longtext: 6ojc-pdb

content
HEADER    HYDROLASE                               11-APR-19   6OJC
TITLE     A HIGH-RESOLUTION CRYSTAL STRUCTURE OF NOCB THIOESTERASE DOMAIN FROM
TITLE    2 NOCARDICIN CLUSTER
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: NOCB;
COMPND   3 CHAIN: A;
COMPND   4 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: NOCARDIA UNIFORMIS SUBSP. TSUYAMANENSIS;
SOURCE   3 ORGANISM_TAXID: 96045;
SOURCE   4 GENE: NOCB;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS    NONRIBOSOMAL PEPTIDE SYNTHETASE (NRPS), THIOESTERASE, EPIMERIZATION,
KEYWDS   2 ALPHA/BETA HYDROLASE FOLD, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.D.PATEL,A.M.GULICK
REVDAT   1   11-SEP-19 6OJC    0
JRNL        AUTH   K.D.PATEL,F.B.D'ANDREA,N.M.GAUDELLI,A.R.BULLER,C.A.TOWNSEND,
JRNL        AUTH 2 A.M.GULICK
JRNL        TITL   STRUCTURE OF A BOUND PEPTIDE PHOSPHONATE REVEALS THE
JRNL        TITL 2 MECHANISM OF NOCARDICIN BIFUNCTIONAL THIOESTERASE
JRNL        TITL 3 EPIMERASE-HYDROLASE HALF-REACTIONS.
JRNL        REF    NAT COMMUN                    V.  10  3868 2019
JRNL        REFN                   ESSN 2041-1723
JRNL        PMID   31455765
JRNL        DOI    10.1038/S41467-019-11740-6
REMARK   2
REMARK   2 RESOLUTION.    1.94 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (1.13_2998: ???)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.94
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.24
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.240
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7
REMARK   3   NUMBER OF REFLECTIONS             : 26292
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.208
REMARK   3   R VALUE            (WORKING SET) : 0.207
REMARK   3   FREE R VALUE                     : 0.230
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.940
REMARK   3   FREE R VALUE TEST SET COUNT      : 1561
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 29.2443 -  4.3103    0.99     2349   153  0.1903 0.1980
REMARK   3     2  4.3103 -  3.4230    1.00     2265   144  0.1835 0.2103
REMARK   3     3  3.4230 -  2.9908    1.00     2272   142  0.2129 0.2182
REMARK   3     4  2.9908 -  2.7175    1.00     2243   139  0.2228 0.2950
REMARK   3     5  2.7175 -  2.5229    1.00     2244   138  0.2240 0.2633
REMARK   3     6  2.5229 -  2.3742    1.00     2248   140  0.2274 0.2402
REMARK   3     7  2.3742 -  2.2553    1.00     2222   141  0.2277 0.2663
REMARK   3     8  2.2553 -  2.1572    0.99     2216   140  0.2457 0.2826
REMARK   3     9  2.1572 -  2.0742    1.00     2239   143  0.2240 0.2730
REMARK   3    10  2.0742 -  2.0026    1.00     2226   143  0.2398 0.2776
REMARK   3    11  2.0026 -  1.9400    1.00     2207   138  0.2956 0.3241
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : NULL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : NULL
REMARK   3   B_SOL              : NULL
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.240
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.260
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 40.76
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.017           1725
REMARK   3   ANGLE     :  1.539           2366
REMARK   3   CHIRALITY :  0.083            263
REMARK   3   PLANARITY :  0.011            312
REMARK   3   DIHEDRAL  : 14.430           1003
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 1
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: ALL
REMARK   3    ORIGIN FOR THE GROUP (A): -44.7209  14.2554  14.8500
REMARK   3    T TENSOR
REMARK   3      T11:   0.2832 T22:   0.2457
REMARK   3      T33:   0.2781 T12:   0.0355
REMARK   3      T13:   0.0174 T23:  -0.0526
REMARK   3    L TENSOR
REMARK   3      L11:   3.0331 L22:   5.1849
REMARK   3      L33:   3.3151 L12:  -1.1812
REMARK   3      L13:   0.5937 L23:  -1.2396
REMARK   3    S TENSOR
REMARK   3      S11:   0.1546 S12:   0.2319 S13:   0.1055
REMARK   3      S21:  -0.3060 S22:  -0.1388 S23:   0.1067
REMARK   3      S31:   0.0024 S32:  -0.0612 S33:  -0.0135
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 6OJC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-19.
REMARK 100 THE DEPOSITION ID IS D_1000240785.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 21-MAR-18
REMARK 200  TEMPERATURE           (KELVIN) : 113.15
REMARK 200  PH                             : 5.0-6.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 23-ID-D
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03321
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26388
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.790
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.370
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7
REMARK 200  DATA REDUNDANCY                : 9.400
REMARK 200  R MERGE                    (I) : 0.04700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 25.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.30
REMARK 200  R MERGE FOR SHELL          (I) : 1.54000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: OCTAHEDRAL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 61.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0M AMMONIUM SULFATE, 0.05M BISTRIS
REMARK 280  PH 5.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z
REMARK 290       3555   -X+Y,-X,Z
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z
REMARK 290       6555   -X,-X+Y,-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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  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: 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 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 S    SO4 A2001  LIES ON A SPECIAL POSITION.
REMARK 375 O1   SO4 A2001  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A2191  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     MET A  1669
REMARK 465     GLY A  1670
REMARK 465     SER A  1671
REMARK 465     SER A  1672
REMARK 465     HIS A  1673
REMARK 465     HIS A  1674
REMARK 465     HIS A  1675
REMARK 465     HIS A  1676
REMARK 465     HIS A  1677
REMARK 465     HIS A  1678
REMARK 465     SER A  1679
REMARK 465     SER A  1680
REMARK 465     GLY A  1681
REMARK 465     LEU A  1682
REMARK 465     VAL A  1683
REMARK 465     PRO A  1684
REMARK 465     ARG A  1685
REMARK 465     GLY A  1686
REMARK 465     SER A  1687
REMARK 465     HIS A  1688
REMARK 465     MET A  1689
REMARK 465     VAL A  1690
REMARK 465     GLU A  1691
REMARK 465     GLY A  1692
REMARK 465     SER A  1693
REMARK 465     GLY A  1694
REMARK 465     ARG A  1815
REMARK 465     THR A  1816
REMARK 465     GLY A  1817
REMARK 465     ASP A  1818
REMARK 465     PRO A  1819
REMARK 465     ARG A  1820
REMARK 465     GLU A  1821
REMARK 465     GLU A  1924
REMARK 465     ARG A  1925
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     VAL A1823    CG1  CG2
REMARK 470     ARG A1826    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU A1830    CG   CD1  CD2
REMARK 470     GLU A1838    CG   CD   OE1  OE2
REMARK 470     ASP A1873    CG   OD1  OD2
REMARK 470     ASP A1875    CG   OD1  OD2
REMARK 470     GLU A1895    CG   CD   OE1  OE2
REMARK 470     ARG A1903    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A1907    CG   CD   OE1  OE2
REMARK 470     GLU A1908    CG   CD   OE1  OE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     ASP A 1747   OD1  OD2
REMARK 480     ARG A 1759   NE   CZ   NH1  NH2
REMARK 480     GLU A 1770   CG   CD   OE1  OE2
REMARK 480     GLU A 1798   CG   OE1
REMARK 480     GLU A 1829   CG   CD   OE1  OE2
REMARK 480     VAL A 1840   CG1
REMARK 480     GLU A 1844   CG   OE2
REMARK 480     HIS A 1848   ND1
REMARK 480     ARG A 1862   NE   CZ   NH1  NH2
REMARK 480     ARG A 1876   CD   NE   CZ   NH1  NH2
REMARK 480     GLU A 1902   CG   OE2
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  2162     O    HOH A  2164              2.09
REMARK 500   O    LEU A  1846     O    HOH A  2101              2.15
REMARK 500   NH1  ARG A  1759     OE1  GLU A  1762              2.16
REMARK 500   O    THR A  1870     O    HOH A  2102              2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH A  2174     O    HOH A  2174     5555     1.93
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    ARG A1765   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 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    SER A1779     -118.54     49.01
REMARK 500    ALA A1812      -63.79    -97.99
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 SO4 A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 2007
DBREF  6OJC A 1690  1925  UNP    Q5J1Q6   Q5J1Q6_9NOCA  1690   1925
SEQADV 6OJC MET A 1669  UNP  Q5J1Q6              INITIATING METHIONINE
SEQADV 6OJC GLY A 1670  UNP  Q5J1Q6              EXPRESSION TAG
SEQADV 6OJC SER A 1671  UNP  Q5J1Q6              EXPRESSION TAG
SEQADV 6OJC SER A 1672  UNP  Q5J1Q6              EXPRESSION TAG
SEQADV 6OJC HIS A 1673  UNP  Q5J1Q6              EXPRESSION TAG
SEQADV 6OJC HIS A 1674  UNP  Q5J1Q6              EXPRESSION TAG
SEQADV 6OJC HIS A 1675  UNP  Q5J1Q6              EXPRESSION TAG
SEQADV 6OJC HIS A 1676  UNP  Q5J1Q6              EXPRESSION TAG
SEQADV 6OJC HIS A 1677  UNP  Q5J1Q6              EXPRESSION TAG
SEQADV 6OJC HIS A 1678  UNP  Q5J1Q6              EXPRESSION TAG
SEQADV 6OJC SER A 1679  UNP  Q5J1Q6              EXPRESSION TAG
SEQADV 6OJC SER A 1680  UNP  Q5J1Q6              EXPRESSION TAG
SEQADV 6OJC GLY A 1681  UNP  Q5J1Q6              EXPRESSION TAG
SEQADV 6OJC LEU A 1682  UNP  Q5J1Q6              EXPRESSION TAG
SEQADV 6OJC VAL A 1683  UNP  Q5J1Q6              EXPRESSION TAG
SEQADV 6OJC PRO A 1684  UNP  Q5J1Q6              EXPRESSION TAG
SEQADV 6OJC ARG A 1685  UNP  Q5J1Q6              EXPRESSION TAG
SEQADV 6OJC GLY A 1686  UNP  Q5J1Q6              EXPRESSION TAG
SEQADV 6OJC SER A 1687  UNP  Q5J1Q6              EXPRESSION TAG
SEQADV 6OJC HIS A 1688  UNP  Q5J1Q6              EXPRESSION TAG
SEQADV 6OJC MET A 1689  UNP  Q5J1Q6              EXPRESSION TAG
SEQRES   1 A  257  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 A  257  LEU VAL PRO ARG GLY SER HIS MET VAL GLU GLY SER GLY
SEQRES   3 A  257  SER ALA TYR VAL HIS THR LEU ASN PRO GLU ALA THR GLY
SEQRES   4 A  257  GLY ALA LEU VAL LEU VAL HIS PRO GLY GLU GLY LEU ALA
SEQRES   5 A  257  LEU PRO TYR HIS GLY LEU ALA PRO LEU LEU PRO ASP VAL
SEQRES   6 A  257  ARG LEU HIS VAL LEU SER ASP PRO ARG PHE GLY GLN SER
SEQRES   7 A  257  ASP ASN ARG PHE ALA THR LEU ALA GLU MET ALA THR ARG
SEQRES   8 A  257  TYR VAL GLU TRP VAL ARG THR THR GLU PRO GLU GLY PRO
SEQRES   9 A  257  TYR ARG LEU GLY GLY TRP SER PHE GLY GLY VAL VAL ALA
SEQRES  10 A  257  LEU GLU MET ALA SER GLN MET THR ALA HIS GLY ASP GLU
SEQRES  11 A  257  VAL SER ASP LEU LEU LEU VAL ASP SER HIS ASN LEU ASN
SEQRES  12 A  257  ALA ALA PRO ARG THR GLY ASP PRO ARG GLU GLY VAL ARG
SEQRES  13 A  257  GLN ARG LEU VAL GLU LEU GLY VAL ASP PRO ASP SER PRO
SEQRES  14 A  257  GLU GLY VAL ASP VAL VAL GLU GLU LEU LEU HIS ASN GLY
SEQRES  15 A  257  ALA LEU ALA ALA GLN TYR ALA PRO PRO ALA TYR ARG GLY
SEQRES  16 A  257  ARG VAL SER LEU LEU VAL THR PRO THR ASP GLY ASP ARG
SEQRES  17 A  257  ASP ALA VAL ARG ALA ARG GLY TRP ASP ARG ALA LEU LEU
SEQRES  18 A  257  PRO ASP LEU VAL VAL GLU PRO VAL PRO GLY ALA HIS GLU
SEQRES  19 A  257  ARG LEU PHE ASP GLU GLU HIS LEU SER ASP THR ALA ASP
SEQRES  20 A  257  ALA ILE ARG ARG ALA LEU GLY GLY GLU ARG
HET    SO4  A2001       5
HET    SO4  A2002       5
HET    SO4  A2003       5
HET    SO4  A2004       5
HET    SO4  A2005       5
HET    SO4  A2006       5
HET    GOL  A2007      13
HETNAM     SO4 SULFATE ION
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2  SO4    6(O4 S 2-)
FORMUL   8  GOL    C3 H8 O3
FORMUL   9  HOH   *91(H2 O)
HELIX    1 AA1 ALA A 1720  LEU A 1730  5                                  11
HELIX    2 AA2 THR A 1752  GLU A 1768  1                                  17
HELIX    3 AA3 SER A 1779  HIS A 1795  1                                  17
HELIX    4 AA4 VAL A 1823  GLY A 1831  1                                   9
HELIX    5 AA5 SER A 1836  TYR A 1856  1                                  21
HELIX    6 AA6 THR A 1872  ARG A 1876  5                                   5
HELIX    7 AA7 VAL A 1879  GLY A 1883  5                                   5
HELIX    8 AA8 ALA A 1900  LEU A 1904  5                                   5
HELIX    9 AA9 HIS A 1909  GLY A 1922  1                                  14
SHEET    1 AA1 7 VAL A1698  LEU A1701  0
SHEET    2 AA1 7 ARG A1734  LEU A1738 -1  O  LEU A1735   N  LEU A1701
SHEET    3 AA1 7 ALA A1709  VAL A1713  1  N  LEU A1712   O  LEU A1738
SHEET    4 AA1 7 TYR A1773  TRP A1778  1  O  GLY A1776   N  VAL A1713
SHEET    5 AA1 7 VAL A1799  VAL A1805  1  O  VAL A1805   N  GLY A1777
SHEET    6 AA1 7 VAL A1865  VAL A1869  1  O  SER A1866   N  LEU A1802
SHEET    7 AA1 7 LEU A1892  PRO A1896  1  O  GLU A1895   N  VAL A1869
CISPEP   1 GLY A 1771    PRO A 1772          0         0.85
SITE     1 AC1  1 ARG A1919
SITE     1 AC2  3 PRO A1741  ARG A1742  ARG A1759
SITE     1 AC3  4 GLY A1899  ALA A1900  HIS A1909  HOH A2111
SITE     1 AC4  5 SER A1800  ASP A1801  ARG A1864  LEU A1921
SITE     2 AC4  5 GLY A1923
SITE     1 AC5  3 HIS A1699  THR A1700  HOH A2104
SITE     1 AC6  3 ARG A1876  ASP A1877  ARG A1880
SITE     1 AC7  7 GLY A1716  SER A1779  PHE A1780  HIS A1808
SITE     2 AC7  7 HIS A1901  HOH A2105  HOH A2163
CRYST1  114.730  114.730   46.601  90.00  90.00 120.00 P 3 2 1       6
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      0.008716  0.005032  0.000000        0.00000
SCALE2      0.000000  0.010065  0.000000        0.00000
SCALE3      0.000000  0.000000  0.021459        0.00000
TER    3204      GLY A1923
MASTER      405    0    7    9    7    0    9    6 1774    1   43   20
END