HEADER HYDROLASE/HYDROLASE INHIBITOR 16-SEP-96 1ODW
TITLE NATIVE HIV-1 PROTEINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIV-1 PROTEASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: RETROPEPSIN;
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_COMMON: HIV-1;
SOURCE 4 ORGANISM_TAXID: 11676;
SOURCE 5 GENE: GAG-POL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PMAL-C2
KEYWDS PROTEINASE, RETROPEPSIN, RETROVIRUS, HIV, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.THANKI,J.KERVINEN,A.WLODAWER
REVDAT 4 14-FEB-24 1ODW 1 REMARK
REVDAT 3 13-JUL-11 1ODW 1 VERSN
REVDAT 2 24-FEB-09 1ODW 1 VERSN
REVDAT 1 01-APR-97 1ODW 0
JRNL AUTH J.KERVINEN,N.THANKI,A.ZDANOV,J.TINO,J.BARRISH,P.F.LIN,
JRNL AUTH 2 R.COLONNO,K.RICCARDI,H.SAMANTA,A.WLODAWER
JRNL TITL STRUCTURAL ANALYSIS OF THE NATIVE AND DRUG-RESISTANT HIV-1
JRNL TITL 2 PROTEINASES COMPLEXED WITH AN AMINODIOL INHIBITOR
JRNL REF PROTEIN PEPT.LETT. V. 3 399 1996
JRNL REFN ISSN 0929-8665
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.9
REMARK 3 NUMBER OF REFLECTIONS : 10837
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 + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 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 : 39
REMARK 3 SOLVENT ATOMS : 65
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 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.021 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.056 ; 0.035
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.066 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.016 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.221 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.197 ; 0.300
REMARK 3 MULTIPLE TORSION (A) : 0.219 ; 0.300
REMARK 3 H-BOND (X...Y) (A) : 0.159 ; 0.300
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 2.900 ; 3.000
REMARK 3 STAGGERED (DEGREES) : 19.000; 10.000
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.608 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.401 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.662 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.494 ; 4.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ODW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175439.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-94
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
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) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10837
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.9
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.06900
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 44.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 26.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 31.10000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.70000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 31.10000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.70000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 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 ASP A 29 CB - CG - OD1 ANGL. DEV. = 9.3 DEGREES
REMARK 500 ASP A 29 CB - CG - OD2 ANGL. DEV. = -14.6 DEGREES
REMARK 500 GLU A 34 CB - CA - C ANGL. DEV. = -16.5 DEGREES
REMARK 500 GLU A 34 CA - CB - CG ANGL. DEV. = 21.9 DEGREES
REMARK 500 GLU A 34 OE1 - CD - OE2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 GLU A 34 CG - CD - OE2 ANGL. DEV. = 13.7 DEGREES
REMARK 500 LYS A 43 CA - CB - CG ANGL. DEV. = 17.7 DEGREES
REMARK 500 ARG A 57 NH1 - CZ - NH2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG A 57 NE - CZ - NH1 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ASP A 60 O - C - N ANGL. DEV. = 10.9 DEGREES
REMARK 500 GLN A 61 CA - CB - CG ANGL. DEV. = 18.9 DEGREES
REMARK 500 ALA A 71 N - CA - CB ANGL. DEV. = -12.5 DEGREES
REMARK 500 GLY A 73 O - C - N ANGL. DEV. = 9.8 DEGREES
REMARK 500 ILE A 84 CA - CB - CG2 ANGL. DEV. = 12.9 DEGREES
REMARK 500 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG A 87 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 PHE A 99 N - CA - CB ANGL. DEV. = 11.3 DEGREES
REMARK 500 VAL B 3 CA - CB - CG2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 GLN B 7 CA - CB - CG ANGL. DEV. = 16.9 DEGREES
REMARK 500 ARG B 8 CD - NE - CZ ANGL. DEV. = 9.7 DEGREES
REMARK 500 ARG B 8 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 8 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 LEU B 19 CB - CA - C ANGL. DEV. = 11.6 DEGREES
REMARK 500 LYS B 20 CA - CB - CG ANGL. DEV. = 17.5 DEGREES
REMARK 500 ASP B 30 CB - CG - OD1 ANGL. DEV. = -7.4 DEGREES
REMARK 500 GLU B 34 CB - CA - C ANGL. DEV. = -13.1 DEGREES
REMARK 500 GLU B 34 OE1 - CD - OE2 ANGL. DEV. = 10.0 DEGREES
REMARK 500 GLU B 34 CG - CD - OE2 ANGL. DEV. = -12.7 DEGREES
REMARK 500 MET B 36 CA - CB - CG ANGL. DEV. = 22.9 DEGREES
REMARK 500 MET B 46 CA - CB - CG ANGL. DEV. = -10.2 DEGREES
REMARK 500 ARG B 57 CD - NE - CZ ANGL. DEV. = 9.9 DEGREES
REMARK 500 ARG B 57 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 TYR B 59 CB - CG - CD1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 GLU B 65 OE1 - CD - OE2 ANGL. DEV. = 12.0 DEGREES
REMARK 500 HIS B 69 CE1 - NE2 - CD2 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ILE B 72 CA - CB - CG2 ANGL. DEV. = 17.6 DEGREES
REMARK 500 THR B 80 CB - CA - C ANGL. DEV. = -17.9 DEGREES
REMARK 500 THR B 80 N - CA - CB ANGL. DEV. = 11.7 DEGREES
REMARK 500 THR B 80 CA - CB - CG2 ANGL. DEV. = 10.9 DEGREES
REMARK 500 ARG B 87 NE - CZ - NH2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 LEU B 90 O - C - N ANGL. DEV. = 12.4 DEGREES
REMARK 500 ILE B 93 O - C - N ANGL. DEV. = -10.8 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 PRO A 79 76.98 -69.83
REMARK 500 PRO B 79 42.21 -73.02
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 0E8 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ODX RELATED DB: PDB
DBREF 1ODW A 1 99 UNP P04585 POL_HV1H2 489 587
DBREF 1ODW B 1 99 UNP P04585 POL_HV1H2 489 587
SEQRES 1 A 99 PRO GLN VAL 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 VAL 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 0E8 A 201 39
HETNAM 0E8 DI-TERT-BUTYL {IMINOBIS[(2S,3S)-3-HYDROXY-1-
HETNAM 2 0E8 PHENYLBUTANE-4,2-DIYL]}BISCARBAMATE
HETSYN 0E8 BMS-182193
FORMUL 3 0E8 C30 H45 N3 O6
FORMUL 4 HOH *65(H2 O)
HELIX 1 1 GLY A 86 ILE A 93 1 8
HELIX 2 2 GLY B 86 ILE B 93 1 8
SHEET 1 A 4 GLN A 18 LEU A 23 0
SHEET 2 A 4 LEU A 10 ILE A 15 -1 N ILE A 15 O GLN A 18
SHEET 3 A 4 ILE A 62 ILE A 66 -1 N GLU A 65 O LYS A 14
SHEET 4 A 4 HIS A 69 GLY A 73 -1 N GLY A 73 O ILE A 62
SHEET 1 B 3 TRP A 42 GLY A 49 0
SHEET 2 B 3 GLY A 52 TYR A 59 -1 N GLN A 58 O LYS A 43
SHEET 3 B 3 VAL A 75 GLY A 78 -1 N VAL A 77 O ARG A 57
SHEET 1 C 2 THR A 96 ASN A 98 0
SHEET 2 C 2 THR B 96 ASN B 98 -1 N ASN B 98 O THR A 96
SHEET 1 D 2 LEU B 10 LYS B 14 0
SHEET 2 D 2 LEU B 19 LEU B 23 -1 N ALA B 22 O VAL B 11
SHEET 1 E 4 VAL B 32 GLU B 34 0
SHEET 2 E 4 VAL B 75 GLY B 78 1 N LEU B 76 O LEU B 33
SHEET 3 E 4 GLY B 52 TYR B 59 -1 N TYR B 59 O VAL B 75
SHEET 4 E 4 LYS B 43 GLY B 49 -1 N GLY B 49 O GLY B 52
SHEET 1 F 2 ILE B 62 GLU B 65 0
SHEET 2 F 2 LYS B 70 GLY B 73 -1 N GLY B 73 O ILE B 62
SITE 1 AC1 16 ASP A 25 GLY A 27 GLY A 48 GLY A 49
SITE 2 AC1 16 ILE A 50 PRO A 81 ILE A 84 HOH A 301
SITE 3 AC1 16 ASP B 25 GLY B 27 ILE B 47 GLY B 48
SITE 4 AC1 16 GLY B 49 ILE B 50 PRO B 81 HOH B 401
SITE 1 ACT 2 ASP A 25 ASP B 25
CRYST1 52.000 59.400 62.200 90.00 90.00 90.00 P 21 21 21 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 0.019231 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016835 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016077 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
