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PDBsum entry 3s0z

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Top Page protein metals Protein-protein interface(s) links
Hydrolase PDB id
3s0z
Jmol
Contents
Protein chains
220 a.a.
Metals
_ZN ×4
Waters ×226
HEADER    HYDROLASE                               13-MAY-11   3S0Z
TITLE     CRYSTAL STRUCTURE OF NEW DELHI METALLO-BETA-LACTAMASE (NDM-1)
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: METALLO-BETA-LACTAMASE;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: UNP RESIDUES 47-270;
COMPND   5 SYNONYM: NEW DELHI METALLO-BETA-LACTAMASE, NDM-1;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 ORGANISM_TAXID: 562;
SOURCE   4 GENE: BLANDM-1;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    NEW DELHI METALLO-BETA-LACTAMASE 1, NDM-1, DRUG RESISTANT, DRUG
KEYWDS   2 DISCOVERY, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.GUO,J.WANG,G.J.NIU,W.Q.SHUI,Y.N.SUN,Z.Y.LOU,Z.H.RAO
REVDAT   2   15-JUN-11 3S0Z    1       JRNL
REVDAT   1   01-JUN-11 3S0Z    0
JRNL        AUTH   Y.GUO,J.WANG,G.NIU,W.SHUI,Y.SUN,H.ZHOU,Y.ZHANG,C.YANG,Z.LOU,
JRNL        AUTH 2 Z.RAO
JRNL        TITL   A STRUCTURAL VIEW OF THE ANTIBIOTIC DEGRADATION ENZYME NDM-1
JRNL        TITL 2 FROM A SUPERBUG.
JRNL        REF    PROTEIN CELL                               2011
JRNL        REFN                   ESSN 1674-8018
JRNL        PMID   21637961
JRNL        DOI    10.1007/S13238-011-1055-9
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0110
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) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 70.9
REMARK   3   NUMBER OF REFLECTIONS             : 9265
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) : 0.236
REMARK   3   R VALUE            (WORKING SET) : 0.234
REMARK   3   FREE R VALUE                     : 0.267
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 502
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) : 2.50
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 828
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.11
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2170
REMARK   3   BIN FREE R VALUE SET COUNT          : 46
REMARK   3   BIN FREE R VALUE                    : 0.1920
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3240
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 4
REMARK   3   SOLVENT ATOMS            : 226
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.77
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.91000
REMARK   3    B22 (A**2) : -0.91000
REMARK   3    B33 (A**2) : 1.36000
REMARK   3    B12 (A**2) : -0.45000
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): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.467
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.210
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.833
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.830
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.777
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3312 ; 0.016 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4506 ; 1.785 ; 1.931
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   436 ; 9.195 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   136 ;39.721 ;24.412
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   486 ;24.402 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;17.242 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   510 ; 0.112 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2534 ; 0.009 ; 0.021
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):  2178 ; 0.529 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3454 ; 0.892 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1134 ; 1.455 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1052 ; 2.163 ; 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  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
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 3S0Z COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAY-11.
REMARK 100 THE RCSB ID CODE IS RCSB065623.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 02-MAR-11
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY
REMARK 200  BEAMLINE                       : AR-NE3A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10177
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 71.3
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   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
REMARK 200 STARTING MODEL: 2WRS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 43.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20MM CDCL2, 20MM CACL2, 20MM COCL2,
REMARK 280  20% (V/W) PEG 3350, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
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       71.76400
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      143.52800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   167
REMARK 465     TRP A   168
REMARK 465     VAL A   169
REMARK 465     GLU A   170
REMARK 465     GLY B   167
REMARK 465     TRP B   168
REMARK 465     VAL B   169
REMARK 465     GLU B   170
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     THR A  62    CG2
REMARK 470     ASN A 110    CG   OD1
REMARK 470     THR B  62    CG2
REMARK 470     ASN B 110    CG   OD1
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  GLN B    60     CB   ASN B    76              2.00
REMARK 500   OE1  GLN B    60     CG   ASN B    76              2.00
REMARK 500   OE1  GLN B    53     O    ALA B    55              2.12
REMARK 500   O    GLU A   108     O    HOH A   298              2.16
REMARK 500   O    ALA A   258     OG1  THR A   262              2.16
REMARK 500   OE1  GLN A    53     O    VAL A    58              2.17
REMARK 500   OE1  GLN B    60     ND2  ASN B    76              2.19
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 B  87   CA  -  CB  -  CG  ANGL. DEV. =  16.5 DEGREES
REMARK 500    PRO B 185   C   -  N   -  CA  ANGL. DEV. =   9.6 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    ALA A  55      161.13    160.77
REMARK 500    ASN A  57      -19.77    101.34
REMARK 500    SER A  63      114.93   -169.84
REMARK 500    ASP A  66       25.02    -78.81
REMARK 500    MET A  67      -97.34    -67.18
REMARK 500    PRO A  68      -86.15    -67.59
REMARK 500    PHE A  70      -88.59     51.49
REMARK 500    ARG A  85      158.00    -25.04
REMARK 500    ASP A  90      148.81     76.33
REMARK 500    ALA A  92     -149.71    -61.51
REMARK 500    THR A  94     -169.45   -124.82
REMARK 500    GLU A 108      -17.96   -147.25
REMARK 500    ILE A 109      -64.27   -104.67
REMARK 500    ASN A 110      -79.28    116.98
REMARK 500    LEU A 111      155.81    -43.06
REMARK 500    ALA A 116      117.49   -162.96
REMARK 500    HIS A 120      169.10    172.02
REMARK 500    MET A 126      -81.25    -90.51
REMARK 500    ASP A 130      -21.04    -38.15
REMARK 500    ASN A 146       35.59    -69.44
REMARK 500    GLN A 147      -25.29   -165.04
REMARK 500    GLU A 152       44.08   -149.78
REMARK 500    MET A 154     -174.48   -173.89
REMARK 500    GLN A 158     -104.32    -58.29
REMARK 500    THR A 162     -143.30   -153.36
REMARK 500    PHE A 163        4.04     46.81
REMARK 500    ALA A 172       45.16    178.67
REMARK 500    ASN A 176     -165.50   -112.71
REMARK 500    PHE A 177       73.89    168.36
REMARK 500    LEU A 209      -76.13    -65.56
REMARK 500    LYS A 216      -53.63     26.09
REMARK 500    SER A 217     -146.44   -121.84
REMARK 500    ASP A 223       94.57    -52.23
REMARK 500    TYR A 229      -56.09    -24.77
REMARK 500    ALA A 235      -58.08     -1.82
REMARK 500    PRO A 241        5.40    -68.11
REMARK 500    LYS A 242      -32.56   -130.46
REMARK 500    ALA A 243       92.44    -50.47
REMARK 500    SER A 249       39.94    -85.81
REMARK 500    HIS A 250       86.55   -166.10
REMARK 500    SER A 251      169.14     72.77
REMARK 500    ASP A 254     -154.50    -81.89
REMARK 500    SER A 255     -166.32   -106.05
REMARK 500    ARG A 256       10.52    -69.22
REMARK 500    PRO B  56      104.44    -54.23
REMARK 500    ASN B  57      -33.34    118.34
REMARK 500    ASP B  66       85.57    -67.58
REMARK 500    MET B  67      -80.29   -134.29
REMARK 500    PHE B  70     -110.05     61.74
REMARK 500    ASP B  90      177.07     76.00
REMARK 500
REMARK 500 THIS ENTRY HAS      75 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    PHE A  70        22.8      L          L   OUTSIDE RANGE
REMARK 500    SER A 251        24.6      L          L   OUTSIDE RANGE
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  40        DISTANCE =  5.40 ANGSTROMS
REMARK 525    HOH A 286        DISTANCE =  5.60 ANGSTROMS
REMARK 525    HOH A 287        DISTANCE =  5.07 ANGSTROMS
REMARK 525    HOH A 288        DISTANCE =  5.24 ANGSTROMS
REMARK 525    HOH A 301        DISTANCE =  5.44 ANGSTROMS
REMARK 525    HOH A 309        DISTANCE =  6.46 ANGSTROMS
REMARK 525    HOH A 312        DISTANCE =  7.96 ANGSTROMS
REMARK 525    HOH A 313        DISTANCE =  5.04 ANGSTROMS
REMARK 525    HOH A 319        DISTANCE =  7.43 ANGSTROMS
REMARK 525    HOH A 321        DISTANCE =  5.63 ANGSTROMS
REMARK 525    HOH A 330        DISTANCE =  7.10 ANGSTROMS
REMARK 525    HOH A 331        DISTANCE =  5.18 ANGSTROMS
REMARK 525    HOH A 332        DISTANCE =  5.33 ANGSTROMS
REMARK 525    HOH A 335        DISTANCE =  6.68 ANGSTROMS
REMARK 525    HOH A 340        DISTANCE =  6.51 ANGSTROMS
REMARK 525    HOH A 341        DISTANCE =  5.07 ANGSTROMS
REMARK 525    HOH A 343        DISTANCE =  9.16 ANGSTROMS
REMARK 525    HOH A 344        DISTANCE =  7.25 ANGSTROMS
REMARK 525    HOH A 345        DISTANCE =  8.50 ANGSTROMS
REMARK 525    HOH A 346        DISTANCE =  8.00 ANGSTROMS
REMARK 525    HOH A 347        DISTANCE =  6.57 ANGSTROMS
REMARK 525    HOH A 348        DISTANCE =  6.92 ANGSTROMS
REMARK 525    HOH A 349        DISTANCE =  6.02 ANGSTROMS
REMARK 525    HOH A 351        DISTANCE =  6.87 ANGSTROMS
REMARK 525    HOH A 352        DISTANCE =  6.69 ANGSTROMS
REMARK 525    HOH A 353        DISTANCE =  6.16 ANGSTROMS
REMARK 525    HOH A 354        DISTANCE =  8.03 ANGSTROMS
REMARK 525    HOH A 355        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 358        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH A 360        DISTANCE =  5.17 ANGSTROMS
REMARK 525    HOH A 361        DISTANCE =  5.77 ANGSTROMS
REMARK 525    HOH A 362        DISTANCE =  7.00 ANGSTROMS
REMARK 525    HOH A 363        DISTANCE =  7.12 ANGSTROMS
REMARK 525    HOH A 365        DISTANCE =  5.08 ANGSTROMS
REMARK 525    HOH A 366        DISTANCE =  7.89 ANGSTROMS
REMARK 525    HOH B 276        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH B 284        DISTANCE =  5.04 ANGSTROMS
REMARK 525    HOH B 297        DISTANCE =  5.08 ANGSTROMS
REMARK 525    HOH B 299        DISTANCE =  6.45 ANGSTROMS
REMARK 525    HOH B 303        DISTANCE =  6.93 ANGSTROMS
REMARK 525    HOH B 304        DISTANCE =  7.27 ANGSTROMS
REMARK 525    HOH B 307        DISTANCE =  6.03 ANGSTROMS
REMARK 525    HOH B 309        DISTANCE =  7.26 ANGSTROMS
REMARK 525    HOH B 310        DISTANCE =  5.87 ANGSTROMS
REMARK 525    HOH B 311        DISTANCE =  5.89 ANGSTROMS
REMARK 525    HOH B 315        DISTANCE =  6.24 ANGSTROMS
REMARK 525    HOH B 320        DISTANCE =  5.85 ANGSTROMS
REMARK 525    HOH B 324        DISTANCE =  5.44 ANGSTROMS
REMARK 525    HOH B 330        DISTANCE =  5.71 ANGSTROMS
REMARK 525    HOH B 332        DISTANCE =  5.86 ANGSTROMS
REMARK 525    HOH B 334        DISTANCE =  5.18 ANGSTROMS
REMARK 525    HOH B 336        DISTANCE =  6.88 ANGSTROMS
REMARK 525    HOH B 337        DISTANCE =  6.41 ANGSTROMS
REMARK 525    HOH B 338        DISTANCE =  6.89 ANGSTROMS
REMARK 525    HOH B 339        DISTANCE =  6.05 ANGSTROMS
REMARK 525    HOH B 340        DISTANCE =  6.93 ANGSTROMS
REMARK 525    HOH B 343        DISTANCE =  6.01 ANGSTROMS
REMARK 525    HOH B 347        DISTANCE =  7.18 ANGSTROMS
REMARK 525    HOH B 349        DISTANCE =  7.01 ANGSTROMS
REMARK 525    HOH B 355        DISTANCE =  5.80 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 A1001  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 208   SG
REMARK 620 2 HOH A 368   O   158.4
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B1002  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 120   NE2
REMARK 620 2 HIS B 122   ND1 104.0
REMARK 620 N                    1
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 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1002
DBREF  3S0Z A   47   270  UNP    E5KIY2   E5KIY2_ECOLX    47    270
DBREF  3S0Z B   47   270  UNP    E5KIY2   E5KIY2_ECOLX    47    270
SEQRES   1 A  224  GLY ASP LEU VAL PHE ARG GLN LEU ALA PRO ASN VAL TRP
SEQRES   2 A  224  GLN HIS THR SER TYR LEU ASP MET PRO GLY PHE GLY ALA
SEQRES   3 A  224  VAL ALA SER ASN GLY LEU ILE VAL ARG ASP GLY GLY ARG
SEQRES   4 A  224  VAL LEU VAL VAL ASP THR ALA TRP THR ASP ASP GLN THR
SEQRES   5 A  224  ALA GLN ILE LEU ASN TRP ILE LYS GLN GLU ILE ASN LEU
SEQRES   6 A  224  PRO VAL ALA LEU ALA VAL VAL THR HIS ALA HIS GLN ASP
SEQRES   7 A  224  LYS MET GLY GLY MET ASP ALA LEU HIS ALA ALA GLY ILE
SEQRES   8 A  224  ALA THR TYR ALA ASN ALA LEU SER ASN GLN LEU ALA PRO
SEQRES   9 A  224  GLN GLU GLY MET VAL ALA ALA GLN HIS SER LEU THR PHE
SEQRES  10 A  224  ALA ALA ASN GLY TRP VAL GLU PRO ALA THR ALA PRO ASN
SEQRES  11 A  224  PHE GLY PRO LEU LYS VAL PHE TYR PRO GLY PRO GLY HIS
SEQRES  12 A  224  THR SER ASP ASN ILE THR VAL GLY ILE ASP GLY THR ASP
SEQRES  13 A  224  ILE ALA PHE GLY GLY CYS LEU ILE LYS ASP SER LYS ALA
SEQRES  14 A  224  LYS SER LEU GLY ASN LEU GLY ASP ALA ASP THR GLU HIS
SEQRES  15 A  224  TYR ALA ALA SER ALA ARG ALA PHE GLY ALA ALA PHE PRO
SEQRES  16 A  224  LYS ALA SER MET ILE VAL MET SER HIS SER ALA PRO ASP
SEQRES  17 A  224  SER ARG ALA ALA ILE THR HIS THR ALA ARG MET ALA ASP
SEQRES  18 A  224  LYS LEU ARG
SEQRES   1 B  224  GLY ASP LEU VAL PHE ARG GLN LEU ALA PRO ASN VAL TRP
SEQRES   2 B  224  GLN HIS THR SER TYR LEU ASP MET PRO GLY PHE GLY ALA
SEQRES   3 B  224  VAL ALA SER ASN GLY LEU ILE VAL ARG ASP GLY GLY ARG
SEQRES   4 B  224  VAL LEU VAL VAL ASP THR ALA TRP THR ASP ASP GLN THR
SEQRES   5 B  224  ALA GLN ILE LEU ASN TRP ILE LYS GLN GLU ILE ASN LEU
SEQRES   6 B  224  PRO VAL ALA LEU ALA VAL VAL THR HIS ALA HIS GLN ASP
SEQRES   7 B  224  LYS MET GLY GLY MET ASP ALA LEU HIS ALA ALA GLY ILE
SEQRES   8 B  224  ALA THR TYR ALA ASN ALA LEU SER ASN GLN LEU ALA PRO
SEQRES   9 B  224  GLN GLU GLY MET VAL ALA ALA GLN HIS SER LEU THR PHE
SEQRES  10 B  224  ALA ALA ASN GLY TRP VAL GLU PRO ALA THR ALA PRO ASN
SEQRES  11 B  224  PHE GLY PRO LEU LYS VAL PHE TYR PRO GLY PRO GLY HIS
SEQRES  12 B  224  THR SER ASP ASN ILE THR VAL GLY ILE ASP GLY THR ASP
SEQRES  13 B  224  ILE ALA PHE GLY GLY CYS LEU ILE LYS ASP SER LYS ALA
SEQRES  14 B  224  LYS SER LEU GLY ASN LEU GLY ASP ALA ASP THR GLU HIS
SEQRES  15 B  224  TYR ALA ALA SER ALA ARG ALA PHE GLY ALA ALA PHE PRO
SEQRES  16 B  224  LYS ALA SER MET ILE VAL MET SER HIS SER ALA PRO ASP
SEQRES  17 B  224  SER ARG ALA ALA ILE THR HIS THR ALA ARG MET ALA ASP
SEQRES  18 B  224  LYS LEU ARG
HET     ZN  A1001       1
HET     ZN  A1002       1
HET     ZN  B1001       1
HET     ZN  B1002       1
HETNAM      ZN ZINC ION
FORMUL   3   ZN    4(ZN 2+)
FORMUL   7  HOH   *226(H2 O)
HELIX    1   1 THR A   98  GLN A  107  1                                  10
HELIX    2   2 GLY A  128  ALA A  135  1                                   8
HELIX    3   3 ASP A  225  PHE A  240  1                                  16
HELIX    4   4 ARG A  256  ASP A  267  1                                  12
HELIX    5   5 THR B   94  GLN B  107  1                                  14
HELIX    6   6 GLY B  128  ASP B  130  5                                   3
HELIX    7   7 ALA B  131  GLY B  136  1                                   6
HELIX    8   8 ASN B  142  ASN B  146  5                                   5
HELIX    9   9 ALA B  149  GLY B  153  5                                   5
HELIX   10  10 ASP B  225  ARG B  234  1                                  10
HELIX   11  11 ALA B  257  LEU B  269  1                                  13
SHEET    1   A 7 VAL A  50  PHE A  51  0
SHEET    2   A 7 VAL A  58  THR A  62 -1  O  THR A  62   N  VAL A  50
SHEET    3   A 7 GLY A  77  ASP A  82 -1  O  ILE A  79   N  TRP A  59
SHEET    4   A 7 ARG A  85  VAL A  89 -1  O  LEU A  87   N  VAL A  80
SHEET    5   A 7 VAL A 113  VAL A 118  1  O  ALA A 114   N  VAL A  86
SHEET    6   A 7 ALA A 138  ASN A 142  1  O  TYR A 140   N  ALA A 116
SHEET    7   A 7 HIS A 159  LEU A 161  1  O  LEU A 161   N  ALA A 141
SHEET    1   B 4 LEU A 180  PHE A 183  0
SHEET    2   B 4 THR A 195  ILE A 198 -1  O  THR A 195   N  PHE A 183
SHEET    3   B 4 ILE A 203  GLY A 207 -1  O  PHE A 205   N  VAL A 196
SHEET    4   B 4 MET A 245  MET A 248  1  O  VAL A 247   N  ALA A 204
SHEET    1   C 3 LEU B  49  ALA B  55  0
SHEET    2   C 3 VAL B  58  LEU B  65 -1  O  THR B  62   N  VAL B  50
SHEET    3   C 3 VAL B  73  ASN B  76 -1  O  SER B  75   N  SER B  63
SHEET    1   D 6 LEU B  49  ALA B  55  0
SHEET    2   D 6 VAL B  58  LEU B  65 -1  O  THR B  62   N  VAL B  50
SHEET    3   D 6 LEU B  78  ASP B  82 -1  O  ILE B  79   N  TRP B  59
SHEET    4   D 6 ARG B  85  VAL B  89 -1  O  ARG B  85   N  ASP B  82
SHEET    5   D 6 VAL B 113  VAL B 117  1  O  ALA B 114   N  VAL B  86
SHEET    6   D 6 ALA B 138  TYR B 140  1  O  ALA B 138   N  ALA B 114
SHEET    1   E 4 LEU B 180  PHE B 183  0
SHEET    2   E 4 THR B 195  ILE B 198 -1  O  THR B 195   N  PHE B 183
SHEET    3   E 4 ILE B 203  GLY B 207 -1  O  ILE B 203   N  ILE B 198
SHEET    4   E 4 MET B 245  MET B 248  1  O  MET B 245   N  ALA B 204
LINK         SG  CYS A 208                ZN    ZN A1001     1555   1555  2.03
LINK         NE2 HIS B 120                ZN    ZN B1002     1555   1555  2.10
LINK         NE2 HIS A 189                ZN    ZN A1002     1555   1555  2.24
LINK         ND1 HIS B 122                ZN    ZN B1002     1555   1555  2.48
LINK         OD2 ASP B 124                ZN    ZN B1001     1555   1555  2.68
LINK        ZN    ZN A1001                 O   HOH A 368     1555   1555  2.01
SITE     1 AC1  5 ASP A 124  CYS A 208  HIS A 250  HOH A 368
SITE     2 AC1  5  ZN A1002
SITE     1 AC2  6 HIS A 120  HIS A 122  ASP A 124  HIS A 189
SITE     2 AC2  6 CYS A 208   ZN A1001
SITE     1 AC3  4 ASP B 124  CYS B 208  HIS B 250  HOH B 341
SITE     1 AC4  5 HIS B 120  HIS B 122  ASP B 124  HIS B 189
SITE     2 AC4  5 CYS B 208
CRYST1   40.696   40.696  215.292  90.00  90.00 120.00 P 31          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      0.024572  0.014187  0.000000        0.00000
SCALE2      0.000000  0.028374  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004645        0.00000
      
PROCHECK
Go to PROCHECK summary
 References