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PDBsum entry 2it4

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Lyase PDB id
2it4
Jmol
Contents
Protein chains
256 a.a.
Ligands
PPF
Metals
_ZN ×2
Waters ×344
HEADER    LYASE                                   19-OCT-06   2IT4
TITLE     X RAY STRUCTURE OF THE COMPLEX BETWEEN CARBONIC ANHYDRASE I
TITLE    2 AND THE PHOSPHONATE ANTIVIRAL DRUG FOSCARNET
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, ANTIVIRAL, CRYSTAL STUCTURE, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.TEMPERINI,A.INNOCENTI,A.GUERRI,A.SCOZZAFAVA,C.T.SUPURAN
REVDAT   2   24-FEB-09 2IT4    1       VERSN
REVDAT   1   11-SEP-07 2IT4    0
JRNL        AUTH   C.TEMPERINI,A.INNOCENTI,A.GUERRI,A.SCOZZAFAVA,
JRNL        AUTH 2 S.RUSCONI,C.T.SUPURAN
JRNL        TITL   PHOSPH(ON)ATE AS A ZINC-BINDING GROUP IN
JRNL        TITL 2 METALLOENZYME INHIBITORS: X-RAY CRYSTAL STRUCTURE
JRNL        TITL 3 OF THE ANTIVIRAL DRUG FOSCARNET COMPLEXED TO HUMAN
JRNL        TITL 4 CARBONIC ANHYDRASE I.
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  17  2210 2007
JRNL        REFN                   ISSN 0960-894X
JRNL        PMID   17314045
JRNL        DOI    10.1016/J.BMCL.2007.01.113
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.0
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 34182
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) : 0.249
REMARK   3   R VALUE            (WORKING SET) : 0.246
REMARK   3   FREE R VALUE                     : 0.316
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1785
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) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07
REMARK   3   REFLECTION IN BIN     (WORKING SET) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3150
REMARK   3   BIN FREE R VALUE SET COUNT          : 134
REMARK   3   BIN FREE R VALUE                    : 0.3780
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4032
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 9
REMARK   3   SOLVENT ATOMS            : 344
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ; 0.014 ;  NULL
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ; 1.530 ;  NULL
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
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 : NULL
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : NULL
REMARK   3   ION PROBE RADIUS   : NULL
REMARK   3   SHRINKAGE RADIUS   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2IT4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-06.
REMARK 100 THE RCSB ID CODE IS RCSB039982.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 13-SEP-06
REMARK 200  TEMPERATURE           (KELVIN) : 100
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 : CRYSALISRED OXFORD
REMARK 200                                   DIFFRACTION2006
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36020
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1
REMARK 200  DATA REDUNDANCY                : 5.900
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.12700
REMARK 200   FOR THE DATA SET  : 8.3000
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) : 2.07
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.030
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: 2FW4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 46.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS.HCL BUFFER PH 9.0, 25%
REMARK 280  (W/V) PEG 4000, LICL4 0.4 M, 10% ETHYLENE GLYCOL , VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 22K
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       31.29000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.22000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.75500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.22000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.29000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.75500
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 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 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     HIS B 103    CB   CG   ND1  CD2  CE1  NE2
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   O    HOH A   618     O    HOH A   669              2.19
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    LYS A  57      -65.10   -120.13
REMARK 500    SER A  65     -165.26   -165.16
REMARK 500    ASN A  75       33.83    -99.90
REMARK 500    ALA A 116      175.36    178.84
REMARK 500    ASN A 244       35.15   -163.55
REMARK 500    PRO B  13      -39.86    -39.71
REMARK 500    LYS B  57      -63.83   -120.15
REMARK 500    SER B  65     -167.65   -162.61
REMARK 500    HIS B 103     -122.72    -67.62
REMARK 500    GLU B 106      -60.80    -96.92
REMARK 500    ASN B 244       35.86   -154.16
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 B 679        DISTANCE =  5.90 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 561  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  94   NE2
REMARK 620 2 HIS A  96   NE2 109.3
REMARK 620 3 HIS A 119   ND1 113.8  92.1
REMARK 620 N                    1     2
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 105.7
REMARK 620 3 HIS B 119   ND1 111.8  99.5
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 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 PPF A 500
DBREF  2IT4 A    5   260  UNP    P00915   CAH1_HUMAN       5    260
DBREF  2IT4 B    5   260  UNP    P00915   CAH1_HUMAN       5    260
SEQRES   1 A  256  TRP GLY TYR ASP ASP LYS ASN GLY PRO GLU GLN TRP SER
SEQRES   2 A  256  LYS LEU TYR PRO ILE ALA ASN GLY ASN ASN GLN SER PRO
SEQRES   3 A  256  VAL ASP ILE LYS THR SER GLU THR LYS HIS ASP THR SER
SEQRES   4 A  256  LEU LYS PRO ILE SER VAL SER TYR ASN PRO ALA THR ALA
SEQRES   5 A  256  LYS GLU ILE ILE ASN VAL GLY HIS SER PHE HIS VAL ASN
SEQRES   6 A  256  PHE GLU ASP ASN ASP ASN ARG SER VAL LEU LYS GLY GLY
SEQRES   7 A  256  PRO PHE SER ASP SER TYR ARG LEU PHE GLN PHE HIS PHE
SEQRES   8 A  256  HIS TRP GLY SER THR ASN GLU HIS GLY SER GLU HIS THR
SEQRES   9 A  256  VAL ASP GLY VAL LYS TYR SER ALA GLU LEU HIS VAL ALA
SEQRES  10 A  256  HIS TRP ASN SER ALA LYS TYR SER SER LEU ALA GLU ALA
SEQRES  11 A  256  ALA SER LYS ALA ASP GLY LEU ALA VAL ILE GLY VAL LEU
SEQRES  12 A  256  MET LYS VAL GLY GLU ALA ASN PRO LYS LEU GLN LYS VAL
SEQRES  13 A  256  LEU ASP ALA LEU GLN ALA ILE LYS THR LYS GLY LYS ARG
SEQRES  14 A  256  ALA PRO PHE THR ASN PHE ASP PRO SER THR LEU LEU PRO
SEQRES  15 A  256  SER SER LEU ASP PHE TRP THR TYR PRO GLY SER LEU THR
SEQRES  16 A  256  HIS PRO PRO LEU TYR GLU SER VAL THR TRP ILE ILE CYS
SEQRES  17 A  256  LYS GLU SER ILE SER VAL SER SER GLU GLN LEU ALA GLN
SEQRES  18 A  256  PHE ARG SER LEU LEU SER ASN VAL GLU GLY ASP ASN ALA
SEQRES  19 A  256  VAL PRO MET GLN HIS ASN ASN ARG PRO THR GLN PRO LEU
SEQRES  20 A  256  LYS GLY ARG THR VAL ARG ALA SER PHE
SEQRES   1 B  256  TRP GLY TYR ASP ASP LYS ASN GLY PRO GLU GLN TRP SER
SEQRES   2 B  256  LYS LEU TYR PRO ILE ALA ASN GLY ASN ASN GLN SER PRO
SEQRES   3 B  256  VAL ASP ILE LYS THR SER GLU THR LYS HIS ASP THR SER
SEQRES   4 B  256  LEU LYS PRO ILE SER VAL SER TYR ASN PRO ALA THR ALA
SEQRES   5 B  256  LYS GLU ILE ILE ASN VAL GLY HIS SER PHE HIS VAL ASN
SEQRES   6 B  256  PHE GLU ASP ASN ASP ASN ARG SER VAL LEU LYS GLY GLY
SEQRES   7 B  256  PRO PHE SER ASP SER TYR ARG LEU PHE GLN PHE HIS PHE
SEQRES   8 B  256  HIS TRP GLY SER THR ASN GLU HIS GLY SER GLU HIS THR
SEQRES   9 B  256  VAL ASP GLY VAL LYS TYR SER ALA GLU LEU HIS VAL ALA
SEQRES  10 B  256  HIS TRP ASN SER ALA LYS TYR SER SER LEU ALA GLU ALA
SEQRES  11 B  256  ALA SER LYS ALA ASP GLY LEU ALA VAL ILE GLY VAL LEU
SEQRES  12 B  256  MET LYS VAL GLY GLU ALA ASN PRO LYS LEU GLN LYS VAL
SEQRES  13 B  256  LEU ASP ALA LEU GLN ALA ILE LYS THR LYS GLY LYS ARG
SEQRES  14 B  256  ALA PRO PHE THR ASN PHE ASP PRO SER THR LEU LEU PRO
SEQRES  15 B  256  SER SER LEU ASP PHE TRP THR TYR PRO GLY SER LEU THR
SEQRES  16 B  256  HIS PRO PRO LEU TYR GLU SER VAL THR TRP ILE ILE CYS
SEQRES  17 B  256  LYS GLU SER ILE SER VAL SER SER GLU GLN LEU ALA GLN
SEQRES  18 B  256  PHE ARG SER LEU LEU SER ASN VAL GLU GLY ASP ASN ALA
SEQRES  19 B  256  VAL PRO MET GLN HIS ASN ASN ARG PRO THR GLN PRO LEU
SEQRES  20 B  256  LYS GLY ARG THR VAL ARG ALA SER PHE
HET     ZN  A 561       1
HET     ZN  B 562       1
HET    PPF  A 500       7
HETNAM      ZN ZINC ION
HETNAM     PPF PHOSPHONOFORMIC ACID
FORMUL   3   ZN    2(ZN 2+)
FORMUL   5  PPF    C H3 O5 P
FORMUL   6  HOH   *344(H2 O)
HELIX    1   1 GLN A   15  LEU A   19  5                                   5
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  LYS A  168  5                                   4
HELIX    8   8 ASP A  180  LEU A  185  5                                   6
HELIX    9   9 SER A  219  LEU A  229  1                                  11
HELIX   10  10 GLY B   12  GLU B   14  5                                   3
HELIX   11  11 GLN B   15  TYR B   20  1                                   6
HELIX   12  12 PRO B   21  GLY B   25  5                                   5
HELIX   13  13 ASN B   52  ALA B   54  5                                   3
HELIX   14  14 SER B  130  ALA B  135  1                                   6
HELIX   15  15 ASN B  154  LYS B  156  5                                   3
HELIX   16  16 LEU B  157  LEU B  164  1                                   8
HELIX   17  17 GLN B  165  LYS B  168  5                                   4
HELIX   18  18 ASP B  180  LEU B  185  5                                   6
HELIX   19  19 SER B  219  SER B  228  1                                  10
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  VAL A 143   O  ILE A 210
SHEET    6   B10 ALA A 116  TRP A 123 -1  N  VAL A 120   O  ILE A 144
SHEET    7   B10 TYR A  88  TRP A  97 -1  N  ARG A  89   O  TRP A 123
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  ILE A  60   O  HIS A  67
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  TRP A 123 -1  O  TRP A 123   N  ARG A  89
SHEET    5   C 6 LEU A 141  VAL A 150 -1  O  ILE A 144   N  VAL A 120
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  VAL B 143   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  VAL B  68   O  PHE B  93
SHEET    9   E10 ALA B  56  ASN B  61 -1  N  ILE B  60   O  HIS B  67
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  SER B  50  0
SHEET    2   F 6 VAL B  78  GLY B  81 -1  O  LYS B  80   N  SER B  48
SHEET    3   F 6 TYR B  88  TRP B  97 -1  O  TYR B  88   N  LEU B  79
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         NE2 HIS A  94                ZN    ZN A 561     1555   1555  1.97
LINK         NE2 HIS A  96                ZN    ZN A 561     1555   1555  2.02
LINK         ND1 HIS A 119                ZN    ZN A 561     1555   1555  2.09
LINK         NE2 HIS B  94                ZN    ZN B 562     1555   1555  2.00
LINK         NE2 HIS B  96                ZN    ZN B 562     1555   1555  2.21
LINK         ND1 HIS B 119                ZN    ZN B 562     1555   1555  2.06
CISPEP   1 SER A   29    PRO A   30          0         2.79
CISPEP   2 PRO A  201    PRO A  202          0         6.05
CISPEP   3 SER B   29    PRO B   30          0         4.35
CISPEP   4 PRO B  201    PRO B  202          0         7.13
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  PPF A 500
SITE     1 AC2  4 HIS B  94  HIS B  96  HIS B 119  HOH B 740
SITE     1 AC3  9 HIS A  94  HIS A  96  HIS A 119  VAL A 143
SITE     2 AC3  9 LEU A 198  THR A 199  HIS A 200   ZN A 561
SITE     3 AC3  9 HOH A 710
CRYST1   62.580   69.510  120.440  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      0.015980  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014386  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008303        0.00000
      
PROCHECK
Go to PROCHECK summary
 References