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PDBsum entry 2fw4

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Lyase PDB id
2fw4
Jmol
Contents
Protein chains
257 a.a.
Ligands
HIS ×2
Metals
_ZN ×2
Waters ×370
HEADER    LYASE                                   01-FEB-06   2FW4
TITLE     CARBONIC ANHYDRASE ACTIVATORS. THE FIRST X-RAY
TITLE    2 CRYSTALLOGRAPHIC STUDY OF AN ACTIVATOR OF ISOFORM I,
TITLE    3 STRUCTURE WITH L-HISTIDINE.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 1;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: CARBONIC ANHYDRASE I, CARBONATE DEHYDRATASE I, CA-
COMPND   5 I;
COMPND   6 EC: 4.2.1.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606
KEYWDS    CARBONIC ANHYDRASE I, ACTIVATORS, CRYSTAL STRUCTURE, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.TEMPERINI,A.SCOZZAFAVA,C.T.SUPURAN
REVDAT   3   24-FEB-09 2FW4    1       VERSN
REVDAT   2   05-SEP-06 2FW4    1       JRNL
REVDAT   1   08-AUG-06 2FW4    0
JRNL        AUTH   C.TEMPERINI,A.SCOZZAFAVA,C.T.SUPURAN
JRNL        TITL   CARBONIC ANHYDRASE ACTIVATORS: THE FIRST X-RAY
JRNL        TITL 2 CRYSTALLOGRAPHIC STUDY OF AN ADDUCT OF ISOFORM I.
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  16  5152 2006
JRNL        REFN                   ISSN 0960-894X
JRNL        PMID   16870440
JRNL        DOI    10.1016/J.BMCL.2006.07.021
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
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) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4
REMARK   3   NUMBER OF REFLECTIONS             : 33884
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) : 0.217
REMARK   3   R VALUE            (WORKING SET) : 0.213
REMARK   3   FREE R VALUE                     : 0.303
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1781
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) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2192
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.21
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2470
REMARK   3   BIN FREE R VALUE SET COUNT          : 113
REMARK   3   BIN FREE R VALUE                    : 0.3260
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4024
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 24
REMARK   3   SOLVENT ATOMS            : 370
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.03
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.20000
REMARK   3    B22 (A**2) : 1.24000
REMARK   3    B33 (A**2) : -0.04000
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): 0.227
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.224
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.170
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.039
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.924
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.838
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4158 ; 0.022 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5655 ; 1.965 ; 1.932
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   511 ; 7.464 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   193 ;38.949 ;24.715
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   663 ;16.812 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;21.492 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   605 ; 0.131 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3216 ; 0.009 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2041 ; 0.251 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2722 ; 0.316 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   350 ; 0.187 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     3 ; 0.033 ; 0.200
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    59 ; 0.203 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    28 ; 0.209 ; 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):  2629 ; 1.033 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4158 ; 1.633 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1758 ; 2.667 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1497 ; 3.501 ; 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 : 1
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A      4       A     260      4
REMARK   3           1     B      5       B     260      4
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   2009 ;  0.49 ;  0.50
REMARK   3   MEDIUM THERMAL     1    A (A**2):   2009 ;  1.67 ;  2.00
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   : 1.20
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
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 2FW4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-FEB-06.
REMARK 100 THE RCSB ID CODE IS RCSB036381.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 02-NOV-05
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 9.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : SEALED TUBE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : OXFORD DIFFRACTION ENHANCED
REMARK 200                                   ULTRA
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : CAPILLARY
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : OXFORD SAPPHIRE CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35706
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.23300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 6.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.0
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 46.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 4000, 0.1M TRIS.HCL, 10%
REMARK 280  ETHYLENE GLYCOL, PH 9.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 298.0K
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       31.06900
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.28650
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.09100
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.28650
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.06900
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.09100
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
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 300 REMARK: TWO BIOLOGICAL UNIT IN THE ASYMMETRIC UNIT
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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     ALA A     1
REMARK 465     SER A     2
REMARK 465     PRO A     3
REMARK 465     ALA B     1
REMARK 465     SER B     2
REMARK 465     PRO B     3
REMARK 465     ASP B     4
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   CD1  ILE B    60     O    HOH B   702              1.99
REMARK 500   CD2  LEU A   198     OXT  HIS A   500              2.05
REMARK 500   O    HOH B   662     O    HOH B   745              2.11
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    TRP A   5      141.23    132.74
REMARK 500    ASP A   8     -172.45    -55.08
REMARK 500    LYS A  57      -61.85   -120.79
REMARK 500    SER A  65     -164.03   -171.47
REMARK 500    HIS A 103       87.88   -154.03
REMARK 500    ILE A 167       46.70   -142.60
REMARK 500    ASN A 244       23.34   -157.89
REMARK 500    LYS B  57      -57.85   -122.69
REMARK 500    SER B  65     -168.95   -160.06
REMARK 500    ASN B  75       31.40    -94.66
REMARK 500    ASP B 110       42.74     38.91
REMARK 500    ALA B 138      -44.57    -28.03
REMARK 500    GLN B 158      -59.59    -26.28
REMARK 500    ASN B 244       33.30   -158.94
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 561  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 562   O
REMARK 620 2 HIS A  94   NE2 116.3
REMARK 620 3 HIS A  96   NE2 118.4  98.9
REMARK 620 4 HIS A 119   ND1 115.7 104.5 100.3
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 562  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B  94   NE2
REMARK 620 2 HIS B  96   NE2  99.2
REMARK 620 3 HIS B 119   ND1 105.9  94.7
REMARK 620 4 HOH B 563   O   118.2 122.9 112.5
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 561
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 562
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HIS A 500
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HIS B 501
DBREF  2FW4 A    1   260  UNP    P00915   CAH1_HUMAN       1    260
DBREF  2FW4 B    1   260  UNP    P00915   CAH1_HUMAN       1    260
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 ASP ASN 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
SEQRES   1 B  260  ALA SER PRO ASP TRP GLY TYR ASP ASP LYS ASN GLY PRO
SEQRES   2 B  260  GLU GLN TRP SER LYS LEU TYR PRO ILE ALA ASN GLY ASN
SEQRES   3 B  260  ASN GLN SER PRO VAL ASP ILE LYS THR SER GLU THR LYS
SEQRES   4 B  260  HIS ASP THR SER LEU LYS PRO ILE SER VAL SER TYR ASN
SEQRES   5 B  260  PRO ALA THR ALA LYS GLU ILE ILE ASN VAL GLY HIS SER
SEQRES   6 B  260  PHE HIS VAL ASN PHE GLU ASP ASN ASP ASN ARG SER VAL
SEQRES   7 B  260  LEU LYS GLY GLY PRO PHE SER ASP SER TYR ARG LEU PHE
SEQRES   8 B  260  GLN PHE HIS PHE HIS TRP GLY SER THR ASN GLU HIS GLY
SEQRES   9 B  260  SER GLU HIS THR VAL ASP GLY VAL LYS TYR SER ALA GLU
SEQRES  10 B  260  LEU HIS VAL ALA HIS TRP ASN SER ALA LYS TYR SER SER
SEQRES  11 B  260  LEU ALA GLU ALA ALA SER LYS ALA ASP GLY LEU ALA VAL
SEQRES  12 B  260  ILE GLY VAL LEU MET LYS VAL GLY GLU ALA ASN PRO LYS
SEQRES  13 B  260  LEU GLN LYS VAL LEU ASP ALA LEU GLN ALA ILE LYS THR
SEQRES  14 B  260  LYS GLY LYS ARG ALA PRO PHE THR ASN PHE ASP PRO SER
SEQRES  15 B  260  THR LEU LEU PRO SER SER LEU ASP PHE TRP THR TYR PRO
SEQRES  16 B  260  GLY SER LEU THR HIS PRO PRO LEU TYR GLU SER VAL THR
SEQRES  17 B  260  TRP ILE ILE CYS LYS GLU SER ILE SER VAL SER SER GLU
SEQRES  18 B  260  GLN LEU ALA GLN PHE ARG SER LEU LEU SER ASN VAL GLU
SEQRES  19 B  260  GLY ASP ASN ALA VAL PRO MET GLN HIS ASN ASN ARG PRO
SEQRES  20 B  260  THR GLN PRO LEU LYS GLY ARG THR VAL ARG ALA SER PHE
HET     ZN  A 561       1
HET     ZN  B 562       1
HET    HIS  A 500      11
HET    HIS  B 501      11
HETNAM      ZN ZINC ION
HETNAM     HIS HISTIDINE
FORMUL   3   ZN    2(ZN 2+)
FORMUL   5  HIS    2(C6 H10 N3 O2 1+)
FORMUL   7  HOH   *370(H2 O)
HELIX    1   1 GLY A   12  LEU A   19  5                                   8
HELIX    2   2 TYR A   20  GLY A   25  5                                   6
HELIX    3   3 ASN A   52  ALA A   54  5                                   3
HELIX    4   4 SER A  130  ALA A  135  1                                   6
HELIX    5   5 ASN A  154  LYS A  156  5                                   3
HELIX    6   6 LEU A  157  LEU A  164  1                                   8
HELIX    7   7 GLN A  165  ILE A  167  5                                   3
HELIX    8   8 ASP A  180  LEU A  185  5                                   6
HELIX    9   9 SER A  219  SER A  228  1                                  10
HELIX   10  10 GLY B   12  LEU B   19  5                                   8
HELIX   11  11 TYR B   20  GLY B   25  5                                   6
HELIX   12  12 SER B  130  ALA B  135  1                                   6
HELIX   13  13 ASN B  154  LYS B  156  5                                   3
HELIX   14  14 LEU B  157  ASP B  162  1                                   6
HELIX   15  15 ALA B  163  ILE B  167  5                                   5
HELIX   16  16 ASP B  180  LEU B  185  5                                   6
HELIX   17  17 SER B  219  ARG B  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  HIS A  40  0
SHEET    2   B10 ARG A 257  ALA A 258  1  O  ALA A 258   N  LYS A  39
SHEET    3   B10 PHE A 191  GLY A 196 -1  N  THR A 193   O  ARG A 257
SHEET    4   B10 VAL A 207  CYS 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  HIS A 122   O  ALA A 142
SHEET    7   B10 TYR A  88  TRP A  97 -1  N  PHE A  91   O  ALA A 121
SHEET    8   B10 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93
SHEET    9   B10 ALA A  56  ASN A  61 -1  N  LYS A  57   O  ASN A  69
SHEET   10   B10 ARG A 173  PRO A 175 -1  O  ALA A 174   N  ILE A  59
SHEET    1   C 6 ILE A  47  SER A  50  0
SHEET    2   C 6 VAL A  78  GLY A  81 -1  O  LYS A  80   N  SER A  48
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  ALA A 121   N  PHE A  91
SHEET    5   C 6 LEU A 141  VAL A 150 -1  O  ALA A 142   N  HIS A 122
SHEET    6   C 6 ILE A 216  VAL A 218  1  O  ILE A 216   N  LYS A 149
SHEET    1   D 2 ASP B  32  ILE B  33  0
SHEET    2   D 2 THR B 108  VAL B 109  1  O  THR B 108   N  ILE B  33
SHEET    1   E10 LYS B  39  HIS B  40  0
SHEET    2   E10 ARG B 257  ALA B 258  1  O  ALA B 258   N  LYS B  39
SHEET    3   E10 PHE B 191  GLY B 196 -1  N  THR B 193   O  ARG B 257
SHEET    4   E10 VAL B 207  CYS B 212 -1  O  VAL B 207   N  GLY B 196
SHEET    5   E10 LEU B 141  VAL B 150  1  N  GLY B 145   O  ILE B 210
SHEET    6   E10 ALA B 116  ASN B 124 -1  N  LEU B 118   O  VAL B 146
SHEET    7   E10 TYR B  88  TRP B  97 -1  N  GLN B  92   O  ALA B 121
SHEET    8   E10 PHE B  66  PHE B  70 -1  N  PHE B  70   O  PHE B  91
SHEET    9   E10 ALA B  56  ASN B  61 -1  N  GLU B  58   O  ASN B  69
SHEET   10   E10 ARG B 173  PRO B 175 -1  O  ALA B 174   N  ILE B  59
SHEET    1   F 6 ILE B  47  TYR B  51  0
SHEET    2   F 6 SER B  77  GLY B  81 -1  O  LYS B  80   N  SER B  48
SHEET    3   F 6 TYR B  88  TRP B  97 -1  O  LEU B  90   N  SER B  77
SHEET    4   F 6 ALA B 116  ASN B 124 -1  O  ALA B 121   N  GLN B  92
SHEET    5   F 6 LEU B 141  VAL B 150 -1  O  VAL B 146   N  LEU B 118
SHEET    6   F 6 ILE B 216  VAL B 218  1  O  ILE B 216   N  LYS B 149
LINK        ZN    ZN A 561                 O   HOH A 562     1555   1555  2.29
LINK        ZN    ZN A 561                 NE2 HIS A  94     1555   1555  2.05
LINK        ZN    ZN A 561                 NE2 HIS A  96     1555   1555  2.32
LINK        ZN    ZN A 561                 ND1 HIS A 119     1555   1555  2.02
LINK        ZN    ZN B 562                 NE2 HIS B  94     1555   1555  2.10
LINK        ZN    ZN B 562                 NE2 HIS B  96     1555   1555  2.03
LINK        ZN    ZN B 562                 ND1 HIS B 119     1555   1555  2.17
LINK        ZN    ZN B 562                 O   HOH B 563     1555   1555  2.35
CISPEP   1 SER A   29    PRO A   30          0        -0.43
CISPEP   2 PRO A  201    PRO A  202          0         7.47
CISPEP   3 SER B   29    PRO B   30          0        -0.32
CISPEP   4 PRO B  201    PRO B  202          0        15.15
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  HOH A 562
SITE     1 AC2  4 HIS B  94  HIS B  96  HIS B 119  HOH B 563
SITE     1 AC3  6 GLN A  92  HIS A  94  ALA A 135  LEU A 198
SITE     2 AC3  6 HIS A 200  HOH A 697
SITE     1 AC4  4 ALA B 135  LEU B 198  HIS B 200  HOH B 689
CRYST1   62.138   70.182  120.573  90.00  90.00  90.00 P 21 21 21    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      0.016093  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014249  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008294        0.00000
      
PROCHECK
Go to PROCHECK summary
 References