HEADER HYDROLASE 29-DEC-99 1C70
TITLE ALTERNATE BINDING SITE FOR THE P1-P3 GROUP OF A CLASS OF POTENT HIV-1
TITLE 2 PROTEASE INHIBITORS AS A RESULT OF CONCERTED STRUCTURAL CHANGE IN
TITLE 3 80'S LOOP.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (PROTEASE);
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.4.23.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: NY5 ISOLATE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 GENE: NY5 ISOLATE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MUNSHI
REVDAT 3 27-DEC-23 1C70 1 REMARK
REVDAT 2 24-FEB-09 1C70 1 VERSN
REVDAT 1 28-DEC-00 1C70 0
JRNL AUTH S.MUNSHI,Z.CHEN,Y.YAN,Y.LI,D.B.OLSEN,H.B.SCHOCK,B.B.GALVIN,
JRNL AUTH 2 B.DORSEY,L.C.KUO
JRNL TITL AN ALTERNATE BINDING SITE FOR THE P1-P3 GROUP OF A CLASS OF
JRNL TITL 2 POTENT HIV-1 PROTEASE INHIBITORS AS A RESULT OF CONCERTED
JRNL TITL 3 STRUCTURAL CHANGE IN THE 80S LOOP OF THE PROTEASE.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 56 381 2000
JRNL REFN ISSN 0907-4449
JRNL PMID 10739910
JRNL DOI 10.1107/S0907444900000469
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
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) : 0.160
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 1514
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 106
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 2.800
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; 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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1C70 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JAN-00.
REMARK 100 THE DEPOSITION ID IS D_1000001413.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7292
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: CRYSTALS OBTAINED BY CO-CRYSTALLIZATION AT PH 5.2, USING
REMARK 200 0.6M NACL AS PRECIPITATING AGENT IN 0.1M SODIUM ACETATE BUFFER.
REMARK 200 PROTEIN WAS AT 5.5 MG/ML CONCENTRATION.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 29.93000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.56000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.93000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.56000
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: THERE IS ONE PROTEASE DIMER IN AN ASYMMETRICAL UNIT. THE
REMARK 300 TWO MOLECULES ARE LABELED AS CHAIN A AND CHAIN B. THERE
REMARK 300 IS ONE L-756,423 INHIBITOR MOLECULE LABELED AS L75.
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: 5040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS B 269 NE2 HIS B 269 CD2 -0.074
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TRP A 6 CD1 - CG - CD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 TRP A 6 CB - CG - CD1 ANGL. DEV. = -9.4 DEGREES
REMARK 500 TRP A 6 CE2 - CD2 - CG ANGL. DEV. = -6.5 DEGREES
REMARK 500 TRP A 6 CG - CD2 - CE3 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG A 41 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG A 41 NE - CZ - NH2 ANGL. DEV. = 4.5 DEGREES
REMARK 500 TRP A 42 CD1 - CG - CD2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 TRP A 42 CE2 - CD2 - CG ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG A 57 NE - CZ - NH2 ANGL. DEV. = 3.9 DEGREES
REMARK 500 TRP B 206 CD1 - CG - CD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 TRP B 206 CB - CG - CD1 ANGL. DEV. = -8.9 DEGREES
REMARK 500 TRP B 206 CE2 - CD2 - CG ANGL. DEV. = -6.1 DEGREES
REMARK 500 TRP B 206 CG - CD2 - CE3 ANGL. DEV. = 5.6 DEGREES
REMARK 500 LEU B 223 CA - CB - CG ANGL. DEV. = 15.8 DEGREES
REMARK 500 ARG B 241 NE - CZ - NH1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ARG B 241 NE - CZ - NH2 ANGL. DEV. = 5.3 DEGREES
REMARK 500 TRP B 242 CD1 - CG - CD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 TRP B 242 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 LYS B 255 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 TYR B 259 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 VAL B 275 CG1 - CB - CG2 ANGL. DEV. = -11.1 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 GLU A 35 105.64 -30.22
REMARK 500 GLU B 235 106.79 -52.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 L-756,423 IS N-[2(R)-HYDROXY-1(S)-INDANYL]-2(R)-PHENYLMETHYL
REMARK 600 -4(S)-HYDROXY-5-[4-[2-BENZOFURANYLMETHYL]-2(S)-[TERT-
REMARK 600 BUTYLAMINOCARBONYL]-PIPERAZINYL]-PENTANEAMIDE
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE L75 B 423
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1C6X RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE WITH L-739,622
REMARK 900 RELATED ID: 1C6Y RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE WITH L-735,524
REMARK 900 RELATED ID: 1C6Z RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE WITH SAQUINAVIR
DBREF 1C70 A 1 99 UNP O92103 O92103_9HIV1 1 99
DBREF 1C70 B 201 299 UNP O92103 O92103_9HIV1 1 99
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 SER 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 SER 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 L75 B 423 48
HETNAM L75 N-[2(R)-HYDROXY-1(S)-INDANYL]-2(R)-PHENYLMETHYL-4(S)-
HETNAM 2 L75 HYDROXY-5-[4-[2-BENZOFURANYLMETHYL]-2(S)-[TERT-
HETNAM 3 L75 BUTYLAMINOCARBONYL]-PIPERAZINYL]-PENTANEAMIDE
HETSYN L75 L-756,423
FORMUL 3 L75 C39 H48 N4 O5
FORMUL 4 HOH *106(H2 O)
HELIX 1 1 GLY A 86 THR A 91 1 6
HELIX 2 2 GLY B 286 THR B 291 1 6
SHEET 1 A 4 GLN A 2 THR A 4 0
SHEET 2 A 4 THR B 296 ASN B 298 -1 O LEU B 297 N ILE A 3
SHEET 3 A 4 THR A 96 ASN A 98 -1 N THR A 96 O ASN B 298
SHEET 4 A 4 GLN B 202 THR B 204 -1 N ILE B 203 O LEU A 97
SHEET 1 B 7 LYS A 43 GLY A 48 0
SHEET 2 B 7 PHE A 53 ILE A 66 -1 N ILE A 54 O ILE A 47
SHEET 3 B 7 HIS A 69 GLY A 78 -1 O HIS A 69 N ILE A 66
SHEET 4 B 7 THR A 31 GLU A 34 1 O THR A 31 N LEU A 76
SHEET 5 B 7 ILE A 84 ILE A 85 -1 N ILE A 84 O VAL A 32
SHEET 6 B 7 GLN A 18 LEU A 24 1 O LEU A 23 N ILE A 85
SHEET 7 B 7 LEU A 10 ILE A 15 -1 O VAL A 11 N ALA A 22
SHEET 1 C 7 LYS B 243 GLY B 249 0
SHEET 2 C 7 GLY B 252 ILE B 266 -1 O GLY B 252 N GLY B 249
SHEET 3 C 7 HIS B 269 GLY B 278 -1 O HIS B 269 N ILE B 266
SHEET 4 C 7 THR B 231 GLU B 234 1 O THR B 231 N LEU B 276
SHEET 5 C 7 ASN B 283 ILE B 285 -1 N ILE B 284 O VAL B 232
SHEET 6 C 7 GLN B 218 LEU B 224 1 O GLU B 221 N ASN B 283
SHEET 7 C 7 LEU B 210 ILE B 215 -1 O VAL B 211 N ALA B 222
SITE 1 AC1 19 TRP A 6 ARG A 8 LEU A 23 ASP A 25
SITE 2 AC1 19 GLY A 48 GLY A 49 ILE A 50 ASP B 225
SITE 3 AC1 19 GLY B 227 ALA B 228 ASP B 229 ASP B 230
SITE 4 AC1 19 VAL B 232 GLY B 248 GLY B 249 PRO B 279
SITE 5 AC1 19 THR B 280 PRO B 281 HOH B 306
CRYST1 59.860 87.120 46.970 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 0.016706 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011478 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021290 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
