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PDBsum entry 1can

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Lyase(oxo-acid) PDB id
1can
Jmol
Contents
Protein chain
260 a.a.
Ligands
NO3
Metals
_HG ×2
Waters ×231
HEADER    LYASE(OXO-ACID)                         02-JUL-92   1CAN
TITLE     CRYSTALLOGRAPHIC STUDIES OF THE BINDING OF PROTONATED AND
TITLE    2 UNPROTONATED INHIBITORS TO CARBONIC ANHYDRASE USING
TITLE    3 HYDROGEN SULPHIDE AND NITRATE ANIONS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE II;
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    S.MANGANI,K.HAKANSSON
REVDAT   2   24-FEB-09 1CAN    1       VERSN
REVDAT   1   31-JAN-94 1CAN    0
JRNL        AUTH   S.MANGANI,K.HAKANSSON
JRNL        TITL   CRYSTALLOGRAPHIC STUDIES OF THE BINDING OF
JRNL        TITL 2 PROTONATED AND UNPROTONATED INHIBITORS TO CARBONIC
JRNL        TITL 3 ANHYDRASE USING HYDROGEN SULPHIDE AND NITRATE
JRNL        TITL 4 ANIONS.
JRNL        REF    EUR.J.BIOCHEM.                V. 210   867 1992
JRNL        REFN                   ISSN 0014-2956
JRNL        PMID   1336460
JRNL        DOI    10.1111/J.1432-1033.1992.TB17490.X
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : TNT
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : NULL
REMARK   3
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.141
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  USING ALL DATA, NO SIGMA CUTOFF.
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            : 2088
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 6
REMARK   3   SOLVENT ATOMS            : 231
REMARK   3
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT
REMARK   3   BOND LENGTHS                 (A) : 0.021 ; NULL  ; NULL
REMARK   3   BOND ANGLES            (DEGREES) : 3.400 ; NULL  ; NULL
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL
REMARK   3
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  RESTRAINT LIBRARIES.
REMARK   3   STEREOCHEMISTRY : NULL
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1CAN 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   (%): 42.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THIS IS THE HIGH-ACTIVITY
REMARK 280  ERYTHROCYTIC FORM OF HUMAN CARBONIC ANHYDRASE, CARBONIC
REMARK 280  ANHYDRASE II, OR CAII. CRYSTALLIZED IN 50 MM TRIS-HCL 2.4 M
REMARK 280  AMMONIUM SULFATE PH 8.5 AND 1 MM HGCL2 AT 4 DEG C (TILANDER,
REMARK 280  B., STRANDBERG, B. AND FRIDBORG, K. (1965). CRYSTAL STRUCTURE
REMARK 280  ON HUMAN ERYTHROCYTIC CARBONIC ANHYDRASE C. J. MOL. BIOL. 12,
REMARK 280  740-760.) THE MERCURY IS SUBSEQUENTLY REMOVED BY
REMARK 280  MERCAPTOETHANOL. THE CRYSTAL IS SOAKED IN 0.6M KNO3 80 MM
REMARK 280  CITRATE 3M AMMONIUM SULFATE PH 6.0., TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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       20.85000
REMARK 290   SMTRY3   2  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 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     ACE A   1    O
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    HOH A   359     O    HOH A   505              2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH A   317     O    HOH A   496     1565     2.08
REMARK 500   OE1  GLN A    53     O    HOH A   508     2455     2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLU A  14   CD    GLU A  14   OE1     0.069
REMARK 500    GLU A  14   CD    GLU A  14   OE1     0.072
REMARK 500    GLU A  26   CD    GLU A  26   OE2     0.078
REMARK 500    GLU A 187   CD    GLU A 187   OE1     0.090
REMARK 500    GLU A 234   CD    GLU A 234   OE1     0.088
REMARK 500    GLU A 236   CD    GLU A 236   OE2     0.093
REMARK 500    GLU A 239   CD    GLU A 239   OE1     0.097
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    HIS A   3   N   -  CA  -  CB  ANGL. DEV. =  13.5 DEGREES
REMARK 500    HIS A   3   C   -  N   -  CA  ANGL. DEV. =  21.5 DEGREES
REMARK 500    HIS A   4   N   -  CA  -  CB  ANGL. DEV. =  20.0 DEGREES
REMARK 500    ASP A  19   CB  -  CG  -  OD1 ANGL. DEV. =   7.3 DEGREES
REMARK 500    ASP A  19   CB  -  CG  -  OD2 ANGL. DEV. =  -8.5 DEGREES
REMARK 500    ARG A  27   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG A  27   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ASP A  41   CB  -  CG  -  OD1 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ASP A  52   CB  -  CG  -  OD1 ANGL. DEV. =   8.9 DEGREES
REMARK 500    ASP A  52   CB  -  CG  -  OD2 ANGL. DEV. = -10.7 DEGREES
REMARK 500    ARG A  58   N   -  CA  -  CB  ANGL. DEV. = -12.2 DEGREES
REMARK 500    ARG A  58   NE  -  CZ  -  NH2 ANGL. DEV. =   4.3 DEGREES
REMARK 500    PHE A  66   CB  -  CG  -  CD2 ANGL. DEV. =  -7.2 DEGREES
REMARK 500    ASP A  71   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ASP A  72   CB  -  CG  -  OD2 ANGL. DEV. =   8.9 DEGREES
REMARK 500    ASP A  75   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES
REMARK 500    TYR A  88   CG  -  CD2 -  CE2 ANGL. DEV. =   6.4 DEGREES
REMARK 500    TYR A  88   CZ  -  CE2 -  CD2 ANGL. DEV. =  -8.4 DEGREES
REMARK 500    ARG A  89   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.0 DEGREES
REMARK 500    ASP A 130   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ASP A 139   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    PHE A 147   CB  -  CG  -  CD2 ANGL. DEV. =  -4.5 DEGREES
REMARK 500    ASP A 162   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ASP A 162   CB  -  CG  -  OD2 ANGL. DEV. =  -8.8 DEGREES
REMARK 500    ASP A 165   CB  -  CG  -  OD2 ANGL. DEV. =  -6.8 DEGREES
REMARK 500    ASP A 175   CB  -  CG  -  OD1 ANGL. DEV. =  11.4 DEGREES
REMARK 500    ARG A 182   NE  -  CZ  -  NH1 ANGL. DEV. =   6.3 DEGREES
REMARK 500    ARG A 182   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    GLU A 221   CG  -  CD  -  OE1 ANGL. DEV. =  15.4 DEGREES
REMARK 500    PHE A 226   CB  -  CG  -  CD2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    ARG A 246   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    ARG A 254   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 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    HIS A   3     -126.40     90.49
REMARK 500    ASN A  11       21.81   -141.70
REMARK 500    ALA A  65     -165.41   -168.47
REMARK 500    PHE A 176       75.50   -152.15
REMARK 500    ASN A 244       56.16    -95.21
REMARK 500    LYS A 252     -138.41     57.10
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    2     HIS A    3                 -121.64
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    SER A   2        -14.22
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 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: (11X,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     HIS A   4        -0.2      L          D   EXPECTING SP3
REMARK 500     HIS A  64        24.1      L          L   OUTSIDE RANGE
REMARK 500     TYR A 128        25.0      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 A 382        DISTANCE =  5.00 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                              HG A 262  HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  96   NE2
REMARK 620 2 HIS A 119   ND1  98.9
REMARK 620 3 HIS A  94   NE2 103.5 115.2
REMARK 620 4 HOH A 263   O   102.7 120.6 112.3
REMARK 620 5 NO3 A 511   O2  169.4  84.2  84.1  67.2
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              HG A 510  HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 205   O
REMARK 620 2 VAL A 135   O   134.8
REMARK 620 3 GLN A 137   N   134.7  68.1
REMARK 620 4 HOH A 362   O   120.3  69.3 103.9
REMARK 620 5 HOH A 448   O    76.9 148.2  91.4  94.1
REMARK 620 6 GLN A 137   O    88.2  90.4  48.4 151.5  93.4
REMARK 620 N                    1     2     3     4     5
REMARK 700
REMARK 700 SHEET
REMARK 700 SHEET B1 OF THIS MOLECULE IS BIFURCATED.  IN ORDER TO
REMARK 700 REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS *B1A* AND *B1B* ARE DEFINED.  STRANDS 5, 6, 7,
REMARK 700 8, 9, AND 10 OF B1A ARE IDENTICAL TO STRANDS 2, 3, 4, 5, 6,
REMARK 700 AND 7 OF B1B, RESPECTIVELY.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZN
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 262
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 510
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 511
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 125 AND 127 ARE ADJACENT IN THE SEQUENCE.
DBREF  1CAN A    2   261  UNP    P00918   CAH2_HUMAN       1    259
SEQRES   1 A  260  ACE 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 THR THR PRO PRO LEU LEU GLU CYS 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    ACE  A   1       3
HET     HG  A 262       1
HET     HG  A 510       1
HET    NO3  A 511       4
HETNAM     ACE ACETYL GROUP
HETNAM      HG MERCURY (II) ION
HETNAM     NO3 NITRATE ION
FORMUL   1  ACE    C2 H4 O
FORMUL   2   HG    2(HG 2+)
FORMUL   4  NO3    N O3 1-
FORMUL   5  HOH   *231(H2 O)
HELIX    1   A PRO A   13  LYS A   18  5                                   6
HELIX    2   B PRO A   21  LYS A   24  5                                   4
HELIX    3   C THR A  125  TYR A  128  5                                   3
HELIX    4   D PHE A  131  ALA A  134  1                                   4
HELIX    5  E1 PRO A  155  LEU A  157  5                                   3
HELIX    6  E2 GLN A  158  VAL A  163  1                                   6
HELIX    7  E3 LEU A  164  ILE A  167  5                                   4
HELIX    8   F PRO A  181  LEU A  184  5                                   4
HELIX    9   G SER A  220  PHE A  226  1                                   7
SHEET    1 B1A10 LYS A  39  TYR A  40  0
SHEET    2 B1A10 LYS A 257  ALA A 258  1  N  ALA A 258   O  LYS A  39
SHEET    3 B1A10 TYR A 191  GLY A 196 -1  N  THR A 193   O  LYS A 257
SHEET    4 B1A10 VAL A 207  LEU A 212 -1  N  VAL A 211   O  TRP A 192
SHEET    5 B1A10 LEU A 141  GLY A 151  1  O  VAL A 143   N  ILE A 210
SHEET    6 B1A10 ALA A 116  ASN A 124 -1  N  LEU A 120   O  LEU A 144
SHEET    7 B1A10 TYR A  88  TRP A  97 -1  O  HIS A  94   N  HIS A 119
SHEET    8 B1A10 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93
SHEET    9 B1A10 SER A  56  ASN A  61 -1  O  ARG A  58   N  GLU A  69
SHEET   10 B1A10 SER A 173  ASP A 175 -1  O  SER A 173   N  ILE A  59
SHEET    1 B1B 7 ILE A 216  SER A 219  0
SHEET    2 B1B 7 LEU A 141  GLY A 151  1  N  GLY A 151   O  VAL A 218
SHEET    3 B1B 7 ALA A 116  ASN A 124 -1  N  LEU A 120   O  LEU A 144
SHEET    4 B1B 7 TYR A  88  TRP A  97 -1  O  HIS A  94   N  HIS A 119
SHEET    5 B1B 7 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93
SHEET    6 B1B 7 SER A  56  ASN A  61 -1  O  ARG A  58   N  GLU A  69
SHEET    7 B1B 7 SER A 173  ASP A 175 -1  O  SER A 173   N  ILE A  59
SHEET    1  B2 2 LEU A  47  SER A  50  0
SHEET    2  B2 2 VAL A  78  GLY A  81 -1  N  LYS A  80   O  SER A  48
SHEET    1  B3 2 ASP A  32  ILE A  33  0
SHEET    2  B3 2 THR A 108  VAL A 109  1  O  THR A 108   N  ILE A  33
LINK         CH3 ACE A   1                 N   SER A   2     1555   1555  1.43
LINK        HG    HG A 262                 NE2 HIS A  96     1555   1555  2.07
LINK        HG    HG A 262                 ND1 HIS A 119     1555   1555  2.02
LINK        HG    HG A 262                 NE2 HIS A  94     1555   1555  2.10
LINK        HG    HG A 262                 O   HOH A 263     1555   1555  1.91
LINK        HG    HG A 262                 O2  NO3 A 511     1555   1555  2.85
LINK        HG    HG A 510                 O   GLU A 205     1555   1555  3.46
LINK        HG    HG A 510                 O   VAL A 135     1555   1555  2.89
LINK        HG    HG A 510                 N   GLN A 137     1555   1555  3.35
LINK        HG    HG A 510                 O   HOH A 362     1555   1555  2.09
LINK        HG    HG A 510                 O   HOH A 448     1555   1555  2.23
LINK        HG    HG A 510                 O   GLN A 137     1555   1555  3.12
CISPEP   1 SER A   29    PRO A   30          0        -5.57
CISPEP   2 PRO A  201    PRO A  202          0        10.45
SITE     1  ZN  3 HIS A  94  HIS A  96  HIS A 119
SITE     1 AC1  5 HIS A  94  HIS A  96  HIS A 119  HOH A 263
SITE     2 AC1  5 NO3 A 511
SITE     1 AC2  7 VAL A 135  GLN A 136  GLN A 137  GLU A 205
SITE     2 AC2  7 CYS A 206  HOH A 362  HOH A 448
SITE     1 AC3 10 HIS A  94  HIS A 119  VAL A 143  LEU A 198
SITE     2 AC3 10 THR A 199  TRP A 209   HG A 262  HOH A 263
SITE     3 AC3 10 HOH A 338  HOH A 505
CRYST1   42.700   41.700   73.000  90.00 104.60  90.00 P 1 21 1      2
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      0.023419  0.000000  0.006100        0.00000
SCALE2      0.000000  0.023981  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014156        0.00000
      
PROCHECK
Go to PROCHECK summary
 References