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PDBsum entry 2fou

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Lyase PDB id
2fou
Jmol
Contents
Protein chain
260 a.a.
Ligands
B22 ×2
GOL
Metals
_ZN
_CU
Waters ×285
HEADER    LYASE                                   14-JAN-06   2FOU
TITLE     HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH TWO-PRONG INHIBITORS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE II;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CARBONIC ANHYDRASE II, CARBONATE DEHYDRATASE II, CA-II,
COMPND   5 CARBONIC ANHYDRASE C;
COMPND   6 EC: 4.2.1.1;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: CA2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 CODON PLUS (DE3) RIL;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMA-5-8
KEYWDS    LYASE, INHIBITOR
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.M.JUDE,D.W.CHRISTIANSON
REVDAT   3   13-JUL-11 2FOU    1       VERSN
REVDAT   2   24-FEB-09 2FOU    1       VERSN
REVDAT   1   04-APR-06 2FOU    0
JRNL        AUTH   K.M.JUDE,A.L.BANERJEE,M.K.HALDAR,S.MANOKARAN,B.ROY,S.MALLIK,
JRNL        AUTH 2 D.K.SRIVASTAVA,D.W.CHRISTIANSON
JRNL        TITL   ULTRAHIGH RESOLUTION CRYSTAL STRUCTURES OF HUMAN CARBONIC
JRNL        TITL 2 ANHYDRASES I AND II COMPLEXED WITH TWO-PRONG INHIBITORS
JRNL        TITL 3 REVEAL THE MOLECULAR BASIS OF HIGH AFFINITY.
JRNL        REF    J.AM.CHEM.SOC.                V. 128  3011 2006
JRNL        REFN                   ISSN 0002-7863
JRNL        PMID   16506782
JRNL        DOI    10.1021/JA057257N
REMARK   2
REMARK   2 RESOLUTION.    0.99 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) : 0.99
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 60.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.8
REMARK   3   CROSS-VALIDATION METHOD           : FREE R
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) : 0.123
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.123
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.135
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 1.100
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 1328
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 126056
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.111
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.111
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.122
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 1.100
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 1112
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 104303
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 2074
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 65
REMARK   3   SOLVENT ATOMS      : 285
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 2392.40
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 2015.64
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 17
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 22361
REMARK   3   NUMBER OF RESTRAINTS                     : 30577
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.013
REMARK   3   ANGLE DISTANCES                      (A) : 0.026
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.020
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.094
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.095
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.098
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.005
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.052
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.103
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: NULL
REMARK   4
REMARK   4 2FOU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-06.
REMARK 100 THE RCSB ID CODE IS RCSB036132.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-APR-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.7
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : CHESS
REMARK 200  BEAMLINE                       : F1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9124
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 127404
REMARK 200  RESOLUTION RANGE HIGH      (A) : 0.990
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0
REMARK 200  DATA REDUNDANCY                : 3.600
REMARK 200  R MERGE                    (I) : 0.09300
REMARK 200  R SYM                      (I) : 0.09300
REMARK 200   FOR THE DATA SET  : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.99
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.03
REMARK 200  COMPLETENESS FOR SHELL     (%) : 53.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90
REMARK 200  R MERGE FOR SHELL          (I) : 0.47900
REMARK 200  R SYM FOR SHELL            (I) : 0.47900
REMARK 200   FOR SHELL         : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 2CBA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 41.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5 M (NH4)2SO4, TRIS-SO4,
REMARK 280  METHYLMERCURIC ACETATE, PH 7.7, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  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       20.85200
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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     LYS A  133   CE   NZ
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  15   CG  -  ND1 -  CE1 ANGL. DEV. =  11.1 DEGREES
REMARK 500    ARG A  27   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES
REMARK 500    ARG A  27   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.1 DEGREES
REMARK 500    ARG A  58   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES
REMARK 500    TYR A  88   CB  -  CG  -  CD1 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ARG A  89   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG A 182   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    PHE A 226   CB  -  CG  -  CD1 ANGL. DEV. =   7.0 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    SER A   2      168.99     56.81
REMARK 500    HIS A   4       -4.22     79.51
REMARK 500    ASN A  11       18.10   -146.26
REMARK 500    ARG A  27       56.81   -145.80
REMARK 500    LEU A  57      -50.29   -122.18
REMARK 500    ALA A  65     -167.65   -161.90
REMARK 500    GLU A 106      -61.11    -91.82
REMARK 500    PHE A 176       48.84   -146.43
REMARK 500    ASN A 244       48.81    -94.40
REMARK 500    LYS A 252     -138.51     55.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     B22 A  301
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                              CU A 302  CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A   2   OG
REMARK 620 2 HIS A   3   N    83.8
REMARK 620 3 HIS A   3   ND1 151.6 103.2
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             B22 A 303  CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A   4   NE2
REMARK 620 2 B22 A 303   OXB 115.2
REMARK 620 3 B22 A 303   OXD  74.1 135.9
REMARK 620 N                    1     2
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  94   NE2
REMARK 620 2 HIS A  96   NE2 104.2
REMARK 620 3 HIS A 119   ND1 111.9  98.6
REMARK 620 4 B22 A 301   N1  111.2 113.9 115.8
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 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B22 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B22 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 351
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CBA   RELATED DB: PDB
REMARK 900 NATIVE CA2
REMARK 900 RELATED ID: 2FOQ   RELATED DB: PDB
REMARK 900 CA2 WITH ANOTHER 2 PRONG INHIBITOR
REMARK 900 RELATED ID: 2FOS   RELATED DB: PDB
REMARK 900 CA2 WITH ANOTHER 2 PRONG INHIBITOR
REMARK 900 RELATED ID: 2FOV   RELATED DB: PDB
REMARK 900 RELATED ID: 2FOY   RELATED DB: PDB
DBREF  2FOU A    2   260  UNP    P00918   CAH2_HUMAN       1    259
SEQADV 2FOU MET A    1  UNP  P00918              INITIATING METHIONINE
SEQADV 2FOU CMH A  206  UNP  P00918    CYS   204 MODIFIED RESIDUE
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 CMH 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
MODRES 2FOU CMH A  206  CYS  S-(METHYLMERCURY)-L-CYSTEINE
HET    CMH  A 206      10
HET     ZN  A 262       1
HET     CU  A 302       1
HET    B22  A 301      33
HET    B22  A 303      35
HET    GOL  A 351       6
HETNAM     CMH S-(METHYLMERCURY)-L-CYSTEINE
HETNAM      ZN ZINC ION
HETNAM      CU COPPER (II) ION
HETNAM     B22 [2,2'-{[2-({3-[({2-[4-(AMINOSULFONYL)
HETNAM   2 B22  PHENYL]ETHYL}AMINO)CARBONYL]PHENYL}AMINO)-2-
HETNAM   3 B22  OXOETHYL]IMINO}DIACETATO(2-)-KAPPAO]COPPER
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   1  CMH    C4 H9 HG N O2 S
FORMUL   2   ZN    ZN 2+
FORMUL   3   CU    CU 2+
FORMUL   4  B22    2(C21 H22 CU N4 O8 S)
FORMUL   6  GOL    C3 H8 O3
FORMUL   7  HOH   *285(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  HIS A  94   O  HIS A 119
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  HIS A 119   N  HIS A  94
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         C   GLU A 205                 N   CMH A 206     1555   1555  1.34
LINK         C   CMH A 206                 N   VAL A 207     1555   1555  1.34
LINK         OG  SER A   2                CU    CU A 302     1555   1555  2.23
LINK         N   HIS A   3                CU    CU A 302     1555   1555  2.03
LINK         ND1 HIS A   3                CU    CU A 302     1555   1555  1.88
LINK         NE2 HIS A   4                CU   B22 A 303     1555   1555  1.84
LINK         NE2 HIS A  94                ZN    ZN A 262     1555   1555  2.00
LINK         NE2 HIS A  96                ZN    ZN A 262     1555   1555  2.00
LINK         ND1 HIS A 119                ZN    ZN A 262     1555   1555  2.03
LINK        ZN    ZN A 262                 N1  B22 A 301     1555   1555  1.93
CISPEP   1 SER A   29    PRO A   30          0        -2.92
CISPEP   2 PRO A  201    PRO A  202          0         8.55
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  B22 A 301
SITE     1 AC2  3 SER A   2  HIS A   3  ASP A  52
SITE     1 AC3 17 ILE A  91  GLN A  92  HIS A  94  HIS A  96
SITE     2 AC3 17 HIS A 119  PHE A 131  LEU A 198  THR A 199
SITE     3 AC3 17 THR A 200  PRO A 202  TRP A 209   ZN A 262
SITE     4 AC3 17 GOL A 351  HOH A 582  HOH A 614  HOH A 636
SITE     5 AC3 17 HOH A 682
SITE     1 AC4 11 HIS A   4  TRP A   5  HIS A  10  HIS A  15
SITE     2 AC4 11 TRP A  16  ASP A  19  PHE A  20  ARG A 182
SITE     3 AC4 11 GLY A 183  HOH A 602  HOH A 664
SITE     1 AC5 10 ASN A  62  HIS A  64  ALA A  65  ASN A  67
SITE     2 AC5 10 GLN A  92  THR A 200  B22 A 301  HOH A 491
SITE     3 AC5 10 HOH A 496  HOH A 614
CRYST1   42.557   41.704   72.710  90.00 104.38  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      0.023498  0.000000  0.006024        0.00000
SCALE2      0.000000  0.023979  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014198        0.00000
      
PROCHECK
Go to PROCHECK summary
 References