7O46_17
  DSViewer          3D                             0

 43 47  0  0  0  0  0  0  0  0999 V2000
   37.6332   -0.2737   43.9679 C   0  0  2  0  0  0
   34.5611   -2.8442   36.8851 C   0  0
   37.3554   -0.9577   45.3265 C   0  0
   36.4411   -0.2174   46.3167 C   0  0
   35.0661   -1.4906   38.8428 C   0  0
   37.6971    0.2351   47.0739 C   0  0
   38.4672   -0.8979   46.3774 C   0  0
   36.3977    0.2261   43.1896 C   0  0
   36.0151   -1.2790   41.1464 C   0  0
   33.7037   -1.2333   38.9721 C   0  0
   33.2108   -2.4980   37.1323 C   0  0
   37.3795    0.4719   40.8158 N   0  0
   35.9995   -0.9447   39.7906 N   0  0
   38.0378   -1.1326   42.7534 C   0  0
   32.7982   -1.7280   38.1205 N   0  0
   36.7490    0.9278   38.6448 O   0  0
   36.7256    0.2398   39.6424 C   0  0
   36.9678   -0.4060   41.8965 C   0  0
   35.3466   -2.1685   41.6375 O   0  0
   34.9708   -3.6654   35.8130 C   0  0
   36.2926   -3.9524   35.6382 C   0  0
   37.2606   -3.4367   36.5183 C   0  0
   36.8930   -2.6460   37.5702 C   0  0
   35.5325   -2.3246   37.7782 C   0  0
   38.3401    0.5454   44.1111 H   0  0
   37.0060   -1.9786   45.1633 H   0  0
   35.7760   -0.8585   46.8966 H   0  0
   35.8192    0.5809   45.9111 H   0  0
   37.6596    0.1865   48.1614 H   0  0
   38.0314    1.2450   46.8343 H   0  0
   39.4579   -0.6540   46.0005 H   0  0
   38.5732   -1.8065   46.9594 H   0  0
   36.2696    1.3046   43.1690 H   0  0
   35.4445   -0.1826   43.5316 H   0  0
   33.3822   -0.6128   39.7961 H   0  0
   32.4687   -2.9285   36.4857 H   0  0
   38.0027    1.2427   40.9244 H   0  0
   37.8827   -2.2059   42.8828 H   0  0
   39.0720   -1.0251   42.4258 H   0  0
   34.2295   -4.1211   35.1682 H   0  0
   36.5834   -4.6255   34.8433 H   0  0
   38.2978   -3.7033   36.3766 H   0  0
   37.6613   -2.2883   38.2376 H   0  0
  1  3  1  0  0  0
  1  8  1  0  0  0
  1 14  1  0  0  0
  1 25  1  0  0  0
  2 11  2  0  0  0
  2 20  1  0  0  0
  2 24  1  0  0  0
  3  4  1  0  0  0
  3  7  1  0  0  0
  3 26  1  0  0  0
  4  6  1  0  0  0
  4 27  1  0  0  0
  4 28  1  0  0  0
  5 10  1  0  0  0
  5 13  1  0  0  0
  5 24  2  0  0  0
  6  7  1  0  0  0
  6 29  1  0  0  0
  6 30  1  0  0  0
  7 31  1  0  0  0
  7 32  1  0  0  0
  8 18  1  0  0  0
  8 33  1  0  0  0
  8 34  1  0  0  0
  9 13  1  0  0  0
  9 18  1  0  0  0
  9 19  2  0  0  0
 10 15  2  0  0  0
 10 35  1  0  0  0
 11 15  1  0  0  0
 11 36  1  0  0  0
 12 17  1  0  0  0
 12 18  1  0  0  0
 12 37  1  0  0  0
 13 17  1  0  0  0
 14 18  1  0  0  0
 14 38  1  0  0  0
 14 39  1  0  0  0
 16 17  2  0  0  0
 20 21  2  0  0  0
 20 40  1  0  0  0
 21 22  1  0  0  0
 21 41  1  0  0  0
 22 23  2  0  0  0
 22 42  1  0  0  0
 23 24  1  0  0  0
 23 43  1  0  0  0
M  END
> <Resolution>
2.23

> <__PDBRemarks__>
HEADER    VIRAL PROTEIN                           05-APR-21   7O46
TITLE     CRYSTAL STRUCTURE OF SARS-COV-2 MAIN PROTEASE (NSP5) IN COMPLEX WITH
TITLE    2 COMPOUND 17
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: 3C-LIKE PROTEINASE NSP5;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: 3CL-PRO,3CLP,MAIN PROTEASE,MPRO,NON-STRUCTURAL PROTEIN 5,
COMPND   5 NSP5,SARS CORONAVIRUS MAIN PROTEINASE;
COMPND   6 EC: 3.4.22.69;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS
SOURCE   3 2;
SOURCE   4 ORGANISM_TAXID: 2697049;
SOURCE   5 GENE: REP, 1A-1B;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS    INHIBITOR, COMPLEX, PROTEASE, VIRAL PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    V.O.TALIBOV
REVDAT   2   02-MAR-22 7O46    1       JRNL
REVDAT   1   23-FEB-22 7O46    0
JRNL        AUTH   A.LUTTENS,H.GULLBERG,E.ABDURAKHMANOV,D.D.VO,D.AKABERI,
JRNL        AUTH 2 V.O.TALIBOV,N.NEKHOTIAEVA,L.VANGEEL,S.DE JONGHE,D.JOCHMANS,
JRNL        AUTH 3 J.KRAMBRICH,A.TAS,B.LUNDGREN,Y.GRAVENFORS,A.J.CRAIG,
JRNL        AUTH 4 Y.ATILAW,A.SANDSTROM,L.W.K.MOODIE,A.LUNDKVIST,
JRNL        AUTH 5 M.J.VAN HEMERT,J.NEYTS,J.LENNERSTRAND,J.KIHLBERG,K.SANDBERG,
JRNL        AUTH 6 U.H.DANIELSON,J.CARLSSON
JRNL        TITL   ULTRALARGE VIRTUAL SCREENING IDENTIFIES SARS-COV-2 MAIN
JRNL        TITL 2 PROTEASE INHIBITORS WITH BROAD-SPECTRUM ACTIVITY AGAINST
JRNL        TITL 3 CORONAVIRUSES.
JRNL        REF    J.AM.CHEM.SOC.                V. 144  2905 2022
JRNL        REFN                   ESSN 1520-5126
JRNL        PMID   35142215
JRNL        DOI    10.1021/JACS.1C08402
REMARK   2
REMARK   2 RESOLUTION.    2.23 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.8.0267
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.23
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.18
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6
REMARK   3   NUMBER OF REFLECTIONS             : 12473
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) : 0.198
REMARK   3   R VALUE            (WORKING SET) : 0.196
REMARK   3   FREE R VALUE                     : 0.249
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900
REMARK   3   FREE R VALUE TEST SET COUNT      : 638
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) : 2.23
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.29
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 868
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.90
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3780
REMARK   3   BIN FREE R VALUE SET COUNT          : 45
REMARK   3   BIN FREE R VALUE                    : 0.4150
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2329
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 24
REMARK   3   SOLVENT ATOMS            : 2
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 79.26
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 4.28000
REMARK   3    B22 (A**2) : -2.38000
REMARK   3    B33 (A**2) : -2.20000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 1.19000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.391
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.245
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.252
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.948
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2409 ; 0.007 ; 0.013
REMARK   3   BOND LENGTHS OTHERS               (A):  2228 ; 0.001 ; 0.017
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3279 ; 1.507 ; 1.642
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5120 ; 1.245 ; 1.576
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   300 ; 8.029 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   120 ;34.802 ;23.083
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   383 ;15.383 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;10.649 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   313 ; 0.059 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2770 ; 0.006 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   573 ; 0.001 ; 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   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK   4
REMARK   4 7O46 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-APR-21.
REMARK 100 THE DEPOSITION ID IS D_1292115090.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 23-FEB-21
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.75
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : MAX IV
REMARK 200  BEAMLINE                       : BIOMAX
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS B. 20200131
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.7.4
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13122
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.230
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.640
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7
REMARK 200  DATA REDUNDANCY                : 6.800
REMARK 200  R MERGE                    (I) : 0.05500
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.31
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00
REMARK 200  R MERGE FOR SHELL          (I) : 1.44300
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: PHASER 2.8.2
REMARK 200 STARTING MODEL: 7B5Z
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 38.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 NL PROTEIN (8.3 MG/ML, 50 MM TRIS
REMARK 280  PH 8.0, 300 MM NACL), 50 NL SEEDS, 450 NL RESERVOIR (200 MM
REMARK 280  HEPES PH 7.75, 5% DMSO, 12.5% PEG4K). SOAKING: 200 MM HEPES PH
REMARK 280  7.75, 6.25 MM COMPOUND, 5% DMSO, 10% PEG300, 20% PEG3K, RT, 2 H.,
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
REMARK 290       4555   -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       56.83300
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       27.03200
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       56.83300
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       27.03200
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH A 502  LIES ON A SPECIAL POSITION.
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     GLY A   302
REMARK 465     VAL A   303
REMARK 465     THR A   304
REMARK 465     PHE A   305
REMARK 465     GLN A   306
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    SER A   144     OG   SER A   147              2.14
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    LYS A   5       92.95    -67.17
REMARK 500    ASP A  33     -126.34     52.61
REMARK 500    HIS A  41        2.23    -68.68
REMARK 500    ASN A  51       80.23   -159.33
REMARK 500    ASN A  84     -113.13     42.57
REMARK 500    TYR A 154     -101.49     78.97
REMARK 500    THR A 225     -169.67   -165.98
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 V18 A 401
DBREF  7O46 A    1   306  UNP    P0DTD1   R1AB_SARS2    3264   3569
HET    V18  A 401      24
HETNAM     V18 2-CYCLOBUTYL-7-ISOQUINOLIN-4-YL-5,7-
HETNAM   2 V18  DIAZASPIRO[3.4]OCTANE-6,8-DIONE
FORMUL   2  V18    C19 H19 N3 O2
FORMUL   3  HOH   *2(H2 O)
CRYST1  113.666   54.064   44.931  90.00 101.47  90.00 C 1 2 1       4
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      0.008798  0.000000  0.001785        0.00000
SCALE2      0.000000  0.018497  0.000000        0.00000
SCALE3      0.000000  0.000000  0.022710        0.00000

> <__PDBSeqres__>
SEQRES   1 A  306  SER GLY PHE ARG LYS MET ALA PHE PRO SER GLY LYS VAL
SEQRES   2 A  306  GLU GLY CYS MET VAL GLN VAL THR CYS GLY THR THR THR
SEQRES   3 A  306  LEU ASN GLY LEU TRP LEU ASP ASP VAL VAL TYR CYS PRO
SEQRES   4 A  306  ARG HIS VAL ILE CYS THR SER GLU ASP MET LEU ASN PRO
SEQRES   5 A  306  ASN TYR GLU ASP LEU LEU ILE ARG LYS SER ASN HIS ASN
SEQRES   6 A  306  PHE LEU VAL GLN ALA GLY ASN VAL GLN LEU ARG VAL ILE
SEQRES   7 A  306  GLY HIS SER MET GLN ASN CYS VAL LEU LYS LEU LYS VAL
SEQRES   8 A  306  ASP THR ALA ASN PRO LYS THR PRO LYS TYR LYS PHE VAL
SEQRES   9 A  306  ARG ILE GLN PRO GLY GLN THR PHE SER VAL LEU ALA CYS
SEQRES  10 A  306  TYR ASN GLY SER PRO SER GLY VAL TYR GLN CYS ALA MET
SEQRES  11 A  306  ARG PRO ASN PHE THR ILE LYS GLY SER PHE LEU ASN GLY
SEQRES  12 A  306  SER CYS GLY SER VAL GLY PHE ASN ILE ASP TYR ASP CYS
SEQRES  13 A  306  VAL SER PHE CYS TYR MET HIS HIS MET GLU LEU PRO THR
SEQRES  14 A  306  GLY VAL HIS ALA GLY THR ASP LEU GLU GLY ASN PHE TYR
SEQRES  15 A  306  GLY PRO PHE VAL ASP ARG GLN THR ALA GLN ALA ALA GLY
SEQRES  16 A  306  THR ASP THR THR ILE THR VAL ASN VAL LEU ALA TRP LEU
SEQRES  17 A  306  TYR ALA ALA VAL ILE ASN GLY ASP ARG TRP PHE LEU ASN
SEQRES  18 A  306  ARG PHE THR THR THR LEU ASN ASP PHE ASN LEU VAL ALA
SEQRES  19 A  306  MET LYS TYR ASN TYR GLU PRO LEU THR GLN ASP HIS VAL
SEQRES  20 A  306  ASP ILE LEU GLY PRO LEU SER ALA GLN THR GLY ILE ALA
SEQRES  21 A  306  VAL LEU ASP MET CYS ALA SER LEU LYS GLU LEU LEU GLN
SEQRES  22 A  306  ASN GLY MET ASN GLY ARG THR ILE LEU GLY SER ALA LEU
SEQRES  23 A  306  LEU GLU ASP GLU PHE THR PRO PHE ASP VAL VAL ARG GLN
SEQRES  24 A  306  CYS SER GLY VAL THR PHE GLN

> <AssignOBJECTID>
1

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  7O46
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <pI>
6.62

> <At pH>
7.4

> <Net Charge>
-2.03

> <Protein Sequence>
SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTI
TVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCS

> <Secondary Structure>
CCCCCCCCCCHHHHTTSSSSSSTTCSSSSSSCTTSSSSSHHHHCCHHHCCCCCHHHHHHTCCHHHSSSSCTTCCCCSSSSSSCTTSSSSSSCCCCTTCCCSSSCCCCTTCSSSSSSSCTTCSSSSSSSSCCTTCCCCCCCCTTCTTCSSSSSCTTCSSSSSSSSSSCTTCCSSSSCTTCCCCCCCCCCCCCCCCCCCCCC
HHHHHHHHHHHHHTTCCTTCCCCCCCHHHHHHHHHHTTCCCCCHHHHHHTHHHHHHHTCCHHHHHHHHHHHHHHCCTTCCCTTCCCCCCCCCHHHHHHHHH

> <PDB Secondary Structure>
CCCCCCCCCHHHHHHCSSSSSSCCSSSSSSSSCCSSSSSCHHHHHHHHHCCCHHHHHHHHHHHHCSSSSSCCSSCCSSSSSSSCCSSSSSSCCCCCCCCSSSSCCCCCCCCSSSSSSSCCSSSSSSSSCCCCCCCCCCCCCCCCCCCSSSSSSCCSSSSSSSSSSSCCCCCSSSSCCCCCCCCCCCCCCCCCCCCCCCCH
HHHHHHHHHHHHHHCCCCCCCCCCCHHHHHHHHHHHHCCCCCHHHHHHHHHHHHHHHHCHHHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCHHHHHHHHHH

> <SEQRES>
SEQRES   1 A  306  SER GLY PHE ARG LYS MET ALA PHE PRO SER GLY LYS VAL
SEQRES   2 A  306  GLU GLY CYS MET VAL GLN VAL THR CYS GLY THR THR THR
SEQRES   3 A  306  LEU ASN GLY LEU TRP LEU ASP ASP VAL VAL TYR CYS PRO
SEQRES   4 A  306  ARG HIS VAL ILE CYS THR SER GLU ASP MET LEU ASN PRO
SEQRES   5 A  306  ASN TYR GLU ASP LEU LEU ILE ARG LYS SER ASN HIS ASN
SEQRES   6 A  306  PHE LEU VAL GLN ALA GLY ASN VAL GLN LEU ARG VAL ILE
SEQRES   7 A  306  GLY HIS SER MET GLN ASN CYS VAL LEU LYS LEU LYS VAL
SEQRES   8 A  306  ASP THR ALA ASN PRO LYS THR PRO LYS TYR LYS PHE VAL
SEQRES   9 A  306  ARG ILE GLN PRO GLY GLN THR PHE SER VAL LEU ALA CYS
SEQRES  10 A  306  TYR ASN GLY SER PRO SER GLY VAL TYR GLN CYS ALA MET
SEQRES  11 A  306  ARG PRO ASN PHE THR ILE LYS GLY SER PHE LEU ASN GLY
SEQRES  12 A  306  SER CYS GLY SER VAL GLY PHE ASN ILE ASP TYR ASP CYS
SEQRES  13 A  306  VAL SER PHE CYS TYR MET HIS HIS MET GLU LEU PRO THR
SEQRES  14 A  306  GLY VAL HIS ALA GLY THR ASP LEU GLU GLY ASN PHE TYR
SEQRES  15 A  306  GLY PRO PHE VAL ASP ARG GLN THR ALA GLN ALA ALA GLY
SEQRES  16 A  306  THR ASP THR THR ILE THR VAL ASN VAL LEU ALA TRP LEU
SEQRES  17 A  306  TYR ALA ALA VAL ILE ASN GLY ASP ARG TRP PHE LEU ASN
SEQRES  18 A  306  ARG PHE THR THR THR LEU ASN ASP PHE ASN LEU VAL ALA
SEQRES  19 A  306  MET LYS TYR ASN TYR GLU PRO LEU THR GLN ASP HIS VAL
SEQRES  20 A  306  ASP ILE LEU GLY PRO LEU SER ALA GLN THR GLY ILE ALA
SEQRES  21 A  306  VAL LEU ASP MET CYS ALA SER LEU LYS GLU LEU LEU GLN
SEQRES  22 A  306  ASN GLY MET ASN GLY ARG THR ILE LEU GLY SER ALA LEU
SEQRES  23 A  306  LEU GLU ASP GLU PHE THR PRO PHE ASP VAL VAL ARG GLN
SEQRES  24 A  306  CYS SER GLY VAL THR PHE GLN

> <RMSD_CA_7B2U>
0.310613

$$$$
