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PDBsum entry 1ym3

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Lyase PDB id
1ym3
Jmol
Contents
Protein chain
193 a.a.
Metals
_MG
_ZN
Waters ×130
HEADER    LYASE                                   20-JAN-05   1YM3
TITLE     CRYSTAL STRUCTURE OF CARBONIC ANHYDRASE RV3588C FROM MYCOBACTERIUM
TITLE    2 TUBERCULOSIS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE (CARBONATE DEHYDRATASE) (CARBONIC
COMPND   3 DEHYDRATASE);
COMPND   4 CHAIN: A;
COMPND   5 EC: 4.2.1.1;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE   3 ORGANISM_TAXID: 83332;
SOURCE   4 STRAIN: H37RV;
SOURCE   5 GENE: RV3588C;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-AI;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCRT7
KEYWDS    ZN PROTEIN, STRUCTURAL PROTEOMICS IN EUROPE, SPINE, STRUCTURAL
KEYWDS   2 GENOMICS, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.S.COVARRUBIAS,A.M.LARSSON,M.HOGBOM,J.LINDBERG,T.BERGFORS,
AUTHOR   2 C.BJORKELID,S.L.MOWBRAY,T.UNGE,T.A.JONES,STRUCTURAL PROTEOMICS IN
AUTHOR   3 EUROPE (SPINE)
REVDAT   5   13-JUL-11 1YM3    1       VERSN
REVDAT   4   24-FEB-09 1YM3    1       VERSN
REVDAT   3   24-MAY-05 1YM3    1       JRNL
REVDAT   2   15-MAR-05 1YM3    1       EXPDTA
REVDAT   1   08-MAR-05 1YM3    0
JRNL        AUTH   A.SUAREZ COVARRUBIAS,A.M.LARSSON,M.HOGBOM,J.LINDBERG,
JRNL        AUTH 2 T.BERGFORS,C.BJORKELID,S.L.MOWBRAY,T.UNGE,T.A.JONES
JRNL        TITL   STRUCTURE AND FUNCTION OF CARBONIC ANHYDRASES FROM
JRNL        TITL 2 MYCOBACTERIUM TUBERCULOSIS.
JRNL        REF    J.BIOL.CHEM.                  V. 280 18782 2005
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   15753099
JRNL        DOI    10.1074/JBC.M414348200
REMARK   2
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.1.24
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.20
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 82.9
REMARK   3   NUMBER OF REFLECTIONS             : 13934
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) : 0.181
REMARK   3   R VALUE            (WORKING SET) : 0.179
REMARK   3   FREE R VALUE                     : 0.229
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 734
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) : 1.75
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.79
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 956
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1860
REMARK   3   BIN FREE R VALUE SET COUNT          : 59
REMARK   3   BIN FREE R VALUE                    : 0.2380
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1435
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 130
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.21
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.36000
REMARK   3    B22 (A**2) : 0.36000
REMARK   3    B33 (A**2) : -0.71000
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): 0.154
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.146
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.085
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.595
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1468 ; 0.016 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  1385 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1994 ; 1.484 ; 1.946
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3186 ; 0.874 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   193 ; 5.556 ; 5.000
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):   234 ; 0.090 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1678 ; 0.008 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   300 ; 0.009 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   288 ; 0.208 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1551 ; 0.229 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):   828 ; 0.080 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    69 ; 0.184 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.007 ; 0.200
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    20 ; 0.619 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    66 ; 0.322 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    18 ; 0.176 ; 0.200
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):   956 ; 0.980 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1532 ; 1.753 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   512 ; 2.682 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   462 ; 4.272 ; 4.500
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     4        A   206
REMARK   3    ORIGIN FOR THE GROUP (A):  20.0998  22.5969  21.0858
REMARK   3    T TENSOR
REMARK   3      T11:   0.0381 T22:   0.0095
REMARK   3      T33:   0.0326 T12:  -0.0001
REMARK   3      T13:  -0.0093 T23:  -0.0022
REMARK   3    L TENSOR
REMARK   3      L11:   0.5139 L22:   0.8383
REMARK   3      L33:   0.9139 L12:   0.1853
REMARK   3      L13:   0.1750 L23:   0.3555
REMARK   3    S TENSOR
REMARK   3      S11:   0.0211 S12:  -0.0526 S13:  -0.0233
REMARK   3      S21:  -0.0872 S22:  -0.0219 S23:   0.0198
REMARK   3      S31:   0.0856 S32:  -0.0211 S33:   0.0009
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
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
REMARK   4
REMARK   4 1YM3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-05.
REMARK 100 THE RCSB ID CODE IS RCSB031674.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 02-MAY-04
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : MAX II
REMARK 200  BEAMLINE                       : I711
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.085
REMARK 200  MONOCHROMATOR                  : SINGLE ASYMMETRICALLY CUT
REMARK 200                                   SI(111) CRYSTAL WITH HORIZONTAL
REMARK 200                                   DIFFRACTION PLANE. THE CRYSTAL IS
REMARK 200                                   BENDABLE FOR HORIZONTAL FOCUSING.
REMARK 200  OPTICS                         : VERTICALLY FOCUSING CYLINDRICAL
REMARK 200                                   MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13934
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.200
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 83.3
REMARK 200  DATA REDUNDANCY                : 4.700
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.04400
REMARK 200   FOR THE DATA SET  : 23.3500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.29800
REMARK 200   FOR SHELL         : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1I6O AND 1DDZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 34.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MGCL2, PEG 400, HEPES, PH 7.0, VAPOR
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z+1/2
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       52.09600
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       28.18850
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       28.18850
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       26.04800
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       28.18850
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       28.18850
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       78.14400
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       28.18850
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       28.18850
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       26.04800
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       28.18850
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       28.18850
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       78.14400
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       52.09600
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 300 REMARK: THE SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED
REMARK 300 BY THE TWO FOLD AXIS: -Y, -X, 1/2-Z
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 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  0.000000 -1.000000  0.000000       56.37700
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000       56.37700
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       52.09600
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 313  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    -7
REMARK 465     ALA A    -6
REMARK 465     HIS A    -5
REMARK 465     HIS A    -4
REMARK 465     HIS A    -3
REMARK 465     HIS A    -2
REMARK 465     HIS A    -1
REMARK 465     HIS A     0
REMARK 465     GLY A     1
REMARK 465     PRO A     2
REMARK 465     ASN A     3
REMARK 465     VAL A    32
REMARK 465     ASP A    33
REMARK 465     HIS A    34
REMARK 465     ARG A    35
REMARK 465     ALA A    36
REMARK 465     GLY A    37
REMARK 465     LEU A    38
REMARK 465     ALA A    39
REMARK 465     ALA A    40
REMARK 465     GLY A    41
REMARK 465     VAL A   207
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   OE1  GLU A   173     O    HOH A   399              2.06
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   OD1  ASP A    80     OD2  ASP A    80     8665     1.49
REMARK 500   CG   ASP A    80     OD1  ASP A    80     8665     2.01
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 A 147       -8.26   -143.79
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 352        DISTANCE =  5.51 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 301  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 104   NE2
REMARK 620 2 CYS A  51   SG  119.1
REMARK 620 3 ASP A  53   OD1  90.8  98.7
REMARK 620 4 CYS A 107   SG  111.5 112.1 123.2
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 302  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 199   O
REMARK 620 2 HOH A 305   O    93.1
REMARK 620 3 HIS A 199   ND1  82.9 174.8
REMARK 620 4 HOH A 307   O   172.7  87.7  96.6
REMARK 620 5 HOH A 315   O    94.7  85.2  91.8  92.6
REMARK 620 6 HOH A 303   O    82.9  96.2  86.6  89.8 177.3
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: RV3588   RELATED DB: TARGETDB
DBREF  1YM3 A    2   207  UNP    O53573   O53573_MYCTU     2    207
SEQADV 1YM3 MET A   -7  UNP  O53573              CLONING ARTIFACT
SEQADV 1YM3 ALA A   -6  UNP  O53573              CLONING ARTIFACT
SEQADV 1YM3 HIS A   -5  UNP  O53573              CLONING ARTIFACT
SEQADV 1YM3 HIS A   -4  UNP  O53573              CLONING ARTIFACT
SEQADV 1YM3 HIS A   -3  UNP  O53573              CLONING ARTIFACT
SEQADV 1YM3 HIS A   -2  UNP  O53573              CLONING ARTIFACT
SEQADV 1YM3 HIS A   -1  UNP  O53573              CLONING ARTIFACT
SEQADV 1YM3 HIS A    0  UNP  O53573              CLONING ARTIFACT
SEQADV 1YM3 GLY A    1  UNP  O53573              CLONING ARTIFACT
SEQRES   1 A  215  MET ALA HIS HIS HIS HIS HIS HIS GLY PRO ASN THR ASN
SEQRES   2 A  215  PRO VAL ALA ALA TRP LYS ALA LEU LYS GLU GLY ASN GLU
SEQRES   3 A  215  ARG PHE VAL ALA GLY ARG PRO GLN HIS PRO SER GLN SER
SEQRES   4 A  215  VAL ASP HIS ARG ALA GLY LEU ALA ALA GLY GLN LYS PRO
SEQRES   5 A  215  THR ALA VAL ILE PHE GLY CYS ALA ASP SER ARG VAL ALA
SEQRES   6 A  215  ALA GLU ILE ILE PHE ASP GLN GLY LEU GLY ASP MET PHE
SEQRES   7 A  215  VAL VAL ARG THR ALA GLY HIS VAL ILE ASP SER ALA VAL
SEQRES   8 A  215  LEU GLY SER ILE GLU TYR ALA VAL THR VAL LEU ASN VAL
SEQRES   9 A  215  PRO LEU ILE VAL VAL LEU GLY HIS ASP SER CYS GLY ALA
SEQRES  10 A  215  VAL ASN ALA ALA LEU ALA ALA ILE ASN ASP GLY THR LEU
SEQRES  11 A  215  PRO GLY GLY TYR VAL ARG ASP VAL VAL GLU ARG VAL ALA
SEQRES  12 A  215  PRO SER VAL LEU LEU GLY ARG ARG ASP GLY LEU SER ARG
SEQRES  13 A  215  VAL ASP GLU PHE GLU GLN ARG HIS VAL HIS GLU THR VAL
SEQRES  14 A  215  ALA ILE LEU MET ALA ARG SER SER ALA ILE SER GLU ARG
SEQRES  15 A  215  ILE ALA GLY GLY SER LEU ALA ILE VAL GLY VAL THR TYR
SEQRES  16 A  215  GLN LEU ASP ASP GLY ARG ALA VAL LEU ARG ASP HIS ILE
SEQRES  17 A  215  GLY ASN ILE GLY GLU GLU VAL
HET     ZN  A 301       1
HET     MG  A 302       1
HETNAM      ZN ZINC ION
HETNAM      MG MAGNESIUM ION
FORMUL   2   ZN    ZN 2+
FORMUL   3   MG    MG 2+
FORMUL   4  HOH   *130(H2 O)
HELIX    1   1 ASN A    5  GLY A   23  1                                  19
HELIX    2   2 HIS A   27  SER A   31  5                                   5
HELIX    3   3 ALA A   57  PHE A   62  1                                   6
HELIX    4   4 ALA A   75  VAL A   78  5                                   4
HELIX    5   5 ASP A   80  VAL A   93  1                                  14
HELIX    6   6 CYS A  107  GLY A  120  1                                  14
HELIX    7   7 TYR A  126  ASP A  144  1                                  19
HELIX    8   8 ARG A  148  SER A  168  1                                  21
HELIX    9   9 SER A  168  GLY A  177  1                                  10
SHEET    1   A 5 MET A  69  THR A  74  0
SHEET    2   A 5 ALA A  46  CYS A  51  1  N  ILE A  48   O  VAL A  72
SHEET    3   A 5 LEU A  98  HIS A 104  1  O  VAL A 100   N  PHE A  49
SHEET    4   A 5 ALA A 181  TYR A 187  1  O  VAL A 185   N  GLY A 103
SHEET    5   A 5 VAL A 195  ILE A 200 -1  O  VAL A 195   N  THR A 186
LINK        ZN    ZN A 301                 NE2 HIS A 104     1555   1555  2.05
LINK        ZN    ZN A 301                 SG  CYS A  51     1555   1555  2.37
LINK        ZN    ZN A 301                 OD1 ASP A  53     1555   1555  2.10
LINK        ZN    ZN A 301                 SG  CYS A 107     1555   1555  2.30
LINK        MG    MG A 302                 O   HIS A 199     1555   1555  2.04
LINK        MG    MG A 302                 O   HOH A 305     1555   1555  2.05
LINK        MG    MG A 302                 ND1 HIS A 199     1555   1555  2.27
LINK        MG    MG A 302                 O   HOH A 307     1555   1555  2.08
LINK        MG    MG A 302                 O   HOH A 315     1555   1555  2.13
LINK        MG    MG A 302                 O   HOH A 303     1555   1555  2.07
SITE     1 AC1  4 CYS A  51  ASP A  53  HIS A 104  CYS A 107
SITE     1 AC2  5 HIS A 199  HOH A 303  HOH A 305  HOH A 307
SITE     2 AC2  5 HOH A 315
CRYST1   56.377   56.377  104.192  90.00  90.00  90.00 P 41 21 2     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      0.017738  0.000000  0.000000        0.00000
SCALE2      0.000000  0.017738  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009598        0.00000
      
PROCHECK
Go to PROCHECK summary
 References