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PDBsum entry 2cab

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Hydro-lyase PDB id
2cab
Jmol
Contents
Protein chain
256 a.a.
Metals
_ZN
HEADER    HYDRO-LYASE                             05-OCT-83   2CAB
TITLE     STRUCTURE, REFINEMENT AND FUNCTION OF CARBONIC ANHYDRASE
TITLE    2 ISOZYMES. REFINEMENT OF HUMAN CARBONIC ANHYDRASE I
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE FORM B;
COMPND   3 CHAIN: A;
COMPND   4 EC: 4.2.1.1;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606
KEYWDS    HYDRO-LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.K.KANNAN,M.RAMANADHAM,T.A.JONES
REVDAT   5   24-FEB-09 2CAB    1       VERSN
REVDAT   4   01-APR-03 2CAB    1       JRNL
REVDAT   3   17-JUL-84 2CAB    1       REMARK
REVDAT   2   30-MAY-84 2CAB    3       REMARK FTNOTE ATOM
REVDAT   1   02-FEB-84 2CAB    0
SPRSDE     02-FEB-84 2CAB      1CAB
JRNL        AUTH   K.K.KANNAN,M.RAMANADHAM,T.A.JONES
JRNL        TITL   STRUCTURE, REFINEMENT, AND FUNCTION OF CARBONIC
JRNL        TITL 2 ANHYDRASE ISOZYMES: REFINEMENT OF HUMAN CARBONIC
JRNL        TITL 3 ANHYDRASE I
JRNL        REF    ANN.N.Y.ACAD.SCI.             V. 429    49 1984
JRNL        REFN                   ISSN 0077-8923
JRNL        PMID   6430186
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   K.K.KANNAN
REMARK   1  TITL   STRUCTURE AND FUNCTION OF CARBONIC ANHYDRASES
REMARK   1  EDIT   R.SRINIVASAN
REMARK   1  REF    BIOMOLECULAR STRUCTURE,       V.   1   165 1980
REMARK   1  REF  2 CONFORMATION, FUNCTION AND
REMARK   1  REF  3 EVOLUTION
REMARK   1  PUBL   PERGAMON PRESS, NEW YORK
REMARK   1  REFN
REMARK   1 REFERENCE 2
REMARK   1  AUTH   K.K.KANNAN
REMARK   1  TITL   CRYSTAL STRUCTURE OF CARBONIC ANHYDRASE
REMARK   1  EDIT   C.BAUER, G.GROS, H.BARTELS
REMARK   1  REF    BIOPHYSICS AND PHYSIOLOGY              184 1980
REMARK   1  REF  2 OF CARBON DIOXIDE
REMARK   1  PUBL   SPRINGER VERLAG, BERLIN
REMARK   1  REFN
REMARK   1 REFERENCE 3
REMARK   1  AUTH   K.K.KANNAN,M.RAMANADHAM
REMARK   1  TITL   STRUCTURE, REFINEMENT, AND FUNCTION OF HUMAN
REMARK   1  TITL 2 CARBONIC ANHYDRASE-B
REMARK   1  REF    INT.J.QUANTUM CHEM.QUANTUM    V.  20   199 1981
REMARK   1  REF  2 CHEM.SYMP.
REMARK   1  REFN                   ISSN 0161-3642
REMARK   1 REFERENCE 4
REMARK   1  AUTH   K.K.KANNAN,M.PETEF,K.FRIDBORG,H.CID-DRESDNER,
REMARK   1  AUTH 2 S.LOVGREN
REMARK   1  TITL   STRUCTURE AND FUNCTION OF CARBONIC ANHYDRASES.
REMARK   1  TITL 2 IMIDAZOLE BINDING TO HUMAN CARBONIC ANHYDRACE B
REMARK   1  TITL 3 AND THE MECHANISM OF ACTION OF CARBONIC ANHYDRASES
REMARK   1  REF    FEBS LETT.                    V.  73   115 1977
REMARK   1  REFN                   ISSN 0014-5793
REMARK   1 REFERENCE 5
REMARK   1  AUTH   K.K.KANNAN,B.NOTSTRAND,K.FRIDBORG,S.LOVGREN,
REMARK   1  AUTH 2 A.OHLSSON,M.PETEF
REMARK   1  TITL   CRYSTAL STRUCTURE OF HUMAN ERYTHROCYTE CARBONIC
REMARK   1  TITL 2 ANHYDRASE B, THREE-DIMENSIONAL STRUCTURE AT A
REMARK   1  TITL 3 NOMINAL 2.2 ANGSTROMS RESOLUTION
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  72    51 1975
REMARK   1  REFN                   ISSN 0027-8424
REMARK   1 REFERENCE 6
REMARK   1  AUTH   B.NOTSTRAND,I.VAARA,K.K.KANNAN
REMARK   1  TITL   STRUCTURAL RELATIONSHIP OF HUMAN ERYTHROCYTE
REMARK   1  TITL 2 CARBONIC ANHYDRASE ISOZYMES B AND C
REMARK   1  EDIT   C.L.MARKERT
REMARK   1  REF    ISOZYMES-MOLECULAR STRUCTURE  V.   1   575 1975
REMARK   1  PUBL   ACADEMIC PRESS,NEW YORK
REMARK   1  REFN
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CORELS
REMARK   3   AUTHORS     : SUSSMAN
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : NULL
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2009
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 1
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
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  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS:  HELICES E1 AND E2 WERE ASSIGNED
REMARK   3  DEFAULT TYPE 1 (ALPHA).
REMARK   4
REMARK   4 2CAB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : NULL
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 36.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       40.75000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       18.55000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.80000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       18.55000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.75000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.80000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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     ALA A     1
REMARK 465     SER A     2
REMARK 465     PRO A     3
REMARK 465     ASP A     4
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 261  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 119   ND1
REMARK 620 2 HIS A  94   NE2 115.4
REMARK 620 3 HIS A  96   NE2  97.9 107.9
REMARK 620 N                    1     2
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 261
REMARK 999
REMARK 999 SEQUENCE
REMARK 999
REMARK 999 RESIDUE 74 IN THIS ENTRY IS IDENTIFIED AS GLN.  HOWEVER,
REMARK 999 CHEMICAL SEQUENCE AND RECENT DIFFRACTION STUDIES ON AN
REMARK 999 INHIBITOR COMPLEX INDICATE THAT IT SHOULD BE ASP.
DBREF  2CAB A    1   260  UNP    P00915   CAH1_HUMAN       1    260
SEQADV 2CAB GLN A   74  UNP  P00915    ASP    74 CONFLICT
SEQADV 2CAB ASP A   75  UNP  P00915    ASN    75 CONFLICT
SEQRES   1 A  260  ALA SER PRO ASP TRP GLY TYR ASP ASP LYS ASN GLY PRO
SEQRES   2 A  260  GLU GLN TRP SER LYS LEU TYR PRO ILE ALA ASN GLY ASN
SEQRES   3 A  260  ASN GLN SER PRO VAL ASP ILE LYS THR SER GLU THR LYS
SEQRES   4 A  260  HIS ASP THR SER LEU LYS PRO ILE SER VAL SER TYR ASN
SEQRES   5 A  260  PRO ALA THR ALA LYS GLU ILE ILE ASN VAL GLY HIS SER
SEQRES   6 A  260  PHE HIS VAL ASN PHE GLU ASP ASN GLN ASP ARG SER VAL
SEQRES   7 A  260  LEU LYS GLY GLY PRO PHE SER ASP SER TYR ARG LEU PHE
SEQRES   8 A  260  GLN PHE HIS PHE HIS TRP GLY SER THR ASN GLU HIS GLY
SEQRES   9 A  260  SER GLU HIS THR VAL ASP GLY VAL LYS TYR SER ALA GLU
SEQRES  10 A  260  LEU HIS VAL ALA HIS TRP ASN SER ALA LYS TYR SER SER
SEQRES  11 A  260  LEU ALA GLU ALA ALA SER LYS ALA ASP GLY LEU ALA VAL
SEQRES  12 A  260  ILE GLY VAL LEU MET LYS VAL GLY GLU ALA ASN PRO LYS
SEQRES  13 A  260  LEU GLN LYS VAL LEU ASP ALA LEU GLN ALA ILE LYS THR
SEQRES  14 A  260  LYS GLY LYS ARG ALA PRO PHE THR ASN PHE ASP PRO SER
SEQRES  15 A  260  THR LEU LEU PRO SER SER LEU ASP PHE TRP THR TYR PRO
SEQRES  16 A  260  GLY SER LEU THR HIS PRO PRO LEU TYR GLU SER VAL THR
SEQRES  17 A  260  TRP ILE ILE CYS LYS GLU SER ILE SER VAL SER SER GLU
SEQRES  18 A  260  GLN LEU ALA GLN PHE ARG SER LEU LEU SER ASN VAL GLU
SEQRES  19 A  260  GLY ASP ASN ALA VAL PRO MET GLN HIS ASN ASN ARG PRO
SEQRES  20 A  260  THR GLN PRO LEU LYS GLY ARG THR VAL ARG ALA SER PHE
HET     ZN  A 261       1
HETNAM      ZN ZINC ION
FORMUL   2   ZN    ZN 2+
HELIX    1   A TRP A   16  TYR A   20  1CONTIGUOUS WITH HELIX B            5
HELIX    2   B TYR A   20  GLY A   25  5CONTIGUOUS WITH HELIX A            6
HELIX    3   D SER A  130  LYS A  137  1ALSO DESIGNATED AS 3/10 HELIX      8
HELIX    4  E1 PRO A  155  ASP A  162  1CONTIGUOUS WITH HELIX E2           8
HELIX    5  E2 ASP A  162  LYS A  168  1CONTIGUOUS WITH HELIX E1           7
HELIX    6   F PRO A  181  LEU A  185  5                                   5
HELIX    7   G SER A  219  LEU A  229  1                                  11
SHEET    1   S10 LYS A  39  ASP A  41  0
SHEET    2   S10 VAL A 256  SER A 259  1  N  ASP A  41   O  ALA A 258
SHEET    3   S10 PHE A 191  GLY A 196 -1  N  THR A 193   O  ARG A 257
SHEET    4   S10 SER A 206  CYS A 212 -1  N  TRP A 209   O  TYR A 194
SHEET    5   S10 GLY A 140  GLY A 151 -1  N  VAL A 143   O  THR A 208
SHEET    6   S10 ALA A 116  ASN A 124 -1  N  VAL A 120   O  ILE A 144
SHEET    7   S10 SER A  87  HIS A  96 -1  N  HIS A  94   O  HIS A 119
SHEET    8   S10 SER A  65  GLU A  71 -1  N  HIS A  67   O  HIS A  94
SHEET    9   S10 THR A  55  VAL A  62 -1  N  ILE A  60   O  HIS A  67
SHEET   10   S10 GLY A 171  PHE A 176 -1  N  ALA A 174   O  ILE A  59
LINK        ZN    ZN A 261                 ND1 HIS A 119     1555   1555  1.90
LINK        ZN    ZN A 261                 NE2 HIS A  94     1555   1555  1.93
LINK        ZN    ZN A 261                 NE2 HIS A  96     1555   1555  1.94
CISPEP   1 SER A   29    PRO A   30          0        -1.75
CISPEP   2 PRO A  201    PRO A  202          0         2.14
SITE     1 AC1  3 HIS A  94  HIS A  96  HIS A 119
CRYST1   81.500   73.600   37.100  90.00  90.00  90.00 P 21 21 21    4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.012270  0.000000  0.000000       -0.02494
SCALE2      0.000000  0.013590  0.000000       -0.33832
SCALE3      0.000000  0.000000  0.026950        0.62129
      
PROCHECK
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 References