HEADER HYDROLASE/HYDROLASE INHIBITOR 26-MAR-13 4JVQ
TITLE CRYSTAL STRUCTURE OF HCV NS5B POLYMERASE IN COMPLEX WITH COMPOUND 9
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GENOME POLYPROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RNA-DIRECTED RNA POLYMERASE, UNP RESIDUES 2420-2989;
COMPND 5 SYNONYM: CORE PROTEIN P21, CAPSID PROTEIN C, P21, CORE PROTEIN P19,
COMPND 6 ENVELOPE GLYCOPROTEIN E1, GP32, GP35, ENVELOPE GLYCOPROTEIN E2, NS1,
COMPND 7 GP68, GP70, P7, PROTEASE NS2-3, P23, SERINE PROTEASE NS3,
COMPND 8 HEPACIVIRIN, NS3P, P70, NON-STRUCTURAL PROTEIN 4A, NS4A, P8, NON-
COMPND 9 STRUCTURAL PROTEIN 4B, NS4B, P27, NON-STRUCTURAL PROTEIN 5A, NS5A,
COMPND 10 P56, RNA-DIRECTED RNA POLYMERASE, NS5B, P68;
COMPND 11 EC: 3.4.22.-, 3.4.21.98, 3.6.1.15, 3.6.4.13, 2.7.7.48;
COMPND 12 ENGINEERED: YES;
COMPND 13 OTHER_DETAILS: PROTEIN CONSTRUCT ID 001
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS;
SOURCE 3 ORGANISM_COMMON: HCV;
SOURCE 4 ORGANISM_TAXID: 420174;
SOURCE 5 STRAIN: 1BJ4;
SOURCE 6 GENE: NS5B;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: JM109(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET29B
KEYWDS RNA-DIRECTED RNA POLYMERASE, TRANSFERASE, TRANSFERASE-TRANSFERASE
KEYWDS 2 INHIBITOR COMPLEX, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.COULOMBE
REVDAT 3 20-SEP-23 4JVQ 1 REMARK SEQADV LINK
REVDAT 2 26-MAR-14 4JVQ 1 JRNL
REVDAT 1 05-FEB-14 4JVQ 0
JRNL AUTH S.R.LAPLANTE,P.FORGIONE,C.BOUCHER,R.COULOMBE,J.GILLARD,
JRNL AUTH 2 O.HUCKE,A.JAKALIAN,M.A.JOLY,G.KUKOLJ,C.LEMKE,R.MCCOLLUM,
JRNL AUTH 3 S.TITOLO,P.L.BEAULIEU,T.STAMMERS
JRNL TITL ENANTIOMERIC ATROPISOMERS INHIBIT HCV POLYMERASE AND/OR HIV
JRNL TITL 2 MATRIX: CHARACTERIZING HINDERED BOND ROTATIONS AND TARGET
JRNL TITL 3 SELECTIVITY.
JRNL REF J.MED.CHEM. V. 57 1944 2014
JRNL REFN ISSN 0022-2623
JRNL PMID 24024973
JRNL DOI 10.1021/JM401202A
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2002
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
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 : 61416
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3071
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 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 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 61488
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 : 8724
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 705
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) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.195
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 4JVQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-13.
REMARK 100 THE DEPOSITION ID IS D_1000078564.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-09
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 : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
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 (%) : 97.3
REMARK 200 DATA REDUNDANCY : 6.690
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.5600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.3
REMARK 200 DATA REDUNDANCY IN SHELL : 6.67
REMARK 200 R MERGE FOR SHELL (I) : 0.38300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.630
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNX 2002
REMARK 200 STARTING MODEL: PDB ENTRY 3MWV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, 21% PEGMME 5000, 400 MM
REMARK 280 AMMONIUM SULFATE, 10% GLYCEROL, PH 5.4, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 284K
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 53.06000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.71000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.01000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.71000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.06000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.01000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLU A 150
REMARK 465 LYS A 151
REMARK 465 GLY A 152
REMARK 465 LEU A 564
REMARK 465 SER A 565
REMARK 465 ARG A 566
REMARK 465 ALA A 567
REMARK 465 ARG A 568
REMARK 465 PRO A 569
REMARK 465 ARG A 570
REMARK 465 HIS A 571
REMARK 465 HIS A 572
REMARK 465 HIS A 573
REMARK 465 HIS A 574
REMARK 465 HIS A 575
REMARK 465 HIS A 576
REMARK 465 GLU B 150
REMARK 465 LYS B 151
REMARK 465 GLY B 152
REMARK 465 LEU B 564
REMARK 465 SER B 565
REMARK 465 ARG B 566
REMARK 465 ALA B 567
REMARK 465 ARG B 568
REMARK 465 PRO B 569
REMARK 465 ARG B 570
REMARK 465 HIS B 571
REMARK 465 HIS B 572
REMARK 465 HIS B 573
REMARK 465 HIS B 574
REMARK 465 HIS B 575
REMARK 465 HIS B 576
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 PRO A 22 C - N - CA ANGL. DEV. = 9.6 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 LEU A 260 -51.43 -130.28
REMARK 500 ASP A 310 73.12 39.35
REMARK 500 SER A 347 54.15 72.96
REMARK 500 ALA A 348 56.04 -150.33
REMARK 500 ILE A 424 -66.72 -103.05
REMARK 500 HIS B 34 22.44 -75.30
REMARK 500 LEU B 260 -57.11 -131.51
REMARK 500 SER B 347 55.54 70.57
REMARK 500 ALA B 348 61.30 -154.26
REMARK 500 ILE B 424 -68.09 -90.48
REMARK 500 SER B 470 -18.97 -48.19
REMARK 500 SER B 513 0.45 -67.72
REMARK 500 PHE B 526 44.94 -103.24
REMARK 500 ALA B 541 32.36 -78.60
REMARK 500 TYR B 555 19.88 -140.97
REMARK 500
REMARK 500 REMARK: NULL
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 A3003 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 194 O
REMARK 620 2 HOH A3346 O 122.2
REMARK 620 3 HOH A3458 O 153.4 83.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A3004 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 220 OD1
REMARK 620 2 THR A 221 O 89.6
REMARK 620 3 HOH A3138 O 167.2 82.9
REMARK 620 4 HOH A3211 O 85.3 78.3 83.0
REMARK 620 5 HOH A3305 O 108.8 84.7 81.0 157.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 603 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 194 O
REMARK 620 2 PHE B 551 O 62.4
REMARK 620 3 HOH B 827 O 124.5 80.4
REMARK 620 4 HOH B 859 O 68.3 79.8 65.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 604 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 220 OD2
REMARK 620 2 THR B 221 O 73.2
REMARK 620 3 HOH B 799 O 60.9 73.1
REMARK 620 4 HOH B 819 O 159.8 89.5 104.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1ML A 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1ML B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 604
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3MWV RELATED DB: PDB
REMARK 900 APO NS5B POLYMERASE
REMARK 900 RELATED ID: 4JTY RELATED DB: PDB
REMARK 900 RELATED ID: 4JTZ RELATED DB: PDB
REMARK 900 RELATED ID: 4JU1 RELATED DB: PDB
REMARK 900 RELATED ID: 4JU2 RELATED DB: PDB
REMARK 900 RELATED ID: 4JU3 RELATED DB: PDB
REMARK 900 RELATED ID: 4JU4 RELATED DB: PDB
REMARK 900 RELATED ID: 4JU6 RELATED DB: PDB
REMARK 900 RELATED ID: 4JU7 RELATED DB: PDB
REMARK 900 RELATED ID: 4JVQ RELATED DB: PDB
REMARK 900 RELATED ID: 4JY0 RELATED DB: PDB
REMARK 900 RELATED ID: 4JY1 RELATED DB: PDB
DBREF 4JVQ A 1 570 UNP O92972 POLG_HCVJ4 2420 2989
DBREF 4JVQ B 1 570 UNP O92972 POLG_HCVJ4 2420 2989
SEQADV 4JVQ HIS A 571 UNP O92972 EXPRESSION TAG
SEQADV 4JVQ HIS A 572 UNP O92972 EXPRESSION TAG
SEQADV 4JVQ HIS A 573 UNP O92972 EXPRESSION TAG
SEQADV 4JVQ HIS A 574 UNP O92972 EXPRESSION TAG
SEQADV 4JVQ HIS A 575 UNP O92972 EXPRESSION TAG
SEQADV 4JVQ HIS A 576 UNP O92972 EXPRESSION TAG
SEQADV 4JVQ HIS B 571 UNP O92972 EXPRESSION TAG
SEQADV 4JVQ HIS B 572 UNP O92972 EXPRESSION TAG
SEQADV 4JVQ HIS B 573 UNP O92972 EXPRESSION TAG
SEQADV 4JVQ HIS B 574 UNP O92972 EXPRESSION TAG
SEQADV 4JVQ HIS B 575 UNP O92972 EXPRESSION TAG
SEQADV 4JVQ HIS B 576 UNP O92972 EXPRESSION TAG
SEQRES 1 A 576 SER MET SER TYR THR TRP THR GLY ALA LEU ILE THR PRO
SEQRES 2 A 576 CYS ALA ALA GLU GLU SER LYS LEU PRO ILE ASN PRO LEU
SEQRES 3 A 576 SER ASN SER LEU LEU ARG HIS HIS ASN MET VAL TYR ALA
SEQRES 4 A 576 THR THR SER ARG SER ALA SER LEU ARG GLN LYS LYS VAL
SEQRES 5 A 576 THR PHE ASP ARG LEU GLN VAL LEU ASP ASP HIS TYR ARG
SEQRES 6 A 576 ASP VAL LEU LYS GLU MET LYS ALA LYS ALA SER THR VAL
SEQRES 7 A 576 LYS ALA LYS LEU LEU SER ILE GLU GLU ALA CYS LYS LEU
SEQRES 8 A 576 THR PRO PRO HIS SER ALA LYS SER LYS PHE GLY TYR GLY
SEQRES 9 A 576 ALA LYS ASP VAL ARG ASN LEU SER SER ARG ALA VAL ASN
SEQRES 10 A 576 HIS ILE ARG SER VAL TRP GLU ASP LEU LEU GLU ASP THR
SEQRES 11 A 576 GLU THR PRO ILE ASP THR THR ILE MET ALA LYS SER GLU
SEQRES 12 A 576 VAL PHE CYS VAL GLN PRO GLU LYS GLY GLY ARG LYS PRO
SEQRES 13 A 576 ALA ARG LEU ILE VAL PHE PRO ASP LEU GLY VAL ARG VAL
SEQRES 14 A 576 CYS GLU LYS MET ALA LEU TYR ASP VAL VAL SER THR LEU
SEQRES 15 A 576 PRO GLN ALA VAL MET GLY SER SER TYR GLY PHE GLN TYR
SEQRES 16 A 576 SER PRO LYS GLN ARG VAL GLU PHE LEU VAL ASN THR TRP
SEQRES 17 A 576 LYS SER LYS LYS CYS PRO MET GLY PHE SER TYR ASP THR
SEQRES 18 A 576 ARG CYS PHE ASP SER THR VAL THR GLU SER ASP ILE ARG
SEQRES 19 A 576 VAL GLU GLU SER ILE TYR GLN CYS CYS ASP LEU ALA PRO
SEQRES 20 A 576 GLU ALA ARG GLN ALA ILE ARG SER LEU THR GLU ARG LEU
SEQRES 21 A 576 TYR ILE GLY GLY PRO LEU THR ASN SER LYS GLY GLN ASN
SEQRES 22 A 576 CYS GLY TYR ARG ARG CYS ARG ALA SER GLY VAL LEU THR
SEQRES 23 A 576 THR SER CYS GLY ASN THR LEU THR CYS TYR LEU LYS ALA
SEQRES 24 A 576 THR ALA ALA CYS ARG ALA ALA LYS LEU GLN ASP CYS THR
SEQRES 25 A 576 MET LEU VAL ASN GLY ASP ASP LEU VAL VAL ILE CYS GLU
SEQRES 26 A 576 SER ALA GLY THR GLN GLU ASP ALA ALA ALA LEU ARG ALA
SEQRES 27 A 576 PHE THR GLU ALA MET THR ARG TYR SER ALA PRO PRO GLY
SEQRES 28 A 576 ASP PRO PRO GLN PRO GLU TYR ASP LEU GLU LEU ILE THR
SEQRES 29 A 576 SER CYS SER SER ASN VAL SER VAL ALA HIS ASP ALA SER
SEQRES 30 A 576 GLY LYS ARG VAL TYR TYR LEU THR ARG ASP PRO THR THR
SEQRES 31 A 576 PRO LEU ALA ARG ALA ALA TRP GLU THR ALA ARG HIS THR
SEQRES 32 A 576 PRO ILE ASN SER TRP LEU GLY ASN ILE ILE MET TYR ALA
SEQRES 33 A 576 PRO THR LEU TRP ALA ARG MET ILE LEU MET THR HIS PHE
SEQRES 34 A 576 PHE SER ILE LEU LEU ALA GLN GLU GLN LEU GLU LYS ALA
SEQRES 35 A 576 LEU ASP CYS GLN ILE TYR GLY ALA CYS TYR SER ILE GLU
SEQRES 36 A 576 PRO LEU ASP LEU PRO GLN ILE ILE GLU ARG LEU HIS GLY
SEQRES 37 A 576 LEU SER ALA PHE THR LEU HIS SER TYR SER PRO GLY GLU
SEQRES 38 A 576 ILE ASN ARG VAL ALA SER CYS LEU ARG LYS LEU GLY VAL
SEQRES 39 A 576 PRO PRO LEU ARG THR TRP ARG HIS ARG ALA ARG SER VAL
SEQRES 40 A 576 ARG ALA LYS LEU LEU SER GLN GLY GLY ARG ALA ALA THR
SEQRES 41 A 576 CYS GLY ARG TYR LEU PHE ASN TRP ALA VAL ARG THR LYS
SEQRES 42 A 576 LEU LYS LEU THR PRO ILE PRO ALA ALA SER GLN LEU ASP
SEQRES 43 A 576 LEU SER GLY TRP PHE VAL ALA GLY TYR SER GLY GLY ASP
SEQRES 44 A 576 ILE TYR HIS SER LEU SER ARG ALA ARG PRO ARG HIS HIS
SEQRES 45 A 576 HIS HIS HIS HIS
SEQRES 1 B 576 SER MET SER TYR THR TRP THR GLY ALA LEU ILE THR PRO
SEQRES 2 B 576 CYS ALA ALA GLU GLU SER LYS LEU PRO ILE ASN PRO LEU
SEQRES 3 B 576 SER ASN SER LEU LEU ARG HIS HIS ASN MET VAL TYR ALA
SEQRES 4 B 576 THR THR SER ARG SER ALA SER LEU ARG GLN LYS LYS VAL
SEQRES 5 B 576 THR PHE ASP ARG LEU GLN VAL LEU ASP ASP HIS TYR ARG
SEQRES 6 B 576 ASP VAL LEU LYS GLU MET LYS ALA LYS ALA SER THR VAL
SEQRES 7 B 576 LYS ALA LYS LEU LEU SER ILE GLU GLU ALA CYS LYS LEU
SEQRES 8 B 576 THR PRO PRO HIS SER ALA LYS SER LYS PHE GLY TYR GLY
SEQRES 9 B 576 ALA LYS ASP VAL ARG ASN LEU SER SER ARG ALA VAL ASN
SEQRES 10 B 576 HIS ILE ARG SER VAL TRP GLU ASP LEU LEU GLU ASP THR
SEQRES 11 B 576 GLU THR PRO ILE ASP THR THR ILE MET ALA LYS SER GLU
SEQRES 12 B 576 VAL PHE CYS VAL GLN PRO GLU LYS GLY GLY ARG LYS PRO
SEQRES 13 B 576 ALA ARG LEU ILE VAL PHE PRO ASP LEU GLY VAL ARG VAL
SEQRES 14 B 576 CYS GLU LYS MET ALA LEU TYR ASP VAL VAL SER THR LEU
SEQRES 15 B 576 PRO GLN ALA VAL MET GLY SER SER TYR GLY PHE GLN TYR
SEQRES 16 B 576 SER PRO LYS GLN ARG VAL GLU PHE LEU VAL ASN THR TRP
SEQRES 17 B 576 LYS SER LYS LYS CYS PRO MET GLY PHE SER TYR ASP THR
SEQRES 18 B 576 ARG CYS PHE ASP SER THR VAL THR GLU SER ASP ILE ARG
SEQRES 19 B 576 VAL GLU GLU SER ILE TYR GLN CYS CYS ASP LEU ALA PRO
SEQRES 20 B 576 GLU ALA ARG GLN ALA ILE ARG SER LEU THR GLU ARG LEU
SEQRES 21 B 576 TYR ILE GLY GLY PRO LEU THR ASN SER LYS GLY GLN ASN
SEQRES 22 B 576 CYS GLY TYR ARG ARG CYS ARG ALA SER GLY VAL LEU THR
SEQRES 23 B 576 THR SER CYS GLY ASN THR LEU THR CYS TYR LEU LYS ALA
SEQRES 24 B 576 THR ALA ALA CYS ARG ALA ALA LYS LEU GLN ASP CYS THR
SEQRES 25 B 576 MET LEU VAL ASN GLY ASP ASP LEU VAL VAL ILE CYS GLU
SEQRES 26 B 576 SER ALA GLY THR GLN GLU ASP ALA ALA ALA LEU ARG ALA
SEQRES 27 B 576 PHE THR GLU ALA MET THR ARG TYR SER ALA PRO PRO GLY
SEQRES 28 B 576 ASP PRO PRO GLN PRO GLU TYR ASP LEU GLU LEU ILE THR
SEQRES 29 B 576 SER CYS SER SER ASN VAL SER VAL ALA HIS ASP ALA SER
SEQRES 30 B 576 GLY LYS ARG VAL TYR TYR LEU THR ARG ASP PRO THR THR
SEQRES 31 B 576 PRO LEU ALA ARG ALA ALA TRP GLU THR ALA ARG HIS THR
SEQRES 32 B 576 PRO ILE ASN SER TRP LEU GLY ASN ILE ILE MET TYR ALA
SEQRES 33 B 576 PRO THR LEU TRP ALA ARG MET ILE LEU MET THR HIS PHE
SEQRES 34 B 576 PHE SER ILE LEU LEU ALA GLN GLU GLN LEU GLU LYS ALA
SEQRES 35 B 576 LEU ASP CYS GLN ILE TYR GLY ALA CYS TYR SER ILE GLU
SEQRES 36 B 576 PRO LEU ASP LEU PRO GLN ILE ILE GLU ARG LEU HIS GLY
SEQRES 37 B 576 LEU SER ALA PHE THR LEU HIS SER TYR SER PRO GLY GLU
SEQRES 38 B 576 ILE ASN ARG VAL ALA SER CYS LEU ARG LYS LEU GLY VAL
SEQRES 39 B 576 PRO PRO LEU ARG THR TRP ARG HIS ARG ALA ARG SER VAL
SEQRES 40 B 576 ARG ALA LYS LEU LEU SER GLN GLY GLY ARG ALA ALA THR
SEQRES 41 B 576 CYS GLY ARG TYR LEU PHE ASN TRP ALA VAL ARG THR LYS
SEQRES 42 B 576 LEU LYS LEU THR PRO ILE PRO ALA ALA SER GLN LEU ASP
SEQRES 43 B 576 LEU SER GLY TRP PHE VAL ALA GLY TYR SER GLY GLY ASP
SEQRES 44 B 576 ILE TYR HIS SER LEU SER ARG ALA ARG PRO ARG HIS HIS
SEQRES 45 B 576 HIS HIS HIS HIS
HET GOL A3001 6
HET 1ML A3002 40
HET MG A3003 1
HET MG A3004 1
HET GOL B 601 6
HET 1ML B 602 40
HET MG B 603 1
HET MG B 604 1
HETNAM GOL GLYCEROL
HETNAM 1ML 5-{4-[(4-METHOXYBENZOYL)AMINO]PHENOXY}-2-{[(TRANS-4-
HETNAM 2 1ML METHYLCYCLOHEXYL)CARBONYL](PROPAN-2-YL)AMINO}BENZOIC
HETNAM 3 1ML ACID
HETNAM MG MAGNESIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 4 1ML 2(C32 H36 N2 O6)
FORMUL 5 MG 4(MG 2+)
FORMUL 11 HOH *705(H2 O)
HELIX 1 1 LEU A 26 LEU A 30 5 5
HELIX 2 2 HIS A 33 ASN A 35 5 3
HELIX 3 3 THR A 41 ARG A 43 5 3
HELIX 4 4 SER A 44 THR A 53 1 10
HELIX 5 5 ASP A 61 SER A 76 1 16
HELIX 6 6 SER A 84 LEU A 91 1 8
HELIX 7 7 GLY A 104 ASN A 110 1 7
HELIX 8 8 SER A 112 ASP A 129 1 18
HELIX 9 9 ASP A 164 GLY A 188 1 25
HELIX 10 10 SER A 189 TYR A 195 5 7
HELIX 11 11 SER A 196 SER A 210 1 15
HELIX 12 12 CYS A 223 VAL A 228 1 6
HELIX 13 13 THR A 229 GLN A 241 1 13
HELIX 14 14 ALA A 246 LEU A 260 1 15
HELIX 15 15 THR A 286 LYS A 307 1 22
HELIX 16 16 GLY A 328 TYR A 346 1 19
HELIX 17 17 ASP A 359 ILE A 363 5 5
HELIX 18 18 PRO A 388 ARG A 401 1 14
HELIX 19 19 ASN A 406 TYR A 415 1 10
HELIX 20 20 THR A 418 ILE A 424 1 7
HELIX 21 21 ILE A 424 GLU A 437 1 14
HELIX 22 22 GLU A 455 LEU A 457 5 3
HELIX 23 23 ASP A 458 GLY A 468 1 11
HELIX 24 24 LEU A 469 THR A 473 5 5
HELIX 25 25 SER A 478 GLY A 493 1 16
HELIX 26 26 PRO A 496 GLY A 515 1 20
HELIX 27 27 GLY A 515 PHE A 526 1 12
HELIX 28 28 ILE A 539 GLN A 544 5 6
HELIX 29 29 LEU A 547 VAL A 552 5 6
HELIX 30 30 LEU B 26 LEU B 30 5 5
HELIX 31 31 THR B 41 ARG B 43 5 3
HELIX 32 32 SER B 44 THR B 53 1 10
HELIX 33 33 ASP B 61 SER B 76 1 16
HELIX 34 34 SER B 84 LYS B 90 1 7
HELIX 35 35 GLY B 104 ASN B 110 1 7
HELIX 36 36 SER B 112 ASP B 129 1 18
HELIX 37 37 ASP B 164 GLY B 188 1 25
HELIX 38 38 SER B 189 TYR B 195 5 7
HELIX 39 39 SER B 196 SER B 210 1 15
HELIX 40 40 CYS B 223 VAL B 228 1 6
HELIX 41 41 THR B 229 GLN B 241 1 13
HELIX 42 42 ALA B 246 LEU B 260 1 15
HELIX 43 43 THR B 286 LYS B 307 1 22
HELIX 44 44 GLY B 328 TYR B 346 1 19
HELIX 45 45 ASP B 359 ILE B 363 5 5
HELIX 46 46 PRO B 388 ARG B 401 1 14
HELIX 47 47 ASN B 406 TYR B 415 1 10
HELIX 48 48 THR B 418 ILE B 424 1 7
HELIX 49 49 ILE B 424 GLN B 436 1 13
HELIX 50 50 GLU B 455 LEU B 457 5 3
HELIX 51 51 ASP B 458 GLY B 468 1 11
HELIX 52 52 LEU B 469 THR B 473 5 5
HELIX 53 53 SER B 478 GLY B 493 1 16
HELIX 54 54 PRO B 496 SER B 513 1 18
HELIX 55 55 GLY B 515 LEU B 525 1 11
HELIX 56 56 PHE B 526 VAL B 530 5 5
HELIX 57 57 ILE B 539 SER B 543 5 5
HELIX 58 58 LEU B 547 PHE B 551 5 5
SHEET 1 A 5 TYR A 4 TRP A 6 0
SHEET 2 A 5 ASN A 273 ARG A 277 -1 O TYR A 276 N THR A 5
SHEET 3 A 5 GLY A 264 THR A 267 -1 N LEU A 266 O GLY A 275
SHEET 4 A 5 THR A 136 ALA A 140 1 N ILE A 138 O THR A 267
SHEET 5 A 5 LEU A 159 PHE A 162 -1 O PHE A 162 N THR A 137
SHEET 1 B 2 VAL A 37 ALA A 39 0
SHEET 2 B 2 VAL A 144 CYS A 146 -1 O PHE A 145 N TYR A 38
SHEET 1 C 3 PRO A 214 TYR A 219 0
SHEET 2 C 3 ASP A 319 GLU A 325 -1 O CYS A 324 N MET A 215
SHEET 3 C 3 GLN A 309 ASN A 316 -1 N THR A 312 O ILE A 323
SHEET 1 D 2 ASN A 369 HIS A 374 0
SHEET 2 D 2 ARG A 380 THR A 385 -1 O VAL A 381 N ALA A 373
SHEET 1 E 2 LEU A 443 ILE A 447 0
SHEET 2 E 2 ALA A 450 ILE A 454 -1 O ILE A 454 N LEU A 443
SHEET 1 F 5 TYR B 4 TRP B 6 0
SHEET 2 F 5 ASN B 273 ARG B 277 -1 O TYR B 276 N THR B 5
SHEET 3 F 5 GLY B 264 THR B 267 -1 N GLY B 264 O ARG B 277
SHEET 4 F 5 THR B 136 ALA B 140 1 N ILE B 138 O THR B 267
SHEET 5 F 5 LEU B 159 PHE B 162 -1 O PHE B 162 N THR B 137
SHEET 1 G 2 VAL B 37 ALA B 39 0
SHEET 2 G 2 VAL B 144 CYS B 146 -1 O PHE B 145 N TYR B 38
SHEET 1 H 3 PRO B 214 TYR B 219 0
SHEET 2 H 3 ASP B 319 GLU B 325 -1 O VAL B 322 N PHE B 217
SHEET 3 H 3 GLN B 309 ASN B 316 -1 N GLN B 309 O GLU B 325
SHEET 1 I 2 SER B 368 HIS B 374 0
SHEET 2 I 2 ARG B 380 ARG B 386 -1 O VAL B 381 N ALA B 373
SHEET 1 J 2 LEU B 443 ILE B 447 0
SHEET 2 J 2 ALA B 450 ILE B 454 -1 O ILE B 454 N LEU B 443
LINK O GLN A 194 MG MG A3003 1555 1555 2.69
LINK OD1 ASP A 220 MG MG A3004 1555 1555 2.53
LINK O THR A 221 MG MG A3004 1555 1555 2.58
LINK MG MG A3003 O HOH A3346 1555 1555 2.79
LINK MG MG A3003 O HOH A3458 1555 1555 2.84
LINK MG MG A3004 O HOH A3138 1555 1555 2.53
LINK MG MG A3004 O HOH A3211 1555 1555 2.70
LINK MG MG A3004 O HOH A3305 1555 1555 2.88
LINK O GLN B 194 MG MG B 603 1555 1555 2.83
LINK OD2 ASP B 220 MG MG B 604 1555 1555 2.55
LINK O THR B 221 MG MG B 604 1555 1555 2.69
LINK O PHE B 551 MG MG B 603 1555 1555 2.98
LINK MG MG B 603 O HOH B 827 1555 1555 2.53
LINK MG MG B 603 O HOH B 859 1555 1555 2.82
LINK MG MG B 604 O HOH B 799 1555 1555 2.93
LINK MG MG B 604 O HOH B 819 1555 1555 2.67
SITE 1 AC1 3 ALA A 97 ARG A 168 HOH A3216
SITE 1 AC2 12 MET A 423 HIS A 475 SER A 476 TYR A 477
SITE 2 AC2 12 ILE A 482 ARG A 490 VAL A 494 PRO A 496
SITE 3 AC2 12 LEU A 497 TRP A 528 HOH A3282 HOH A3383
SITE 1 AC3 5 GLN A 194 GLN A 199 PHE A 551 HOH A3346
SITE 2 AC3 5 HOH A3458
SITE 1 AC4 5 ASP A 220 THR A 221 HOH A3138 HOH A3211
SITE 2 AC4 5 HOH A3305
SITE 1 AC5 6 SER B 96 ALA B 97 PHE B 162 ARG B 168
SITE 2 AC5 6 HOH B 783 HOH B 916
SITE 1 AC6 16 LYS A 209 SER A 210 HOH A3454 ARG B 422
SITE 2 AC6 16 LEU B 474 HIS B 475 SER B 476 TYR B 477
SITE 3 AC6 16 ILE B 482 ALA B 486 LEU B 489 ARG B 490
SITE 4 AC6 16 VAL B 494 PRO B 496 LEU B 497 HOH B 974
SITE 1 AC7 4 GLN B 194 PHE B 551 HOH B 827 HOH B 859
SITE 1 AC8 4 ASP B 220 THR B 221 HOH B 799 HOH B 819
CRYST1 106.120 108.020 135.420 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 0.009423 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009258 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007384 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
