HEADER HYDROLASE/HYDROLASE INHIBITOR 17-APR-07 2PK5
TITLE CRYSTAL STRUCTURE OF HIV-1 PROTEASE (Q7K, L33I, L63I ) IN COMPLEX WITH
TITLE 2 KNI-10075
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 STRAIN: SUBTYPE B;
SOURCE 5 GENE: GAG-POL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24A+
KEYWDS PROTEASE COMPLEX, VIRAL PROTEIN, HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.ARMSTRONG,V.LAFONT,Y.KISO,E.FREIRE,L.M.AMZEL
REVDAT 7 30-AUG-23 2PK5 1 REMARK
REVDAT 6 20-OCT-21 2PK5 1 COMPND REMARK SEQADV HETNAM
REVDAT 5 18-OCT-17 2PK5 1 REMARK
REVDAT 4 13-JUL-11 2PK5 1 VERSN
REVDAT 3 24-FEB-09 2PK5 1 VERSN
REVDAT 2 14-AUG-07 2PK5 1 JRNL
REVDAT 1 08-MAY-07 2PK5 0
JRNL AUTH V.LAFONT,A.A.ARMSTRONG,H.OHTAKA,Y.KISO,L.MARIO AMZEL,
JRNL AUTH 2 E.FREIRE
JRNL TITL COMPENSATING ENTHALPIC AND ENTROPIC CHANGES HINDER BINDING
JRNL TITL 2 AFFINITY OPTIMIZATION.
JRNL REF CHEM.BIOL.DRUG DES. V. 69 413 2007
JRNL REFN ISSN 1747-0277
JRNL PMID 17581235
JRNL DOI 10.1111/J.1747-0285.2007.00519.X
REMARK 2
REMARK 2 RESOLUTION. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 18976
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) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1940
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1196
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.11
REMARK 3 BIN R VALUE (WORKING SET) : 0.1650
REMARK 3 BIN FREE R VALUE SET COUNT : 156
REMARK 3 BIN FREE R VALUE : 0.2260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1516
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 241
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.26000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.26000
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): 0.143
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.133
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.081
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.192
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1722 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2348 ; 1.591 ; 2.067
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 204 ; 6.276 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 53 ;41.089 ;24.717
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 300 ;11.633 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;16.876 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 279 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1230 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 772 ; 0.205 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1178 ; 0.313 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 170 ; 0.161 ; 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): 44 ; 0.222 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.108 ; 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): 1090 ; 0.952 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1667 ; 1.294 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 757 ; 2.183 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 681 ; 3.166 ; 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 : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 99
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6570 -11.2880 -10.0800
REMARK 3 T TENSOR
REMARK 3 T11: 0.0248 T22: -0.0340
REMARK 3 T33: -0.1038 T12: 0.0027
REMARK 3 T13: -0.0145 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 0.9441 L22: 0.9824
REMARK 3 L33: 1.1740 L12: -0.2948
REMARK 3 L13: -0.4869 L23: 0.3869
REMARK 3 S TENSOR
REMARK 3 S11: 0.0194 S12: -0.0934 S13: 0.0355
REMARK 3 S21: 0.0706 S22: 0.0178 S23: -0.0501
REMARK 3 S31: -0.0569 S32: 0.0963 S33: -0.0371
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 99
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4990 -22.3010 -28.6470
REMARK 3 T TENSOR
REMARK 3 T11: 0.0049 T22: -0.0310
REMARK 3 T33: -0.0955 T12: -0.0038
REMARK 3 T13: -0.0032 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.4110 L22: 1.7422
REMARK 3 L33: 0.9764 L12: -0.6777
REMARK 3 L13: -0.2732 L23: 0.5189
REMARK 3 S TENSOR
REMARK 3 S11: -0.0259 S12: 0.0181 S13: -0.0165
REMARK 3 S21: -0.0578 S22: 0.0337 S23: 0.0414
REMARK 3 S31: -0.0217 S32: -0.0063 S33: -0.0078
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 900 A 900
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7750 -20.8780 -17.1210
REMARK 3 T TENSOR
REMARK 3 T11: -0.0525 T22: -0.0635
REMARK 3 T33: -0.1500 T12: 0.0126
REMARK 3 T13: -0.0125 T23: 0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 1.8195 L22: 13.3364
REMARK 3 L33: 4.1193 L12: -3.5304
REMARK 3 L13: -2.0699 L23: 0.6332
REMARK 3 S TENSOR
REMARK 3 S11: 0.0788 S12: 0.1200 S13: -0.3766
REMARK 3 S21: -0.1510 S22: -0.2267 S23: 0.5015
REMARK 3 S31: 0.0314 S32: -0.1566 S33: 0.1479
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 2PK5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-07.
REMARK 100 THE DEPOSITION ID IS D_1000042466.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.10
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19013
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.11300
REMARK 200 R SYM (I) : 0.11300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.41500
REMARK 200 R SYM FOR SHELL (I) : 0.41500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.630
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1MSM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM CITRATE BUFFER PH 5.4, NACL 750
REMARK 280 MM, 10 MM DTT, 3 MM NAN3, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298KK
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 29.42100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.99550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.42100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.99550
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: 5480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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 35 121.99 -37.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE INHIBITOR
REMARK 630 MOLECULE NAME: (4R)-N-[(1S,2R)-2-HYDROXY-2,3-DIHYDRO-1H-INDEN-1-YL]
REMARK 630 -3-[(2S,3S)-2-HYDROXY-3-({N-[(ISOQUINOLIN-5-YLOXY)ACETYL]-3-
REMARK 630 (METHYL SULFONYL)-L-ALANYL}AMINO)-4-PHENYLBUTANOYL]-5,5-DIMETHYL-1,
REMARK 630 3-THIAZOLIDINE-4-CARBOXAMIDE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 075 A 900
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: TUC KNB 005 00B 00X
REMARK 630 DETAILS: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 075 A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 401
DBREF 2PK5 A 1 99 UNP P03367 POL_HV1BR 501 599
DBREF 2PK5 B 1 99 UNP P03367 POL_HV1BR 501 599
SEQADV 2PK5 LYS A 7 UNP P03367 GLN 507 ENGINEERED MUTATION
SEQADV 2PK5 ILE A 33 UNP P03367 LEU 533 ENGINEERED MUTATION
SEQADV 2PK5 ILE A 63 UNP P03367 LEU 563 ENGINEERED MUTATION
SEQADV 2PK5 LYS B 7 UNP P03367 GLN 507 ENGINEERED MUTATION
SEQADV 2PK5 ILE B 33 UNP P03367 LEU 533 ENGINEERED MUTATION
SEQADV 2PK5 ILE B 63 UNP P03367 LEU 563 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 ILE 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 ILE 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 LYS 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 ILE 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 ILE 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 075 A 900 112
HET GOL A 401 6
HETNAM 075 (4R)-N-[(1S,2R)-2-HYDROXY-2,3-DIHYDRO-1H-INDEN-1-YL]-3-
HETNAM 2 075 [(2S,3S)-2-HYDROXY-3-({N-[(ISOQUINOLIN-5-YLOXY)
HETNAM 3 075 ACETYL]-3-(METHYL SULFONYL)-L-ALANYL}AMINO)-4-
HETNAM 4 075 PHENYLBUTANOYL]-5,5-DIMETHYL-1,3-THIAZOLIDINE-4-
HETNAM 5 075 CARBOXAMIDE
HETNAM GOL GLYCEROL
HETSYN 075 KNI-10075
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 075 C40 H45 N5 O9 S2
FORMUL 4 GOL C3 H8 O3
FORMUL 5 HOH *241(H2 O)
HELIX 1 1 GLY A 86 THR A 91 1 6
HELIX 2 2 GLY B 86 THR B 91 1 6
SHEET 1 A 4 GLN A 2 ILE A 3 0
SHEET 2 A 4 THR B 96 ASN B 98 -1 O LEU B 97 N ILE A 3
SHEET 3 A 4 THR A 96 ASN A 98 -1 N ASN A 98 O THR B 96
SHEET 4 A 4 GLN B 2 ILE B 3 -1 O ILE B 3 N LEU A 97
SHEET 1 B 8 TRP A 42 GLY A 49 0
SHEET 2 B 8 GLY A 52 ILE A 66 -1 O VAL A 56 N LYS A 45
SHEET 3 B 8 HIS A 69 VAL A 77 -1 O VAL A 75 N TYR A 59
SHEET 4 B 8 VAL A 32 ILE A 33 1 N ILE A 33 O LEU A 76
SHEET 5 B 8 ILE A 84 ILE A 85 -1 O ILE A 84 N VAL A 32
SHEET 6 B 8 GLN A 18 LEU A 24 1 N LEU A 23 O ILE A 85
SHEET 7 B 8 LEU A 10 ILE A 15 -1 N ILE A 13 O LYS A 20
SHEET 8 B 8 GLY A 52 ILE A 66 -1 O GLU A 65 N LYS A 14
SHEET 1 C 8 LYS B 43 GLY B 48 0
SHEET 2 C 8 PHE B 53 ILE B 66 -1 O GLN B 58 N LYS B 43
SHEET 3 C 8 HIS B 69 VAL B 77 -1 O HIS B 69 N ILE B 66
SHEET 4 C 8 VAL B 32 ILE B 33 1 N ILE B 33 O LEU B 76
SHEET 5 C 8 ILE B 84 ILE B 85 -1 O ILE B 84 N VAL B 32
SHEET 6 C 8 GLN B 18 LEU B 24 1 N LEU B 23 O ILE B 85
SHEET 7 C 8 LEU B 10 ILE B 15 -1 N ILE B 13 O LYS B 20
SHEET 8 C 8 PHE B 53 ILE B 66 -1 O GLU B 65 N LYS B 14
SITE 1 AC1 43 TRP A 6 LEU A 23 ASP A 25 GLY A 27
SITE 2 AC1 43 ALA A 28 ASP A 29 ASP A 30 VAL A 32
SITE 3 AC1 43 ILE A 47 GLY A 48 GLY A 49 ILE A 50
SITE 4 AC1 43 PRO A 81 VAL A 82 ILE A 84 HOH A 903
SITE 5 AC1 43 HOH A 941 HOH A 956 HOH A 977 HOH A 988
SITE 6 AC1 43 HOH A1010 HOH A1011 ARG B 8 LEU B 23
SITE 7 AC1 43 ASP B 25 GLY B 27 ALA B 28 ASP B 29
SITE 8 AC1 43 ASP B 30 VAL B 32 ILE B 47 GLY B 48
SITE 9 AC1 43 GLY B 49 ILE B 50 PRO B 81 VAL B 82
SITE 10 AC1 43 ILE B 84 HOH B 103 HOH B 127 HOH B 198
SITE 11 AC1 43 HOH B 213 HOH B 217 HOH B 219
SITE 1 AC2 7 GLN A 18 MET A 36 SER A 37 THR B 12
SITE 2 AC2 7 GLU B 65 CYS B 67 GLY B 68
CRYST1 58.842 85.991 46.210 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 0.016995 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011629 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021640 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
