HEADER HYDROLASE 09-APR-01 1IEG
TITLE CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT S134A/H157A OF THE
TITLE 2 HUMAN CYTOMEGALOVIRUS PROTEASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAPSID PROTEIN P40: ASSEMBLIN PROTEASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 1-256;
COMPND 5 SYNONYM: HCMV PROTEASE;
COMPND 6 EC: 3.4.21.97;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 5;
SOURCE 3 ORGANISM_TAXID: 10360;
SOURCE 4 STRAIN: AD169;
SOURCE 5 GENE: UL80;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS COAT PROTEIN, HYDROLASE, SERINE PROTEASE, CATALYTIC TRIAD, VIRAL
KEYWDS 2 PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.KHAYAT,R.BATRA,M.J.MASSARIOL,L.LAGACE,L.TONG
REVDAT 6 07-FEB-24 1IEG 1 REMARK
REVDAT 5 27-OCT-21 1IEG 1 SEQADV
REVDAT 4 13-JUL-11 1IEG 1 VERSN
REVDAT 3 24-FEB-09 1IEG 1 VERSN
REVDAT 2 01-APR-03 1IEG 1 JRNL
REVDAT 1 06-JUN-01 1IEG 0
JRNL AUTH R.KHAYAT,R.BATRA,M.J.MASSARIOL,L.LAGACE,L.TONG
JRNL TITL INVESTIGATING THE ROLE OF HISTIDINE 157 IN THE CATALYTIC
JRNL TITL 2 ACTIVITY OF HUMAN CYTOMEGALOVIRUS PROTEASE.
JRNL REF BIOCHEMISTRY V. 40 6344 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11371196
JRNL DOI 10.1021/BI010158B
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2999950.290
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 32752
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) : 0.226
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.500
REMARK 3 FREE R VALUE TEST SET COUNT : 2471
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4785
REMARK 3 BIN R VALUE (WORKING SET) : 0.2210
REMARK 3 BIN FREE R VALUE : 0.2470
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 399
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3341
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 183
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.38000
REMARK 3 B22 (A**2) : -4.38000
REMARK 3 B33 (A**2) : 8.77000
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) : 0.07
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) : 0.11
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.900
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) : 1.420 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.250 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.030 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.970 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.41
REMARK 3 BSOL : 48.48
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.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IEG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013206.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-NOV-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : FUJI
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32752
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 5.160
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.1100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.16100
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: GLRF
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 19% PEG3350, 0.1M MES 6.0, 15%
REMARK 280 GLYCEROL, 5% T-BUOH, 0.3M NACL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 294K, PH 6.0
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 83.80000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 38.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 38.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 41.90000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 38.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 38.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 125.70000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 38.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 38.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 41.90000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 38.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 38.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 125.70000
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 83.80000
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: 3070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 MET A 3
REMARK 465 ASP A 4
REMARK 465 GLU A 5
REMARK 465 GLN A 6
REMARK 465 GLN A 7
REMARK 465 SER A 8
REMARK 465 HIS A 44
REMARK 465 ALA A 45
REMARK 465 GLN A 46
REMARK 465 GLY A 47
REMARK 465 GLN A 48
REMARK 465 GLY A 49
REMARK 465 GLN A 50
REMARK 465 PRO A 51
REMARK 465 SER A 52
REMARK 465 LEU A 53
REMARK 465 SER A 54
REMARK 465 VAL A 55
REMARK 465 SER A 135
REMARK 465 ARG A 136
REMARK 465 ARG A 137
REMARK 465 CYS A 138
REMARK 465 ASP A 139
REMARK 465 ASP A 140
REMARK 465 VAL A 141
REMARK 465 GLU A 142
REMARK 465 GLN A 143
REMARK 465 ALA A 144
REMARK 465 THR A 145
REMARK 465 SER A 146
REMARK 465 LEU A 147
REMARK 465 SER A 148
REMARK 465 GLY A 149
REMARK 465 SER A 150
REMARK 465 GLU A 151
REMARK 465 THR A 152
REMARK 465 THR A 153
REMARK 465 ARG A 201
REMARK 465 CYS A 202
REMARK 465 GLY A 203
REMARK 465 SER A 204
REMARK 465 THR A 205
REMARK 465 ALA A 206
REMARK 465 VAL A 207
REMARK 465 ASP A 208
REMARK 465 ALA A 209
REMARK 465 SER A 210
REMARK 465 MET B 301
REMARK 465 THR B 302
REMARK 465 MET B 303
REMARK 465 ASP B 304
REMARK 465 HIS B 344
REMARK 465 ALA B 345
REMARK 465 GLN B 346
REMARK 465 GLY B 347
REMARK 465 GLN B 348
REMARK 465 GLY B 349
REMARK 465 GLN B 350
REMARK 465 PRO B 351
REMARK 465 SER B 352
REMARK 465 LEU B 353
REMARK 465 SER B 354
REMARK 465 ARG B 436
REMARK 465 ARG B 437
REMARK 465 CYS B 438
REMARK 465 ASP B 439
REMARK 465 ASP B 440
REMARK 465 VAL B 441
REMARK 465 GLU B 442
REMARK 465 GLN B 443
REMARK 465 ALA B 444
REMARK 465 THR B 445
REMARK 465 SER B 446
REMARK 465 LEU B 447
REMARK 465 SER B 448
REMARK 465 GLY B 449
REMARK 465 SER B 450
REMARK 465 GLU B 451
REMARK 465 THR B 452
REMARK 465 ARG B 550
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 4 O HOH B 31 2.17
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 TRP A 42 28.64 -79.22
REMARK 500 SER A 113 -73.12 22.48
REMARK 500 TYR A 128 73.73 -118.23
REMARK 500 PHE A 155 -117.30 -87.98
REMARK 500 LYS A 156 -64.19 177.65
REMARK 500 ALA A 157 164.92 177.08
REMARK 500 THR A 169 37.90 -92.46
REMARK 500 SER A 216 -165.08 -127.56
REMARK 500 LEU B 334 81.43 -154.24
REMARK 500 SER B 413 -84.68 -0.92
REMARK 500 ASP B 418 88.27 -150.60
REMARK 500 TYR B 428 68.11 -110.49
REMARK 500 THR B 469 35.55 -91.61
REMARK 500 ASP B 508 55.96 -94.31
REMARK 500 ALA B 509 -113.86 -54.59
REMARK 500 SER B 510 30.92 -99.31
REMARK 500 SER B 516 -159.36 -125.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IEF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT S134A OF THE HUMAN
REMARK 900 CYTOMEGALOVIRUS PROTEASE
REMARK 900 RELATED ID: 1IED RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE H157E MUTANT OF THE HUMAN CYTOMEGALOVIRUS
REMARK 900 PROTEASE
REMARK 900 RELATED ID: 1IEC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE H157A MUTANT OF THE HUMAN CYTOMEGALOVIRUS
REMARK 900 PROTEASE
REMARK 900 RELATED ID: 1ID4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE H157Q MUTANT OF THE HUMAN CYTOMEGALOVIRUS
REMARK 900 PROTEASE
REMARK 900 RELATED ID: 2WPO RELATED DB: PDB
REMARK 900 CONSERVED MODE OF PEPTIDOMIMETIC INHIBITION AND SUBSTRATE
REMARK 900 RECOGNITION OF HUMAN CYTOMEGALOVIRUS PROTEASE
REMARK 900 RELATED ID: 1WPO RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN CYTOMEGALOVIRUS PROTEASE
DBREF 1IEG A 1 256 UNP P16753 VP40_HCMVA 1 256
DBREF 1IEG B 301 556 UNP P16753 VP40_HCMVA 1 256
SEQADV 1IEG ALA A 134 UNP P16753 SER 134 ENGINEERED MUTATION
SEQADV 1IEG GLN A 143 UNP P16753 ALA 143 ENGINEERED MUTATION
SEQADV 1IEG ALA A 157 UNP P16753 HIS 157 ENGINEERED MUTATION
SEQADV 1IEG ALA B 434 UNP P16753 SER 134 ENGINEERED MUTATION
SEQADV 1IEG GLN B 443 UNP P16753 ALA 143 ENGINEERED MUTATION
SEQADV 1IEG ALA B 457 UNP P16753 HIS 157 ENGINEERED MUTATION
SEQRES 1 A 256 MET THR MET ASP GLU GLN GLN SER GLN ALA VAL ALA PRO
SEQRES 2 A 256 VAL TYR VAL GLY GLY PHE LEU ALA ARG TYR ASP GLN SER
SEQRES 3 A 256 PRO ASP GLU ALA GLU LEU LEU LEU PRO ARG ASP VAL VAL
SEQRES 4 A 256 GLU HIS TRP LEU HIS ALA GLN GLY GLN GLY GLN PRO SER
SEQRES 5 A 256 LEU SER VAL ALA LEU PRO LEU ASN ILE ASN HIS ASP ASP
SEQRES 6 A 256 THR ALA VAL VAL GLY HIS VAL ALA ALA MET GLN SER VAL
SEQRES 7 A 256 ARG ASP GLY LEU PHE CYS LEU GLY CYS VAL THR SER PRO
SEQRES 8 A 256 ARG PHE LEU GLU ILE VAL ARG ARG ALA SER GLU LYS SER
SEQRES 9 A 256 GLU LEU VAL SER ARG GLY PRO VAL SER PRO LEU GLN PRO
SEQRES 10 A 256 ASP LYS VAL VAL GLU PHE LEU SER GLY SER TYR ALA GLY
SEQRES 11 A 256 LEU SER LEU ALA SER ARG ARG CYS ASP ASP VAL GLU GLN
SEQRES 12 A 256 ALA THR SER LEU SER GLY SER GLU THR THR PRO PHE LYS
SEQRES 13 A 256 ALA VAL ALA LEU CYS SER VAL GLY ARG ARG ARG GLY THR
SEQRES 14 A 256 LEU ALA VAL TYR GLY ARG ASP PRO GLU TRP VAL THR GLN
SEQRES 15 A 256 ARG PHE PRO ASP LEU THR ALA ALA ASP ARG ASP GLY LEU
SEQRES 16 A 256 ARG ALA GLN TRP GLN ARG CYS GLY SER THR ALA VAL ASP
SEQRES 17 A 256 ALA SER GLY ASP PRO PHE ARG SER ASP SER TYR GLY LEU
SEQRES 18 A 256 LEU GLY ASN SER VAL ASP ALA LEU TYR ILE ARG GLU ARG
SEQRES 19 A 256 LEU PRO LYS LEU ARG TYR ASP LYS GLN LEU VAL GLY VAL
SEQRES 20 A 256 THR GLU ARG GLU SER TYR VAL LYS ALA
SEQRES 1 B 256 MET THR MET ASP GLU GLN GLN SER GLN ALA VAL ALA PRO
SEQRES 2 B 256 VAL TYR VAL GLY GLY PHE LEU ALA ARG TYR ASP GLN SER
SEQRES 3 B 256 PRO ASP GLU ALA GLU LEU LEU LEU PRO ARG ASP VAL VAL
SEQRES 4 B 256 GLU HIS TRP LEU HIS ALA GLN GLY GLN GLY GLN PRO SER
SEQRES 5 B 256 LEU SER VAL ALA LEU PRO LEU ASN ILE ASN HIS ASP ASP
SEQRES 6 B 256 THR ALA VAL VAL GLY HIS VAL ALA ALA MET GLN SER VAL
SEQRES 7 B 256 ARG ASP GLY LEU PHE CYS LEU GLY CYS VAL THR SER PRO
SEQRES 8 B 256 ARG PHE LEU GLU ILE VAL ARG ARG ALA SER GLU LYS SER
SEQRES 9 B 256 GLU LEU VAL SER ARG GLY PRO VAL SER PRO LEU GLN PRO
SEQRES 10 B 256 ASP LYS VAL VAL GLU PHE LEU SER GLY SER TYR ALA GLY
SEQRES 11 B 256 LEU SER LEU ALA SER ARG ARG CYS ASP ASP VAL GLU GLN
SEQRES 12 B 256 ALA THR SER LEU SER GLY SER GLU THR THR PRO PHE LYS
SEQRES 13 B 256 ALA VAL ALA LEU CYS SER VAL GLY ARG ARG ARG GLY THR
SEQRES 14 B 256 LEU ALA VAL TYR GLY ARG ASP PRO GLU TRP VAL THR GLN
SEQRES 15 B 256 ARG PHE PRO ASP LEU THR ALA ALA ASP ARG ASP GLY LEU
SEQRES 16 B 256 ARG ALA GLN TRP GLN ARG CYS GLY SER THR ALA VAL ASP
SEQRES 17 B 256 ALA SER GLY ASP PRO PHE ARG SER ASP SER TYR GLY LEU
SEQRES 18 B 256 LEU GLY ASN SER VAL ASP ALA LEU TYR ILE ARG GLU ARG
SEQRES 19 B 256 LEU PRO LYS LEU ARG TYR ASP LYS GLN LEU VAL GLY VAL
SEQRES 20 B 256 THR GLU ARG GLU SER TYR VAL LYS ALA
FORMUL 3 HOH *183(H2 O)
HELIX 1 1 GLU A 29 LEU A 33 5 5
HELIX 2 2 PRO A 35 TRP A 42 1 8
HELIX 3 3 SER A 90 GLU A 102 1 13
HELIX 4 4 SER A 104 GLY A 110 1 7
HELIX 5 5 ASP A 118 TYR A 128 1 11
HELIX 6 6 ASP A 176 GLN A 182 1 7
HELIX 7 7 THR A 188 GLN A 200 1 13
HELIX 8 8 ASP A 217 TYR A 230 1 14
HELIX 9 9 GLU A 233 GLY A 246 1 14
HELIX 10 10 GLU B 305 VAL B 311 1 7
HELIX 11 11 GLU B 329 LEU B 333 5 5
HELIX 12 12 PRO B 335 LEU B 343 1 9
HELIX 13 13 SER B 390 GLU B 402 1 13
HELIX 14 14 SER B 404 GLY B 410 1 7
HELIX 15 15 ASP B 418 TYR B 428 1 11
HELIX 16 16 ASP B 476 GLN B 482 1 7
HELIX 17 17 THR B 488 CYS B 502 1 15
HELIX 18 18 ASP B 517 LEU B 529 1 13
HELIX 19 19 GLU B 533 VAL B 545 1 13
SHEET 1 A 7 GLY A 130 ALA A 134 0
SHEET 2 A 7 ALA A 157 CYS A 161 -1 O ALA A 157 N ALA A 134
SHEET 3 A 7 PRO A 58 ILE A 61 1 O PRO A 58 N VAL A 158
SHEET 4 A 7 ASP A 64 VAL A 78 -1 N ASP A 64 O ILE A 61
SHEET 5 A 7 GLY A 81 VAL A 88 -1 O GLY A 81 N VAL A 78
SHEET 6 A 7 VAL A 14 ARG A 22 -1 O VAL A 14 N VAL A 88
SHEET 7 A 7 VAL A 172 GLY A 174 -1 N VAL A 172 O GLY A 17
SHEET 1 B 7 GLY B 430 ALA B 434 0
SHEET 2 B 7 ALA B 457 CYS B 461 -1 O ALA B 457 N ALA B 434
SHEET 3 B 7 PRO B 358 ILE B 361 1 O PRO B 358 N VAL B 458
SHEET 4 B 7 ASP B 364 VAL B 378 -1 N ASP B 364 O ILE B 361
SHEET 5 B 7 GLY B 381 VAL B 388 -1 O GLY B 381 N VAL B 378
SHEET 6 B 7 VAL B 314 ARG B 322 -1 O VAL B 314 N VAL B 388
SHEET 7 B 7 VAL B 472 GLY B 474 -1 N VAL B 472 O GLY B 317
CRYST1 76.000 76.000 167.600 90.00 90.00 90.00 P 41 21 2 16
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 0.013158 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013158 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005967 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
