HEADER HYDROLASE 29-MAR-07 2PC0
TITLE APO WILD-TYPE HIV PROTEASE IN THE OPEN CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.23.16;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 STRAIN: BH10;
SOURCE 5 GENE: POL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21.DE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PLYS S
KEYWDS HIV PROTEASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.HEASLET,R.ROSENFELD,M.J.GIFFIN,J.H.ELDER,D.E.MCREE,C.D.STOUT
REVDAT 7 30-AUG-23 2PC0 1 REMARK
REVDAT 6 20-OCT-21 2PC0 1 REMARK SEQADV LINK
REVDAT 5 18-OCT-17 2PC0 1 REMARK
REVDAT 4 13-JUL-11 2PC0 1 VERSN
REVDAT 3 24-FEB-09 2PC0 1 VERSN
REVDAT 2 21-AUG-07 2PC0 1 JRNL
REVDAT 1 26-JUN-07 2PC0 0
JRNL AUTH H.HEASLET,R.ROSENFELD,M.GIFFIN,Y.C.LIN,K.TAM,B.E.TORBETT,
JRNL AUTH 2 J.H.ELDER,D.E.MCREE,C.D.STOUT
JRNL TITL CONFORMATIONAL FLEXIBILITY IN THE FLAP DOMAINS OF
JRNL TITL 2 LIGAND-FREE HIV PROTEASE.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 63 866 2007
JRNL REFN ISSN 0907-4449
JRNL PMID 17642513
JRNL DOI 10.1107/S0907444907029125
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 22398
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) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1165
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1502
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.54
REMARK 3 BIN R VALUE (WORKING SET) : 0.2090
REMARK 3 BIN FREE R VALUE SET COUNT : 82
REMARK 3 BIN FREE R VALUE : 0.2430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 760
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 112
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.30000
REMARK 3 B22 (A**2) : 0.30000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.060
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.057
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.034
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.871
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 868 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 860 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1189 ; 1.196 ; 1.995
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2007 ; 0.593 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 117 ; 6.325 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 29 ;43.646 ;24.483
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 165 ; 9.025 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;18.353 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 142 ; 0.390 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 974 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 157 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 116 ; 0.296 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 837 ; 0.202 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 432 ; 0.166 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 518 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 54 ; 0.158 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 25 ; 0.216 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 89 ; 0.317 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 23 ; 0.107 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 720 ; 2.151 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 227 ; 1.610 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 907 ; 2.672 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 361 ; 3.752 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 282 ; 5.026 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 5
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1001 A 1021
REMARK 3 RESIDUE RANGE : A 1022 A 1040
REMARK 3 RESIDUE RANGE : A 1041 A 1055
REMARK 3 RESIDUE RANGE : A 1056 A 1079
REMARK 3 RESIDUE RANGE : A 1080 A 1099
REMARK 3 ORIGIN FOR THE GROUP (A): 3.0660 4.6361 -11.3929
REMARK 3 T TENSOR
REMARK 3 T11: -0.0169 T22: 0.0011
REMARK 3 T33: -0.0262 T12: 0.0168
REMARK 3 T13: -0.0052 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.2187 L22: 0.2088
REMARK 3 L33: 0.6463 L12: 0.1052
REMARK 3 L13: -0.1084 L23: -0.2261
REMARK 3 S TENSOR
REMARK 3 S11: -0.0351 S12: -0.0004 S13: -0.0038
REMARK 3 S21: -0.0032 S22: 0.0249 S23: -0.0077
REMARK 3 S31: 0.0672 S32: 0.0960 S33: 0.0102
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2PC0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-07.
REMARK 100 THE DEPOSITION ID IS D_1000042210.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 103
REMARK 200 PH : 5.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL1-5
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, PARALLEL
REMARK 200 OPTICS : DOUBLE-CRYSTAL MONOCHROMATOR, 1M
REMARK 200 LONG RH COATED BENT CYLINDRICAL
REMARK 200 MIRROR FOR HORIZONTAL AND
REMARK 200 VERTICAL FOCUSING
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22409
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 20.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.52200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2AZ8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE, 20% W/V PEG
REMARK 280 3350, PH 5.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 50.68500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 23.20800
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 23.20800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 25.34250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 23.20800
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 23.20800
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 76.02750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 23.20800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 23.20800
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 25.34250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 23.20800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 23.20800
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 76.02750
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 50.68500
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
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 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 1 O
REMARK 620 2 HOH A 1 O 17.9
REMARK 620 3 HOH A 50 O 86.4 68.5
REMARK 620 4 HOH A 50 O 102.5 120.3 170.4
REMARK 620 5 HOH A 62 O 175.4 157.6 89.1 82.0
REMARK 620 6 HOH A 62 O 140.2 122.3 54.0 116.8 35.2
REMARK 620 7 HOH A 85 O 82.2 79.0 75.7 108.8 97.2 90.4
REMARK 620 8 HOH A 85 O 80.7 75.8 74.4 103.3 97.6 84.5 146.2
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGR A 907
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2HB4 RELATED DB: PDB
REMARK 900 APO WILD-TYPE HIV PROTEASE IN THE CURLED CONFORMATION.
REMARK 900 RELATED ID: 2HB2 RELATED DB: PDB
REMARK 900 APO 6X MUTANT HIV PROTEASE IN THE CURLED CONFORMATION.
REMARK 900 RELATED ID: 2AZ8 RELATED DB: PDB
REMARK 900 WILD-TYPE HIV PROTEASE IN COMPLEX WITH TL-3.
DBREF 2PC0 A 1001 1099 UNP A3FH86 A3FH86_9HIV1 1 99
SEQADV 2PC0 LYS A 1007 UNP A3FH86 GLN 7 ENGINEERED MUTATION
SEQRES 1 A 99 PRO GLN ILE THR LEU TRP LYS 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
HET MG A 201 1
HET PGR A 907 5
HETNAM MG MAGNESIUM ION
HETNAM PGR R-1,2-PROPANEDIOL
FORMUL 2 MG MG 2+
FORMUL 3 PGR C3 H8 O2
FORMUL 4 HOH *112(H2 O)
HELIX 1 1 GLY A 1086 ILE A 1093 1 8
SHEET 1 A 8 TRP A1042 GLY A1048 0
SHEET 2 A 8 PHE A1053 ILE A1066 -1 O GLN A1058 N LYS A1043
SHEET 3 A 8 HIS A1069 VAL A1077 -1 O VAL A1077 N ARG A1057
SHEET 4 A 8 VAL A1032 LEU A1033 1 N LEU A1033 O LEU A1076
SHEET 5 A 8 ILE A1084 ILE A1085 -1 O ILE A1084 N VAL A1032
SHEET 6 A 8 GLN A1018 LEU A1024 1 N LEU A1023 O ILE A1085
SHEET 7 A 8 LEU A1010 ILE A1015 -1 N ILE A1013 O LYS A1020
SHEET 8 A 8 PHE A1053 ILE A1066 -1 O GLU A1065 N LYS A1014
LINK O HOH A 1 MG MG A 201 1555 1555 2.04
LINK O HOH A 1 MG MG A 201 7555 1555 2.23
LINK O HOH A 50 MG MG A 201 1555 1555 2.69
LINK O HOH A 50 MG MG A 201 7555 1555 1.53
LINK O HOH A 62 MG MG A 201 1555 1555 1.94
LINK O HOH A 62 MG MG A 201 7555 1555 2.31
LINK O HOH A 85 MG MG A 201 1555 1555 2.15
LINK O HOH A 85 MG MG A 201 7555 1555 2.26
SITE 1 AC1 4 HOH A 1 HOH A 50 HOH A 62 HOH A 85
SITE 1 AC2 6 HOH A 7 HOH A 100 GLY A1052 PHE A1053
SITE 2 AC2 6 LEU A1063 ILE A1072
CRYST1 46.416 46.416 101.370 90.00 90.00 90.00 P 41 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 0.021544 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021544 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009865 0.00000
(ATOM LINES ARE NOT SHOWN.)
END