HEADER VIRAL PROTEIN 26-OCT-18 6MVP
TITLE HCV NS5B 1B N316 BOUND TO COMPOUND 18
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GENOME POLYPROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.4.22.-,3.4.21.98,3.6.1.15,3.6.4.13,2.7.7.48;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS GENOTYPE 1B (ISOLATE BK);
SOURCE 3 ORGANISM_COMMON: HCV;
SOURCE 4 ORGANISM_TAXID: 11105;
SOURCE 5 STRAIN: ISOLATE BK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
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: PET28
KEYWDS HEPATITUS C, NS5B, VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.P.WILLIAMS,K.KAHLER,D.J.PRICE,A.J.PEAT
REVDAT 2 13-MAR-24 6MVP 1 REMARK
REVDAT 1 04-SEP-19 6MVP 0
JRNL AUTH P.Y.CHONG,J.B.SHOTWELL,J.MILLER,D.J.PRICE,A.MAYNARD,
JRNL AUTH 2 C.VOITENLEITNER,A.MATHIS,S.WILLIAMS,J.J.POULIOT,K.CREECH,
JRNL AUTH 3 F.WANG,J.FANG,H.ZHANG,V.W.TAI,E.TURNER,K.M.KAHLER,R.CROSBY,
JRNL AUTH 4 A.J.PEAT
JRNL TITL DESIGN OF N-BENZOXABOROLE BENZOFURAN GSK8175-OPTIMIZATION OF
JRNL TITL 2 HUMAN PHARMACOKINETICS INSPIRED BY METABOLITES OF A FAILED
JRNL TITL 3 CLINICAL HCV INHIBITOR.
JRNL REF J.MED.CHEM. V. 62 3254 2019
JRNL REFN ISSN 0022-2623
JRNL PMID 30763090
JRNL DOI 10.1021/ACS.JMEDCHEM.8B01719
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0081
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 72491
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) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5457
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5425
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE SET COUNT : 401
REMARK 3 BIN FREE R VALUE : 0.2500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8356
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 74
REMARK 3 SOLVENT ATOMS : 528
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.26000
REMARK 3 B22 (A**2) : 1.15000
REMARK 3 B33 (A**2) : -0.89000
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): 0.223
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.176
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.122
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.907
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8637 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8065 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11774 ; 1.200 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18530 ; 1.041 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1100 ; 5.328 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 335 ;33.003 ;23.164
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1377 ;11.855 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 57 ;13.577 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1345 ; 0.066 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9742 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1941 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 563 B 1 563 64778 0.070 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 563
REMARK 3 RESIDUE RANGE : A 601 A 601
REMARK 3 ORIGIN FOR THE GROUP (A): 11.581 46.034 47.082
REMARK 3 T TENSOR
REMARK 3 T11: 0.0520 T22: 0.0480
REMARK 3 T33: 0.0117 T12: -0.0335
REMARK 3 T13: -0.0122 T23: 0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 0.3835 L22: 0.1418
REMARK 3 L33: 0.8983 L12: -0.1055
REMARK 3 L13: 0.3422 L23: -0.0804
REMARK 3 S TENSOR
REMARK 3 S11: 0.0904 S12: -0.0418 S13: 0.0164
REMARK 3 S21: 0.0000 S22: -0.0552 S23: -0.0234
REMARK 3 S31: 0.1091 S32: -0.0310 S33: -0.0352
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 563
REMARK 3 RESIDUE RANGE : B 601 B 601
REMARK 3 ORIGIN FOR THE GROUP (A): -11.599 46.196 -7.851
REMARK 3 T TENSOR
REMARK 3 T11: 0.0304 T22: 0.0337
REMARK 3 T33: 0.0081 T12: 0.0247
REMARK 3 T13: -0.0052 T23: -0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 0.4916 L22: 0.1710
REMARK 3 L33: 0.6596 L12: 0.0877
REMARK 3 L13: 0.1682 L23: 0.0697
REMARK 3 S TENSOR
REMARK 3 S11: 0.0631 S12: 0.0504 S13: 0.0130
REMARK 3 S21: 0.0078 S22: -0.0372 S23: 0.0283
REMARK 3 S31: 0.0484 S32: 0.0417 S33: -0.0259
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED HYDROGENS
REMARK 3 HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 6MVP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1000237686.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-MAR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
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 : 79393
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.3000
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.48900
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NA CITRATE PH5.0, 10% GLYCEROL,
REMARK 280 15% PEG3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 43.19950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.12050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.65550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.12050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.19950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.65550
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 MET A -1
REMARK 465 ALA A 0
REMARK 465 GLU A 150
REMARK 465 LYS A 151
REMARK 465 GLY A 152
REMARK 465 GLY A 153
REMARK 465 ALA A 541
REMARK 465 ALA A 542
REMARK 465 SER A 543
REMARK 465 ARG A 544
REMARK 465 LEU A 545
REMARK 465 ASP A 546
REMARK 465 LEU A 547
REMARK 465 SER A 548
REMARK 465 GLY A 549
REMARK 465 TRP A 550
REMARK 465 PHE A 551
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 LEU A 571
REMARK 465 GLU A 572
REMARK 465 HIS A 573
REMARK 465 HIS A 574
REMARK 465 HIS A 575
REMARK 465 HIS A 576
REMARK 465 HIS A 577
REMARK 465 HIS A 578
REMARK 465 MET B -1
REMARK 465 ALA B 0
REMARK 465 GLU B 150
REMARK 465 LYS B 151
REMARK 465 GLY B 152
REMARK 465 GLY B 153
REMARK 465 ALA B 541
REMARK 465 ALA B 542
REMARK 465 SER B 543
REMARK 465 ARG B 544
REMARK 465 LEU B 545
REMARK 465 ASP B 546
REMARK 465 LEU B 547
REMARK 465 SER B 548
REMARK 465 GLY B 549
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 LEU B 571
REMARK 465 GLU B 572
REMARK 465 HIS B 573
REMARK 465 HIS B 574
REMARK 465 HIS B 575
REMARK 465 HIS B 576
REMARK 465 HIS B 577
REMARK 465 HIS B 578
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 ARG A 43 CD NE CZ NH1 NH2
REMARK 470 GLN A 47 CG CD OE1 NE2
REMARK 470 LYS A 50 CD CE NZ
REMARK 470 LYS A 51 CG CD CE NZ
REMARK 470 LYS A 81 CD CE NZ
REMARK 470 GLU A 86 CG CD OE1 OE2
REMARK 470 LYS A 90 CG CD CE NZ
REMARK 470 LYS A 100 CG CD CE NZ
REMARK 470 LYS A 106 CD CE NZ
REMARK 470 ARG A 114 CG CD NE CZ NH1 NH2
REMARK 470 PRO A 149 CG CD
REMARK 470 ARG A 158 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 212 CG CD CE NZ
REMARK 470 ARG A 222 CD NE CZ NH1 NH2
REMARK 470 LYS A 270 CE NZ
REMARK 470 LYS A 307 CD CE NZ
REMARK 470 GLN A 309 CG CD OE1 NE2
REMARK 470 ARG A 380 CD NE CZ NH1 NH2
REMARK 470 GLU A 440 CG CD OE1 OE2
REMARK 470 GLN A 461 CG CD OE1 NE2
REMARK 470 ARG A 498 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 501 NE CZ NH1 NH2
REMARK 470 LYS A 523 CD CE NZ
REMARK 470 LYS A 531 CD CE NZ
REMARK 470 THR A 532 OG1 CG2
REMARK 470 LEU A 534 CG CD1 CD2
REMARK 470 LYS A 535 CG CD CE NZ
REMARK 470 VAL A 552 CG1 CG2
REMARK 470 SER A 563 OG
REMARK 470 ARG B 32 NE CZ NH1 NH2
REMARK 470 LYS B 100 CG CD CE NZ
REMARK 470 ARG B 114 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 141 CE NZ
REMARK 470 GLN B 148 CG CD OE1 NE2
REMARK 470 PRO B 149 CG CD
REMARK 470 ARG B 154 CZ NH1 NH2
REMARK 470 LYS B 155 CE NZ
REMARK 470 ARG B 158 NE CZ NH1 NH2
REMARK 470 GLU B 202 CD OE1 OE2
REMARK 470 LYS B 212 CG CD CE NZ
REMARK 470 ARG B 222 CD NE CZ NH1 NH2
REMARK 470 LYS B 270 CE NZ
REMARK 470 LYS B 307 CE NZ
REMARK 470 GLN B 309 CG CD OE1 NE2
REMARK 470 ASP B 352 CG OD1 OD2
REMARK 470 ARG B 380 CZ NH1 NH2
REMARK 470 GLN B 461 CG CD OE1 NE2
REMARK 470 ARG B 501 NE CZ NH1 NH2
REMARK 470 ARG B 505 NE CZ NH1 NH2
REMARK 470 LYS B 523 CG CD CE NZ
REMARK 470 LYS B 531 CG CD CE NZ
REMARK 470 THR B 532 OG1 CG2
REMARK 470 LEU B 534 CG CD1 CD2
REMARK 470 LYS B 535 CG CD CE NZ
REMARK 470 TRP B 550 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 550 CZ3 CH2
REMARK 470 SER B 563 OG
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 NH1 ARG A 200 O HOH A 701 1.85
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 -57.03 -125.95
REMARK 500 SER A 347 5.59 92.48
REMARK 500 ALA A 348 70.30 -116.45
REMARK 500 LEU B 260 -56.51 -125.81
REMARK 500 SER B 347 6.11 91.24
REMARK 500 ALA B 348 70.26 -115.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 968 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH A 969 DISTANCE = 6.05 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K4S A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K4S B 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6MVK RELATED DB: PDB
REMARK 900 RELATED ID: 6MVQ RELATED DB: PDB
REMARK 900 RELATED ID: 6MVO RELATED DB: PDB
DBREF 6MVP A 1 570 UNP P26663 POLG_HCVBK 2420 2989
DBREF 6MVP B 1 570 UNP P26663 POLG_HCVBK 2420 2989
SEQADV 6MVP MET A -1 UNP P26663 EXPRESSION TAG
SEQADV 6MVP ALA A 0 UNP P26663 EXPRESSION TAG
SEQADV 6MVP GLN A 47 UNP P26663 LEU 2466 CONFLICT
SEQADV 6MVP TYR A 101 UNP P26663 PHE 2520 CONFLICT
SEQADV 6MVP ARG A 114 UNP P26663 LYS 2533 CONFLICT
SEQADV 6MVP VAL A 329 UNP P26663 THR 2748 CONFLICT
SEQADV 6MVP LEU A 571 UNP P26663 EXPRESSION TAG
SEQADV 6MVP GLU A 572 UNP P26663 EXPRESSION TAG
SEQADV 6MVP HIS A 573 UNP P26663 EXPRESSION TAG
SEQADV 6MVP HIS A 574 UNP P26663 EXPRESSION TAG
SEQADV 6MVP HIS A 575 UNP P26663 EXPRESSION TAG
SEQADV 6MVP HIS A 576 UNP P26663 EXPRESSION TAG
SEQADV 6MVP HIS A 577 UNP P26663 EXPRESSION TAG
SEQADV 6MVP HIS A 578 UNP P26663 EXPRESSION TAG
SEQADV 6MVP MET B -1 UNP P26663 EXPRESSION TAG
SEQADV 6MVP ALA B 0 UNP P26663 EXPRESSION TAG
SEQADV 6MVP GLN B 47 UNP P26663 LEU 2466 CONFLICT
SEQADV 6MVP TYR B 101 UNP P26663 PHE 2520 CONFLICT
SEQADV 6MVP ARG B 114 UNP P26663 LYS 2533 CONFLICT
SEQADV 6MVP VAL B 329 UNP P26663 THR 2748 CONFLICT
SEQADV 6MVP LEU B 571 UNP P26663 EXPRESSION TAG
SEQADV 6MVP GLU B 572 UNP P26663 EXPRESSION TAG
SEQADV 6MVP HIS B 573 UNP P26663 EXPRESSION TAG
SEQADV 6MVP HIS B 574 UNP P26663 EXPRESSION TAG
SEQADV 6MVP HIS B 575 UNP P26663 EXPRESSION TAG
SEQADV 6MVP HIS B 576 UNP P26663 EXPRESSION TAG
SEQADV 6MVP HIS B 577 UNP P26663 EXPRESSION TAG
SEQADV 6MVP HIS B 578 UNP P26663 EXPRESSION TAG
SEQRES 1 A 580 MET ALA SER MET SER TYR THR TRP THR GLY ALA LEU ILE
SEQRES 2 A 580 THR PRO CYS ALA ALA GLU GLU SER LYS LEU PRO ILE ASN
SEQRES 3 A 580 ALA LEU SER ASN SER LEU LEU ARG HIS HIS ASN MET VAL
SEQRES 4 A 580 TYR ALA THR THR SER ARG SER ALA GLY GLN ARG GLN LYS
SEQRES 5 A 580 LYS VAL THR PHE ASP ARG LEU GLN VAL LEU ASP ASP HIS
SEQRES 6 A 580 TYR ARG ASP VAL LEU LYS GLU MET LYS ALA LYS ALA SER
SEQRES 7 A 580 THR VAL LYS ALA LYS LEU LEU SER VAL GLU GLU ALA CYS
SEQRES 8 A 580 LYS LEU THR PRO PRO HIS SER ALA LYS SER LYS TYR GLY
SEQRES 9 A 580 TYR GLY ALA LYS ASP VAL ARG ASN LEU SER SER ARG ALA
SEQRES 10 A 580 VAL ASN HIS ILE HIS SER VAL TRP LYS ASP LEU LEU GLU
SEQRES 11 A 580 ASP THR VAL THR PRO ILE ASP THR THR ILE MET ALA LYS
SEQRES 12 A 580 ASN GLU VAL PHE CYS VAL GLN PRO GLU LYS GLY GLY ARG
SEQRES 13 A 580 LYS PRO ALA ARG LEU ILE VAL PHE PRO ASP LEU GLY VAL
SEQRES 14 A 580 ARG VAL CYS GLU LYS MET ALA LEU TYR ASP VAL VAL SER
SEQRES 15 A 580 THR LEU PRO GLN VAL VAL MET GLY SER SER TYR GLY PHE
SEQRES 16 A 580 GLN TYR SER PRO GLY GLN ARG VAL GLU PHE LEU VAL ASN
SEQRES 17 A 580 THR TRP LYS SER LYS LYS ASN PRO MET GLY PHE SER TYR
SEQRES 18 A 580 ASP THR ARG CYS PHE ASP SER THR VAL THR GLU ASN ASP
SEQRES 19 A 580 ILE ARG VAL GLU GLU SER ILE TYR GLN CYS CYS ASP LEU
SEQRES 20 A 580 ALA PRO GLU ALA ARG GLN ALA ILE LYS SER LEU THR GLU
SEQRES 21 A 580 ARG LEU TYR ILE GLY GLY PRO LEU THR ASN SER LYS GLY
SEQRES 22 A 580 GLN ASN CYS GLY TYR ARG ARG CYS ARG ALA SER GLY VAL
SEQRES 23 A 580 LEU THR THR SER CYS GLY ASN THR LEU THR CYS TYR LEU
SEQRES 24 A 580 LYS ALA SER ALA ALA CYS ARG ALA ALA LYS LEU GLN ASP
SEQRES 25 A 580 CYS THR MET LEU VAL ASN GLY ASP ASP LEU VAL VAL ILE
SEQRES 26 A 580 CYS GLU SER ALA GLY VAL GLN GLU ASP ALA ALA SER LEU
SEQRES 27 A 580 ARG VAL PHE THR GLU ALA MET THR ARG TYR SER ALA PRO
SEQRES 28 A 580 PRO GLY ASP PRO PRO GLN PRO GLU TYR ASP LEU GLU LEU
SEQRES 29 A 580 ILE THR SER CYS SER SER ASN VAL SER VAL ALA HIS ASP
SEQRES 30 A 580 ALA SER GLY LYS ARG VAL TYR TYR LEU THR ARG ASP PRO
SEQRES 31 A 580 THR THR PRO LEU ALA ARG ALA ALA TRP GLU THR ALA ARG
SEQRES 32 A 580 HIS THR PRO VAL ASN SER TRP LEU GLY ASN ILE ILE MET
SEQRES 33 A 580 TYR ALA PRO THR LEU TRP ALA ARG MET ILE LEU MET THR
SEQRES 34 A 580 HIS PHE PHE SER ILE LEU LEU ALA GLN GLU GLN LEU GLU
SEQRES 35 A 580 LYS ALA LEU ASP CYS GLN ILE TYR GLY ALA CYS TYR SER
SEQRES 36 A 580 ILE GLU PRO LEU ASP LEU PRO GLN ILE ILE GLU ARG LEU
SEQRES 37 A 580 HIS GLY LEU SER ALA PHE SER LEU HIS SER TYR SER PRO
SEQRES 38 A 580 GLY GLU ILE ASN ARG VAL ALA SER CYS LEU ARG LYS LEU
SEQRES 39 A 580 GLY VAL PRO PRO LEU ARG VAL TRP ARG HIS ARG ALA ARG
SEQRES 40 A 580 SER VAL ARG ALA ARG LEU LEU SER GLN GLY GLY ARG ALA
SEQRES 41 A 580 ALA THR CYS GLY LYS TYR LEU PHE ASN TRP ALA VAL LYS
SEQRES 42 A 580 THR LYS LEU LYS LEU THR PRO ILE PRO ALA ALA SER ARG
SEQRES 43 A 580 LEU ASP LEU SER GLY TRP PHE VAL ALA GLY TYR SER GLY
SEQRES 44 A 580 GLY ASP ILE TYR HIS SER LEU SER ARG ALA ARG PRO ARG
SEQRES 45 A 580 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 580 MET ALA SER MET SER TYR THR TRP THR GLY ALA LEU ILE
SEQRES 2 B 580 THR PRO CYS ALA ALA GLU GLU SER LYS LEU PRO ILE ASN
SEQRES 3 B 580 ALA LEU SER ASN SER LEU LEU ARG HIS HIS ASN MET VAL
SEQRES 4 B 580 TYR ALA THR THR SER ARG SER ALA GLY GLN ARG GLN LYS
SEQRES 5 B 580 LYS VAL THR PHE ASP ARG LEU GLN VAL LEU ASP ASP HIS
SEQRES 6 B 580 TYR ARG ASP VAL LEU LYS GLU MET LYS ALA LYS ALA SER
SEQRES 7 B 580 THR VAL LYS ALA LYS LEU LEU SER VAL GLU GLU ALA CYS
SEQRES 8 B 580 LYS LEU THR PRO PRO HIS SER ALA LYS SER LYS TYR GLY
SEQRES 9 B 580 TYR GLY ALA LYS ASP VAL ARG ASN LEU SER SER ARG ALA
SEQRES 10 B 580 VAL ASN HIS ILE HIS SER VAL TRP LYS ASP LEU LEU GLU
SEQRES 11 B 580 ASP THR VAL THR PRO ILE ASP THR THR ILE MET ALA LYS
SEQRES 12 B 580 ASN GLU VAL PHE CYS VAL GLN PRO GLU LYS GLY GLY ARG
SEQRES 13 B 580 LYS PRO ALA ARG LEU ILE VAL PHE PRO ASP LEU GLY VAL
SEQRES 14 B 580 ARG VAL CYS GLU LYS MET ALA LEU TYR ASP VAL VAL SER
SEQRES 15 B 580 THR LEU PRO GLN VAL VAL MET GLY SER SER TYR GLY PHE
SEQRES 16 B 580 GLN TYR SER PRO GLY GLN ARG VAL GLU PHE LEU VAL ASN
SEQRES 17 B 580 THR TRP LYS SER LYS LYS ASN PRO MET GLY PHE SER TYR
SEQRES 18 B 580 ASP THR ARG CYS PHE ASP SER THR VAL THR GLU ASN ASP
SEQRES 19 B 580 ILE ARG VAL GLU GLU SER ILE TYR GLN CYS CYS ASP LEU
SEQRES 20 B 580 ALA PRO GLU ALA ARG GLN ALA ILE LYS SER LEU THR GLU
SEQRES 21 B 580 ARG LEU TYR ILE GLY GLY PRO LEU THR ASN SER LYS GLY
SEQRES 22 B 580 GLN ASN CYS GLY TYR ARG ARG CYS ARG ALA SER GLY VAL
SEQRES 23 B 580 LEU THR THR SER CYS GLY ASN THR LEU THR CYS TYR LEU
SEQRES 24 B 580 LYS ALA SER ALA ALA CYS ARG ALA ALA LYS LEU GLN ASP
SEQRES 25 B 580 CYS THR MET LEU VAL ASN GLY ASP ASP LEU VAL VAL ILE
SEQRES 26 B 580 CYS GLU SER ALA GLY VAL GLN GLU ASP ALA ALA SER LEU
SEQRES 27 B 580 ARG VAL PHE THR GLU ALA MET THR ARG TYR SER ALA PRO
SEQRES 28 B 580 PRO GLY ASP PRO PRO GLN PRO GLU TYR ASP LEU GLU LEU
SEQRES 29 B 580 ILE THR SER CYS SER SER ASN VAL SER VAL ALA HIS ASP
SEQRES 30 B 580 ALA SER GLY LYS ARG VAL TYR TYR LEU THR ARG ASP PRO
SEQRES 31 B 580 THR THR PRO LEU ALA ARG ALA ALA TRP GLU THR ALA ARG
SEQRES 32 B 580 HIS THR PRO VAL ASN SER TRP LEU GLY ASN ILE ILE MET
SEQRES 33 B 580 TYR ALA PRO THR LEU TRP ALA ARG MET ILE LEU MET THR
SEQRES 34 B 580 HIS PHE PHE SER ILE LEU LEU ALA GLN GLU GLN LEU GLU
SEQRES 35 B 580 LYS ALA LEU ASP CYS GLN ILE TYR GLY ALA CYS TYR SER
SEQRES 36 B 580 ILE GLU PRO LEU ASP LEU PRO GLN ILE ILE GLU ARG LEU
SEQRES 37 B 580 HIS GLY LEU SER ALA PHE SER LEU HIS SER TYR SER PRO
SEQRES 38 B 580 GLY GLU ILE ASN ARG VAL ALA SER CYS LEU ARG LYS LEU
SEQRES 39 B 580 GLY VAL PRO PRO LEU ARG VAL TRP ARG HIS ARG ALA ARG
SEQRES 40 B 580 SER VAL ARG ALA ARG LEU LEU SER GLN GLY GLY ARG ALA
SEQRES 41 B 580 ALA THR CYS GLY LYS TYR LEU PHE ASN TRP ALA VAL LYS
SEQRES 42 B 580 THR LYS LEU LYS LEU THR PRO ILE PRO ALA ALA SER ARG
SEQRES 43 B 580 LEU ASP LEU SER GLY TRP PHE VAL ALA GLY TYR SER GLY
SEQRES 44 B 580 GLY ASP ILE TYR HIS SER LEU SER ARG ALA ARG PRO ARG
SEQRES 45 B 580 LEU GLU HIS HIS HIS HIS HIS HIS
HET K4S A 601 37
HET K4S B 601 37
HETNAM K4S (4-{[5-CYCLOPROPYL-2-(4-FLUOROPHENYL)-3-
HETNAM 2 K4S (METHYLCARBAMOYL)-1-BENZOFURAN-6-YL](METHYLSULFONYL)
HETNAM 3 K4S AMINO}PHENYL)BORONIC ACID
FORMUL 3 K4S 2(C26 H24 B F N2 O6 S)
FORMUL 5 HOH *528(H2 O)
HELIX 1 AA1 LEU A 26 LEU A 31 1 6
HELIX 2 AA2 HIS A 33 ASN A 35 5 3
HELIX 3 AA3 THR A 41 ARG A 43 5 3
HELIX 4 AA4 SER A 44 THR A 53 1 10
HELIX 5 AA5 ASP A 61 SER A 76 1 16
HELIX 6 AA6 SER A 84 LEU A 91 1 8
HELIX 7 AA7 GLY A 104 ASN A 110 1 7
HELIX 8 AA8 SER A 112 ASP A 129 1 18
HELIX 9 AA9 ASP A 164 GLY A 188 1 25
HELIX 10 AB1 SER A 189 TYR A 195 5 7
HELIX 11 AB2 SER A 196 SER A 210 1 15
HELIX 12 AB3 CYS A 223 VAL A 228 1 6
HELIX 13 AB4 THR A 229 CYS A 242 1 14
HELIX 14 AB5 ALA A 246 LEU A 260 1 15
HELIX 15 AB6 THR A 286 ALA A 306 1 21
HELIX 16 AB7 GLY A 328 TYR A 346 1 19
HELIX 17 AB8 ASP A 359 ILE A 363 5 5
HELIX 18 AB9 PRO A 388 ARG A 401 1 14
HELIX 19 AC1 ASN A 406 TYR A 415 1 10
HELIX 20 AC2 THR A 418 ILE A 424 1 7
HELIX 21 AC3 ILE A 424 GLU A 437 1 14
HELIX 22 AC4 GLU A 455 LEU A 457 5 3
HELIX 23 AC5 ASP A 458 GLY A 468 1 11
HELIX 24 AC6 LEU A 469 SER A 473 5 5
HELIX 25 AC7 SER A 478 GLY A 493 1 16
HELIX 26 AC8 PRO A 496 GLY A 515 1 20
HELIX 27 AC9 GLY A 515 PHE A 526 1 12
HELIX 28 AD1 ASN A 527 VAL A 530 5 4
HELIX 29 AD2 LEU B 26 LEU B 31 1 6
HELIX 30 AD3 HIS B 33 ASN B 35 5 3
HELIX 31 AD4 THR B 41 ARG B 43 5 3
HELIX 32 AD5 SER B 44 THR B 53 1 10
HELIX 33 AD6 ASP B 61 SER B 76 1 16
HELIX 34 AD7 SER B 84 LEU B 91 1 8
HELIX 35 AD8 GLY B 104 ASN B 110 1 7
HELIX 36 AD9 SER B 112 ASP B 129 1 18
HELIX 37 AE1 ASP B 164 GLY B 188 1 25
HELIX 38 AE2 SER B 189 TYR B 195 5 7
HELIX 39 AE3 SER B 196 SER B 210 1 15
HELIX 40 AE4 CYS B 223 VAL B 228 1 6
HELIX 41 AE5 THR B 229 CYS B 242 1 14
HELIX 42 AE6 ALA B 246 LEU B 260 1 15
HELIX 43 AE7 THR B 286 ALA B 306 1 21
HELIX 44 AE8 GLY B 328 TYR B 346 1 19
HELIX 45 AE9 ASP B 359 ILE B 363 5 5
HELIX 46 AF1 PRO B 388 ARG B 401 1 14
HELIX 47 AF2 ASN B 406 TYR B 415 1 10
HELIX 48 AF3 THR B 418 ILE B 424 1 7
HELIX 49 AF4 ILE B 424 GLU B 437 1 14
HELIX 50 AF5 GLU B 455 LEU B 457 5 3
HELIX 51 AF6 ASP B 458 GLY B 468 1 11
HELIX 52 AF7 LEU B 469 SER B 473 5 5
HELIX 53 AF8 SER B 478 GLY B 493 1 16
HELIX 54 AF9 PRO B 496 GLY B 515 1 20
HELIX 55 AG1 GLY B 515 PHE B 526 1 12
HELIX 56 AG2 ASN B 527 VAL B 530 5 4
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 LEU A 266 O CYS A 274
SHEET 4 AA1 5 THR A 136 ALA A 140 1 N THR A 136 O THR A 267
SHEET 5 AA1 5 LEU A 159 PHE A 162 -1 O PHE A 162 N THR A 137
SHEET 1 AA2 2 VAL A 37 ALA A 39 0
SHEET 2 AA2 2 VAL A 144 CYS A 146 -1 O PHE A 145 N TYR A 38
SHEET 1 AA3 3 PRO A 214 ASP A 220 0
SHEET 2 AA3 3 ASP A 319 GLU A 325 -1 O CYS A 324 N MET A 215
SHEET 3 AA3 3 GLN A 309 ASN A 316 -1 N THR A 312 O ILE A 323
SHEET 1 AA4 2 SER A 368 HIS A 374 0
SHEET 2 AA4 2 ARG A 380 ARG A 386 -1 O VAL A 381 N ALA A 373
SHEET 1 AA5 3 LEU A 443 ILE A 447 0
SHEET 2 AA5 3 ALA A 450 ILE A 454 -1 O TYR A 452 N CYS A 445
SHEET 3 AA5 3 TYR A 561 HIS A 562 1 O HIS A 562 N CYS A 451
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 LEU B 266 O CYS B 274
SHEET 4 AA6 5 THR B 136 ALA B 140 1 N THR B 136 O THR B 267
SHEET 5 AA6 5 LEU B 159 PHE B 162 -1 O PHE B 162 N THR B 137
SHEET 1 AA7 2 VAL B 37 ALA B 39 0
SHEET 2 AA7 2 VAL B 144 CYS B 146 -1 O PHE B 145 N TYR B 38
SHEET 1 AA8 3 PRO B 214 ASP B 220 0
SHEET 2 AA8 3 ASP B 319 GLU B 325 -1 O CYS B 324 N MET B 215
SHEET 3 AA8 3 GLN B 309 ASN B 316 -1 N THR B 312 O ILE B 323
SHEET 1 AA9 2 SER B 368 HIS B 374 0
SHEET 2 AA9 2 ARG B 380 ARG B 386 -1 O VAL B 381 N ALA B 373
SHEET 1 AB1 3 LEU B 443 ILE B 447 0
SHEET 2 AB1 3 ALA B 450 ILE B 454 -1 O TYR B 452 N CYS B 445
SHEET 3 AB1 3 TYR B 561 HIS B 562 1 O HIS B 562 N CYS B 451
SITE 1 AC1 18 PRO A 197 ARG A 200 LEU A 204 LEU A 314
SITE 2 AC1 18 ASN A 316 VAL A 321 LEU A 360 ILE A 363
SITE 3 AC1 18 SER A 365 CYS A 366 SER A 368 LEU A 384
SITE 4 AC1 18 MET A 414 TYR A 415 TYR A 448 HOH A 701
SITE 5 AC1 18 HOH A 702 HOH A 705
SITE 1 AC2 16 PRO B 197 ARG B 200 LEU B 204 LEU B 314
SITE 2 AC2 16 ASN B 316 ASP B 319 LEU B 360 ILE B 363
SITE 3 AC2 16 SER B 365 CYS B 366 SER B 368 LEU B 384
SITE 4 AC2 16 MET B 414 TYR B 415 TYR B 448 HOH B 701
CRYST1 86.399 107.311 126.241 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 0.011574 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009319 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007921 0.00000
(ATOM LINES ARE NOT SHOWN.)
END