HEADER TRANSFERASE/TRANSFERASE INHIBITOR 14-NOV-16 5TWN
TITLE CRYSTAL STRUCTURE OF THE HEPATITIS C VIRUS NS5B RNA- DEPENDENT RNA
TITLE 2 POLYMERASE IN COMPLEX WITH 5-[3-(TERT-BUTYLCARBAMOYL)PHENYL]-6-
TITLE 3 (ETHYLAMINO)-2-(4-FLUOROPHENYL)-N-METHYLFURO[2,3-B]PYRIDINE-3-
TITLE 4 CARBOXAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NS5B RNA- DEPENDENT RNA POLYMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 2420-2992;
COMPND 5 EC: 2.7.7.48;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS GENOTYPE 1B (ISOLATE CON1);
SOURCE 3 ORGANISM_COMMON: HCV;
SOURCE 4 ORGANISM_TAXID: 333284;
SOURCE 5 STRAIN: ISOLATE CON1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) STAR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21B
KEYWDS NS5B, POLYMERASE, HCV, FINGERS, PALM, THUMB, TRANSFERASE,
KEYWDS 2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SHERIFF
REVDAT 4 04-OCT-23 5TWN 1 REMARK
REVDAT 3 31-OCT-18 5TWN 1 SOURCE JRNL
REVDAT 2 26-APR-17 5TWN 1 JRNL
REVDAT 1 15-MAR-17 5TWN 0
JRNL AUTH K.J.EASTMAN,K.PARCELLA,K.S.YEUNG,K.A.GRANT-YOUNG,J.ZHU,
JRNL AUTH 2 T.WANG,Z.ZHANG,Z.YIN,B.R.BENO,S.SHERIFF,K.KISH,J.TREDUP,
JRNL AUTH 3 A.G.JARDEL,V.HALAN,K.GHOSH,D.PARKER,K.MOSURE,H.FANG,
JRNL AUTH 4 Y.K.WANG,J.LEMM,X.ZHUO,U.HANUMEGOWDA,K.RIGAT,M.DONOSO,
JRNL AUTH 5 M.TUTTLE,T.ZVYAGA,Z.HAARHOFF,N.A.MEANWELL,M.G.SOARS,
JRNL AUTH 6 S.B.ROBERTS,J.F.KADOW
JRNL TITL THE DISCOVERY OF A PAN-GENOTYPIC, PRIMER GRIP INHIBITOR OF
JRNL TITL 2 HCV NS5B POLYMERASE.
JRNL REF MEDCHEMCOMM V. 8 796 2017
JRNL REFN ISSN 2040-2503
JRNL PMID 30108798
JRNL DOI 10.1039/C6MD00636A
REMARK 2
REMARK 2 RESOLUTION. 3.04 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.7
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.04
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.12
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 27867
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.810
REMARK 3 FREE R VALUE TEST SET COUNT : 1063
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 14
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.04
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.15
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.65
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2856
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2150
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2768
REMARK 3 BIN R VALUE (WORKING SET) : 0.2140
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.08
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 88
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 : 8374
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 190
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 76.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -14.06210
REMARK 3 B22 (A**2) : 2.52040
REMARK 3 B33 (A**2) : 11.54170
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) : 0.350
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.369
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.926
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 8853 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 12130 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2997 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 158 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1429 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 8853 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1144 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 10380 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.11
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.86
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.66
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5TWN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1000224942.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAY-12
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27952
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.030
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.03
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.58900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 3QOZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM SODIUM POTASSIUM TARTRATE, 100
REMARK 280 MM SODIUM CITRATE, 1.75 M (NH4)2SO4, PH 5.6, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
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 33.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 116.65000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.55000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 116.65000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.55000
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 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 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 MET A 0
REMARK 465 ALA A 15
REMARK 465 ALA A 16
REMARK 465 GLU A 17
REMARK 465 GLU A 18
REMARK 465 THR A 19
REMARK 465 LYS A 20
REMARK 465 LEU A 21
REMARK 465 PRO A 22
REMARK 465 ILE A 23
REMARK 465 ASN A 24
REMARK 465 ALA A 25
REMARK 465 LEU A 26
REMARK 465 SER A 27
REMARK 465 ASN A 28
REMARK 465 SER A 29
REMARK 465 LEU A 30
REMARK 465 LEU A 31
REMARK 465 ARG A 32
REMARK 465 HIS A 33
REMARK 465 HIS A 34
REMARK 465 ASN A 35
REMARK 465 LEU A 36
REMARK 465 VAL A 37
REMARK 465 MET B 0
REMARK 465 ALA B 15
REMARK 465 ALA B 16
REMARK 465 GLU B 17
REMARK 465 GLU B 18
REMARK 465 THR B 19
REMARK 465 LYS B 20
REMARK 465 LEU B 21
REMARK 465 PRO B 22
REMARK 465 ILE B 23
REMARK 465 ASN B 24
REMARK 465 ALA B 25
REMARK 465 LEU B 26
REMARK 465 SER B 27
REMARK 465 ASN B 28
REMARK 465 SER B 29
REMARK 465 LEU B 30
REMARK 465 LEU B 31
REMARK 465 ARG B 32
REMARK 465 HIS B 33
REMARK 465 HIS B 34
REMARK 465 ASN B 35
REMARK 465 LEU B 36
REMARK 465 VAL B 37
REMARK 465 GLU B 150
REMARK 465 LYS B 151
REMARK 465 GLY B 152
REMARK 465 GLY B 153
REMARK 465 ARG B 154
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 TRP B 571
REMARK 465 PHE B 572
REMARK 465 MET B 573
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LEU A 57 CG CD1 CD2
REMARK 470 LYS A 100 CD CE NZ
REMARK 470 GLU A 131 CG CD OE1 OE2
REMARK 470 GLN A 148 CG CD OE1 NE2
REMARK 470 ARG A 154 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 355 CG CD CE NZ
REMARK 470 MET A 414 CG SD CE
REMARK 470 ARG A 568 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 57 CG CD1 CD2
REMARK 470 LYS B 90 CD CE NZ
REMARK 470 LYS B 100 CG CD CE NZ
REMARK 470 GLU B 131 CG CD OE1 OE2
REMARK 470 GLU B 143 CG CD OE1 OE2
REMARK 470 LYS B 355 CG CD CE NZ
REMARK 470 GLN B 446 CG CD OE1 NE2
REMARK 470 TYR B 448 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN B 544 CG CD OE1 NE2
REMARK 470 TRP B 550 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 550 CZ3 CH2
REMARK 470 TYR B 555 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER B 556 OG
REMARK 470 LEU B 564 CG CD1 CD2
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 ALA B 450 C - N - CA ANGL. DEV. = 15.0 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 VAL A 147 89.36 -69.17
REMARK 500 GLU A 150 -88.25 -66.08
REMARK 500 ARG A 154 94.29 -66.40
REMARK 500 LYS A 155 118.17 -32.78
REMARK 500 LEU A 260 -53.15 -122.02
REMARK 500 SER A 347 54.88 74.60
REMARK 500 SER A 367 -8.51 66.08
REMARK 500 HIS A 402 92.51 -62.40
REMARK 500 ILE A 424 -65.26 -107.82
REMARK 500 SER A 513 20.04 -76.83
REMARK 500 PHE A 551 53.02 -110.12
REMARK 500 TYR A 555 38.16 -143.88
REMARK 500 ARG A 568 75.80 69.89
REMARK 500 PHE A 572 9.51 -65.37
REMARK 500 ALA B 97 126.15 -36.91
REMARK 500 VAL B 147 89.30 -69.53
REMARK 500 PHE B 193 5.98 -61.87
REMARK 500 LEU B 260 -62.98 -125.09
REMARK 500 SER B 347 54.40 75.32
REMARK 500 SER B 367 -9.57 66.10
REMARK 500 HIS B 402 93.79 -64.21
REMARK 500 ILE B 424 -65.82 -107.15
REMARK 500 ALA B 450 103.23 138.53
REMARK 500 SER B 513 23.59 -77.32
REMARK 500 VAL B 552 -120.54 -96.66
REMARK 500 ALA B 553 136.61 -172.93
REMARK 500 SER B 556 23.23 49.88
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 23E A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 23E B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7NG B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 608
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5TWM RELATED DB: PDB
DBREF 5TWN A 1 573 UNP Q9WMX2 POLG_HCVCO 2420 2992
DBREF 5TWN B 1 573 UNP Q9WMX2 POLG_HCVCO 2420 2992
SEQADV 5TWN MET A 0 UNP Q9WMX2 INITIATING METHIONINE
SEQADV 5TWN MET B 0 UNP Q9WMX2 INITIATING METHIONINE
SEQRES 1 A 574 MET SER MET SER TYR THR TRP THR GLY ALA LEU ILE THR
SEQRES 2 A 574 PRO CYS ALA ALA GLU GLU THR LYS LEU PRO ILE ASN ALA
SEQRES 3 A 574 LEU SER ASN SER LEU LEU ARG HIS HIS ASN LEU VAL TYR
SEQRES 4 A 574 ALA THR THR SER ARG SER ALA SER LEU ARG GLN LYS LYS
SEQRES 5 A 574 VAL THR PHE ASP ARG LEU GLN VAL LEU ASP ASP HIS TYR
SEQRES 6 A 574 ARG ASP VAL LEU LYS GLU MET LYS ALA LYS ALA SER THR
SEQRES 7 A 574 VAL LYS ALA LYS LEU LEU SER VAL GLU GLU ALA CYS LYS
SEQRES 8 A 574 LEU THR PRO PRO HIS SER ALA ARG SER LYS PHE GLY TYR
SEQRES 9 A 574 GLY ALA LYS ASP VAL ARG ASN LEU SER SER LYS ALA VAL
SEQRES 10 A 574 ASN HIS ILE ARG SER VAL TRP LYS ASP LEU LEU GLU ASP
SEQRES 11 A 574 THR GLU THR PRO ILE ASP THR THR ILE MET ALA LYS ASN
SEQRES 12 A 574 GLU VAL PHE CYS VAL GLN PRO GLU LYS GLY GLY ARG LYS
SEQRES 13 A 574 PRO ALA ARG LEU ILE VAL PHE PRO ASP LEU GLY VAL ARG
SEQRES 14 A 574 VAL CYS GLU LYS MET ALA LEU TYR ASP VAL VAL SER THR
SEQRES 15 A 574 LEU PRO GLN ALA VAL MET GLY SER SER TYR GLY PHE GLN
SEQRES 16 A 574 TYR SER PRO GLY GLN ARG VAL GLU PHE LEU VAL ASN ALA
SEQRES 17 A 574 TRP LYS ALA LYS LYS CYS PRO MET GLY PHE ALA TYR ASP
SEQRES 18 A 574 THR ARG CYS PHE ASP SER THR VAL THR GLU ASN ASP ILE
SEQRES 19 A 574 ARG VAL GLU GLU SER ILE TYR GLN CYS CYS ASP LEU ALA
SEQRES 20 A 574 PRO GLU ALA ARG GLN ALA ILE ARG SER LEU THR GLU ARG
SEQRES 21 A 574 LEU TYR ILE GLY GLY PRO LEU THR ASN SER LYS GLY GLN
SEQRES 22 A 574 ASN CYS GLY TYR ARG ARG CYS ARG ALA SER GLY VAL LEU
SEQRES 23 A 574 THR THR SER CYS GLY ASN THR LEU THR CYS TYR LEU LYS
SEQRES 24 A 574 ALA ALA ALA ALA CYS ARG ALA ALA LYS LEU GLN ASP CYS
SEQRES 25 A 574 THR MET LEU VAL CYS GLY ASP ASP LEU VAL VAL ILE CYS
SEQRES 26 A 574 GLU SER ALA GLY THR GLN GLU ASP GLU ALA SER LEU ARG
SEQRES 27 A 574 ALA PHE THR GLU ALA MET THR ARG TYR SER ALA PRO PRO
SEQRES 28 A 574 GLY ASP PRO PRO LYS PRO GLU TYR ASP LEU GLU LEU ILE
SEQRES 29 A 574 THR SER CYS SER SER ASN VAL SER VAL ALA HIS ASP ALA
SEQRES 30 A 574 SER GLY LYS ARG VAL TYR TYR LEU THR ARG ASP PRO THR
SEQRES 31 A 574 THR PRO LEU ALA ARG ALA ALA TRP GLU THR ALA ARG HIS
SEQRES 32 A 574 THR PRO VAL ASN SER TRP LEU GLY ASN ILE ILE MET TYR
SEQRES 33 A 574 ALA PRO THR LEU TRP ALA ARG MET ILE LEU MET THR HIS
SEQRES 34 A 574 PHE PHE SER ILE LEU LEU ALA GLN GLU GLN LEU GLU LYS
SEQRES 35 A 574 ALA LEU ASP CYS GLN ILE TYR GLY ALA CYS TYR SER ILE
SEQRES 36 A 574 GLU PRO LEU ASP LEU PRO GLN ILE ILE GLN ARG LEU HIS
SEQRES 37 A 574 GLY LEU SER ALA PHE SER LEU HIS SER TYR SER PRO GLY
SEQRES 38 A 574 GLU ILE ASN ARG VAL ALA SER CYS LEU ARG LYS LEU GLY
SEQRES 39 A 574 VAL PRO PRO LEU ARG VAL TRP ARG HIS ARG ALA ARG SER
SEQRES 40 A 574 VAL ARG ALA ARG LEU LEU SER GLN GLY GLY ARG ALA ALA
SEQRES 41 A 574 THR CYS GLY LYS TYR LEU PHE ASN TRP ALA VAL ARG THR
SEQRES 42 A 574 LYS LEU LYS LEU THR PRO ILE PRO ALA ALA SER GLN LEU
SEQRES 43 A 574 ASP LEU SER SER TRP PHE VAL ALA GLY TYR SER GLY GLY
SEQRES 44 A 574 ASP ILE TYR HIS SER LEU SER ARG ALA ARG PRO ARG TRP
SEQRES 45 A 574 PHE MET
SEQRES 1 B 574 MET SER MET SER TYR THR TRP THR GLY ALA LEU ILE THR
SEQRES 2 B 574 PRO CYS ALA ALA GLU GLU THR LYS LEU PRO ILE ASN ALA
SEQRES 3 B 574 LEU SER ASN SER LEU LEU ARG HIS HIS ASN LEU VAL TYR
SEQRES 4 B 574 ALA THR THR SER ARG SER ALA SER LEU ARG GLN LYS LYS
SEQRES 5 B 574 VAL THR PHE ASP ARG LEU GLN VAL LEU ASP ASP HIS TYR
SEQRES 6 B 574 ARG ASP VAL LEU LYS GLU MET LYS ALA LYS ALA SER THR
SEQRES 7 B 574 VAL LYS ALA LYS LEU LEU SER VAL GLU GLU ALA CYS LYS
SEQRES 8 B 574 LEU THR PRO PRO HIS SER ALA ARG SER LYS PHE GLY TYR
SEQRES 9 B 574 GLY ALA LYS ASP VAL ARG ASN LEU SER SER LYS ALA VAL
SEQRES 10 B 574 ASN HIS ILE ARG SER VAL TRP LYS ASP LEU LEU GLU ASP
SEQRES 11 B 574 THR GLU THR PRO ILE ASP THR THR ILE MET ALA LYS ASN
SEQRES 12 B 574 GLU VAL PHE CYS VAL GLN PRO GLU LYS GLY GLY ARG LYS
SEQRES 13 B 574 PRO ALA ARG LEU ILE VAL PHE PRO ASP LEU GLY VAL ARG
SEQRES 14 B 574 VAL CYS GLU LYS MET ALA LEU TYR ASP VAL VAL SER THR
SEQRES 15 B 574 LEU PRO GLN ALA VAL MET GLY SER SER TYR GLY PHE GLN
SEQRES 16 B 574 TYR SER PRO GLY GLN ARG VAL GLU PHE LEU VAL ASN ALA
SEQRES 17 B 574 TRP LYS ALA LYS LYS CYS PRO MET GLY PHE ALA TYR ASP
SEQRES 18 B 574 THR ARG CYS PHE ASP SER THR VAL THR GLU ASN ASP ILE
SEQRES 19 B 574 ARG VAL GLU GLU SER ILE TYR GLN CYS CYS ASP LEU ALA
SEQRES 20 B 574 PRO GLU ALA ARG GLN ALA ILE ARG SER LEU THR GLU ARG
SEQRES 21 B 574 LEU TYR ILE GLY GLY PRO LEU THR ASN SER LYS GLY GLN
SEQRES 22 B 574 ASN CYS GLY TYR ARG ARG CYS ARG ALA SER GLY VAL LEU
SEQRES 23 B 574 THR THR SER CYS GLY ASN THR LEU THR CYS TYR LEU LYS
SEQRES 24 B 574 ALA ALA ALA ALA CYS ARG ALA ALA LYS LEU GLN ASP CYS
SEQRES 25 B 574 THR MET LEU VAL CYS GLY ASP ASP LEU VAL VAL ILE CYS
SEQRES 26 B 574 GLU SER ALA GLY THR GLN GLU ASP GLU ALA SER LEU ARG
SEQRES 27 B 574 ALA PHE THR GLU ALA MET THR ARG TYR SER ALA PRO PRO
SEQRES 28 B 574 GLY ASP PRO PRO LYS PRO GLU TYR ASP LEU GLU LEU ILE
SEQRES 29 B 574 THR SER CYS SER SER ASN VAL SER VAL ALA HIS ASP ALA
SEQRES 30 B 574 SER GLY LYS ARG VAL TYR TYR LEU THR ARG ASP PRO THR
SEQRES 31 B 574 THR PRO LEU ALA ARG ALA ALA TRP GLU THR ALA ARG HIS
SEQRES 32 B 574 THR PRO VAL ASN SER TRP LEU GLY ASN ILE ILE MET TYR
SEQRES 33 B 574 ALA PRO THR LEU TRP ALA ARG MET ILE LEU MET THR HIS
SEQRES 34 B 574 PHE PHE SER ILE LEU LEU ALA GLN GLU GLN LEU GLU LYS
SEQRES 35 B 574 ALA LEU ASP CYS GLN ILE TYR GLY ALA CYS TYR SER ILE
SEQRES 36 B 574 GLU PRO LEU ASP LEU PRO GLN ILE ILE GLN ARG LEU HIS
SEQRES 37 B 574 GLY LEU SER ALA PHE SER LEU HIS SER TYR SER PRO GLY
SEQRES 38 B 574 GLU ILE ASN ARG VAL ALA SER CYS LEU ARG LYS LEU GLY
SEQRES 39 B 574 VAL PRO PRO LEU ARG VAL TRP ARG HIS ARG ALA ARG SER
SEQRES 40 B 574 VAL ARG ALA ARG LEU LEU SER GLN GLY GLY ARG ALA ALA
SEQRES 41 B 574 THR CYS GLY LYS TYR LEU PHE ASN TRP ALA VAL ARG THR
SEQRES 42 B 574 LYS LEU LYS LEU THR PRO ILE PRO ALA ALA SER GLN LEU
SEQRES 43 B 574 ASP LEU SER SER TRP PHE VAL ALA GLY TYR SER GLY GLY
SEQRES 44 B 574 ASP ILE TYR HIS SER LEU SER ARG ALA ARG PRO ARG TRP
SEQRES 45 B 574 PHE MET
HET 23E A 601 85
HET SO4 A 602 5
HET SO4 A 603 5
HET SO4 A 604 5
HET SO4 A 605 5
HET SO4 A 606 5
HET SO4 A 607 5
HET 23E B 601 85
HET 7NG B 602 65
HET SO4 B 603 5
HET SO4 B 604 5
HET SO4 B 605 5
HET SO4 B 606 5
HET SO4 B 607 5
HET SO4 B 608 5
HETNAM 23E (2E)-3-(4-{[(1-{[(13-CYCLOHEXYL-6-OXO-6,7-DIHYDRO-5H-
HETNAM 2 23E INDOLO[1,2-D][1,4]BENZODIAZEPIN-10-YL)
HETNAM 3 23E CARBONYL]AMINO}CYCLOPENTYL)CARBONYL]AMINO}PHENYL)PROP-
HETNAM 4 23E 2-ENOIC ACID
HETNAM SO4 SULFATE ION
HETNAM 7NG 5-[3-(TERT-BUTYLCARBAMOYL)PHENYL]-6-(ETHYLAMINO)-2-(4-
HETNAM 2 7NG FLUOROPHENYL)-N-METHYLFURO[2,3-B]PYRIDINE-3-
HETNAM 3 7NG CARBOXAMIDE
FORMUL 3 23E 2(C38 H38 N4 O5)
FORMUL 4 SO4 12(O4 S 2-)
FORMUL 11 7NG C28 H29 F N4 O3
HELIX 1 AA1 SER A 44 THR A 53 1 10
HELIX 2 AA2 ASP A 61 SER A 76 1 16
HELIX 3 AA3 SER A 84 LYS A 90 1 7
HELIX 4 AA4 GLY A 104 ASN A 110 1 7
HELIX 5 AA5 SER A 112 ASP A 129 1 18
HELIX 6 AA6 ASP A 164 GLY A 188 1 25
HELIX 7 AA7 SER A 189 TYR A 195 5 7
HELIX 8 AA8 SER A 196 LYS A 211 1 16
HELIX 9 AA9 CYS A 223 VAL A 228 1 6
HELIX 10 AB1 THR A 229 GLN A 241 1 13
HELIX 11 AB2 ALA A 246 LEU A 260 1 15
HELIX 12 AB3 THR A 286 ALA A 306 1 21
HELIX 13 AB4 GLY A 328 TYR A 346 1 19
HELIX 14 AB5 PRO A 388 ARG A 401 1 14
HELIX 15 AB6 ASN A 406 TYR A 415 1 10
HELIX 16 AB7 THR A 418 ILE A 424 1 7
HELIX 17 AB8 ILE A 424 GLN A 436 1 13
HELIX 18 AB9 GLU A 455 LEU A 457 5 3
HELIX 19 AC1 ASP A 458 GLY A 468 1 11
HELIX 20 AC2 LEU A 469 SER A 473 5 5
HELIX 21 AC3 SER A 478 GLY A 493 1 16
HELIX 22 AC4 PRO A 496 SER A 513 1 18
HELIX 23 AC5 GLY A 515 PHE A 526 1 12
HELIX 24 AC6 ASN A 527 VAL A 530 5 4
HELIX 25 AC7 ILE A 539 SER A 543 5 5
HELIX 26 AC8 SER B 44 THR B 53 1 10
HELIX 27 AC9 ASP B 61 SER B 76 1 16
HELIX 28 AD1 SER B 84 LYS B 90 1 7
HELIX 29 AD2 GLY B 104 ASN B 110 1 7
HELIX 30 AD3 SER B 112 ASP B 129 1 18
HELIX 31 AD4 ASP B 164 GLY B 188 1 25
HELIX 32 AD5 SER B 189 TYR B 195 5 7
HELIX 33 AD6 SER B 196 LYS B 211 1 16
HELIX 34 AD7 CYS B 223 VAL B 228 1 6
HELIX 35 AD8 THR B 229 GLN B 241 1 13
HELIX 36 AD9 ALA B 246 LEU B 260 1 15
HELIX 37 AE1 THR B 286 ALA B 306 1 21
HELIX 38 AE2 GLY B 328 TYR B 346 1 19
HELIX 39 AE3 ASP B 359 LEU B 362 5 4
HELIX 40 AE4 PRO B 388 ARG B 401 1 14
HELIX 41 AE5 SER B 407 TYR B 415 1 9
HELIX 42 AE6 THR B 418 ILE B 424 1 7
HELIX 43 AE7 ILE B 424 GLN B 436 1 13
HELIX 44 AE8 GLU B 455 LEU B 457 5 3
HELIX 45 AE9 ASP B 458 GLY B 468 1 11
HELIX 46 AF1 LEU B 469 SER B 473 5 5
HELIX 47 AF2 SER B 478 GLY B 493 1 16
HELIX 48 AF3 PRO B 496 SER B 513 1 18
HELIX 49 AF4 GLY B 515 PHE B 526 1 12
HELIX 50 AF5 ILE B 539 SER B 543 5 5
HELIX 51 AF6 LEU B 547 VAL B 552 5 6
SHEET 1 AA1 5 TYR A 4 TRP A 6 0
SHEET 2 AA1 5 ASN A 273 ARG A 277 -1 O TYR A 276 N THR A 5
SHEET 3 AA1 5 GLY A 264 THR A 267 -1 N GLY A 264 O ARG A 277
SHEET 4 AA1 5 THR A 136 ALA A 140 1 N ILE A 138 O THR A 267
SHEET 5 AA1 5 LEU A 159 PRO A 163 -1 O ILE A 160 N MET A 139
SHEET 1 AA2 3 PRO A 214 TYR A 219 0
SHEET 2 AA2 3 ASP A 319 GLU A 325 -1 O CYS A 324 N MET A 215
SHEET 3 AA2 3 GLN A 309 CYS A 316 -1 N GLN A 309 O GLU A 325
SHEET 1 AA3 3 THR A 364 SER A 365 0
SHEET 2 AA3 3 SER A 368 HIS A 374 -1 O SER A 368 N SER A 365
SHEET 3 AA3 3 ARG A 380 ARG A 386 -1 O VAL A 381 N ALA A 373
SHEET 1 AA4 3 LEU A 443 ILE A 447 0
SHEET 2 AA4 3 ALA A 450 ILE A 454 -1 O TYR A 452 N CYS A 445
SHEET 3 AA4 3 TYR A 561 SER A 563 1 O HIS A 562 N CYS A 451
SHEET 1 AA5 2 LEU A 545 ASP A 546 0
SHEET 2 AA5 2 SER A 565 ARG A 566 -1 O SER A 565 N ASP A 546
SHEET 1 AA6 5 TYR B 4 TRP B 6 0
SHEET 2 AA6 5 ASN B 273 ARG B 277 -1 O TYR B 276 N THR B 5
SHEET 3 AA6 5 GLY B 264 THR B 267 -1 N GLY B 264 O ARG B 277
SHEET 4 AA6 5 THR B 136 LYS B 141 1 N ILE B 138 O THR B 267
SHEET 5 AA6 5 ARG B 158 PRO B 163 -1 O ILE B 160 N MET B 139
SHEET 1 AA7 3 PRO B 214 TYR B 219 0
SHEET 2 AA7 3 ASP B 319 GLU B 325 -1 O CYS B 324 N MET B 215
SHEET 3 AA7 3 GLN B 309 CYS B 316 -1 N GLN B 309 O GLU B 325
SHEET 1 AA8 3 THR B 364 SER B 365 0
SHEET 2 AA8 3 SER B 368 HIS B 374 -1 O SER B 368 N SER B 365
SHEET 3 AA8 3 ARG B 380 THR B 385 -1 O VAL B 381 N ALA B 373
SHEET 1 AA9 3 LEU B 443 GLN B 446 0
SHEET 2 AA9 3 CYS B 451 ILE B 454 -1 O ILE B 454 N LEU B 443
SHEET 3 AA9 3 HIS B 562 SER B 563 1 O HIS B 562 N SER B 453
CISPEP 1 GLY B 449 ALA B 450 0 -3.20
SITE 1 AC1 11 ALA A 395 ALA A 396 LEU A 492 GLY A 493
SITE 2 AC1 11 VAL A 494 PRO A 495 PRO A 496 ARG A 498
SITE 3 AC1 11 VAL A 499 ARG A 503 23E B 601
SITE 1 AC2 3 SER A 84 VAL A 85 ARG A 120
SITE 1 AC3 5 ARG A 48 LYS A 51 ARG A 158 THR A 221
SITE 2 AC3 5 CYS A 223
SITE 1 AC4 4 HIS A 374 SER A 476 ARG A 517 MET A 573
SITE 1 AC5 4 PRO A 496 LEU A 497 ARG A 498 ARG A 570
SITE 1 AC6 3 GLU A 361 SER A 371 SER A 478
SITE 1 AC7 4 LYS A 79 ASP A 244 LEU B 60 LEU B 68
SITE 1 AC8 17 THR A 399 ALA A 400 HIS A 428 23E A 601
SITE 2 AC8 17 LEU B 392 ALA B 395 ALA B 396 ILE B 424
SITE 3 AC8 17 HIS B 428 LEU B 492 GLY B 493 VAL B 494
SITE 4 AC8 17 PRO B 495 PRO B 496 ARG B 498 VAL B 499
SITE 5 AC8 17 ARG B 503
SITE 1 AC9 15 ARG B 200 LEU B 204 LEU B 314 CYS B 316
SITE 2 AC9 15 ASP B 319 VAL B 321 ILE B 363 SER B 365
SITE 3 AC9 15 CYS B 366 SER B 368 LEU B 384 MET B 414
SITE 4 AC9 15 TYR B 415 TYR B 452 PHE B 551
SITE 1 AD1 4 SER B 84 VAL B 85 GLU B 86 ARG B 120
SITE 1 AD2 2 GLY B 516 ARG B 517
SITE 1 AD3 3 SER A 1 LYS B 379 ARG B 380
SITE 1 AD4 2 HIS B 475 SER B 476
SITE 1 AD5 3 ARG B 48 LYS B 51 CYS B 223
SITE 1 AD6 3 MET B 187 GLY B 188 SER B 189
CRYST1 66.000 91.100 233.300 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 0.015152 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010977 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004286 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
