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PDBsum entry 1lgd

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Lyase PDB id
1lgd
Jmol
Contents
Protein chain
257 a.a. *
Ligands
BCT
Metals
_ZN
Waters ×161
* Residue conservation analysis
HEADER    LYASE                                   15-APR-02   1LGD
TITLE     CRYSTAL STRUCTURE ANALYSIS OF HCA II MUTANT T199P IN
TITLE    2 COMPLEX WITH BICARBONATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE II;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE II, CA-II;
COMPND   5 EC: 4.2.1.1;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    HCAII MUTANT T199P-BCT COMPLEX, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.HUANG,B.SJOBLOM,A.E.SAUER-ERIKSSON,B.-H.JONSSON
REVDAT   3   24-FEB-09 1LGD    1       VERSN
REVDAT   2   01-APR-03 1LGD    1       JRNL
REVDAT   1   24-JUL-02 1LGD    0
JRNL        AUTH   S.HUANG,B.SJOBLOM,A.E.SAUER-ERIKSSON,B.H.JONSSON
JRNL        TITL   ORGANIZATION OF AN EFFICIENT CARBONIC ANHYDRASE:
JRNL        TITL 2 IMPLICATIONS FOR THE MECHANISM BASED ON
JRNL        TITL 3 STRUCTURE-FUNCTION STUDIES OF A T199P/C206S MUTANT.
JRNL        REF    BIOCHEMISTRY                  V.  41  7628 2002
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   12056894
JRNL        DOI    10.1021/BI020053O
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.7
REMARK   3   NUMBER OF REFLECTIONS             : 16497
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) : 0.189
REMARK   3   R VALUE            (WORKING SET) : 0.188
REMARK   3   FREE R VALUE                     : 0.214
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 894
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) : 1.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1185
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2650
REMARK   3   BIN FREE R VALUE SET COUNT          : 54
REMARK   3   BIN FREE R VALUE                    : 0.2820
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2049
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 5
REMARK   3   SOLVENT ATOMS            : 161
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.46
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.27000
REMARK   3    B22 (A**2) : 0.70000
REMARK   3    B33 (A**2) : -0.49000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.54000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.203
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.158
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.111
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.799
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2113 ; 0.011 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2865 ; 1.443 ; 1.945
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   255 ; 3.938 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   381 ;19.336 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   298 ; 0.108 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1631 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   878 ; 0.233 ; 0.300
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):   213 ; 0.150 ; 0.500
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):    16 ; 0.259 ; 0.300
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.150 ; 0.500
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):  1283 ; 0.786 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2063 ; 1.464 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   830 ; 2.188 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   802 ; 3.569 ; 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 : 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   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1LGD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-APR-02.
REMARK 100 THE RCSB ID CODE IS RCSB015925.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-98
REMARK 200  TEMPERATURE           (KELVIN) : 298
REMARK 200  PH                             : 7.8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : ENRAF-NONIUS FR591
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MAC SCIENCE DIP-2030H
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16497
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
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     (%) : 88.6
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.08900
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) : 1.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.8
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: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 2000 OR 3350, TRIS-HCL, BME.
REMARK 280  CRYSTALS ARE SOAKED IN BME-FREE SOLUTION IN THE PRESENCE OF
REMARK 280  BICARBONATE, PH 7.8, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       36.50600
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       22.29450
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       36.50600
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       22.29450
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     SER A     2
REMARK 465     HIS A     3
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    THR A 125   O   -  C   -  N   ANGL. DEV. = -14.1 DEGREES
REMARK 500    ASP A 162   CB  -  CG  -  OD2 ANGL. DEV. =   6.9 DEGREES
REMARK 500    ASP A 180   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 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    LYS A   9      -54.89     43.37
REMARK 500    LYS A  76      -81.70    -79.20
REMARK 500    LYS A 111       -1.71     74.66
REMARK 500    PHE A 176       79.55   -154.74
REMARK 500    ASN A 244       49.27    -91.09
REMARK 500    LYS A 252     -123.61     56.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    THR A 125         14.41
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 262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 119   ND1
REMARK 620 2 HIS A  94   NE2 116.9
REMARK 620 3 HIS A  96   NE2  96.8 108.9
REMARK 620 4 BCT A 263   O1  114.1  96.1 125.3
REMARK 620 5 BCT A 263   O2  150.6  92.3  74.6  56.0
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 ZN A 262
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT A 263
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LG5   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF HCA II MUTANT T199P IN
REMARK 900 COMPLEX WITH BETA-MERCAPTOETHANOL
REMARK 900 RELATED ID: 1LG6   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF HCA II MUTANT T199P IN
REMARK 900 COMPLEX WITH THIOCYANATE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE COORDINATE NUMBERING IS NOT SEQUENTIAL.
REMARK 999 THE RESIDUE NUMBER 126 IS NOT USED IN THE
REMARK 999 NUMBERING SCHEME.
DBREF  1LGD A    1   261  UNP    P00918   CAH2_HUMAN       0    259
SEQADV 1LGD PRO A  199  UNP  P00918    THR   197 ENGINEERED
SEQADV 1LGD SER A  206  UNP  P00918    CYS   204 CONFLICT
SEQRES   1 A  260  MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO
SEQRES   2 A  260  GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU
SEQRES   3 A  260  ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS
SEQRES   4 A  260  TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP
SEQRES   5 A  260  GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA
SEQRES   6 A  260  PHE ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL
SEQRES   7 A  260  LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE
SEQRES   8 A  260  GLN PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY
SEQRES   9 A  260  SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU
SEQRES  10 A  260  LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE
SEQRES  11 A  260  GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU
SEQRES  12 A  260  GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU
SEQRES  13 A  260  GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS
SEQRES  14 A  260  GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY
SEQRES  15 A  260  LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY
SEQRES  16 A  260  SER LEU PRO THR PRO PRO LEU LEU GLU SER VAL THR TRP
SEQRES  17 A  260  ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN
SEQRES  18 A  260  VAL LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES  19 A  260  GLU PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA
SEQRES  20 A  260  GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET     ZN  A 262       1
HET    BCT  A 263       4
HETNAM      ZN ZINC ION
HETNAM     BCT BICARBONATE ION
FORMUL   2   ZN    ZN 2+
FORMUL   3  BCT    C H O3 1-
FORMUL   4  HOH   *161(H2 O)
HELIX    1   1 HIS A   15  ASP A   19  5                                   5
HELIX    2   2 PHE A   20  GLY A   25  5                                   6
HELIX    3   3 LYS A  127  GLY A  129  5                                   3
HELIX    4   4 ASP A  130  VAL A  135  1                                   6
HELIX    5   5 LYS A  154  GLY A  156  5                                   3
HELIX    6   6 LEU A  157  ASP A  162  1                                   6
HELIX    7   7 VAL 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
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   B16 LYS A  39  TYR A  40  0
SHEET    2   B16 LYS A 257  ALA A 258  1  N  ALA A 258   O  LYS A  39
SHEET    3   B16 TYR A 191  GLY A 196 -1  O  THR A 193   N  LYS A 257
SHEET    4   B16 VAL A 207  LEU A 212 -1  O  VAL A 207   N  GLY A 196
SHEET    5   B16 LEU A 141  VAL A 150  1  O  LEU A 141   N  THR A 208
SHEET    6   B16 ILE A 216  VAL A 218  1  N  ILE A 216   O  PHE A 147
SHEET    7   B16 LEU A 141  VAL A 150  1  O  PHE A 147   N  ILE A 216
SHEET    8   B16 ALA A 116  ASN A 124 -1  O  ALA A 116   N  LEU A 148
SHEET    9   B16 TYR A  88  TRP A  97 -1  N  ARG A  89   O  TRP A 123
SHEET   10   B16 VAL A  78  GLY A  81 -1  N  LEU A  79   O  TYR A  88
SHEET   11   B16 LEU A  47  SER A  50 -1  N  SER A  48   O  LYS A  80
SHEET   12   B16 VAL A  78  GLY A  81 -1  O  VAL A  78   N  SER A  50
SHEET   13   B16 TYR A  88  TRP A  97 -1  O  TYR A  88   N  LEU A  79
SHEET   14   B16 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93
SHEET   15   B16 SER A  56  ASN A  61 -1  N  LEU A  57   O  GLU A  69
SHEET   16   B16 SER A 173  ASP A 175 -1  O  ALA A 174   N  ILE A  59
LINK        ZN    ZN A 262                 ND1 HIS A 119     1555   1555  2.09
LINK        ZN    ZN A 262                 NE2 HIS A  94     1555   1555  1.98
LINK        ZN    ZN A 262                 NE2 HIS A  96     1555   1555  2.02
LINK        ZN    ZN A 262                 O1  BCT A 263     1555   1555  2.00
LINK        ZN    ZN A 262                 O2  BCT A 263     1555   1555  2.69
CISPEP   1 SER A   29    PRO A   30          0         1.41
CISPEP   2 PRO A  201    PRO A  202          0         7.33
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  BCT A 263
SITE     1 AC2  9 HIS A  94  HIS A  96  HIS A 119  PRO A 199
SITE     2 AC2  9 THR A 200   ZN A 262  HOH A 292  HOH A 389
SITE     3 AC2  9 HOH A 502
CRYST1   73.012   44.589   76.636  90.00  92.82  90.00 C 1 2 1       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      0.013696  0.000000  0.000674        0.00000
SCALE2      0.000000  0.022427  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013064        0.00000
      
PROCHECK
Go to PROCHECK summary
 References

 

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