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PDBsum entry 1hug

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Lyase(oxo-acid) PDB id
1hug
Jmol
Contents
Protein chain
256 a.a.
Ligands
AUC ×4
Metals
_ZN
Waters ×231
HEADER    LYASE(OXO-ACID)                         28-OCT-93   1HUG
TITLE     DIFFERENCES IN ANIONIC INHIBITION OF HUMAN CARBONIC
TITLE    2 ANHYDRASE I REVEALED FROM THE STRUCTURES OF IODIDE AND GOLD
TITLE    3 CYANIDE INHIBITOR COMPLEXES
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE I;
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    LYASE(OXO-ACID)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    V.KUMAR,K.K.KANNAN
REVDAT   3   10-NOV-09 1HUG    1       HETATM
REVDAT   2   24-FEB-09 1HUG    1       VERSN
REVDAT   1   30-APR-94 1HUG    0
JRNL        AUTH   V.KUMAR,K.K.KANNAN,P.SATHYAMURTHI
JRNL        TITL   DIFFERENCES IN ANIONIC INHIBITION OF HUMAN CARBONIC
JRNL        TITL 2 ANHYDRASE I REVEALED FROM THE STRUCTURES OF IODIDE
JRNL        TITL 3 AND GOLD CYANIDE INHIBITOR COMPLEXES.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  50   731 1994
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   15299369
JRNL        DOI    10.1107/S0907444994001873
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   V.KUMAR,K.K.KANNAN
REMARK   1  TITL   STRUCTURE OF HUMAN CARBONIC ANHYDRASE COMPLEXED
REMARK   1  TITL 2 WITH GOLD CYANIDE INHIBITOR: INHIBITION MECHANISM
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.A      V.  49    92 1993
REMARK   1  REFN                   ISSN 0108-7673
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PROLSQ
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 14549
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 + TEST SET) : 0.171
REMARK   3   R VALUE            (WORKING SET) : NULL
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
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2008
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 11
REMARK   3   SOLVENT ATOMS            : 231
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  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : 0.017 ; NULL
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS:
REMARK   3  THE POTENTIAL SOLVENT SITES WERE IDENTIFIED FROM FO-FC MAP
REMARK   3  IF THE PEAK HEIGHT WERE MORE THAN 3 TIMES THE  S.D  OF THE
REMARK   3  MAP AND WERE WITHIN THE H-BONDING DISTANCE TO A
REMARK   3  DONOR/ACCEPTOR ATOM.  SOLVENTS WERE ADDED TO THE COORDINATE
REMARK   3  LIST IF ELECTRON DENSITY WAS ALSO OBSERVED IN (2FO - FC)
REMARK   3  MAP.  IN ADDITION TO POSITIONAL AND ISOTROPIC THERMAL
REMARK   3  PARAMETER, OCCUPANCY WAS ALSO REFINED FOR THE SOLVENT
REMARK   3  MOLECULES.  SOLVENTS WHICH REFINED TO HIGH B-VALUE (>58A2),
REMARK   3  LOW OCCUPANCY (<30 PER CENT) WERE NOT INCLUDED IN THE MODEL
REMARK   3  DURING SUBSEQUENT STAGES OF REFINEMENT.  THE SUBMITTED
REMARK   3  MODEL HAS 231 SOLVENT MOLECULES OUT OF WHICH 70 SOLVENTS
REMARK   3  ARE WITH PARTIAL OXYGEN OCCUPANCY.
REMARK   3
REMARK   3  THE SIDE CHAINS OF RESIDUES ASP 9, LYS 10, ARG 173 AND GLU
REMARK   3  221 SHOW VERY POOR ELECTRON DENSITY IN THE FOURIER MAPS.
REMARK   3
REMARK   3  ATOM AU 501 IS THE PARTIAL OVERLAPPING BINDING SITE OF THE HET
REMARK   3  AUC 500 GROUP.
REMARK   4
REMARK   4 1HUG 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   (%): 37.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
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       40.90000
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       37.60000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       18.55000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.90000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.60000
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 400
REMARK 400 COMPOUND
REMARK 400 THE RESIDUES DEFINING THE CAT SITE CONSTITUTE THE CATALYTIC
REMARK 400 ACTIVE SITE OF THE ENZYME. INHIBITOR GOLD CYANIDE ANION BINDS IN
REMARK 400 THE POCKET DEFINED BY THESE RESIDUES AND ACCEPTS A H-BOND FROM
REMARK 400 THE ACTIVITY LINKED HYDROXYL GROUP BOUND TO THE ZINC ION. THE
REMARK 400 CONFORMATIONAL REORIENTATION IN THE HYDROXYL GROUP DUE TO H-BOND
REMARK 400 WITH THE INHIBITOR ANION, RENDERS THE ENZYME INACTIVE.
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 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    ASP A  86   CB  -  CA  -  C   ANGL. DEV. =  13.7 DEGREES
REMARK 500    ASP A  86   CB  -  CG  -  OD2 ANGL. DEV. =   9.3 DEGREES
REMARK 500    ARG A  89   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES
REMARK 500    ASP A 162   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES
REMARK 500    ARG A 173   CG  -  CD  -  NE  ANGL. DEV. =  16.5 DEGREES
REMARK 500    ARG A 173   CD  -  NE  -  CZ  ANGL. DEV. =  14.0 DEGREES
REMARK 500    ARG A 173   NH1 -  CZ  -  NH2 ANGL. DEV. =   7.1 DEGREES
REMARK 500    ARG A 173   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES
REMARK 500    ASP A 190   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES
REMARK 500    ARG A 227   CD  -  NE  -  CZ  ANGL. DEV. =   9.5 DEGREES
REMARK 500    ARG A 227   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    ARG A 246   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.6 DEGREES
REMARK 500    ARG A 246   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG A 246   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG A 257   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 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       19.05   -143.34
REMARK 500    LYS A  57      -62.28   -122.39
REMARK 500    SER A  65     -170.06   -172.05
REMARK 500    ASN A  75       31.54    -97.09
REMARK 500    VAL A 218      149.49   -170.45
REMARK 500    ASN A 244       36.57   -151.48
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 A 391        DISTANCE =  6.15 ANGSTROMS
REMARK 525    HOH A 393        DISTANCE =  5.51 ANGSTROMS
REMARK 525    HOH A 396        DISTANCE = 13.32 ANGSTROMS
REMARK 525    HOH A 412        DISTANCE =  7.52 ANGSTROMS
REMARK 525    HOH A 429        DISTANCE = 36.74 ANGSTROMS
REMARK 525    HOH A 430        DISTANCE =  6.87 ANGSTROMS
REMARK 525    HOH A 465        DISTANCE =  5.11 ANGSTROMS
REMARK 525    HOH A 477        DISTANCE = 35.55 ANGSTROMS
REMARK 525    HOH A 479        DISTANCE =  6.93 ANGSTROMS
REMARK 525    HOH A 485        DISTANCE =  5.01 ANGSTROMS
REMARK 525    HOH A 490        DISTANCE =  5.05 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 ATOM ZN IS ESSENTIAL METAL ION
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     AUC A  501
REMARK 610     AUC A  502
REMARK 610     AUC A  503
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  94   NE2
REMARK 620 2 HIS A  96   NE2 103.9
REMARK 620 3 HIS A 119   ND1 111.2  98.1
REMARK 620 4 HOH A 300   O   114.6 117.8 110.1
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 261
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC A 500
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC A 501
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC A 502
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC A 503
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 ON THE BASIS OF HUMAN CARBONIC ANHYDRASE - BICARBONATE
REMARK 999 COMPLEX STRUCTURE (VINAY KUMAR AND K.K. KANNAN,
REMARK 999 UNPUBLISHED RESULTS) AND REFINED STRUCTURE OF THE TITLE
REMARK 999 COMPOUND, THE FOLLOWING SEQUENCE MODIFICATION IN THE
REMARK 999 NATIVE HUMAN CARBONIC ANHYDRASE ATOMIC MODEL (PDB IDENT
REMARK 999 CODE 2CAB, VERSION OF 10/84) HAVE BEEN MADE IN THE
REMARK 999 SUBMITTED ATOMIC MODEL.
REMARK 999
REMARK 999 SEQUENCE NUMBER     74     75
REMARK 999 RESIDUE TYPE        ASP    ASN
REMARK 999 THESE CHANGES ARE CONSISTENT WITH THE KNOWN CHEMICAL
REMARK 999 SEQUENCE OF HUMAN CARBONIC ANHYDRASE I ENZYME.
DBREF  1HUG A    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
HET     ZN  A 261       1
HET    AUC  A 500       5
HET    AUC  A 501       1
HET    AUC  A 502       1
HET    AUC  A 503       3
HETNAM      ZN ZINC ION
HETNAM     AUC GOLD (I) CYANIDE ION
FORMUL   2   ZN    ZN 2+
FORMUL   3  AUC    4(C2 AU N2)
FORMUL   7  HOH   *231(H2 O)
HELIX    1  HA PRO A   13  LYS A   18  5                                   6
HELIX    2  HB PRO A   21  ASN A   24  5                                   4
HELIX    3  HC PRO A   53  THR A   55  5                                   3
HELIX    4  HD LEU A  131  ALA A  134  1                                   4
HELIX    5  HE PRO A  155  LEU A  157  5                                   3
HELIX    6  HF GLN A  158  ASP A  162  1                                   5
HELIX    7  HG ALA A  163  ILE A  167  5                                   5
HELIX    8  HH PRO A  181  LEU A  184  5                                   4
HELIX    9  HI SER A  219  ARG A  227  1                                   9
SHEET    1 B1A10 LYS A  39  HIS A  40  0
SHEET    2 B1A10 ARG A 257  ALA A 258  1
SHEET    3 B1A10 PHE A 191  GLY A 196 -1
SHEET    4 B1A10 VAL A 207  CYS A 212 -1
SHEET    5 B1A10 LEU A 141  VAL A 150  1
SHEET    6 B1A10 ALA A 116  TRP A 123 -1
SHEET    7 B1A10 TYR A  88  TRP A  97 -1
SHEET    8 B1A10 PHE A  66  PHE A  70 -1
SHEET    9 B1A10 ALA A  56  ASN A  61 -1
SHEET   10 B1A10 ARG A 173  PRO A 175 -1
SHEET    1 B1B 7 ILE A 216  VAL A 218  0
SHEET    2 B1B 7 LEU A 141  VAL A 150  1
SHEET    3 B1B 7 ALA A 116  TRP A 123 -1
SHEET    4 B1B 7 TYR A  88  TRP A  97 -1
SHEET    5 B1B 7 PHE A  66  PHE A  70 -1
SHEET    6 B1B 7 ALA A  56  ASN A  61 -1
SHEET    7 B1B 7 ARG A 173  PRO A 175 -1
SHEET    1  B2 3 ILE A  47  SER A  50  0
SHEET    2  B2 3 VAL A  78  GLY A  81 -1
SHEET    3  B2 3 TYR A  88  TRP A  97 -1
LINK         NE2 HIS A  94                ZN    ZN A 261     1555   1555  1.92
LINK         NE2 HIS A  96                ZN    ZN A 261     1555   1555  1.99
LINK         ND1 HIS A 119                ZN    ZN A 261     1555   1555  2.02
LINK        ZN    ZN A 261                 O   HOH A 300     1555   1555  2.34
CISPEP   1 SER A   29    PRO A   30          0        -0.40
CISPEP   2 PRO A  201    PRO A  202          0         2.05
SITE     1 AC1  5 HIS A  94  HIS A  96  HIS A 119  HOH A 300
SITE     2 AC1  5 AUC A 500
SITE     1 AC2  5 PHE A  91  HIS A  94   ZN A 261  HOH A 300
SITE     2 AC2  5 HOH A 423
SITE     1 AC3  1 PHE A  91
SITE     1 AC4  1 ASN A 178
SITE     1 AC5  3 ASN A  26  ASN A  27  HOH A 380
CRYST1   81.800   75.200   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      0.012225  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013298  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026954        0.00000
      
PROCHECK
Go to PROCHECK summary
 References