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PDBsum entry 1j9w

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Lyase PDB id
1j9w
Jmol
Contents
Protein chains
257 a.a. *
Ligands
EDO ×2
Metals
_ZN ×2
Waters ×321
* Residue conservation analysis
HEADER    LYASE                                   29-MAY-01   1J9W
TITLE     SOLUTION STRUCTURE OF THE CAI MICHIGAN 1 VARIANT
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE I;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE I;
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;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PKK232-2
KEYWDS    10-STRANDED-BETA-SHEET, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    F.BRIGANTI,M FERRARONI,W.R.CHEDWIGGEN,A.SCOZZAFAVA,C.T.SUPURAN,
AUTHOR   2 S.TILLI
REVDAT   4   26-MAR-14 1J9W    1       REMARK VERSN
REVDAT   3   24-FEB-09 1J9W    1       VERSN
REVDAT   2   21-JUN-05 1J9W    1       JRNL
REVDAT   1   13-JUN-01 1J9W    0
JRNL        AUTH   M.FERRARONI,S.TILLI,F.BRIGANTI,W.R.CHEGWIDDEN,C.T.SUPURAN,
JRNL        AUTH 2 K.E.WIEBAUER,R.E.TASHIAN,A.SCOZZAFAVA
JRNL        TITL   CRYSTAL STRUCTURE OF A ZINC-ACTIVATED VARIANT OF HUMAN
JRNL        TITL 2 CARBONIC ANHYDRASE I, CA I MICHIGAN 1: EVIDENCE FOR A SECOND
JRNL        TITL 3 ZINC BINDING SITE INVOLVING ARGININE COORDINATION.
JRNL        REF    BIOCHEMISTRY                  V.  41  6237 2002
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   12009884
JRNL        DOI    10.1021/BI0120446
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   C.R.SHAW,F.N.SYNER,R.E.TASHIAN
REMARK   1  TITL   NEW GENETICALLY DETERMINED MOLECULAR FORM OF ERYTHROCYTE
REMARK   1  TITL 2 ESTERASE IN MAN.
REMARK   1  REF    SCIENCE                       V. 138    31 1962
REMARK   1  REFN                   ISSN 0036-8075
REMARK   1  PMID   13911449
REMARK   1 REFERENCE 2
REMARK   1  AUTH   W.R.CHEGWIDDEN,L.E.WAGNER,P.J.VENTA,N.C.BERGENHEM,Y.S.YU,
REMARK   1  AUTH 2 R.E.TASHIAN
REMARK   1  TITL   MARKED ZINC ACTIVATION OF ESTER HYDROLYSIS BY A MUTATION,
REMARK   1  TITL 2 67-HIS (CAT) TO ARG (CGT), IN THE ACTIVE SITE OF HUMAN
REMARK   1  TITL 3 CARBONIC ANHYDRASE I.
REMARK   1  REF    HUM.MUTAT.                    V.   4   294 1994
REMARK   1  REFN                   ISSN 1059-7794
REMARK   1  PMID   7866410
REMARK   1  DOI    10.1002/HUMU.1380040411
REMARK   1 REFERENCE 3
REMARK   1  AUTH   F.BRIGANTI,W.R.CHEGWIDDEN,A.SCOZZAFAVA,C.T.SUPURAN,
REMARK   1  AUTH 2 R.E.TASHIAN,K.E.WIEBAUER
REMARK   1  TITL   POINT MUTATION IN THE VARIANT OF HUMAN CARBONIC ANHYDRASE
REMARK   1  TITL 2 ISOZYME I (CAI MICHIGAN ) ACTIVE SITE DECREASES AFFINITY FOR
REMARK   1  TITL 3 AROMATIC SULFONAMIDE INHIBITORS
REMARK   1  REF    GENE FAM.LSOZYME BULL.        V.  31    43 1998
REMARK   1  REFN
REMARK   2
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : NULL
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) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.205
REMARK   3   FREE R VALUE                     : 0.311
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 877
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3974
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 10
REMARK   3   SOLVENT ATOMS            : 321
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 24.36
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.82
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  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : 0.008 ; 0.020
REMARK   3    ANGLE DISTANCE                  (A) : 0.040 ; 0.050
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.079 ; 0.050
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) : 13.200; 7.000
REMARK   3    STAGGERED                 (DEGREES) : 16.400; 15.000
REMARK   3    TRANSVERSE                (DEGREES) : 29.700; 20.000
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.030 ; 2.000
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.795 ; 3.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.087 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 1.793 ; 3.000
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1J9W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAY-01.
REMARK 100 THE RCSB ID CODE IS RCSB013542.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 26-MAY-00
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               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : MACSCIENCE M12XHF
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GOBEL MIRRORS
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : BRUKER SMART 1000
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200  DATA SCALING SOFTWARE          : SAINT
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58715
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9
REMARK 200  DATA REDUNDANCY                : 3.300
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.09400
REMARK 200   FOR THE DATA SET  : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.24400
REMARK 200   FOR SHELL         : 1.500
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: PDB ENTRY 1CZM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 45.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, LITIUM CHLORIDE,ETHYLENE
REMARK 280  GLICOL , PH 9.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
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       30.93750
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.19600
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.86600
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.19600
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.93750
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.86600
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER GENERATED BY A
REMARK 300 TRANSLATION
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     ALA A     1
REMARK 465     SER A     2
REMARK 465     PRO A     3
REMARK 465     ALA B     1
REMARK 465     SER B     2
REMARK 465     PRO B     3
REMARK 465     ASP B     4
REMARK 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     LYS A  39    CG   CD   CE   NZ
REMARK 470     LYS A  45    CG   CD   CE   NZ
REMARK 470     LYS A  80    CB   CG   CD   CE   NZ
REMARK 470     LEU A 189    CB   CG   CD1  CD2
REMARK 470     ASN A 237    CG   OD1  ND2
REMARK 470     ASP B   9    CB   CG   OD1  OD2
REMARK 470     LYS B  10    CB   CG   CD   CE   NZ
REMARK 470     GLU B  14    CG   CD   OE1  OE2
REMARK 470     LYS B  34    CG   CD   CE   NZ
REMARK 470     LYS B  80    CG   CD   CE   NZ
REMARK 470     GLU B 102    CB   CG   CD   OE1  OE2
REMARK 470     HIS B 103    CB   CG   ND1  CD2  CE1  NE2
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    TRP A   5   N   -  CA  -  CB  ANGL. DEV. =  11.8 DEGREES
REMARK 500    TRP A   5   C   -  N   -  CA  ANGL. DEV. =  15.4 DEGREES
REMARK 500    GLU A  14   CA  -  CB  -  CG  ANGL. DEV. =  16.0 DEGREES
REMARK 500    SER A  29   CA  -  C   -  O   ANGL. DEV. = -15.7 DEGREES
REMARK 500    PRO A  30   CA  -  N   -  CD  ANGL. DEV. = -13.8 DEGREES
REMARK 500    PRO A  30   N   -  CA  -  CB  ANGL. DEV. =   7.5 DEGREES
REMARK 500    PRO A  30   N   -  CD  -  CG  ANGL. DEV. =   8.4 DEGREES
REMARK 500    SER A  29   O   -  C   -  N   ANGL. DEV. =  15.2 DEGREES
REMARK 500    GLU A  58   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.2 DEGREES
REMARK 500    ARG A  67   CD  -  NE  -  CZ  ANGL. DEV. =   9.2 DEGREES
REMARK 500    ASP A  74   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ARG A  76   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ARG A  76   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ARG A  89   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    ASP A 110   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES
REMARK 500    ASP A 162   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES
REMARK 500    GLN A 165   CB  -  CA  -  C   ANGL. DEV. =  18.6 DEGREES
REMARK 500    GLN A 165   N   -  CA  -  CB  ANGL. DEV. = -11.1 DEGREES
REMARK 500    ALA A 166   CB  -  CA  -  C   ANGL. DEV. =  -9.6 DEGREES
REMARK 500    GLN A 165   O   -  C   -  N   ANGL. DEV. = -12.5 DEGREES
REMARK 500    ARG A 173   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ASP A 180   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ASP A 190   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ASP A 190   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES
REMARK 500    PRO A 201   CA  -  C   -  O   ANGL. DEV. = -27.9 DEGREES
REMARK 500    PRO A 202   CA  -  N   -  CD  ANGL. DEV. = -19.2 DEGREES
REMARK 500    PRO A 201   CA  -  C   -  N   ANGL. DEV. =  25.0 DEGREES
REMARK 500    PRO A 201   O   -  C   -  N   ANGL. DEV. = -14.1 DEGREES
REMARK 500    PRO A 202   C   -  N   -  CD  ANGL. DEV. = -16.7 DEGREES
REMARK 500    ARG A 227   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ARG A 246   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG A 246   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES
REMARK 500    ARG A 257   NE  -  CZ  -  NH1 ANGL. DEV. =   7.0 DEGREES
REMARK 500    ARG A 257   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES
REMARK 500    SER B  29   N   -  CA  -  C   ANGL. DEV. =  17.2 DEGREES
REMARK 500    SER B  29   CA  -  C   -  O   ANGL. DEV. = -12.7 DEGREES
REMARK 500    SER B  29   O   -  C   -  N   ANGL. DEV. =  20.2 DEGREES
REMARK 500    TYR B 114   CB  -  CG  -  CD2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    MET B 148   CA  -  CB  -  CG  ANGL. DEV. =  10.3 DEGREES
REMARK 500    LYS B 149   CA  -  CB  -  CG  ANGL. DEV. =  24.2 DEGREES
REMARK 500    ASP B 190   CB  -  CG  -  OD2 ANGL. DEV. =  -7.2 DEGREES
REMARK 500    PRO B 201   CA  -  C   -  O   ANGL. DEV. = -24.8 DEGREES
REMARK 500    PRO B 202   CA  -  N   -  CD  ANGL. DEV. = -20.5 DEGREES
REMARK 500    PRO B 201   CA  -  C   -  N   ANGL. DEV. =  21.7 DEGREES
REMARK 500    PRO B 202   C   -  N   -  CD  ANGL. DEV. = -15.1 DEGREES
REMARK 500    ARG B 257   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 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    TRP A   5      148.73    169.69
REMARK 500    ASN A  24       31.66    -89.58
REMARK 500    PRO A  30      156.90    -21.98
REMARK 500    LYS A  57      -50.54   -135.78
REMARK 500    SER A  65     -169.10   -168.77
REMARK 500    ASN A  75       33.98    -91.36
REMARK 500    GLU A 106      -73.37   -101.21
REMARK 500    ILE A 167       60.92   -108.55
REMARK 500    ALA A 174      142.31   -174.78
REMARK 500    PRO A 202      -13.38    -33.90
REMARK 500    ASN A 244       35.50   -153.57
REMARK 500    LYS B  57      -57.88   -144.52
REMARK 500    GLU B 102      -83.54    -52.03
REMARK 500    GLU B 106      -61.12    -98.62
REMARK 500    GLU B 152      152.03    -49.89
REMARK 500    ALA B 174      139.58    179.94
REMARK 500    ASN B 178       63.42     70.81
REMARK 500    PRO B 201      174.32    -52.71
REMARK 500    PRO B 202      -19.36    -35.56
REMARK 500    ASN B 244       49.45   -158.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 SER A   29     PRO A   30                  -68.04
REMARK 500 PRO A  201     PRO A  202                  -43.03
REMARK 500 SER B   29     PRO B   30                   85.16
REMARK 500 PRO B  201     PRO B  202                  -45.42
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 ANGLE, 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    SER A  29        -13.03
REMARK 500    PRO A 201        -44.24
REMARK 500    PRO B 201        -37.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    PRO A  30        22.2      L          L   OUTSIDE RANGE
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 435        DISTANCE =  5.10 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 261  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 EDO A 401   O1
REMARK 620 2 HIS A  94   NE2 105.1
REMARK 620 3 HIS A  96   NE2 105.0 100.5
REMARK 620 4 HIS A 119   ND1 126.5 117.1  98.4
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 119   ND1
REMARK 620 2 EDO B 402   O2  107.3
REMARK 620 3 HIS B  96   NE2 106.7 125.9
REMARK 620 4 HIS B  94   NE2 116.5  99.9 101.0
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
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 402
DBREF  1J9W A    1   260  UNP    P00915   CAH1_HUMAN       1    260
DBREF  1J9W B    1   260  UNP    P00915   CAH1_HUMAN       1    260
SEQADV 1J9W ARG A   67  UNP  P00915    HIS    67 ENGINEERED
SEQADV 1J9W ARG B   67  UNP  P00915    HIS    67 ENGINEERED
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 ARG 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 ARG VAL ASN PHE GLU ASP ASN ASP ASN ARG SER VAL
SEQRES   7 B  260  LEU LYS GLY GLY PRO PHE SER ASP SER TYR ARG LEU PHE
SEQRES   8 B  260  GLN PHE HIS PHE HIS TRP GLY SER THR ASN GLU HIS GLY
SEQRES   9 B  260  SER GLU HIS THR VAL ASP GLY VAL LYS TYR SER ALA GLU
SEQRES  10 B  260  LEU HIS VAL ALA HIS TRP ASN SER ALA LYS TYR SER SER
SEQRES  11 B  260  LEU ALA GLU ALA ALA SER LYS ALA ASP GLY LEU ALA VAL
SEQRES  12 B  260  ILE GLY VAL LEU MET LYS VAL GLY GLU ALA ASN PRO LYS
SEQRES  13 B  260  LEU GLN LYS VAL LEU ASP ALA LEU GLN ALA ILE LYS THR
SEQRES  14 B  260  LYS GLY LYS ARG ALA PRO PHE THR ASN PHE ASP PRO SER
SEQRES  15 B  260  THR LEU LEU PRO SER SER LEU ASP PHE TRP THR TYR PRO
SEQRES  16 B  260  GLY SER LEU THR HIS PRO PRO LEU TYR GLU SER VAL THR
SEQRES  17 B  260  TRP ILE ILE CYS LYS GLU SER ILE SER VAL SER SER GLU
SEQRES  18 B  260  GLN LEU ALA GLN PHE ARG SER LEU LEU SER ASN VAL GLU
SEQRES  19 B  260  GLY ASP ASN ALA VAL PRO MET GLN HIS ASN ASN ARG PRO
SEQRES  20 B  260  THR GLN PRO LEU LYS GLY ARG THR VAL ARG ALA SER PHE
HET     ZN  A 261       1
HET     ZN  B 262       1
HET    EDO  A 401       4
HET    EDO  B 402       4
HETNAM      ZN ZINC ION
HETNAM     EDO 1,2-ETHANEDIOL
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   3   ZN    2(ZN 2+)
FORMUL   5  EDO    2(C2 H6 O2)
FORMUL   7  HOH   *321(H2 O)
HELIX    1   1 GLY A   12  LEU A   19  5                                   8
HELIX    2   2 TYR A   20  GLY A   25  5                                   6
HELIX    3   3 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  ALA A  135  1                                   6
HELIX    6   6 ASN A  154  LYS A  156  5                                   3
HELIX    7   7 LEU A  157  LEU A  164  1                                   8
HELIX    8   8 GLN A  165  ILE A  167  5                                   3
HELIX    9   9 ASP A  180  LEU A  185  5                                   6
HELIX   10  10 SER A  220  LEU A  229  1                                  10
HELIX   11  11 GLY B   12  LEU B   19  5                                   8
HELIX   12  12 TYR B   20  GLY B   25  5                                   6
HELIX   13  13 LYS B   34  THR B   38  5                                   5
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  ILE B  167  5                                   3
HELIX   18  18 ASP B  180  LEU B  185  5                                   6
HELIX   19  19 SER B  219  LEU B  229  1                                  11
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  HIS A  40  0
SHEET    2   B16 ARG A 257  ALA A 258  1  N  ALA A 258   O  LYS A  39
SHEET    3   B16 PHE A 191  GLY A 196 -1  O  THR A 193   N  ARG A 257
SHEET    4   B16 VAL A 207  CYS A 212 -1  O  VAL A 207   N  GLY A 196
SHEET    5   B16 LEU A 141  GLY A 151  1  O  LEU A 141   N  THR A 208
SHEET    6   B16 ILE A 216  SER A 219  1  O  ILE A 216   N  LYS A 149
SHEET    7   B16 LEU A 141  GLY A 151  1  O  LEU A 147   N  ILE A 216
SHEET    8   B16 ALA A 116  ASN A 124 -1  O  ALA A 116   N  MET A 148
SHEET    9   B16 PHE A  84  TRP A  97 -1  N  ARG A  89   O  TRP A 123
SHEET   10   B16 VAL A  78  GLY A  81 -1  O  LEU A  79   N  TYR A  88
SHEET   11   B16 ILE A  47  SER A  50 -1  N  SER A  48   O  LYS A  80
SHEET   12   B16 VAL A  78  GLY A  81 -1  N  VAL A  78   O  SER A  50
SHEET   13   B16 PHE A  84  TRP A  97 -1  N  PHE A  84   O  GLY A  81
SHEET   14   B16 PHE A  66  PHE A  70 -1  O  PHE A  66   N  PHE A  95
SHEET   15   B16 ALA A  56  ASN A  61 -1  N  LYS A  57   O  ASN A  69
SHEET   16   B16 ARG A 173  PRO A 175 -1  O  ALA A 174   N  ILE A  59
SHEET    1   C 2 ASP B  32  ILE B  33  0
SHEET    2   C 2 THR B 108  VAL B 109  1  O  THR B 108   N  ILE B  33
SHEET    1   D16 LYS B  39  HIS B  40  0
SHEET    2   D16 ARG B 257  ALA B 258  1  N  ALA B 258   O  LYS B  39
SHEET    3   D16 PHE B 191  GLY B 196 -1  O  THR B 193   N  ARG B 257
SHEET    4   D16 VAL B 207  CYS B 212 -1  O  VAL B 207   N  GLY B 196
SHEET    5   D16 LEU B 141  VAL B 150  1  O  LEU B 141   N  THR B 208
SHEET    6   D16 ILE B 216  VAL B 218  1  O  ILE B 216   N  LYS B 149
SHEET    7   D16 LEU B 141  VAL B 150  1  O  LEU B 147   N  ILE B 216
SHEET    8   D16 ALA B 116  TRP B 123 -1  O  ALA B 116   N  MET B 148
SHEET    9   D16 TYR B  88  TRP B  97 -1  N  ARG B  89   O  TRP B 123
SHEET   10   D16 VAL B  78  GLY B  81 -1  O  LEU B  79   N  TYR B  88
SHEET   11   D16 ILE B  47  SER B  50 -1  N  SER B  48   O  LYS B  80
SHEET   12   D16 VAL B  78  GLY B  81 -1  O  VAL B  78   N  SER B  50
SHEET   13   D16 TYR B  88  TRP B  97 -1  N  TYR B  88   O  LEU B  79
SHEET   14   D16 PHE B  66  PHE B  70 -1  N  VAL B  68   O  PHE B  93
SHEET   15   D16 ALA B  56  ASN B  61 -1  N  LYS B  57   O  ASN B  69
SHEET   16   D16 ARG B 173  PRO B 175 -1  O  ALA B 174   N  ILE B  59
LINK        ZN    ZN A 261                 O1  EDO A 401     1555   1555  1.74
LINK        ZN    ZN A 261                 NE2 HIS A  94     1555   1555  1.87
LINK        ZN    ZN A 261                 NE2 HIS A  96     1555   1555  2.21
LINK        ZN    ZN A 261                 ND1 HIS A 119     1555   1555  2.18
LINK        ZN    ZN B 262                 ND1 HIS B 119     1555   1555  2.04
LINK        ZN    ZN B 262                 O2  EDO B 402     1555   1555  1.75
LINK        ZN    ZN B 262                 NE2 HIS B  96     1555   1555  2.01
LINK        ZN    ZN B 262                 NE2 HIS B  94     1555   1555  1.94
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  EDO A 401
SITE     1 AC2  5 HIS B  94  HIS B  96  HIS B 119  THR B 199
SITE     2 AC2  5 EDO B 402
SITE     1 AC3  6 HIS A  94  HIS A  96  HIS A 119  LEU A 198
SITE     2 AC3  6 THR A 199   ZN A 261
SITE     1 AC4  6 HIS B  94  HIS B  96  HIS B 119  LEU B 198
SITE     2 AC4  6 THR B 199   ZN B 262
CRYST1   61.875   71.732  120.392  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      0.016162  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013941  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008306        0.00000
      
PROCHECK
Go to PROCHECK summary
 References