HEADER HYDROLASE 10-JUL-06 2HM1
TITLE CRYSTAL STRUCTURE OF HUMAN BETA-SECRETASE (BACE) IN THE PRESENCE OF AN
TITLE 2 INHIBITOR (2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-SECRETASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BETA-SITE APP CLEAVING ENZYME 1, BETA-SITE AMYLOID PROTEIN
COMPND 5 CLEAVING ENZYME 1, ASPARTYL PROTEASE 2, ASP 2, ASP2, MEMBRANE-
COMPND 6 ASSOCIATED ASPARTIC PROTEASE 2, MEMAPSIN-2;
COMPND 7 EC: 3.4.23.46;
COMPND 8 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: BACE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN-INHIBITOR COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.E.BENSON,D.B.PRINCE,A.G.TOMASSELLI,T.L.EMMONS,D.J.PADDOCK
REVDAT 3 18-OCT-17 2HM1 1 REMARK
REVDAT 2 24-FEB-09 2HM1 1 VERSN
REVDAT 1 23-JAN-07 2HM1 0
JRNL AUTH J.N.FRESKOS,Y.M.FOBIAN,T.E.BENSON,J.B.MOON,M.J.BIENKOWSKI,
JRNL AUTH 2 D.L.BROWN,T.L.EMMONS,R.HEINTZ,A.LABORDE,J.J.MCDONALD,
JRNL AUTH 3 B.V.MISCHKE,J.M.MOLYNEAUX,P.B.MULLINS,D.BRYAN PRINCE,
JRNL AUTH 4 D.J.PADDOCK,A.G.TOMASSELLI,G.WINTERROWD
JRNL TITL DESIGN OF POTENT INHIBITORS OF HUMAN BETA-SECRETASE. PART 2.
JRNL REF BIOORG.MED.CHEM.LETT. V. 17 78 2007
JRNL REFN ISSN 0960-894X
JRNL PMID 17049233
JRNL DOI 10.1016/J.BMCL.2006.09.091
REMARK 2
REMARK 2 RESOLUTION. 2.20 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 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.9
REMARK 3 NUMBER OF REFLECTIONS : 17501
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1711
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 34
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.22
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 309
REMARK 3 BIN R VALUE (WORKING SET) : 0.2230
REMARK 3 BIN FREE R VALUE : 0.3010
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 27
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2952
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 168
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 11.52000
REMARK 3 B22 (A**2) : 4.16200
REMARK 3 B33 (A**2) : -15.68200
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 5.58400
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.013 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.769 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.288 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.946 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : MSI_CNX_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : MSI_CNX_TOPPAR:DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : MSI_CNX_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : MSI_CNX_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 5 : LIG.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : MSI_CNX_TOPPAR:PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : MSI_CNX_TOPPAR:DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : MSI_CNX_TOPPAR:WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : MSI_CNX_TOPPAR:ION.TOP
REMARK 3 TOPOLOGY FILE 5 : LIG.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HM1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-06.
REMARK 100 THE DEPOSITION ID IS D_1000038501.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-DEC-01
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18026
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.14100
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP, 14-26 % PEG 750MME,
REMARK 280 SODIUM ACETATE PH 4.6-5.2, 293
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 36.49500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.44000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 36.49500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 52.44000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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 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 58P
REMARK 465 ARG A 59P
REMARK 465 GLY A 60P
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 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 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 ARG A 393
REMARK 465 SER A 394
REMARK 465 HIS A 395
REMARK 465 HIS A 396
REMARK 465 HIS A 397
REMARK 465 HIS A 398
REMARK 465 HIS A 399
REMARK 465 HIS A 400
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 TYR A 71 -157.93 -103.76
REMARK 500 HIS A 89 41.25 -103.67
REMARK 500 PHE A 108 -61.74 -99.20
REMARK 500 ASN A 148 73.27 -68.69
REMARK 500 LEU A 149 145.66 -171.45
REMARK 500 VAL A 166 149.80 -26.17
REMARK 500 TRP A 197 -84.70 -141.92
REMARK 500 TYR A 222 100.15 -51.53
REMARK 500 ASP A 223 -61.18 99.10
REMARK 500 LYS A 224 166.99 178.32
REMARK 500 ALA A 323 33.37 -87.64
REMARK 500 CYS A 359 43.56 -101.68
REMARK 500 HIS A 360 168.07 -48.32
REMARK 500 HIS A 362 -145.63 -37.15
REMARK 500 ASP A 363 144.03 81.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2HIZ RELATED DB: PDB
DBREF 2HM1 A 59 392 UNP P56817 BACE1_HUMAN 57 453
SEQADV 2HM1 MET A 58P UNP P56817 CLONING ARTIFACT
SEQADV 2HM1 ARG A 393 UNP P56817 CLONING ARTIFACT
SEQADV 2HM1 SER A 394 UNP P56817 CLONING ARTIFACT
SEQADV 2HM1 HIS A 395 UNP P56817 EXPRESSION TAG
SEQADV 2HM1 HIS A 396 UNP P56817 EXPRESSION TAG
SEQADV 2HM1 HIS A 397 UNP P56817 EXPRESSION TAG
SEQADV 2HM1 HIS A 398 UNP P56817 EXPRESSION TAG
SEQADV 2HM1 HIS A 399 UNP P56817 EXPRESSION TAG
SEQADV 2HM1 HIS A 400 UNP P56817 EXPRESSION TAG
SEQRES 1 A 406 MET ARG GLY SER PHE VAL GLU MET VAL ASP ASN LEU ARG
SEQRES 2 A 406 GLY LYS SER GLY GLN GLY TYR TYR VAL GLU MET THR VAL
SEQRES 3 A 406 GLY SER PRO PRO GLN THR LEU ASN ILE LEU VAL ASP THR
SEQRES 4 A 406 GLY SER SER ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO
SEQRES 5 A 406 PHE LEU HIS ARG TYR TYR GLN ARG GLN LEU SER SER THR
SEQRES 6 A 406 TYR ARG ASP LEU ARG LYS GLY VAL TYR VAL PRO TYR THR
SEQRES 7 A 406 GLN GLY LYS TRP GLU GLY GLU LEU GLY THR ASP LEU VAL
SEQRES 8 A 406 SER ILE PRO HIS GLY PRO ASN VAL THR VAL ARG ALA ASN
SEQRES 9 A 406 ILE ALA ALA ILE THR GLU SER ASP LYS PHE PHE ILE ASN
SEQRES 10 A 406 GLY SER ASN TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA
SEQRES 11 A 406 GLU ILE ALA ARG PRO ASP ASP SER LEU GLU PRO PHE PHE
SEQRES 12 A 406 ASP SER LEU VAL LYS GLN THR HIS VAL PRO ASN LEU PHE
SEQRES 13 A 406 SER LEU GLN LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN
SEQRES 14 A 406 SER GLU VAL LEU ALA SER VAL GLY GLY SER MET ILE ILE
SEQRES 15 A 406 GLY GLY ILE ASP HIS SER LEU TYR THR GLY SER LEU TRP
SEQRES 16 A 406 TYR THR PRO ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE
SEQRES 17 A 406 ILE VAL ARG VAL GLU ILE ASN GLY GLN ASP LEU LYS MET
SEQRES 18 A 406 ASP CYS LYS GLU TYR ASN TYR ASP LYS SER ILE VAL ASP
SEQRES 19 A 406 SER GLY THR THR ASN LEU ARG LEU PRO LYS LYS VAL PHE
SEQRES 20 A 406 GLU ALA ALA VAL LYS SER ILE LYS ALA ALA SER SER THR
SEQRES 21 A 406 GLU LYS PHE PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU
SEQRES 22 A 406 VAL CYS TRP GLN ALA GLY THR THR PRO TRP ASN ILE PHE
SEQRES 23 A 406 PRO VAL ILE SER LEU TYR LEU MET GLY GLU VAL THR ASN
SEQRES 24 A 406 GLN SER PHE ARG ILE THR ILE LEU PRO GLN GLN TYR LEU
SEQRES 25 A 406 ARG PRO VAL GLU ASP VAL ALA THR SER GLN ASP ASP CYS
SEQRES 26 A 406 TYR LYS PHE ALA ILE SER GLN SER SER THR GLY THR VAL
SEQRES 27 A 406 MET GLY ALA VAL ILE MET GLU GLY PHE TYR VAL VAL PHE
SEQRES 28 A 406 ASP ARG ALA ARG LYS ARG ILE GLY PHE ALA VAL SER ALA
SEQRES 29 A 406 CYS HIS VAL HIS ASP GLU PHE ARG THR ALA ALA VAL GLU
SEQRES 30 A 406 GLY PRO PHE VAL THR LEU ASP MET GLU ASP CYS GLY TYR
SEQRES 31 A 406 ASN ILE PRO GLN THR ASP GLU SER ARG SER HIS HIS HIS
SEQRES 32 A 406 HIS HIS HIS
HET LIQ A 801 45
HETNAM LIQ N-{(1S)-2-({(1S,2R)-1-(3,5-DIFLUOROBENZYL)-3-[(3-
HETNAM 2 LIQ ETHYLBENZYL)AMINO]-2-HYDROXYPROPYL}AMINO)-2-OXO-1-
HETNAM 3 LIQ [(PENTYLSULFONYL)METHYL]ETHYL}NICOTINAMIDE
FORMUL 2 LIQ C33 H42 F2 N4 O5 S
FORMUL 3 HOH *168(H2 O)
HELIX 1 1 GLN A 53 SER A 57 5 5
HELIX 2 2 TYR A 123 ALA A 127 5 5
HELIX 3 3 PRO A 135 THR A 144 1 10
HELIX 4 4 ASP A 180 SER A 182 5 3
HELIX 5 5 ASP A 216 ASN A 221 1 6
HELIX 6 6 LYS A 238 SER A 252 1 15
HELIX 7 7 PRO A 258 LEU A 263 1 6
HELIX 8 8 PRO A 276 PHE A 280 5 5
HELIX 9 9 LEU A 301 TYR A 305 1 5
HELIX 10 10 GLY A 334 GLU A 339 1 6
HELIX 11 11 ASP A 378 GLY A 383 5 6
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 15 VAL A 20 -1 N THR A 19 O SER A 86
SHEET 4 A 9 LEU A 6 LYS A 9 -1 N ARG A 7 O TYR A 15
SHEET 5 A 9 SER A 169 ILE A 176 -1 O VAL A 170 N GLY A 8
SHEET 6 A 9 PHE A 150 LEU A 154 -1 N GLN A 153 O SER A 173
SHEET 7 A 9 PHE A 341 ASP A 346 -1 O VAL A 343 N LEU A 152
SHEET 8 A 9 ARG A 351 SER A 357 -1 O ALA A 355 N TYR A 342
SHEET 9 A 9 TYR A 184 PRO A 192 -1 N THR A 191 O ILE A 352
SHEET 1 B13 ARG A 61 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 VAL A 95 ASP A 106 -1 O GLU A 104 N GLU A 77
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 15 VAL A 20 -1 N VAL A 16 O ILE A 29
SHEET 8 B13 LEU A 6 LYS A 9 -1 N ARG A 7 O TYR A 15
SHEET 9 B13 SER A 169 ILE A 176 -1 O VAL A 170 N GLY A 8
SHEET 10 B13 PHE A 150 LEU A 154 -1 N GLN A 153 O SER A 173
SHEET 11 B13 PHE A 341 ASP A 346 -1 O VAL A 343 N LEU A 152
SHEET 12 B13 ARG A 351 SER A 357 -1 O ALA A 355 N TYR A 342
SHEET 13 B13 TYR A 184 PRO A 192 -1 N THR A 191 O ILE A 352
SHEET 1 C 5 GLU A 200 VAL A 201 0
SHEET 2 C 5 SER A 225 VAL A 227 -1 O SER A 225 N VAL A 201
SHEET 3 C 5 THR A 331 MET A 333 1 O MET A 333 N ILE A 226
SHEET 4 C 5 LEU A 234 PRO A 237 -1 N ARG A 235 O VAL A 332
SHEET 5 C 5 ILE A 324 SER A 327 1 O SER A 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 PRO A 308 -1 N ARG A 307 O LYS A 321
SSBOND 1 CYS A 155 CYS A 359 1555 1555 2.56
SSBOND 2 CYS A 217 CYS A 382 1555 1555 2.52
SSBOND 3 CYS A 269 CYS A 319 1555 1555 2.80
CISPEP 1 SER A 22 PRO A 23 0 -0.33
CISPEP 2 ARG A 128 PRO A 129 0 0.42
CISPEP 3 GLY A 372 PRO A 373 0 -0.05
CRYST1 72.990 104.880 50.060 90.00 94.99 90.00 C 1 2 1 4
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 0.013701 0.000000 0.001196 0.00000
SCALE2 0.000000 0.009535 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020052 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
