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PDBsum entry 3k34

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Lyase/lyase inhibitor PDB id
3k34
Jmol
Contents
Protein chain
258 a.a.
Ligands
HGB
SUA
GOL ×3
Metals
_ZN
Waters ×249
HEADER    LYASE/LYASE INHIBITOR                   01-OCT-09   3K34
TITLE     HUMAN CARBONIC ANHYDRASE II WITH A SULFONAMIDE INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CARBONIC ANHYDRASE II, CA-II, CARBONATE DEHYDRATASE II,
COMPND   5 CARBONIC ANHYDRASE C, CAC;
COMPND   6 EC: 4.2.1.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 OTHER_DETAILS: THE PROTEIN WAS PURCHASED FROM SIGMA
KEYWDS    CARBONIC ANHYDRASE, ATOMIC RESOLUTION, SULFONAMIDE INHIBITOR, DISEASE
KEYWDS   2 MUTATION, LYASE, METAL-BINDING, LYASE-LYASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.A.BEHNKE,I.LE TRONG,E.A.MERRITT,D.C.TELLER,R.E.STENKAMP
REVDAT   2   21-MAR-12 3K34    1       JRNL   VERSN  HEADER
REVDAT   1   12-MAY-10 3K34    0
JRNL        AUTH   C.A.BEHNKE,I.LE TRONG,J.W.GODDEN,E.A.MERRITT,D.C.TELLER,
JRNL        AUTH 2 J.BAJORATH,R.E.STENKAMP
JRNL        TITL   ATOMIC RESOLUTION STUDIES OF CARBONIC ANHYDRASE II.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  66   616 2010
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   20445237
JRNL        DOI    10.1107/S0907444910006554
REMARK   2
REMARK   2 RESOLUTION.    0.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : SHELXL-97
REMARK   3   AUTHORS     : G.M.SHELDRICK
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 0.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 18.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   CROSS-VALIDATION METHOD           : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.141
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.160
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 8614
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 172451
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 2059
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 50
REMARK   3   SOLVENT ATOMS      : 249
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : NULL
REMARK   3   NUMBER OF RESTRAINTS                     : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.033
REMARK   3   ANGLE DISTANCES                      (A) : 0.052
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : NULL
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : NULL
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : NULL
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : NULL
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: NULL
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: ELECTRON DENSITY WAS OBSERVED FOR ONLY
REMARK   3  THE HG AND C1 ATOMS OF A SECOND CONFORMER OF THE HGB LIGAND.
REMARK   3  PRESUMABLY THE LIGAND IS SUFFICIENTLY DISORDERED BEYOND C1 TO
REMARK   3  RENDER IT UNOBSERVED
REMARK   4
REMARK   4 3K34 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-09.
REMARK 100 THE RCSB ID CODE IS RCSB055485.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JUL-99
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL9-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.78
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 172463
REMARK 200  RESOLUTION RANGE HIGH      (A) : 0.900
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     (%) : 98.0
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.06900
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 17.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 0.92
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.44000
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: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2CBA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3M AMMONIUM SULFATE, 50 MM TRIS-CL 2MM
REMARK 280  PHMB , PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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       20.63450
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 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 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  2169     O    HOH A  2233              1.32
REMARK 500   O    HOH A  2091     O    HOH A  2200              1.58
REMARK 500   CG   ASP A    34     O    HOH A  2248              1.62
REMARK 500   O    HOH A  2065     O    HOH A  2218              1.64
REMARK 500   OD2  ASP A    34     O    HOH A  2248              1.92
REMARK 500   C7   HGB A   265     O    HOH A  2284              1.95
REMARK 500   OD2  ASP A   130     NZ   LYS A   133              2.01
REMARK 500   OD1  ASP A   162     O    HOH A  2243              2.09
REMARK 500   O    TYR A     7     O    HOH A  2383              2.14
REMARK 500   O    HOH A  2314     O    HOH A  2315              2.17
REMARK 500   O    HOH A  2419     O    HOH A  2426              2.18
REMARK 500   OD1  ASP A    34     O    HOH A  2248              2.18
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   O1   GOL A  1004     O    HOH A  2112     2546     1.13
REMARK 500   C1   GOL A  1004     O    HOH A  2117     2546     1.39
REMARK 500   CG   ASP A   130     O    HOH A  2208     1565     1.51
REMARK 500   O    HOH A  2084     O    HOH A  2233     1655     1.65
REMARK 500   OD2  ASP A   130     O    HOH A  2208     1565     1.66
REMARK 500   CB   ASP A   130     O    HOH A  2208     1565     1.74
REMARK 500   NE2  GLN A    53     OD2  ASP A   165     2455     2.09
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    HIS A   3   C     HIS A   3   O       0.117
REMARK 500    GLU A  14   CD    GLU A  14   OE2     0.160
REMARK 500    ARG A  27   CD    ARG A  27   NE     -0.232
REMARK 500    ARG A  27   CZ    ARG A  27   NH2    -0.092
REMARK 500    TYR A  40   CZ    TYR A  40   CE2    -0.086
REMARK 500    HIS A  64   CE1   HIS A  64   NE2     0.168
REMARK 500    HIS A  64   NE2   HIS A  64   CD2    -0.195
REMARK 500    ASP A 130   CA    ASP A 130   CB      0.138
REMARK 500    LYS A 159   CE    LYS A 159   NZ      0.195
REMARK 500    SER A 220   CB    SER A 220   OG     -0.086
REMARK 500    GLU A 234   CG    GLU A 234   CD     -0.098
REMARK 500    GLU A 234   CD    GLU A 234   OE1     0.069
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   CA  -  C   -  O   ANGL. DEV. = -15.6 DEGREES
REMARK 500    HIS A   3   O   -  C   -  N   ANGL. DEV. =  13.8 DEGREES
REMARK 500    HIS A  10   ND1 -  CE1 -  NE2 ANGL. DEV. =  -6.7 DEGREES
REMARK 500    HIS A  10   CE1 -  NE2 -  CD2 ANGL. DEV. =   5.1 DEGREES
REMARK 500    GLU A  14   CG  -  CD  -  OE1 ANGL. DEV. = -12.2 DEGREES
REMARK 500    ASP A  19   OD1 -  CG  -  OD2 ANGL. DEV. = -11.7 DEGREES
REMARK 500    ASP A  19   CB  -  CG  -  OD1 ANGL. DEV. =   7.8 DEGREES
REMARK 500    PHE A  20   CB  -  CG  -  CD2 ANGL. DEV. =  -4.6 DEGREES
REMARK 500    GLU A  26   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.1 DEGREES
REMARK 500    ARG A  27   CG  -  CD  -  NE  ANGL. DEV. =  26.8 DEGREES
REMARK 500    ARG A  27   CD  -  NE  -  CZ  ANGL. DEV. =  14.2 DEGREES
REMARK 500    ARG A  27   NE  -  CZ  -  NH1 ANGL. DEV. =  10.1 DEGREES
REMARK 500    ARG A  27   NE  -  CZ  -  NH2 ANGL. DEV. = -11.7 DEGREES
REMARK 500    ASP A  34   OD1 -  CG  -  OD2 ANGL. DEV. = -12.0 DEGREES
REMARK 500    ASP A  34   CB  -  CG  -  OD1 ANGL. DEV. =   6.9 DEGREES
REMARK 500    TYR A  40   CB  -  CG  -  CD1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ARG A  58   NE  -  CZ  -  NH1 ANGL. DEV. =   6.5 DEGREES
REMARK 500    ARG A  58   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 DEGREES
REMARK 500    HIS A  64   CB  -  CG  -  CD2 ANGL. DEV. =   7.4 DEGREES
REMARK 500    HIS A  64   ND1 -  CE1 -  NE2 ANGL. DEV. = -12.3 DEGREES
REMARK 500    ASP A  71   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 DEGREES
REMARK 500    GLN A  74   OE1 -  CD  -  NE2 ANGL. DEV. =  31.7 DEGREES
REMARK 500    GLN A  74   CG  -  CD  -  OE1 ANGL. DEV. = -22.4 DEGREES
REMARK 500    ASP A  75   OD1 -  CG  -  OD2 ANGL. DEV. = -13.2 DEGREES
REMARK 500    ASP A  75   CB  -  CG  -  OD1 ANGL. DEV. =  15.2 DEGREES
REMARK 500    ALA A  77   N   -  CA  -  CB  ANGL. DEV. = -14.0 DEGREES
REMARK 500    LYS A  76   O   -  C   -  N   ANGL. DEV. = -11.9 DEGREES
REMARK 500    LYS A  80   CD  -  CE  -  NZ  ANGL. DEV. =  33.0 DEGREES
REMARK 500    ARG A  89   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ASP A 130   OD1 -  CG  -  OD2 ANGL. DEV. = -20.8 DEGREES
REMARK 500    ASP A 130   CB  -  CG  -  OD1 ANGL. DEV. =  13.1 DEGREES
REMARK 500    LYS A 159   CG  -  CD  -  CE  ANGL. DEV. =  19.0 DEGREES
REMARK 500    ASP A 162   CA  -  CB  -  CG  ANGL. DEV. =  32.7 DEGREES
REMARK 500    ASP A 162   OD1 -  CG  -  OD2 ANGL. DEV. = -15.9 DEGREES
REMARK 500    ASP A 162   CB  -  CG  -  OD1 ANGL. DEV. = -13.1 DEGREES
REMARK 500    ASP A 162   CB  -  CG  -  OD2 ANGL. DEV. =  28.8 DEGREES
REMARK 500    ASP A 165   OD1 -  CG  -  OD2 ANGL. DEV. =  12.5 DEGREES
REMARK 500    ASP A 165   CB  -  CG  -  OD2 ANGL. DEV. =  -8.9 DEGREES
REMARK 500    LYS A 168   CD  -  CE  -  NZ  ANGL. DEV. =  16.9 DEGREES
REMARK 500    LYS A 170   CD  -  CE  -  NZ  ANGL. DEV. =  23.1 DEGREES
REMARK 500    ASP A 175   CA  -  CB  -  CG  ANGL. DEV. = -18.6 DEGREES
REMARK 500    ASP A 175   OD1 -  CG  -  OD2 ANGL. DEV. =  18.2 DEGREES
REMARK 500    ASP A 175   CB  -  CG  -  OD1 ANGL. DEV. = -15.9 DEGREES
REMARK 500    ASP A 180   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES
REMARK 500    ARG A 182   NE  -  CZ  -  NH1 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ARG A 182   NE  -  CZ  -  NH2 ANGL. DEV. = -10.1 DEGREES
REMARK 500    GLU A 221   OE1 -  CD  -  OE2 ANGL. DEV. = -10.0 DEGREES
REMARK 500    PHE A 226   CB  -  CG  -  CD2 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    PHE A 226   CB  -  CG  -  CD1 ANGL. DEV. =   8.9 DEGREES
REMARK 500    GLU A 239   OE1 -  CD  -  OE2 ANGL. DEV. =  14.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      53 ANGLE DEVIATIONS.
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    ARG A  27       58.73   -146.21
REMARK 500    LYS A  76      -84.35   -122.66
REMARK 500    GLU A 106      -61.74    -93.27
REMARK 500    LYS A 111       -2.76     74.15
REMARK 500    PHE A 176       66.46   -152.04
REMARK 500    ASN A 244       48.29    -95.48
REMARK 500    LYS A 252     -143.58     56.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    ASP A  34         0.07    SIDE CHAIN
REMARK 500    HIS A  64         0.11    SIDE CHAIN
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 A2432        DISTANCE =  6.34 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 A1002  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  94   NE2
REMARK 620 2 HIS A  96   NE2 103.3
REMARK 620 3 HIS A 119   ND1 113.0  98.8
REMARK 620 4 SUA A1003   N1  110.5 113.9 116.1
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HGB A 265  HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 206   SG
REMARK 620 2 HGB A 265   C7  174.8
REMARK 620 3 HOH A2284   O    83.0  91.8
REMARK 620 4 GLN A 137   O    83.2 100.7 132.0
REMARK 620 5 GLU A 205   O    94.2  88.9 133.0  93.7
REMARK 620 6 VAL A 135   O    51.8 124.3  45.1  92.0 144.5
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HGB A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SUA A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1006
DBREF  3K34 A    1   261  UNP    P00918   CAH2_HUMAN       1    260
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 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    HGB  A 265      12
HET     ZN  A1002       1
HET    SUA  A1003      21
HET    GOL  A1004       6
HET    GOL  A1005       6
HET    GOL  A1006       6
HETNAM     HGB 4-(HYDROXYMERCURY)BENZOIC ACID
HETNAM      ZN ZINC ION
HETNAM     SUA (4-SULFAMOYL-PHENYL)-THIOCARBAMIC ACID O-(2-THIOPHEN-3-
HETNAM   2 SUA  YL-ETHYL) ESTER
HETNAM     GOL GLYCEROL
HETSYN     SUA CARBONIC ANHYDRASE II INHIBITOR 16923
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2  HGB    C7 H6 HG O3
FORMUL   3   ZN    ZN 2+
FORMUL   4  SUA    C13 H14 N2 O3 S3
FORMUL   5  GOL    3(C3 H8 O3)
FORMUL   8  HOH   *249(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  LEU A  164  1                                   8
HELIX    7   7 ASP A  165  ILE A  167  5                                   3
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   B10 LYS A  39  TYR A  40  0
SHEET    2   B10 LYS A 257  ALA A 258  1  O  ALA A 258   N  LYS A  39
SHEET    3   B10 TYR A 191  GLY A 196 -1  N  THR A 193   O  LYS A 257
SHEET    4   B10 VAL A 207  LEU A 212 -1  O  VAL A 207   N  GLY A 196
SHEET    5   B10 LEU A 141  VAL A 150  1  N  GLY A 145   O  ILE A 210
SHEET    6   B10 ALA A 116  ASN A 124 -1  N  LEU A 118   O  ILE A 146
SHEET    7   B10 TYR A  88  TRP A  97 -1  N  GLN A  92   O  VAL A 121
SHEET    8   B10 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93
SHEET    9   B10 SER A  56  ASN A  61 -1  N  LEU A  57   O  GLU A  69
SHEET   10   B10 SER A 173  ASP A 175 -1  O  ALA A 174   N  ILE A  59
SHEET    1   C 6 LYS A  45  SER A  50  0
SHEET    2   C 6 VAL A  78  GLY A  82 -1  O  LYS A  80   N  SER A  48
SHEET    3   C 6 TYR A  88  TRP A  97 -1  O  TYR A  88   N  LEU A  79
SHEET    4   C 6 ALA A 116  ASN A 124 -1  O  VAL A 121   N  GLN A  92
SHEET    5   C 6 LEU A 141  VAL A 150 -1  O  ILE A 146   N  LEU A 118
SHEET    6   C 6 ILE A 216  VAL A 218  1  O  ILE A 216   N  PHE A 147
LINK         NE2 HIS A  94                ZN    ZN A1002     1555   1555  1.97
LINK         NE2 HIS A  96                ZN    ZN A1002     1555   1555  2.02
LINK         ND1 HIS A 119                ZN    ZN A1002     1555   1555  2.01
LINK        ZN    ZN A1002                 N1  SUA A1003     1555   1555  1.94
LINK        HG  AHGB A 265                 SG ACYS A 206     1555   1555  2.31
LINK        HG  BHGB A 265                 SG BCYS A 206     1555   1555  2.27
LINK        HG  BHGB A 265                 O   HOH A2284     1555   1555  2.58
LINK        HG  AHGB A 265                 O   HOH A2284     1555   1555  2.91
LINK         O   GLN A 137                HG  AHGB A 265     1555   1555  2.94
LINK         O   GLU A 205                HG  AHGB A 265     1555   1555  2.98
LINK         O   VAL A 135                HG  BHGB A 265     1555   1555  3.03
LINK         O   GLN A 137                HG  BHGB A 265     1555   1555  3.17
CISPEP   1 SER A   29    PRO A   30          0        -2.84
CISPEP   2 PRO A  201    PRO A  202          0        11.37
SITE     1 AC1  7 VAL A 135  GLN A 136  GLN A 137  PRO A 138
SITE     2 AC1  7 GLU A 205  CYS A 206  HOH A2284
SITE     1 AC2  4 HIS A  94  HIS A  96  HIS A 119  SUA A1003
SITE     1 AC3 12 GLN A  92  HIS A  94  HIS A  96  HIS A 119
SITE     2 AC3 12 LEU A 198  THR A 199  THR A 200  TRP A 209
SITE     3 AC3 12  ZN A1002  GOL A1006  HOH A2138  HOH A2235
SITE     1 AC4  7 LYS A 111  LYS A 112  TYR A 128  HOH A2146
SITE     2 AC4  7 HOH A2425  HOH A2426  HOH A2457
SITE     1 AC5  7 GLU A  14  LYS A  24  GLN A 249  HOH A2012
SITE     2 AC5  7 HOH A2030  HOH A2053  HOH A2361
SITE     1 AC6  9 ASN A  62  HIS A  64  ALA A  65  ASN A  67
SITE     2 AC6  9 GLN A  92  HIS A  94  SUA A1003  HOH A2131
SITE     3 AC6  9 HOH A2158
CRYST1   42.045   41.269   71.821  90.00 104.23  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      0.023784  0.000000  0.006032        0.00000
SCALE2      0.000000  0.024231  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014364        0.00000
      
PROCHECK
Go to PROCHECK summary
 References