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PDBsum entry 3w6h

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Lyase PDB id
3w6h
Jmol
Contents
Protein chains
256 a.a.
Ligands
FLB ×2
AZM ×2
Metals
_ZN ×2
HEADER    LYASE                                   14-FEB-13   3W6H
TITLE     CRYSTAL STRUCTURE OF 19F PROBE-LABELED HCAI IN COMPLEX WITH
TITLE    2 ACETAZOLAMIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 1;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE I, CARBONIC ANHYDRASE B, CAB, CARBONIC
COMPND   5 ANHYDRASE I, CA-I;
COMPND   6 EC: 4.2.1.1;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: CA1;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    19F-NMR, SEMISYNTHETIC BIOSENSOR, CHEMICAL BIOLOGY, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.TAKAOKA,Y.KIOI,A.MORITO,J.OTANI,K.ARITA,E.ASHIHARA,M.ARIYOSHI,
AUTHOR   2 H.TOCHIO,M.SHIRAKAWA,I.HAMACHI
REVDAT   1   13-MAR-13 3W6H    0
JRNL        AUTH   Y.TAKAOKA,Y.KIOI,A.MORITO,J.OTANI,K.ARITA,E.ASHIHARA,
JRNL        AUTH 2 M.ARIYOSHI,H.TOCHIO,M.SHIRAKAWA,I.HAMACHI
JRNL        TITL   QUANTITATIVE COMPARISON OF PROTEIN DYNAMICS IN LIVE CELLS
JRNL        TITL 2 AND IN VITRO BY IN-CELL 19F-NMR
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.96 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.1_743)
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) : 2.96
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.21
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 10451
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.228
REMARK   3   R VALUE            (WORKING SET) : 0.222
REMARK   3   FREE R VALUE                     : 0.283
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.850
REMARK   3   FREE R VALUE TEST SET COUNT      : 1029
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 34.2088 -  5.6620    1.00     1437   179  0.2214 0.2693
REMARK   3     2  5.6620 -  4.4973    1.00     1399   142  0.1818 0.2226
REMARK   3     3  4.4973 -  3.9297    1.00     1354   156  0.1916 0.2620
REMARK   3     4  3.9297 -  3.5709    1.00     1357   155  0.2170 0.2883
REMARK   3     5  3.5709 -  3.3151    1.00     1344   147  0.2511 0.3119
REMARK   3     6  3.3151 -  3.1198    1.00     1335   141  0.2662 0.3511
REMARK   3     7  3.1198 -  2.9637    0.87     1196   109  0.3110 0.4345
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.30
REMARK   3   SHRINKAGE RADIUS   : 1.06
REMARK   3   K_SOL              : 0.32
REMARK   3   B_SOL              : 20.54
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.740
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.010
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) : -1.63210
REMARK   3    B22 (A**2) : 14.62450
REMARK   3    B33 (A**2) : -12.99240
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  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      :  0.009           4198
REMARK   3   ANGLE     :  1.235           5722
REMARK   3   CHIRALITY :  0.102            602
REMARK   3   PLANARITY :  0.005            740
REMARK   3   DIHEDRAL  : 19.904           1554
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : 1
REMARK   3   NCS GROUP : 1
REMARK   3    NCS OPERATOR : 1
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 5:17 OR RESSEQ 20:66
REMARK   3                          OR RESSEQ 68:260 )
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 5:17 OR RESSEQ 20:66
REMARK   3                          OR RESSEQ 68:260 )
REMARK   3     ATOM PAIRS NUMBER  : 1981
REMARK   3     RMSD               : 0.076
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3W6H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-FEB-13.
REMARK 100 THE RCSB ID CODE IS RCSB095946.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 28-JUN-09
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : 6.3
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SPRING-8
REMARK 200  BEAMLINE                       : BL38B1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10494
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.964
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 4.700
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.15700
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.55100
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2CBA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 41.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23 OR 25% POLYETHYLENE GLYCOL (PEG)
REMARK 280  3350, 200MM NACL, 100MM MES (PH 6.3), VAPOR DIFFUSION, HANGING
REMARK 280  DROP, TEMPERATURE 297K
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       31.01950
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.24250
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.64000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.24250
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.01950
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.64000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     ALA A     1
REMARK 465     SER A     2
REMARK 465     PRO A     3
REMARK 465     ASP A     4
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   OG1  THR B   199     N1   AZM B   303              2.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG A 246   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ARG A 246   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.5 DEGREES
REMARK 500    ARG A 257   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.7 DEGREES
REMARK 500    ARG A 257   NE  -  CZ  -  NH2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ARG B 246   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ARG B 246   NE  -  CZ  -  NH2 ANGL. DEV. =   7.0 DEGREES
REMARK 500    ARG B 257   NE  -  CZ  -  NH1 ANGL. DEV. =   6.0 DEGREES
REMARK 500    ARG B 257   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASN A  11       14.28   -154.50
REMARK 500    LYS A  18       31.80    -69.17
REMARK 500    LEU A  19      -59.57   -155.23
REMARK 500    LYS A  57      -66.72   -101.41
REMARK 500    SER A  65     -169.33   -164.22
REMARK 500    THR A 100     -163.77   -122.18
REMARK 500    HIS A 103       84.70   -174.36
REMARK 500    ASN A 178       78.83     53.87
REMARK 500    ASN A 237     -160.98    -56.79
REMARK 500    ASN A 244       41.00   -158.16
REMARK 500    ASN B  11       15.30   -155.74
REMARK 500    SER B  17       14.81    -54.27
REMARK 500    LYS B  18      -75.19   -104.71
REMARK 500    LYS B  57      -67.39   -103.43
REMARK 500    SER B  65     -166.70   -164.95
REMARK 500    THR B 100     -164.89   -125.77
REMARK 500    HIS B 103       85.02   -172.58
REMARK 500    ASN B 178       78.88     52.75
REMARK 500    ASN B 237     -160.38    -55.33
REMARK 500    ASN B 244       39.86   -160.33
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 B 302  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B  94   NE2
REMARK 620 2 HIS B  96   NE2 105.0
REMARK 620 3 HIS B 119   ND1 112.9 100.4
REMARK 620 4 AZM B 303   O2   95.5 144.9  97.3
REMARK 620 5 AZM B 303   N1  124.0  95.9 113.5  49.2
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 302  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  94   NE2
REMARK 620 2 HIS A  96   NE2 105.0
REMARK 620 3 AZM A 303   N1  117.1 102.0
REMARK 620 4 HIS A 119   ND1 111.9 103.9 115.0
REMARK 620 5 AZM A 303   O2   83.5 152.4  52.0  96.8
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLB A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZM A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLB B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZM B 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3W6I   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 19F PROBE-LABELED HCAI
DBREF  3W6H A    1   260  UNP    P00915   CAH1_HUMAN       2    261
DBREF  3W6H B    1   260  UNP    P00915   CAH1_HUMAN       2    261
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    FLB  A 301      20
HET     ZN  A 302       1
HET    AZM  A 303      13
HET    FLB  B 301      20
HET     ZN  B 302       1
HET    AZM  B 303      13
HETNAM     FLB 1-(2-ETHOXYETHOXY)-3,5-BIS(TRIFLUOROMETHYL)BENZENE
HETNAM      ZN ZINC ION
HETNAM     AZM 5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE
FORMUL   3  FLB    2(C12 H12 F6 O2)
FORMUL   4   ZN    2(ZN 2+)
FORMUL   5  AZM    2(C4 H6 N4 O3 S2)
HELIX    1   1 GLY A   12  TRP A   16  5                                   5
HELIX    2   2 TYR A   20  GLY A   25  5                                   6
HELIX    3   3 LYS A   34  THR A   38  5                                   5
HELIX    4   4 ASN A   52  ALA A   54  5                                   3
HELIX    5   5 SER A  130  SER A  136  1                                   7
HELIX    6   6 ASN A  154  ASP A  162  1                                   9
HELIX    7   7 ALA A  163  LYS A  168  5                                   6
HELIX    8   8 ASP A  180  LEU A  185  5                                   6
HELIX    9   9 SER A  219  ARG A  227  1                                   9
HELIX   10  10 GLY B   12  TRP B   16  5                                   5
HELIX   11  11 TYR B   20  GLY B   25  5                                   6
HELIX   12  12 LYS B   34  THR B   38  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  ASP B  162  1                                   9
HELIX   16  16 ALA B  163  LYS B  168  5                                   6
HELIX   17  17 ASP B  180  LEU B  185  5                                   6
HELIX   18  18 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  ILE A 211   N  TRP A 192
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  VAL A 146
SHEET    7   B10 PHE A  84  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  GLU A  58   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 PHE A  84  TRP A  97 -1  O  TYR A  88   N  LEU A  79
SHEET    4   C 6 ALA A 116  ASN A 124 -1  O  TRP A 123   N  ARG A  89
SHEET    5   C 6 LEU A 141  VAL A 150 -1  O  VAL A 146   N  LEU A 118
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   E 9 LYS B  39  HIS B  40  0
SHEET    2   E 9 ARG B 257  ALA B 258  1  O  ALA B 258   N  LYS B  39
SHEET    3   E 9 PHE B 191  GLY B 196 -1  N  THR B 193   O  ARG B 257
SHEET    4   E 9 VAL B 207  VAL B 218 -1  O  ILE B 211   N  TRP B 192
SHEET    5   E 9 LEU B 141  VAL B 150  1  N  GLY B 145   O  ILE B 210
SHEET    6   E 9 ALA B 116  ASN B 124 -1  N  LEU B 118   O  VAL B 146
SHEET    7   E 9 PHE B  84  TRP B  97 -1  N  ARG B  89   O  TRP B 123
SHEET    8   E 9 VAL B  78  GLY B  81 -1  N  LEU B  79   O  TYR B  88
SHEET    9   E 9 ILE B  47  SER B  50 -1  N  SER B  48   O  LYS B  80
SHEET    1   F10 LYS B  39  HIS B  40  0
SHEET    2   F10 ARG B 257  ALA B 258  1  O  ALA B 258   N  LYS B  39
SHEET    3   F10 PHE B 191  GLY B 196 -1  N  THR B 193   O  ARG B 257
SHEET    4   F10 VAL B 207  VAL B 218 -1  O  ILE B 211   N  TRP B 192
SHEET    5   F10 LEU B 141  VAL B 150  1  N  GLY B 145   O  ILE B 210
SHEET    6   F10 ALA B 116  ASN B 124 -1  N  LEU B 118   O  VAL B 146
SHEET    7   F10 PHE B  84  TRP B  97 -1  N  ARG B  89   O  TRP B 123
SHEET    8   F10 PHE B  66  PHE B  70 -1  N  VAL B  68   O  PHE B  93
SHEET    9   F10 ALA B  56  ASN B  61 -1  N  GLU B  58   O  ASN B  69
SHEET   10   F10 ARG B 173  PRO B 175 -1  O  ALA B 174   N  ILE B  59
LINK         ND1 HIS A  67                 C1  FLB A 301     1555   1555  1.48
LINK         ND1 HIS B  67                 C1  FLB B 301     1555   1555  1.48
LINK         NE2 HIS B  94                ZN    ZN B 302     1555   1555  2.02
LINK         NE2 HIS A  94                ZN    ZN A 302     1555   1555  2.10
LINK         NE2 HIS A  96                ZN    ZN A 302     1555   1555  2.16
LINK        ZN    ZN A 302                 N1  AZM A 303     1555   1555  2.17
LINK         ND1 HIS A 119                ZN    ZN A 302     1555   1555  2.19
LINK         NE2 HIS B  96                ZN    ZN B 302     1555   1555  2.21
LINK         ND1 HIS B 119                ZN    ZN B 302     1555   1555  2.25
LINK        ZN    ZN B 302                 O2  AZM B 303     1555   1555  2.47
LINK        ZN    ZN A 302                 O2  AZM A 303     1555   1555  2.63
LINK        ZN    ZN B 302                 N1  AZM B 303     1555   1555  2.68
CISPEP   1 SER A   29    PRO A   30          0         0.09
CISPEP   2 PRO A  201    PRO A  202          0        10.22
CISPEP   3 SER B   29    PRO B   30          0        -0.63
CISPEP   4 PRO B  201    PRO B  202          0        10.90
SITE     1 AC1 13 VAL A  62  HIS A  67  ASN A  69  PHE A  91
SITE     2 AC1 13 GLN A  92  ALA A 132  ALA A 135  LEU A 198
SITE     3 AC1 13 PRO A 202  AZM A 303  ALA B 132  TYR B 204
SITE     4 AC1 13 FLB B 301
SITE     1 AC2  4 HIS A  94  HIS A  96  HIS A 119  AZM A 303
SITE     1 AC3  9 GLN A  92  HIS A  94  HIS A  96  HIS A 119
SITE     2 AC3  9 LEU A 198  THR A 199  HIS A 200  FLB A 301
SITE     3 AC3  9  ZN A 302
SITE     1 AC4 15 SER A 130  LEU A 131  ALA A 132  FLB A 301
SITE     2 AC4 15 VAL B  62  HIS B  67  ASN B  69  PHE B  91
SITE     3 AC4 15 GLN B  92  LEU B 131  ALA B 132  ALA B 135
SITE     4 AC4 15 LEU B 141  LEU B 198  AZM B 303
SITE     1 AC5  4 HIS B  94  HIS B  96  HIS B 119  AZM B 303
SITE     1 AC6  9 GLN B  92  HIS B  94  HIS B  96  HIS B 119
SITE     2 AC6  9 LEU B 198  THR B 199  HIS B 200  FLB B 301
SITE     3 AC6  9  ZN B 302
CRYST1   62.039   65.280  120.485  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      0.016119  0.000000  0.000000        0.00000
SCALE2      0.000000  0.015319  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008300        0.00000
      
PROCHECK
Go to PROCHECK summary
 References

 

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