HEADER HYDROLASE 21-NOV-05 2F3F
TITLE CRYSTAL STRUCTURE OF THE BACE COMPLEX WITH BDF488, A MACROCYCLIC
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-SECRETASE 1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: BETA-SITE APP CLEAVING ENZYME 1, BETA-SITE AMYLOID PRECURSOR
COMPND 6 PROTEIN CLEAVING ENZYME 1, ASPARTYL PROTEASE 2, ASP 2, ASP2,
COMPND 7 MEMBRANE-ASSOCIATED ASPARTIC PROTEASE 2, MEMAPSIN-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;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET24
KEYWDS BETA-SECRETASE, MEMAPSIN2, ALZHEIMER'S DISEASE, ASPARTIC PROTEASE,
KEYWDS 2 MACROCYCLIC PEPTIDOMIMETIC INHIBITOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.-M.RONDEAU
REVDAT 3 18-OCT-17 2F3F 1 REMARK
REVDAT 2 24-FEB-09 2F3F 1 VERSN
REVDAT 1 05-SEP-06 2F3F 0
JRNL AUTH S.HANESSIAN,G.YANG,J.-M.RONDEAU,U.NEUMANN,C.BETSCHART,
JRNL AUTH 2 M.TINTELNOT-BLOMLEY
JRNL TITL STRUCTURE-BASED DESIGN AND SYNTHESIS OF MACROHETEROCYCLIC
JRNL TITL 2 PEPTIDOMIMETIC INHIBITORS OF THE ASPARTIC PROTEASE BETA-SITE
JRNL TITL 3 AMYLOID PRECURSOR PROTEIN CLEAVING ENZYME (BACE).
JRNL REF J.MED.CHEM. V. 49 4544 2006
JRNL REFN ISSN 0022-2623
JRNL PMID 16854060
JRNL DOI 10.1021/JM060154A
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.29
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 16369373.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 72197
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3670
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.1920
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1900
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 3670
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 72197
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 10821
REMARK 3 BIN R VALUE (WORKING SET) : 0.2410
REMARK 3 BIN FREE R VALUE : 0.2750
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 576
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8885
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 102
REMARK 3 SOLVENT ATOMS : 508
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.00000
REMARK 3 B22 (A**2) : 7.59000
REMARK 3 B33 (A**2) : 0.41000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.23
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.29
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.000
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.630
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 3.170 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.610 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.840 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.410 ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 52.70
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN.TOP
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 PARAMETER FILE 3 : WATER.TOP
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN_REP.PARAM
REMARK 3 TOPOLOGY FILE 2 : NVP-BDF488.PRM
REMARK 3 TOPOLOGY FILE 3 : WATER_REP.PARAM
REMARK 3 TOPOLOGY FILE 4 : CIS_PEPTIDE.PARAM
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2F3F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000035404.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-DEC-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97840
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72219
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7000
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.40700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNX 2002
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M AMMONIUM SULFATE, PH 5.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 292K
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 51.60100
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER
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 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 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 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 GLY A 33P
REMARK 465 PRO 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 SER A 169
REMARK 465 VAL A 170
REMARK 465 ILE A 386
REMARK 465 GLY B 33P
REMARK 465 PRO 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 ILE B 386
REMARK 465 GLY C 33P
REMARK 465 PRO 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 ILE C 386
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 HOH B 667 O HOH B 703 2.19
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 PHE A 108 -63.40 -98.65
REMARK 500 TRP A 197 -82.10 -137.78
REMARK 500 GLU A 265 -65.65 -98.53
REMARK 500 ALA A 313 -158.90 -129.74
REMARK 500 CYS A 359 58.66 -102.07
REMARK 500 LYS B 9 -145.68 -77.32
REMARK 500 HIS B 89 40.69 -103.76
REMARK 500 PHE B 108 -61.43 -99.40
REMARK 500 TRP B 197 -82.85 -139.79
REMARK 500 GLU B 265 -65.85 -99.48
REMARK 500 GLN B 303 -8.88 -58.18
REMARK 500 ALA B 313 -158.99 -129.31
REMARK 500 CYS B 359 49.98 -108.03
REMARK 500 ASP B 363 -126.90 -105.99
REMARK 500 HIS C 89 40.02 -103.91
REMARK 500 PHE C 108 -62.32 -99.09
REMARK 500 VAL C 170 -72.41 -152.73
REMARK 500 TRP C 197 -82.40 -138.64
REMARK 500 ARG C 205 140.19 -172.85
REMARK 500 GLU C 265 -66.79 -98.90
REMARK 500 ALA C 313 -159.54 -129.63
REMARK 500 CYS C 359 60.75 -101.67
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 AXF A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AXF B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AXF C 603
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2F3E RELATED DB: PDB
REMARK 900 BACE1 IN COMPLEX WITH RELATED MACROCYCLIC PEPTIDOMIMETIC INHIBITOR
DBREF 2F3F A 35P 386 UNP P56817 BACE1_HUMAN 48 447
DBREF 2F3F B 35P 386 UNP P56817 BACE1_HUMAN 48 447
DBREF 2F3F C 35P 386 UNP P56817 BACE1_HUMAN 48 447
SEQADV 2F3F GLY A 33P UNP P56817 CLONING ARTIFACT
SEQADV 2F3F PRO A 34P UNP P56817 CLONING ARTIFACT
SEQADV 2F3F GLY B 33P UNP P56817 CLONING ARTIFACT
SEQADV 2F3F PRO B 34P UNP P56817 CLONING ARTIFACT
SEQADV 2F3F GLY C 33P UNP P56817 CLONING ARTIFACT
SEQADV 2F3F PRO C 34P UNP P56817 CLONING ARTIFACT
SEQRES 1 A 402 GLY PRO ASP GLU GLU PRO GLU GLU PRO GLY ARG ARG GLY
SEQRES 2 A 402 SER PHE VAL GLU MET VAL ASP ASN LEU ARG GLY LYS SER
SEQRES 3 A 402 GLY GLN GLY TYR TYR VAL GLU MET THR VAL GLY SER PRO
SEQRES 4 A 402 PRO GLN THR LEU ASN ILE LEU VAL ASP THR GLY SER SER
SEQRES 5 A 402 ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO PHE LEU HIS
SEQRES 6 A 402 ARG TYR TYR GLN ARG GLN LEU SER SER THR TYR ARG ASP
SEQRES 7 A 402 LEU ARG LYS GLY VAL TYR VAL PRO TYR THR GLN GLY LYS
SEQRES 8 A 402 TRP GLU GLY GLU LEU GLY THR ASP LEU VAL SER ILE PRO
SEQRES 9 A 402 HIS GLY PRO ASN VAL THR VAL ARG ALA ASN ILE ALA ALA
SEQRES 10 A 402 ILE THR GLU SER ASP LYS PHE PHE ILE ASN GLY SER ASN
SEQRES 11 A 402 TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA GLU ILE ALA
SEQRES 12 A 402 ARG PRO ASP ASP SER LEU GLU PRO PHE PHE ASP SER LEU
SEQRES 13 A 402 VAL LYS GLN THR HIS VAL PRO ASN LEU PHE SER LEU GLN
SEQRES 14 A 402 LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN SER GLU VAL
SEQRES 15 A 402 LEU ALA SER VAL GLY GLY SER MET ILE ILE GLY GLY ILE
SEQRES 16 A 402 ASP HIS SER LEU TYR THR GLY SER LEU TRP TYR THR PRO
SEQRES 17 A 402 ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE ILE VAL ARG
SEQRES 18 A 402 VAL GLU ILE ASN GLY GLN ASP LEU LYS MET ASP CYS LYS
SEQRES 19 A 402 GLU TYR ASN TYR ASP LYS SER ILE VAL ASP SER GLY THR
SEQRES 20 A 402 THR ASN LEU ARG LEU PRO LYS LYS VAL PHE GLU ALA ALA
SEQRES 21 A 402 VAL LYS SER ILE LYS ALA ALA SER SER THR GLU LYS PHE
SEQRES 22 A 402 PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU VAL CYS TRP
SEQRES 23 A 402 GLN ALA GLY THR THR PRO TRP ASN ILE PHE PRO VAL ILE
SEQRES 24 A 402 SER LEU TYR LEU MET GLY GLU VAL THR ASN GLN SER PHE
SEQRES 25 A 402 ARG ILE THR ILE LEU PRO GLN GLN TYR LEU ARG PRO VAL
SEQRES 26 A 402 GLU ASP VAL ALA THR SER GLN ASP ASP CYS TYR LYS PHE
SEQRES 27 A 402 ALA ILE SER GLN SER SER THR GLY THR VAL MET GLY ALA
SEQRES 28 A 402 VAL ILE MET GLU GLY PHE TYR VAL VAL PHE ASP ARG ALA
SEQRES 29 A 402 ARG LYS ARG ILE GLY PHE ALA VAL SER ALA CYS HIS VAL
SEQRES 30 A 402 HIS ASP GLU PHE ARG THR ALA ALA VAL GLU GLY PRO PHE
SEQRES 31 A 402 VAL THR LEU ASP MET GLU ASP CYS GLY TYR ASN ILE
SEQRES 1 B 402 GLY PRO ASP GLU GLU PRO GLU GLU PRO GLY ARG ARG GLY
SEQRES 2 B 402 SER PHE VAL GLU MET VAL ASP ASN LEU ARG GLY LYS SER
SEQRES 3 B 402 GLY GLN GLY TYR TYR VAL GLU MET THR VAL GLY SER PRO
SEQRES 4 B 402 PRO GLN THR LEU ASN ILE LEU VAL ASP THR GLY SER SER
SEQRES 5 B 402 ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO PHE LEU HIS
SEQRES 6 B 402 ARG TYR TYR GLN ARG GLN LEU SER SER THR TYR ARG ASP
SEQRES 7 B 402 LEU ARG LYS GLY VAL TYR VAL PRO TYR THR GLN GLY LYS
SEQRES 8 B 402 TRP GLU GLY GLU LEU GLY THR ASP LEU VAL SER ILE PRO
SEQRES 9 B 402 HIS GLY PRO ASN VAL THR VAL ARG ALA ASN ILE ALA ALA
SEQRES 10 B 402 ILE THR GLU SER ASP LYS PHE PHE ILE ASN GLY SER ASN
SEQRES 11 B 402 TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA GLU ILE ALA
SEQRES 12 B 402 ARG PRO ASP ASP SER LEU GLU PRO PHE PHE ASP SER LEU
SEQRES 13 B 402 VAL LYS GLN THR HIS VAL PRO ASN LEU PHE SER LEU GLN
SEQRES 14 B 402 LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN SER GLU VAL
SEQRES 15 B 402 LEU ALA SER VAL GLY GLY SER MET ILE ILE GLY GLY ILE
SEQRES 16 B 402 ASP HIS SER LEU TYR THR GLY SER LEU TRP TYR THR PRO
SEQRES 17 B 402 ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE ILE VAL ARG
SEQRES 18 B 402 VAL GLU ILE ASN GLY GLN ASP LEU LYS MET ASP CYS LYS
SEQRES 19 B 402 GLU TYR ASN TYR ASP LYS SER ILE VAL ASP SER GLY THR
SEQRES 20 B 402 THR ASN LEU ARG LEU PRO LYS LYS VAL PHE GLU ALA ALA
SEQRES 21 B 402 VAL LYS SER ILE LYS ALA ALA SER SER THR GLU LYS PHE
SEQRES 22 B 402 PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU VAL CYS TRP
SEQRES 23 B 402 GLN ALA GLY THR THR PRO TRP ASN ILE PHE PRO VAL ILE
SEQRES 24 B 402 SER LEU TYR LEU MET GLY GLU VAL THR ASN GLN SER PHE
SEQRES 25 B 402 ARG ILE THR ILE LEU PRO GLN GLN TYR LEU ARG PRO VAL
SEQRES 26 B 402 GLU ASP VAL ALA THR SER GLN ASP ASP CYS TYR LYS PHE
SEQRES 27 B 402 ALA ILE SER GLN SER SER THR GLY THR VAL MET GLY ALA
SEQRES 28 B 402 VAL ILE MET GLU GLY PHE TYR VAL VAL PHE ASP ARG ALA
SEQRES 29 B 402 ARG LYS ARG ILE GLY PHE ALA VAL SER ALA CYS HIS VAL
SEQRES 30 B 402 HIS ASP GLU PHE ARG THR ALA ALA VAL GLU GLY PRO PHE
SEQRES 31 B 402 VAL THR LEU ASP MET GLU ASP CYS GLY TYR ASN ILE
SEQRES 1 C 402 GLY PRO ASP GLU GLU PRO GLU GLU PRO GLY ARG ARG GLY
SEQRES 2 C 402 SER PHE VAL GLU MET VAL ASP ASN LEU ARG GLY LYS SER
SEQRES 3 C 402 GLY GLN GLY TYR TYR VAL GLU MET THR VAL GLY SER PRO
SEQRES 4 C 402 PRO GLN THR LEU ASN ILE LEU VAL ASP THR GLY SER SER
SEQRES 5 C 402 ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO PHE LEU HIS
SEQRES 6 C 402 ARG TYR TYR GLN ARG GLN LEU SER SER THR TYR ARG ASP
SEQRES 7 C 402 LEU ARG LYS GLY VAL TYR VAL PRO TYR THR GLN GLY LYS
SEQRES 8 C 402 TRP GLU GLY GLU LEU GLY THR ASP LEU VAL SER ILE PRO
SEQRES 9 C 402 HIS GLY PRO ASN VAL THR VAL ARG ALA ASN ILE ALA ALA
SEQRES 10 C 402 ILE THR GLU SER ASP LYS PHE PHE ILE ASN GLY SER ASN
SEQRES 11 C 402 TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA GLU ILE ALA
SEQRES 12 C 402 ARG PRO ASP ASP SER LEU GLU PRO PHE PHE ASP SER LEU
SEQRES 13 C 402 VAL LYS GLN THR HIS VAL PRO ASN LEU PHE SER LEU GLN
SEQRES 14 C 402 LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN SER GLU VAL
SEQRES 15 C 402 LEU ALA SER VAL GLY GLY SER MET ILE ILE GLY GLY ILE
SEQRES 16 C 402 ASP HIS SER LEU TYR THR GLY SER LEU TRP TYR THR PRO
SEQRES 17 C 402 ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE ILE VAL ARG
SEQRES 18 C 402 VAL GLU ILE ASN GLY GLN ASP LEU LYS MET ASP CYS LYS
SEQRES 19 C 402 GLU TYR ASN TYR ASP LYS SER ILE VAL ASP SER GLY THR
SEQRES 20 C 402 THR ASN LEU ARG LEU PRO LYS LYS VAL PHE GLU ALA ALA
SEQRES 21 C 402 VAL LYS SER ILE LYS ALA ALA SER SER THR GLU LYS PHE
SEQRES 22 C 402 PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU VAL CYS TRP
SEQRES 23 C 402 GLN ALA GLY THR THR PRO TRP ASN ILE PHE PRO VAL ILE
SEQRES 24 C 402 SER LEU TYR LEU MET GLY GLU VAL THR ASN GLN SER PHE
SEQRES 25 C 402 ARG ILE THR ILE LEU PRO GLN GLN TYR LEU ARG PRO VAL
SEQRES 26 C 402 GLU ASP VAL ALA THR SER GLN ASP ASP CYS TYR LYS PHE
SEQRES 27 C 402 ALA ILE SER GLN SER SER THR GLY THR VAL MET GLY ALA
SEQRES 28 C 402 VAL ILE MET GLU GLY PHE TYR VAL VAL PHE ASP ARG ALA
SEQRES 29 C 402 ARG LYS ARG ILE GLY PHE ALA VAL SER ALA CYS HIS VAL
SEQRES 30 C 402 HIS ASP GLU PHE ARG THR ALA ALA VAL GLU GLY PRO PHE
SEQRES 31 C 402 VAL THR LEU ASP MET GLU ASP CYS GLY TYR ASN ILE
HET AXF A 601 34
HET AXF B 602 34
HET AXF C 603 34
HETNAM AXF (2R,4S)-N-BUTYL-4-HYDROXY-2-METHYL- 4-((E)-(4AS,12R,
HETNAM 2 AXF 15S,17AS)-15-METHYL -14,17-DIOXO-2,3,4,4A,6,9,11,12,
HETNAM 3 AXF 13, 14,15,16,17,17A-TETRADECAHYDRO-1H-5 ,10-DITHIA-1,
HETNAM 4 AXF 13,16-TRIAZA-BENZOCYCL OPENTADECEN-12-YL)-BUTYRAMIDE
FORMUL 4 AXF 3(C24 H42 N4 O4 S2)
FORMUL 7 HOH *508(H2 O)
HELIX 1 2 GLN A 53 SER A 57 5 5
HELIX 2 3 TYR A 123 ALA A 127 5 5
HELIX 3 4 PRO A 135 THR A 144 1 10
HELIX 4 5 ASP A 180 SER A 182 5 3
HELIX 5 6 ASP A 216 TYR A 222 5 7
HELIX 6 7 LYS A 238 SER A 252 1 15
HELIX 7 8 PRO A 276 PHE A 280 5 5
HELIX 8 9 LEU A 301 TYR A 305 1 5
HELIX 9 10 GLY A 334 GLU A 339 1 6
HELIX 10 11 ARG A 347 ARG A 349 5 3
HELIX 11 12 ASP A 378 GLY A 383 5 6
HELIX 12 14 GLN B 53 SER B 57 5 5
HELIX 13 15 TYR B 123 ALA B 127 5 5
HELIX 14 16 PRO B 135 THR B 144 1 10
HELIX 15 17 ASP B 180 SER B 182 5 3
HELIX 16 18 ASP B 216 TYR B 222 5 7
HELIX 17 19 LYS B 238 SER B 252 1 15
HELIX 18 20 PRO B 276 PHE B 280 5 5
HELIX 19 21 LEU B 301 TYR B 305 1 5
HELIX 20 22 GLY B 334 GLU B 339 1 6
HELIX 21 23 ARG B 347 ARG B 349 5 3
HELIX 22 24 ASP B 378 GLY B 383 5 6
HELIX 23 26 GLN C 53 SER C 57 5 5
HELIX 24 27 TYR C 123 ALA C 127 5 5
HELIX 25 28 PRO C 135 THR C 144 1 10
HELIX 26 29 ASP C 180 SER C 182 5 3
HELIX 27 30 ASP C 216 TYR C 222 5 7
HELIX 28 31 LYS C 238 SER C 252 1 15
HELIX 29 32 PRO C 276 PHE C 280 5 5
HELIX 30 33 LEU C 301 TYR C 305 1 5
HELIX 31 34 GLY C 334 GLU C 339 1 6
HELIX 32 35 ARG C 347 ARG C 349 5 3
HELIX 33 36 ASP C 378 GLY C 383 1 6
SHEET 1 A 8 LEU A 6 LYS A 9 0
SHEET 2 A 8 GLY A 13 VAL A 20 -1 O TYR A 15 N ARG A 7
SHEET 3 A 8 GLN A 25 ASP A 32 -1 O ILE A 29 N VAL A 16
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 79 O ALA A 101
SHEET 8 A 8 ARG A 61 PRO A 70 -1 N LYS A 65 O LEU A 80
SHEET 1 B 4 LEU A 6 LYS A 9 0
SHEET 2 B 4 GLY A 13 VAL A 20 -1 O TYR A 15 N ARG A 7
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 LYS A 65 O LEU A 80
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 PHE A 345 N PHE A 150
SHEET 4 C 5 ARG A 351 SER A 357 -1 O ALA A 355 N TYR A 342
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 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 GLU A 371 N ARG A 297
SHEET 1 E 4 SER A 225 VAL A 227 0
SHEET 2 E 4 THR A 331 MET A 333 1 O MET A 333 N ILE A 226
SHEET 3 E 4 LEU A 234 PRO A 237 -1 N ARG A 235 O VAL A 332
SHEET 4 E 4 ILE A 324 SER A 327 1 O SER A 327 N LEU A 236
SHEET 1 F 3 VAL A 268 TRP A 270 0
SHEET 2 F 3 ASP A 318 PHE A 322 -1 O TYR A 320 N VAL A 268
SHEET 3 F 3 LEU A 306 VAL A 309 -1 N ARG A 307 O LYS A 321
SHEET 1 G 9 ARG B 61 PRO B 70 0
SHEET 2 G 9 LYS B 75 SER B 86 -1 O LEU B 80 N LYS B 65
SHEET 3 G 9 TYR B 15 VAL B 20 -1 N THR B 19 O SER B 86
SHEET 4 G 9 LEU B 6 ARG B 7 -1 N ARG B 7 O TYR B 15
SHEET 5 G 9 GLY B 171 ILE B 176 -1 O GLY B 172 N LEU B 6
SHEET 6 G 9 PHE B 150 CYS B 155 -1 N GLN B 153 O SER B 173
SHEET 7 G 9 PHE B 341 ASP B 346 -1 O PHE B 345 N PHE B 150
SHEET 8 G 9 ARG B 351 SER B 357 -1 O ALA B 355 N TYR B 342
SHEET 9 G 9 TYR B 184 PRO B 192 -1 N THR B 191 O ILE B 352
SHEET 1 H13 ARG B 61 PRO B 70 0
SHEET 2 H13 LYS B 75 SER B 86 -1 O LEU B 80 N LYS B 65
SHEET 3 H13 VAL B 95 ASP B 106 -1 O ALA B 101 N GLU B 79
SHEET 4 H13 PHE B 38 GLY B 41 1 N VAL B 40 O ILE B 102
SHEET 5 H13 GLY B 117 GLY B 120 -1 O ILE B 118 N ALA B 39
SHEET 6 H13 GLN B 25 ASP B 32 1 N LEU B 30 O LEU B 119
SHEET 7 H13 TYR B 15 VAL B 20 -1 N VAL B 16 O ILE B 29
SHEET 8 H13 LEU B 6 ARG B 7 -1 N ARG B 7 O TYR B 15
SHEET 9 H13 GLY B 171 ILE B 176 -1 O GLY B 172 N LEU B 6
SHEET 10 H13 PHE B 150 CYS B 155 -1 N GLN B 153 O SER B 173
SHEET 11 H13 PHE B 341 ASP B 346 -1 O PHE B 345 N PHE B 150
SHEET 12 H13 ARG B 351 SER B 357 -1 O ALA B 355 N TYR B 342
SHEET 13 H13 TYR B 184 PRO B 192 -1 N THR B 191 O ILE B 352
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 MET B 288 -1 O TYR B 286 N ARG B 205
SHEET 4 I 5 GLN B 294 ILE B 300 -1 O ILE B 300 N ILE B 283
SHEET 5 I 5 ALA B 369 VAL B 375 -1 O GLU B 371 N ARG B 297
SHEET 1 J 4 SER B 225 VAL B 227 0
SHEET 2 J 4 THR B 331 MET B 333 1 O MET B 333 N ILE B 226
SHEET 3 J 4 LEU B 234 PRO B 237 -1 N ARG B 235 O VAL B 332
SHEET 4 J 4 ILE B 324 SER B 327 1 O SER B 327 N LEU B 236
SHEET 1 K 3 VAL B 268 TRP B 270 0
SHEET 2 K 3 ASP B 318 PHE B 322 -1 O ASP B 318 N TRP B 270
SHEET 3 K 3 LEU B 306 VAL B 309 -1 N ARG B 307 O LYS B 321
SHEET 1 L 8 LEU C 6 LYS C 9 0
SHEET 2 L 8 GLY C 13 VAL C 20 -1 O TYR C 15 N ARG C 7
SHEET 3 L 8 GLN C 25 ASP C 32 -1 O ILE C 29 N VAL C 16
SHEET 4 L 8 GLY C 117 GLY C 120 1 O LEU C 119 N LEU C 30
SHEET 5 L 8 PHE C 38 GLY C 41 -1 N ALA C 39 O ILE C 118
SHEET 6 L 8 VAL C 95 ASP C 106 1 O ILE C 102 N VAL C 40
SHEET 7 L 8 LYS C 75 SER C 86 -1 N GLY C 81 O ILE C 99
SHEET 8 L 8 ARG C 61 PRO C 70 -1 N LYS C 65 O LEU C 80
SHEET 1 M 4 LEU C 6 LYS C 9 0
SHEET 2 M 4 GLY C 13 VAL C 20 -1 O TYR C 15 N ARG C 7
SHEET 3 M 4 LYS C 75 SER C 86 -1 O SER C 86 N THR C 19
SHEET 4 M 4 ARG C 61 PRO C 70 -1 N LYS C 65 O LEU C 80
SHEET 1 N 5 GLY C 172 ILE C 176 0
SHEET 2 N 5 PHE C 150 LEU C 154 -1 N GLN C 153 O SER C 173
SHEET 3 N 5 PHE C 341 ASP C 346 -1 O VAL C 343 N LEU C 152
SHEET 4 N 5 ARG C 351 SER C 357 -1 O ALA C 355 N TYR C 342
SHEET 5 N 5 TYR C 184 PRO C 192 -1 N THR C 191 O ILE C 352
SHEET 1 O 5 GLN C 211 ASP C 212 0
SHEET 2 O 5 ILE C 203 ILE C 208 -1 N ILE C 208 O GLN C 211
SHEET 3 O 5 ILE C 283 LEU C 287 -1 O TYR C 286 N ARG C 205
SHEET 4 O 5 SER C 295 ILE C 300 -1 O ILE C 300 N ILE C 283
SHEET 5 O 5 ALA C 369 PHE C 374 -1 O GLU C 371 N ARG C 297
SHEET 1 P 4 SER C 225 VAL C 227 0
SHEET 2 P 4 THR C 331 MET C 333 1 O MET C 333 N ILE C 226
SHEET 3 P 4 LEU C 234 PRO C 237 -1 N ARG C 235 O VAL C 332
SHEET 4 P 4 ILE C 324 SER C 327 1 O SER C 327 N LEU C 236
SHEET 1 Q 3 VAL C 268 TRP C 270 0
SHEET 2 Q 3 ASP C 318 PHE C 322 -1 O ASP C 318 N TRP C 270
SHEET 3 Q 3 LEU C 306 VAL C 309 -1 N ARG C 307 O LYS C 321
SSBOND 1 CYS A 155 CYS A 359 1555 1555 2.04
SSBOND 2 CYS A 217 CYS A 382 1555 1555 2.04
SSBOND 3 CYS A 269 CYS A 319 1555 1555 2.04
SSBOND 4 CYS B 155 CYS B 359 1555 1555 2.04
SSBOND 5 CYS B 217 CYS B 382 1555 1555 2.04
SSBOND 6 CYS B 269 CYS B 319 1555 1555 2.04
SSBOND 7 CYS C 155 CYS C 359 1555 1555 2.04
SSBOND 8 CYS C 217 CYS C 382 1555 1555 2.05
SSBOND 9 CYS C 269 CYS C 319 1555 1555 2.04
CISPEP 1 SER A 22 PRO A 23 0 -0.48
CISPEP 2 ARG A 128 PRO A 129 0 0.38
CISPEP 3 TYR A 222 ASP A 223 0 1.12
CISPEP 4 GLY A 372 PRO A 373 0 -0.93
CISPEP 5 SER B 22 PRO B 23 0 -0.69
CISPEP 6 ARG B 128 PRO B 129 0 0.52
CISPEP 7 TYR B 222 ASP B 223 0 1.17
CISPEP 8 GLY B 372 PRO B 373 0 -0.62
CISPEP 9 SER C 22 PRO C 23 0 -0.57
CISPEP 10 ARG C 128 PRO C 129 0 -0.58
CISPEP 11 TYR C 222 ASP C 223 0 0.71
CISPEP 12 GLY C 372 PRO C 373 0 0.75
SITE 1 AC1 13 GLY A 11 GLN A 12 GLY A 13 ASP A 32
SITE 2 AC1 13 GLY A 34 TYR A 71 THR A 72 GLN A 73
SITE 3 AC1 13 PHE A 108 ASP A 228 GLY A 230 THR A 232
SITE 4 AC1 13 HOH A 643
SITE 1 AC2 13 GLY B 11 GLN B 12 GLY B 13 ASP B 32
SITE 2 AC2 13 GLY B 34 TYR B 71 THR B 72 GLN B 73
SITE 3 AC2 13 PHE B 108 ASP B 228 GLY B 230 THR B 232
SITE 4 AC2 13 HOH B 689
SITE 1 AC3 15 GLY C 11 GLN C 12 GLY C 13 ASP C 32
SITE 2 AC3 15 GLY C 34 VAL C 69 PRO C 70 TYR C 71
SITE 3 AC3 15 THR C 72 GLN C 73 PHE C 108 ASP C 228
SITE 4 AC3 15 GLY C 230 THR C 232 HOH C 666
CRYST1 82.250 103.202 100.997 90.00 103.03 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 0.012158 0.000000 0.002814 0.00000
SCALE2 0.000000 0.009690 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010163 0.00000
(ATOM LINES ARE NOT SHOWN.)
END