7B5Z_6
  DSViewer          3D                             0

 35 37  0  0  0  0  0  0  0  0999 V2000
   37.1355   -2.0001   44.3723 C   0  0
   36.4181    0.7332   44.9094 C   0  0
   35.9016   -1.4846   42.2941 C   0  0
   35.4775   -0.4797   41.2360 C   0  0
   36.4160   -2.0628   38.5851 C   0  0
   33.9854   -2.1482   38.4252 C   0  0
   34.0450   -2.8707   37.2249 C   0  0
   35.2896   -3.1689   36.7489 C   0  0
   36.4549   -2.7764   37.4145 C   0  0
   35.1421   -1.7476   39.0659 C   0  0
   36.9943    0.3122   43.5779 C   0  0
   36.6379   -1.0843   43.3430 N   0  0
   34.7028   -1.1190   40.1915 N   0  0
   36.6238   -1.6002   45.7452 C   0  0
   33.3413   -1.0625   40.2007 N   0  0
   37.6338    0.2995   47.0414 C   0  0
   36.9271   -0.1508   46.0091 C   0  0
   32.9032   -1.7187   39.1616 N   0  0
   35.6067   -2.6562   42.1445 O   0  0
   38.2255   -1.9813   44.3639 H   0  0
   36.8433   -3.0315   44.1635 H   0  0
   35.3279    0.7252   44.8953 H   0  0
   36.7441    1.7436   45.1178 H   0  0
   36.3503    0.0190   40.8130 H   0  0
   34.8609    0.2723   41.7274 H   0  0
   37.3136   -1.7791   39.1132 H   0  0
   33.1598   -3.2566   36.7420 H   0  0
   35.3595   -3.7990   35.8717 H   0  0
   37.4112   -3.0848   37.0168 H   0  0
   38.0787    0.3968   43.5797 H   0  0
   36.6423    0.9908   42.8038 H   0  0
   37.0832   -2.2317   46.5042 H   0  0
   35.5479   -1.7638   45.8090 H   0  0
   37.8416    1.3461   47.1780 H   0  0
   38.0299   -0.3601   47.7901 H   0  0
  1 12  1  0  0  0
  1 14  1  0  0  0
  1 20  1  0  0  0
  1 21  1  0  0  0
  2 11  1  0  0  0
  2 17  1  0  0  0
  2 22  1  0  0  0
  2 23  1  0  0  0
  3  4  1  0  0  0
  3 12  1  0  0  0
  3 19  2  0  0  0
  4 13  1  0  0  0
  4 24  1  0  0  0
  4 25  1  0  0  0
  5  9  2  0  0  0
  5 10  1  0  0  0
  5 26  1  0  0  0
  6  7  1  0  0  0
  6 10  2  0  0  0
  6 18  1  0  0  0
  7  8  2  0  0  0
  7 27  1  0  0  0
  8  9  1  0  0  0
  8 28  1  0  0  0
  9 29  1  0  0  0
 10 13  1  0  0  0
 11 12  1  0  0  0
 11 30  1  0  0  0
 11 31  1  0  0  0
 13 15  1  0  0  0
 14 17  1  0  0  0
 14 32  1  0  0  0
 14 33  1  0  0  0
 15 18  2  0  0  0
 16 17  2  0  0  0
 16 34  1  0  0  0
 16 35  1  0  0  0
M  END
> <Resolution>
1.65

> <__PDBRemarks__>
HEADER    VIRAL PROTEIN                           07-DEC-20   7B5Z
TITLE     CRYSTAL STRUCTURE OF SARS-COV-2 MAIN PROTEASE (NSP5) IN COMPLEX WITH
TITLE    2 COMPOUND 6
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 7B5Z    1       JRNL
REVDAT   1   23-FEB-22 7B5Z    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.    1.65 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN
REMARK   3
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.43
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.370
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5
REMARK   3   NUMBER OF REFLECTIONS             : 31551
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : FREE R-VALUE
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.157
REMARK   3   R VALUE            (WORKING SET) : 0.155
REMARK   3   FREE R VALUE                     : 0.196
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.770
REMARK   3   FREE R VALUE TEST SET COUNT      : 1504
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) : 1.65
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.70
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2646
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.46
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1620
REMARK   3   BIN FREE R VALUE SET COUNT          : 128
REMARK   3   BIN FREE R VALUE                    : 0.2230
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2358
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 43
REMARK   3   SOLVENT ATOMS            : 266
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 17.65
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.25
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.132
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
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  : 1
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     1        A   766
REMARK   3    ORIGIN FOR THE GROUP (A):  12.4741   1.7132   4.4946
REMARK   3    T TENSOR
REMARK   3      T11:   0.1148 T22:   0.1252
REMARK   3      T33:   0.1179 T12:  -0.0063
REMARK   3      T13:   0.0017 T23:  -0.0095
REMARK   3    L TENSOR
REMARK   3      L11:   0.2756 L22:   0.5381
REMARK   3      L33:   0.4002 L12:  -0.0189
REMARK   3      L13:   0.0331 L23:  -0.3036
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0120 S12:   0.0060 S13:  -0.0143
REMARK   3      S21:   0.0057 S22:   0.0317 S23:  -0.0086
REMARK   3      S31:   0.0015 S32:  -0.0253 S33:   0.0000
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : FLAT BULK SOLVENT MODEL
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.11
REMARK   3   ION PROBE RADIUS   : NULL
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 7B5Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-DEC-20.
REMARK 100 THE DEPOSITION ID IS D_1292112722.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 12-NOV-20
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   : 31557
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.430
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6
REMARK 200  DATA REDUNDANCY                : 6.500
REMARK 200  R MERGE                    (I) : 0.05800
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.68
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.33500
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.200
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: 7B2J
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 38.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
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, 12.5 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       57.22850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.82800
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       57.22850
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       26.82800
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: 5080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 700  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     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    HOH A   678     O    HOH A   706              2.16
REMARK 500   O    HOH A   514     O    HOH A   570              2.17
REMARK 500   O    HOH A   720     O    HOH A   726              2.18
REMARK 500
REMARK 500 REMARK: NULL
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    LEU A  27   CB  -  CG  -  CD1 ANGL. DEV. =  12.4 DEGREES
REMARK 500    LEU A  27   CB  -  CG  -  CD2 ANGL. DEV. = -15.2 DEGREES
REMARK 500    MET A  82   CG  -  SD  -  CE  ANGL. DEV. =  10.9 DEGREES
REMARK 500    ASP A 187   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES
REMARK 500    ARG A 217   CG  -  CD  -  NE  ANGL. DEV. = -34.8 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    ASP A  33     -136.57     53.20
REMARK 500    ASN A  51       77.69   -161.35
REMARK 500    ASN A  84     -126.75     54.22
REMARK 500    TYR A 154     -106.77     61.31
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 765        DISTANCE =  6.00 ANGSTROMS
REMARK 525    HOH A 766        DISTANCE =  6.03 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SYH A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 407
DBREF  7B5Z A    1   306  UNP    P0DTD1   R1AB_SARS2    3264   3569
HET    DMS  A 401       4
HET    DMS  A 402       4
HET    DMS  A 403       4
HET    DMS  A 404       4
HET    SYH  A 405      19
HET    DMS  A 406       4
HET    DMS  A 407       4
HETNAM     DMS DIMETHYL SULFOXIDE
HETNAM     SYH 2-(1H-BENZO[D][1,2,3]TRIAZOL-1-YL)-1-(4-
HETNAM   2 SYH  METHYLENEPIPERIDIN-1-YL)ETHAN-1-ONE
HETSYN     SYH 2-(1H-1,2,3-BENZOTRIAZOL-1-YL)-1-(4-
HETSYN   2 SYH  METHYLIDENEPIPERIDIN-1-YL)ETHAN-1-ONE; 2-
HETSYN   3 SYH  (BENZOTRIAZOL-1-YL)-1-(4-METHYLIDENEPIPERIDIN-1-YL)
HETSYN   4 SYH  ETHANONE
FORMUL   2  DMS    6(C2 H6 O S)
FORMUL   6  SYH    C14 H16 N4 O
FORMUL   9  HOH   *266(H2 O)
CRYST1  114.457   53.656   44.476  90.00 100.51  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      0.008737  0.000000  0.001621        0.00000
SCALE2      0.000000  0.018637  0.000000        0.00000
SCALE3      0.000000  0.000000  0.022868        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  7B5Z
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <pI>
6.69

> <At pH>
7.4

> <Net Charge>
-1.86

> <Protein Sequence>
SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTI
TVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTF

> <Secondary Structure>
CCCCCCCCCCHHHHTTSSSSSSTTCSSSSSSCTTSSSSSHHHHCCHHHTTCCCHHHHHHTCCHHHSSSSCTTCSSCSSSSSSCTTSSSSSSCCCCTTCCCSSSCCCCCCSSSSSSSSCTTCSSSSSSSSSCTTCCCCCCCCTTCTTCSSSSSCTTCSSSSSSSSSSCTTCCSSSSCTTCCCCCCCCCCCCCCCCCCCCCC
HHHHHHHHHHHHHHTCCTTCCCCCCCHHHHHHHHHHTTCCCCCHHHHHHTHHHHHHHTCCHHHHHHHHTHHHHHCCTTCCCCCCCCCCCCCCHHHHHHHHHTCCC

> <PDB Secondary Structure>
CCCCCCCCCHHHHHHCSSSSSSCCSSSSSSSSCCSSSSSCHHHHHHHHHCCCHHHHHHHHHHHHCSSSSSCCSSSCSSSSSSSCCSSSSSSCCCCCCCCSSSSCCCCCCCCSSSSSSSCCSSSSSSSSCCCCCCCCCCCCCCCCCCCSSSSSSCCSSSSSSSSSSSCCCCCSSSSCCCCCCCCCCCCCCCCCCCCCCCCH
HHHHHHHHHHHHHHHCCCCCCCCCCHHHHHHHHHHHHCCCCCHHHHHHHHHHHHHHHHCHHHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCHHHHHHHHHHHCCC

> <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>
0.175429

$$$$
