 N ARG B 235 O VAL B 332
SHEET 5 H 5 ILE B 324 SER B 327 1 O SER B 327 N LEU B 236
SHEET 1 I 5 GLN B 211 ASP B 212 0
SHEET 2 I 5 ILE B 203 ILE B 208 -1 N ILE B 208 O GLN B 211
SHEET 3 I 5 ILE B 283 LEU B 287 -1 O SER B 284 N GLU B 207
SHEET 4 I 5 SER B 295 ILE B 300 -1 O ILE B 300 N ILE B 283
SHEET 5 I 5 ALA B 369 PHE B 374 -1 O PHE B 374 N SER B 295
SHEET 1 J 3 VAL B 268 TRP B 270 0
SHEET 2 J 3 ASP B 318 PHE B 322 -1 O ASP B 318 N TRP B 270
SHEET 3 J 3 LEU B 306 ARG B 307 -1 N ARG B 307 O LYS B 321
SHEET 1 K 9 ARG C 61 TYR C 71 0
SHEET 2 K 9 GLY C 74 SER C 86 -1 O GLY C 74 N TYR C 71
SHEET 3 K 9 TYR C 14 VAL C 20 -1 N THR C 19 O SER C 86
SHEET 4 K 9 LEU C 6 GLY C 8 -1 N ARG C 7 O TYR C 15
SHEET 5 K 9 VAL C 170 ILE C 176 -1 O GLY C 172 N LEU C 6
SHEET 6 K 9 PHE C 150 CYS C 155 -1 N GLN C 153 O SER C 173
SHEET 7 K 9 PHE C 341 ASP C 346 -1 O VAL C 343 N LEU C 152
SHEET 8 K 9 ARG C 351 SER C 357 -1 O GLY C 353 N VAL C 344
SHEET 9 K 9 TYR C 184 PRO C 192 -1 N THR C 191 O ILE C 352
SHEET 1 L13 ARG C 61 TYR C 71 0
SHEET 2 L13 GLY C 74 SER C 86 -1 O GLY C 74 N TYR C 71
SHEET 3 L13 VAL C 95 ASP C 106 -1 O ILE C 99 N GLY C 81
SHEET 4 L13 PHE C 38 GLY C 41 1 N VAL C 40 O ILE C 102
SHEET 5 L13 GLY C 117 GLY C 120 -1 O ILE C 118 N ALA C 39
SHEET 6 L13 GLN C 25 ASP C 32 1 N LEU C 30 O LEU C 119
SHEET 7 L13 TYR C 14 VAL C 20 -1 N VAL C 20 O GLN C 25
SHEET 8 L13 LEU C 6 GLY C 8 -1 N ARG C 7 O TYR C 15
SHEET 9 L13 VAL C 170 ILE C 176 -1 O GLY C 172 N LEU C 6
SHEET 10 L13 PHE C 150 CYS C 155 -1 N GLN C 153 O SER C 173
SHEET 11 L13 PHE C 341 ASP C 346 -1 O VAL C 343 N LEU C 152
SHEET 12 L13 ARG C 351 SER C 357 -1 O GLY C 353 N VAL C 344
SHEET 13 L13 TYR C 184 PRO C 192 -1 N THR C 191 O ILE C 352
SHEET 1 M 5 GLU C 200 VAL C 201 0
SHEET 2 M 5 SER C 225 VAL C 227 -1 O SER C 225 N VAL C 201
SHEET 3 M 5 VAL C 332 MET C 333 1 O MET C 333 N ILE C 226
SHEET 4 M 5 LEU C 234 PRO C 237 -1 N ARG C 235 O VAL C 332
SHEET 5 M 5 ILE C 324 SER C 327 1 O SER C 325 N LEU C 236
SHEET 1 N 5 GLN C 211 ASP C 212 0
SHEET 2 N 5 ILE C 203 ILE C 208 -1 N ILE C 208 O GLN C 211
SHEET 3 N 5 ILE C 283 MET C 288 -1 O SER C 284 N GLU C 207
SHEET 4 N 5 GLN C 294 ILE C 300 -1 O ILE C 300 N ILE C 283
SHEET 5 N 5 ALA C 369 VAL C 375 -1 O GLU C 371 N ARG C 297
SHEET 1 O 3 VAL C 268 CYS C 269 0
SHEET 2 O 3 CYS C 319 PHE C 322 -1 O TYR C 320 N VAL C 268
SHEET 3 O 3 LEU C 306 PRO C 308 -1 N ARG C 307 O LYS C 321
SSBOND 1 CYS A 155 CYS A 359 1555 1555 2.06
SSBOND 2 CYS A 217 CYS A 382 1555 1555 2.07
SSBOND 3 CYS A 269 CYS A 319 1555 1555 2.05
SSBOND 4 CYS B 155 CYS B 359 1555 1555 2.10
SSBOND 5 CYS B 217 CYS B 382 1555 1555 2.08
SSBOND 6 CYS B 269 CYS B 319 1555 1555 2.08
SSBOND 7 CYS C 155 CYS C 359 1555 1555 2.05
SSBOND 8 CYS C 217 CYS C 382 1555 1555 2.09
SSBOND 9 CYS C 269 CYS C 319 1555 1555 2.90
CISPEP 1 SER A 22 PRO A 23 0 -7.24
CISPEP 2 ARG A 128 PRO A 129 0 -5.56
CISPEP 3 GLY A 372 PRO A 373 0 -3.21
CISPEP 4 SER B 22 PRO B 23 0 -1.70
CISPEP 5 ARG B 128 PRO B 129 0 8.30
CISPEP 6 GLY B 372 PRO B 373 0 1.69
CISPEP 7 SER C 22 PRO C 23 0 -8.11
CISPEP 8 ARG C 128 PRO C 129 0 1.46
CISPEP 9 GLY C 372 PRO C 373 0 -0.34
SITE 1 AC1 17 GLY A 34 SER A 35 TYR A 68 VAL A 69
SITE 2 AC1 17 PRO A 70 TYR A 71 THR A 72 LYS A 75
SITE 3 AC1 17 ILE A 126 ARG A 128 TYR A 198 LYS A 224
SITE 4 AC1 17 ILE A 226 ASP A 228 ARG A 235 THR A 329
SITE 5 AC1 17 HOH A 401
SITE 1 AC2 12 ASP A 4 GLY B 34 TYR B 68 VAL B 69
SITE 2 AC2 12 PRO B 70 TYR B 71 THR B 72 ARG B 128
SITE 3 AC2 12 TYR B 198 ASP B 228 ARG B 235 THR B 329
SITE 1 AC3 12 GLY C 34 TYR C 68 VAL C 69 PRO C 70
SITE 2 AC3 12 TYR C 71 THR C 72 ARG C 128 TYR C 198
SITE 3 AC3 12 LYS C 224 ASP C 228 THR C 231 ARG C 235
CRYST1 81.762 102.774 101.427 90.00 102.90 90.00 P 1 21 1 6
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 0.012231 0.000000 0.002802 0.00000
SCALE2 0.000000 0.009730 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010115 0.00000
(ATOM LINES ARE NOT SHOWN.)
END