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PDBsum entry 3mzc

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Lyase/lyase inhibitor PDB id
3mzc
Jmol
Contents
Protein chain
257 a.a.
Ligands
S6I
GOL
Metals
_ZN
Waters ×306
HEADER    LYASE/LYASE INHIBITOR                   12-MAY-10   3MZC
TITLE     HUMAN CARBONIC AHYDRASE II IN COMPLEX WITH A BENZENESULFONAMIDE
TITLE    2 INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: HUMAN CARBONIC ANHYDRASE II;
COMPND   5 SYNONYM: CARBONIC ANHYDRASE II, CA-II, CARBONATE DEHYDRATASE II,
COMPND   6 CARBONIC ANHYDRASE C, CAC;
COMPND   7 EC: 4.2.1.1;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_TAXID: 9606;
SOURCE   4 GENE: CAH2_HUMAN;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS    LYASE, BENZENESULFONAMIDE INHIBITOR, ZINC METALLOENZYME, ZINC
KEYWDS   2 COORDINATION, LYASE-LYASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.S.AVVARU,J.WAGNER,A.H.ROBBINS,R.MCKENNA
REVDAT   1   09-MAR-11 3MZC    0
JRNL        AUTH   F.PACCHIANO,M.AGGARWAL,B.S.AVVARU,A.H.ROBBINS,A.SCOZZAFAVA,
JRNL        AUTH 2 R.MCKENNA,C.T.SUPURAN
JRNL        TITL   SELECTIVE HYDROPHOBIC POCKET BINDING OBSERVED WITHIN THE
JRNL        TITL 2 CARBONIC ANHYDRASE II ACTIVE SITE ACCOMMODATE DIFFERENT
JRNL        TITL 3 4-SUBSTITUTED-UREIDO-BENZENESULFONAMIDES AND CORRELATE TO
JRNL        TITL 4 INHIBITOR POTENCY.
JRNL        REF    CHEM.COMMUN.(CAMB.)           V.  46  8371 2010
JRNL        REFN                   ISSN 1359-7345
JRNL        PMID   20922253
JRNL        DOI    10.1039/C0CC02707C
REMARK   2
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.1_348)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.87
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.070
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.7
REMARK   3   NUMBER OF REFLECTIONS             : 35281
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.157
REMARK   3   R VALUE            (WORKING SET) : 0.156
REMARK   3   FREE R VALUE                     : 0.187
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.950
REMARK   3   FREE R VALUE TEST SET COUNT      : 1747
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 19.8700 -  3.4240    0.91     2915   150  0.1590 0.2050
REMARK   3     2  3.4240 -  2.7200    0.97     3041   160  0.1310 0.1490
REMARK   3     3  2.7200 -  2.3770    0.96     2985   157  0.1320 0.1690
REMARK   3     4  2.3770 -  2.1600    0.89     2807   137  0.1190 0.1460
REMARK   3     5  2.1600 -  2.0050    0.93     2895   159  0.1150 0.1400
REMARK   3     6  2.0050 -  1.8870    0.90     2794   140  0.1220 0.1370
REMARK   3     7  1.8870 -  1.7930    0.90     2773   152  0.1220 0.1510
REMARK   3     8  1.7930 -  1.7150    0.90     2788   141  0.1300 0.1830
REMARK   3     9  1.7150 -  1.6490    0.88     2726   143  0.1350 0.1680
REMARK   3    10  1.6490 -  1.5920    0.87     2690   139  0.1330 0.1730
REMARK   3    11  1.5920 -  1.5420    0.86     2667   135  0.1460 0.1690
REMARK   3    12  1.5420 -  1.4980    0.79     2453   134  0.1650 0.1970
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : 0.48
REMARK   3   B_SOL              : 48.18
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.210
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 26.20
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.54
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.64900
REMARK   3    B22 (A**2) : -0.32700
REMARK   3    B33 (A**2) : 1.97600
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.25900
REMARK   3    B23 (A**2) : 0.00000
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      :  0.010           2177
REMARK   3   ANGLE     :  1.355           2963
REMARK   3   CHIRALITY :  0.078            306
REMARK   3   PLANARITY :  0.010            386
REMARK   3   DIHEDRAL  : 13.108            814
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 2
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: CHAIN A OR ELEMENT ZN AND NOT ELEMENT H
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.7333  -1.8025  15.8890
REMARK   3    T TENSOR
REMARK   3      T11:   0.0776 T22:   0.0734
REMARK   3      T33:   0.0805 T12:  -0.0028
REMARK   3      T13:  -0.0004 T23:   0.0009
REMARK   3    L TENSOR
REMARK   3      L11:   0.4514 L22:   0.1900
REMARK   3      L33:   0.3711 L12:  -0.0930
REMARK   3      L13:   0.0132 L23:  -0.0523
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0033 S12:  -0.0266 S13:   0.0125
REMARK   3      S21:  -0.0169 S22:   0.0089 S23:   0.0075
REMARK   3      S31:   0.0184 S32:   0.0036 S33:  -0.0068
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: CHAIN I AND NOT ELEMENT H
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.8690   4.4752  14.9239
REMARK   3    T TENSOR
REMARK   3      T11:   0.0721 T22:   0.1135
REMARK   3      T33:   0.0958 T12:  -0.0102
REMARK   3      T13:   0.0002 T23:   0.0225
REMARK   3    L TENSOR
REMARK   3      L11:   5.9280 L22:   3.5312
REMARK   3      L33:   8.8996 L12:   1.2838
REMARK   3      L13:  -6.8338 L23:   0.3431
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0453 S12:   0.0426 S13:   0.0076
REMARK   3      S21:  -0.1782 S22:   0.1074 S23:  -0.0094
REMARK   3      S31:   0.0863 S32:  -0.0387 S33:  -0.0096
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 3MZC COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAY-10.
REMARK 100 THE RCSB ID CODE IS RCSB059183.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 12-APR-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH3R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : RIGAKU OPTIMAX
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35690
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.860
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.4
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.04100
REMARK 200  R SYM                      (I) : 0.04100
REMARK 200   FOR THE DATA SET  : 24.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.25300
REMARK 200   FOR SHELL         : 4.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.6.1.348
REMARK 200 STARTING MODEL: PDB ENTRY 2ILI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 41.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M SODIUM CITRATE, 50 MM TRIS-HCL,
REMARK 280  5UL + 5UL DROPLET, PH 7.8, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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       20.72400
REMARK 290   SMTRY3   2  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 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 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     1
REMARK 465     SER A     2
REMARK 465     HIS A     3
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  HD21  ASN A    62     HO2  GOL A   401              1.57
REMARK 500   OD1  ASP A    75     HE   ARG A    89              1.76
REMARK 500   HE2  HIS A   107     OH   TYR A   194              1.87
REMARK 500   HG   SER A   219     O    HOH A   333              1.88
REMARK 500   OE1  GLU A   106     HG1  THR A   199              1.88
REMARK 500   OE2  GLU A   117     HE2  HIS A   119              1.90
REMARK 500   HD1  HIS A   107     OE2  GLU A   117              1.90
REMARK 500   H    GLY A   196     O    VAL A   207              1.91
REMARK 500   HH   TYR A   191     O    HOH A   534              1.91
REMARK 500   OD1  ASP A    32     HG1  THR A   108              1.94
REMARK 500   HD1  HIS A    96     O    ASN A   244              1.95
REMARK 500   H    LEU A   118     O    ILE A   146              1.95
REMARK 500   H    GLY A   145     O    ILE A   210              1.95
REMARK 500   O    GLY A    12     H    HIS A    15              1.95
REMARK 500   O    LEU A   229     H    MET A   241              1.95
REMARK 500   O    LYS A    39     H    ALA A   258              1.95
REMARK 500   H    ASN A   124     O    GLY A   140              1.96
REMARK 500   OE1  GLN A    92     HD1  HIS A    94              1.96
REMARK 500   ND1  HIS A    15     HZ1  LYS A    18              1.96
REMARK 500   OD1  ASP A    32     H    LYS A   111              1.97
REMARK 500   HZ2  LYS A   154     O    HOH A   507              1.97
REMARK 500   H    ASN A   178     O    HOH A   325              1.97
REMARK 500   H    ILE A    33     O    THR A   108              1.97
REMARK 500   O    ASN A    61     H    GLY A   171              1.97
REMARK 500   O    PRO A   247    HE22  GLN A   249              1.97
REMARK 500   O    PRO A    30     H    GLN A   249              1.97
REMARK 500   H    LEU A    79     O    TYR A    88              1.97
REMARK 500   O    GLN A    92     H    VAL A   121              1.97
REMARK 500   O    LEU A   251     HE   ARG A   254              1.98
REMARK 500   HH   TYR A   128     OD1  ASP A   139              1.98
REMARK 500   H    GLY A   151     O    VAL A   218              1.98
REMARK 500   HD1  HIS A    17     O    HOH A   363              1.98
REMARK 500   H    GLU A    26     O    HOH A   350              1.98
REMARK 500   H    TRP A    97     OD1  ASN A   244              1.98
REMARK 500   O    TRP A   192     H    VAL A   211              1.98
REMARK 500   H    LEU A    57     O    GLU A    69              1.98
REMARK 500   H    PHE A   147     O    HOH A   318              1.99
REMARK 500   O    ILE A    33     H    ASP A   110              1.99
REMARK 500  HE22  GLN A   103     OD1  ASP A   243              2.00
REMARK 500   OD1  ASP A   101    HH22  ARG A   227              2.00
REMARK 500   O    HIS A    94     H    HIS A   119              2.00
REMARK 500   O    VAL A   109     H    LYS A   112              2.00
REMARK 500   H    GLY A   104     O    HOH A   303              2.01
REMARK 500   OH   TYR A    51     HE2  HIS A   122              2.01
REMARK 500   HG1  THR A   193     O    TRP A   209              2.01
REMARK 500   HN7  S6I A   263     O    HOH A   341              2.01
REMARK 500   OE1  GLN A    28    HH12  ARG A   246              2.01
REMARK 500   H    THR A    35     OD1  ASP A   110              2.01
REMARK 500   O    PHE A    20     H    ALA A    23              2.01
REMARK 500   H    GLY A   233     OE1  GLU A   236              2.01
REMARK 500
REMARK 500 THIS ENTRY HAS     220 CLOSE CONTACTS
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   HZ1  LYS A   127     O    HOH A   526     2556     1.87
REMARK 500  HH12  ARG A    89     O    HOH A   408     1565     1.88
REMARK 500   HZ3  LYS A    18     O    PRO A   186     1655     1.90
REMARK 500   OD1  ASN A   178     HZ2  LYS A   225     2455     1.94
REMARK 500   H    GLY A   102     OD2  ASP A   130     1545     1.96
REMARK 500   HE2  HIS A    17     O    GLU A   187     1655     1.96
REMARK 500   H    VAL A    49     O    HOH A   403     1455     2.00
REMARK 500  HH22  ARG A    58     O    GLU A   238     2555     2.02
REMARK 500   H    GLU A   238     O    HOH A   384     2545     2.02
REMARK 500   HD1  HIS A    10     O    HOH A   507     1655     2.05
REMARK 500   HZ2  LYS A    39     O    HOH A   567     2546     2.08
REMARK 500   OE1  GLN A   103     HZ1  LYS A   133     1545     2.09
REMARK 500   HE2  HIS A    17     O    GLU A   187     1655     2.10
REMARK 500  HH12  ARG A    58     O    GLU A   238     2555     2.15
REMARK 500   HG   SER A    99     O    HOH A   430     2545     2.17
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    ARG A  27       56.47   -145.11
REMARK 500    ALA A  65     -169.49   -164.47
REMARK 500    LYS A 111       -3.07     73.14
REMARK 500    PHE A 176       69.00   -150.87
REMARK 500    ASN A 244       48.32    -93.52
REMARK 500    LYS A 252     -138.29     55.66
REMARK 500
REMARK 500 REMARK: NULL
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 262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 S6I A 263   N1
REMARK 620 2 HIS A  94   NE2 113.9
REMARK 620 3 HIS A  96   NE2 112.1 104.5
REMARK 620 4 HIS A 119   ND1 115.7 110.7  98.3
REMARK 620 N                    1     2     3
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 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S6I A 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3N2P   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH A SIMILAR INHIBITOR
REMARK 900 RELATED ID: 3N0N   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH A SIMILAR INHIBITOR
REMARK 900 RELATED ID: 3N3J   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH A SIMILAR INHIBITOR
REMARK 900 RELATED ID: 3N4B   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH A SIMILAR INHIBITOR
DBREF  3MZC A    1   261  UNP    P00918   CAH2_HUMAN       1    260
SEQRES   1 A  260  MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO
SEQRES   2 A  260  GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU
SEQRES   3 A  260  ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS
SEQRES   4 A  260  TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP
SEQRES   5 A  260  GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA
SEQRES   6 A  260  PHE ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL
SEQRES   7 A  260  LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE
SEQRES   8 A  260  GLN PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY
SEQRES   9 A  260  SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU
SEQRES  10 A  260  LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE
SEQRES  11 A  260  GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU
SEQRES  12 A  260  GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU
SEQRES  13 A  260  GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS
SEQRES  14 A  260  GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY
SEQRES  15 A  260  LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY
SEQRES  16 A  260  SER LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP
SEQRES  17 A  260  ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN
SEQRES  18 A  260  VAL LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES  19 A  260  GLU PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA
SEQRES  20 A  260  GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET     ZN  A 262       1
HET    S6I  A 263      35
HET    GOL  A 401      14
HETNAM      ZN ZINC ION
HETNAM     S6I 4-[(CYCLOPENTYLCARBAMOYL)AMINO]BENZENESULFONAMIDE
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2   ZN    ZN 2+
FORMUL   3  S6I    C12 H17 N3 O3 S
FORMUL   4  GOL    C3 H8 O3
FORMUL   5  HOH   *306(H2 O)
HELIX    1   1 HIS A   15  ASP A   19  5                                   5
HELIX    2   2 PHE A   20  GLY A   25  5                                   6
HELIX    3   3 LYS A  127  GLY A  129  5                                   3
HELIX    4   4 ASP A  130  VAL A  135  1                                   6
HELIX    5   5 LYS A  154  GLY A  156  5                                   3
HELIX    6   6 LEU A  157  LEU A  164  1                                   8
HELIX    7   7 ASP A  165  LYS A  168  5                                   4
HELIX    8   8 ASP A  180  LEU A  185  5                                   6
HELIX    9   9 SER A  219  ARG A  227  1                                   9
SHEET    1   A 2 ASP A  32  ILE A  33  0
SHEET    2   A 2 THR A 108  VAL A 109  1  O  THR A 108   N  ILE A  33
SHEET    1   B10 LYS A  39  TYR A  40  0
SHEET    2   B10 LYS A 257  ALA A 258  1  O  ALA A 258   N  LYS A  39
SHEET    3   B10 TYR A 191  GLY A 196 -1  N  THR A 193   O  LYS A 257
SHEET    4   B10 VAL A 207  LEU A 212 -1  O  VAL A 207   N  GLY A 196
SHEET    5   B10 LEU A 141  VAL A 150  1  N  GLY A 145   O  ILE A 210
SHEET    6   B10 ALA A 116  ASN A 124 -1  N  LEU A 118   O  ILE A 146
SHEET    7   B10 TYR A  88  TRP A  97 -1  N  HIS A  94   O  HIS A 119
SHEET    8   B10 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93
SHEET    9   B10 SER A  56  ASN A  61 -1  N  LEU A  57   O  GLU A  69
SHEET   10   B10 SER A 173  ASP A 175 -1  O  ALA A 174   N  ILE A  59
SHEET    1   C 6 LEU A  47  SER A  50  0
SHEET    2   C 6 VAL A  78  GLY A  81 -1  O  VAL A  78   N  SER A  50
SHEET    3   C 6 TYR A  88  TRP A  97 -1  O  TYR A  88   N  LEU A  79
SHEET    4   C 6 ALA A 116  ASN A 124 -1  O  HIS A 119   N  HIS A  94
SHEET    5   C 6 LEU A 141  VAL A 150 -1  O  ILE A 146   N  LEU A 118
SHEET    6   C 6 ILE A 216  VAL A 218  1  O  VAL A 218   N  LYS A 149
LINK        ZN    ZN A 262                 N1  S6I A 263     1555   1555  1.92
LINK         NE2 HIS A  94                ZN    ZN A 262     1555   1555  2.03
LINK         NE2 HIS A  96                ZN    ZN A 262     1555   1555  2.03
LINK         ND1 HIS A 119                ZN    ZN A 262     1555   1555  2.04
CISPEP   1 SER A   29    PRO A   30          0        -1.83
CISPEP   2 PRO A  201    PRO A  202          0         8.54
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  S6I A 263
SITE     1 AC2 12 HIS A  94  HIS A  96  HIS A 119  PHE A 131
SITE     2 AC2 12 LEU A 198  THR A 199  THR A 200  TRP A 209
SITE     3 AC2 12  ZN A 262  HOH A 329  HOH A 341  GOL A 401
SITE     1 AC3  9 ASN A  62  HIS A  64  ALA A  65  ASN A  67
SITE     2 AC3  9 GLN A  92  S6I A 263  HOH A 331  HOH A 382
SITE     3 AC3  9 HOH A 462
CRYST1   42.452   41.448   72.032  90.00 104.11  90.00 P 1 21 1      2
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      0.023556  0.000000  0.005921        0.00000
SCALE2      0.000000  0.024127  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014315        0.00000
      
PROCHECK
Go to PROCHECK summary
 References