HEADER HYDROLASE/HYDROLASE INHIBITOR 25-JAN-00 1EBY
TITLE HIV-1 PROTEASE IN COMPLEX WITH THE INHIBITOR BEA369
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIV-1 PROTEASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: FRAGMENT 69-167;
COMPND 5 EC: 3.4.23.16;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DIMER, PROTEIN-INHIBITOR COMPLEX, HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.UNGE
REVDAT 4 07-FEB-24 1EBY 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1EBY 1 VERSN
REVDAT 2 29-MAR-05 1EBY 1 JRNL REMARK
REVDAT 1 26-JUN-02 1EBY 0
JRNL AUTH H.O.ANDERSSON,K.FRIDBORG,S.LOWGREN,M.ALTERMAN,A.MUHLMAN,
JRNL AUTH 2 M.BJORSNE,N.GARG,I.KVARNSTROM,W.SCHAAL,B.CLASSON,A.KARLEN,
JRNL AUTH 3 U.H.DANIELSSON,G.AHLSEN,U.NILLROTH,L.VRANG,B.OBERG,
JRNL AUTH 4 B.SAMUELSSON,A.HALLBERG,T.UNGE
JRNL TITL OPTIMIZATION OF P1-P3 GROUPS IN SYMMETRIC AND ASYMMETRIC
JRNL TITL 2 HIV-1 PROTEASE INHIBITORS
JRNL REF EUR.J.BIOCHEM. V. 270 1746 2003
JRNL REFN ISSN 0014-2956
JRNL PMID 12694187
JRNL DOI 10.1046/J.1432-1033.2003.03533.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.LINDBERG,D.PYRING,S.LOWGREN,A.ROSENQUIST,G.ZUCCARELLO,
REMARK 1 AUTH 2 I.KVARNSTROM,H.ZHANG,L.VRANG,B.CLASSON,A.HALLBERG,
REMARK 1 AUTH 3 B.SAMUELSSON,T.UNGE
REMARK 1 TITL SYMMETRIC FLUORO-SUBSTITUTED DIOL-BASED HIV PROTEASE
REMARK 1 TITL 2 INHIBITORS. ORTHO-FLUORINATED AND META-FLUORINATED
REMARK 1 TITL 3 P1/P1'-BENZYLOXY SIDE GROUPS SIGNIFICANTLY IMPROVE THE
REMARK 1 TITL 4 ANTIVIRAL ACTIVITY AND PRESERVE BINDING EFFICACY
REMARK 1 REF EUR.J.BIOCHEM. V. 271 4594 2004
REMARK 1 REFN ISSN 0014-2956
REMARK 1 PMID 15560801
REMARK 1 DOI 10.1111/J.1432-1033.2004.04431.X
REMARK 2
REMARK 2 RESOLUTION. 2.29 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.29
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 38857615.050
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 10685
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 SET) : 0.185
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 519
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
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) : 2.29
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1657
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 75
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.031
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1520
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 95
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.52000
REMARK 3 B22 (A**2) : -5.11000
REMARK 3 B33 (A**2) : 0.60000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.20
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) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.740
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) : 3.230 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.050 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 8.250 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.630 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.32
REMARK 3 BSOL : 34.53
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_REP.PA
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARA
REMARK 3 PARAMETER FILE 3 : BEA369.PAR
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : BEA369.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINED WITH CNS PROGRAM SYSTEM
REMARK 4
REMARK 4 1EBY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JAN-00.
REMARK 100 THE DEPOSITION ID IS D_1000010441.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUL-96
REMARK 200 TEMPERATURE (KELVIN) : 277
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 3
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LURE
REMARK 200 BEAMLINE : D41A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.386
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
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 : 10685
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.294
REMARK 200 RESOLUTION RANGE LOW (A) : 21.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.60
REMARK 200 R MERGE FOR SHELL (I) : 0.12200
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: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4 M SODIUM CHLORIDE, 0.05 M MES,
REMARK 280 0.02 % (W/V) SODIUM AZIDE, PH 5.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 29.57500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.49000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.57500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.49000
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 GLU B 135 128.28 -39.61
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 BEB B 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AJV RELATED DB: PDB
REMARK 900 1AJV CONTAINS THE SAME PROTEIN COMPLEXED WITH THE CYCLIC SULFAMIDE
REMARK 900 INHIBITOR AHA006
REMARK 900 RELATED ID: 1AJX RELATED DB: PDB
REMARK 900 1AJX CONTAINS THE SAME PROTEIN COMPLEXED WITH THE CYCLIC UREA
REMARK 900 INHIBITOR AHA001
REMARK 900 RELATED ID: 1D4I RELATED DB: PDB
REMARK 900 1D4I CONTAINS THE SAME PROTEIN COMPLEXED WITH THE INHIBITOR BEA425
REMARK 900 RELATED ID: 1D4H RELATED DB: PDB
REMARK 900 1D4H CONTAINS THE SAME PROTEIN COMPLEXED WITH THE INHIBITOR BEA435
REMARK 900 RELATED ID: 1D4J RELATED DB: PDB
REMARK 900 1D4J CONTAINS THE SAME PROTEIN COMPLEXED WITH THE INHIBITOR MSL370
REMARK 900 RELATED ID: 1EBW RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE IN COMPLEX WITH THE INHIBITOR BEA322
REMARK 900 RELATED ID: 1EBZ RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE IN COMPLEX WITH THE INHIBITOR BEA388
REMARK 900 RELATED ID: 1EC0 RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE IN COMPLEX WITH THE INHIBITOR BEA403
REMARK 900 RELATED ID: 1EC1 RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE IN COMPLEX WITH THE INHIBITOR BEA409
REMARK 900 RELATED ID: 1EC2 RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE IN COMPLEX WITH THE INHIBITOR BEA428
REMARK 900 RELATED ID: 1EC3 RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE IN COMPLEX WITH THE INHIBITOR MSA367
DBREF 1EBY A 1 99 UNP P03366 POL_HV1B1 69 167
DBREF 1EBY B 101 199 UNP P03366 POL_HV1B1 69 167
SEQADV 1EBY ASN A 37 UNP P03366 SER 105 CONFLICT
SEQADV 1EBY ASN B 137 UNP P03366 SER 105 CONFLICT
SEQRES 1 A 99 PRO GLN ILE THR LEU TRP GLN ARG PRO LEU VAL THR ILE
SEQRES 2 A 99 LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR
SEQRES 3 A 99 GLY ALA ASP ASP THR VAL LEU GLU GLU MET ASN LEU PRO
SEQRES 4 A 99 GLY ARG TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY
SEQRES 5 A 99 PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE LEU ILE GLU
SEQRES 6 A 99 ILE CYS GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY
SEQRES 7 A 99 PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR
SEQRES 8 A 99 GLN ILE GLY CYS THR LEU ASN PHE
SEQRES 1 B 99 PRO GLN ILE THR LEU TRP GLN ARG PRO LEU VAL THR ILE
SEQRES 2 B 99 LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR
SEQRES 3 B 99 GLY ALA ASP ASP THR VAL LEU GLU GLU MET ASN LEU PRO
SEQRES 4 B 99 GLY ARG TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY
SEQRES 5 B 99 PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE LEU ILE GLU
SEQRES 6 B 99 ILE CYS GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY
SEQRES 7 B 99 PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR
SEQRES 8 B 99 GLN ILE GLY CYS THR LEU ASN PHE
HET BEB B 501 48
HETNAM BEB N,N-[2,5-O-DIBENZYL-GLUCARYL]-DI-[1-AMINO-INDAN-2-OL]
HETSYN BEB INHIBITOR BEA369
FORMUL 3 BEB C38 H40 N2 O8
FORMUL 4 HOH *95(H2 O)
HELIX 1 1 GLY A 86 THR A 91 1 6
HELIX 2 2 GLN A 92 GLY A 94 5 3
HELIX 3 3 GLY B 186 THR B 191 1 6
SHEET 1 A 4 GLN A 2 ILE A 3 0
SHEET 2 A 4 THR B 196 ASN B 198 -1 O LEU B 197 N ILE A 3
SHEET 3 A 4 THR A 96 ASN A 98 -1 N THR A 96 O ASN B 198
SHEET 4 A 4 GLN B 102 ILE B 103 -1 N ILE B 103 O LEU A 97
SHEET 1 B 8 LYS A 43 GLY A 49 0
SHEET 2 B 8 GLY A 52 ILE A 66 -1 O GLY A 52 N GLY A 49
SHEET 3 B 8 LEU A 10 ILE A 15 -1 O LYS A 14 N GLU A 65
SHEET 4 B 8 GLN A 18 LEU A 24 -1 O GLN A 18 N ILE A 15
SHEET 5 B 8 ILE A 84 ILE A 85 1 N ILE A 85 O LEU A 23
SHEET 6 B 8 VAL A 32 LEU A 33 -1 O VAL A 32 N ILE A 84
SHEET 7 B 8 HIS A 69 VAL A 77 1 O LEU A 76 N LEU A 33
SHEET 8 B 8 GLY A 52 ILE A 66 -1 N ARG A 57 O VAL A 77
SHEET 1 C 8 LYS B 143 GLY B 149 0
SHEET 2 C 8 GLY B 152 ILE B 166 -1 O GLY B 152 N GLY B 149
SHEET 3 C 8 LEU B 110 ILE B 115 -1 O LYS B 114 N GLU B 165
SHEET 4 C 8 GLN B 118 LEU B 124 -1 O GLN B 118 N ILE B 115
SHEET 5 C 8 ILE B 184 ILE B 185 1 N ILE B 185 O LEU B 123
SHEET 6 C 8 VAL B 132 LEU B 133 -1 O VAL B 132 N ILE B 184
SHEET 7 C 8 HIS B 169 VAL B 177 1 O LEU B 176 N LEU B 133
SHEET 8 C 8 GLY B 152 ILE B 166 -1 N ARG B 157 O VAL B 177
SITE 1 AC1 23 ARG A 8 ASP A 25 GLY A 27 ALA A 28
SITE 2 AC1 23 ASP A 29 ASP A 30 GLY A 48 GLY A 49
SITE 3 AC1 23 VAL A 82 ILE A 84 ARG B 108 ASP B 125
SITE 4 AC1 23 GLY B 127 ALA B 128 ASP B 129 ASP B 130
SITE 5 AC1 23 VAL B 132 GLY B 148 GLY B 149 PRO B 181
SITE 6 AC1 23 VAL B 182 ILE B 184 HOH B 316
CRYST1 59.150 86.980 47.160 90.00 90.00 90.00 P 21 21 2 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 0.016906 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011497 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021204 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
