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PDBsum entry 2foy

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Lyase PDB id
2foy
Jmol
Contents
Protein chains
256 a.a.
Ligands
B30 ×6
Metals
_ZN ×2
Waters ×574
HEADER    LYASE                                   14-JAN-06   2FOY
TITLE     HUMAN CARBONIC ANHYDRASE I COMPLEXED WITH A TWO-PRONG
TITLE    2 INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 1;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: CARBONIC ANHYDRASE I, CARBONATE DEHYDRATASE I, CA-
COMPND   5 I;
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: CA1;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21CODON PLUSDE3(RIL);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET20B
KEYWDS    LYASE, ZINC, INHIBITOR, COPPER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.M.JUDE,A.L.BANERJEE,M.K.HALDAR,S.MANOKARAN,B.ROY,S.MALLIK,
AUTHOR   2 D.K.SRIVASTAVA,D.W.CHRISTIANSON
REVDAT   2   24-FEB-09 2FOY    1       VERSN
REVDAT   1   04-APR-06 2FOY    0
JRNL        AUTH   K.M.JUDE,A.L.BANERJEE,M.K.HALDAR,S.MANOKARAN,B.ROY,
JRNL        AUTH 2 S.MALLIK,D.K.SRIVASTAVA,D.W.CHRISTIANSON
JRNL        TITL   ULTRAHIGH RESOLUTION CRYSTAL STRUCTURES OF HUMAN
JRNL        TITL 2 CARBONIC ANHYDRASES I AND II COMPLEXED WITH
JRNL        TITL 3 TWO-PRONG INHIBITORS REVEAL THE MOLECULAR BASIS OF
JRNL        TITL 4 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   1
REMARK   2
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 60.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.6
REMARK   3   NUMBER OF REFLECTIONS             : 75232
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : FREE R
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.220
REMARK   3   FREE R VALUE                     : 0.243
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1860
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.56
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.55
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3258
REMARK   3   BIN FREE R VALUE                    : 0.3487
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 34
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : NULL
REMARK   3   NUCLEIC ACID ATOMS       : NULL
REMARK   3   HETEROGEN ATOMS          : NULL
REMARK   3   SOLVENT ATOMS            : NULL
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 20.70
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.57
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.90100
REMARK   3    B22 (A**2) : -6.49000
REMARK   3    B33 (A**2) : 4.58900
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.30
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.90
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.84
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; 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  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2FOY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAR-06.
REMARK 100 THE RCSB ID CODE IS RCSB036134.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 17-JUL-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.4
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : CHESS
REMARK 200  BEAMLINE                       : A1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9777
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   : 80682
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550
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     (%) : 98.2
REMARK 200  DATA REDUNDANCY                : 5.500
REMARK 200  R MERGE                    (I) : 0.07200
REMARK 200  R SYM                      (I) : 0.07200
REMARK 200   FOR THE DATA SET  : 23.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.57500
REMARK 200  R SYM FOR SHELL            (I) : 0.57500
REMARK 200   FOR SHELL         : 2.050
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1HCB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 47.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS-SULFATE, MES, PEG 3350, NACL,
REMARK 280  PH 6.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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       31.60950
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.97450
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.30400
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.97450
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.60950
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.30400
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 UNIT IS A MONOMER. THERE ARE 2 BIOLOGICAL
REMARK 300 UNITS IN THE ASYMMETRIC UNIT
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     ASP A     4
REMARK 465     ALA B     1
REMARK 465     SER B     2
REMARK 465     PRO B     3
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    LYS A  57      -55.74   -125.84
REMARK 500    SER A  65     -166.93   -170.93
REMARK 500    ASN A  75       40.39    -96.22
REMARK 500    PRO A 201      139.17    -37.43
REMARK 500    ASN A 244       34.23   -154.37
REMARK 500    ASP B   8     -159.20    -79.55
REMARK 500    LYS B  57      -57.53   -126.82
REMARK 500    SER B  65     -168.79   -170.82
REMARK 500    PRO B 201      138.40    -38.02
REMARK 500    ASN B 244       37.72   -150.71
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 962        DISTANCE =  5.63 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 301  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 B30 A 311   N1
REMARK 620 2 HIS A 119   ND1 119.3
REMARK 620 3 HIS A  94   NE2 109.2 112.5
REMARK 620 4 HIS A  96   NE2 107.9  99.6 107.3
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             B30 A 311  CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 200   NE2
REMARK 620 2 HOH A 958   O   108.0
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 302  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 B30 B 312   N1
REMARK 620 2 HIS B 119   ND1 118.6
REMARK 620 3 HIS B  96   NE2 108.8  98.2
REMARK 620 4 HIS B  94   NE2 110.8 112.2 106.8
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 301
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 302
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B30 A 311
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B30 B 312
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B30 A 313
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B30 B 314
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B30 A 315
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B30 B 316
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HCB   RELATED DB: PDB
REMARK 900 CAI COMPLEXED WITH BICARBONATE
REMARK 900 RELATED ID: 2FOV   RELATED DB: PDB
REMARK 900 CAII COMPLEXED WITH BR30
REMARK 900 RELATED ID: 2FOQ   RELATED DB: PDB
REMARK 900 RELATED ID: 2FOS   RELATED DB: PDB
REMARK 900 RELATED ID: 2FOU   RELATED DB: PDB
DBREF  2FOY A    1   260  UNP    P00915   CAH1_HUMAN       1    260
DBREF  2FOY B    1   260  UNP    P00915   CAH1_HUMAN       1    260
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 HIS 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 HIS 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 301       1
HET     ZN  B 302       1
HET    B30  A 311      25
HET    B30  B 312      25
HET    B30  A 313      25
HET    B30  B 314      25
HET    B30  A 315      25
HET    B30  B 316      25
HETNAM      ZN ZINC ION
HETNAM     B30 {2,2'-[(2-{[4-(AMINOSULFONYL)BENZOYL]AMINO}ETHYL)
HETNAM   2 B30  IMINO]DIACETATO(2-)-KAPPAO}COPPER
FORMUL   3   ZN    2(ZN 2+)
FORMUL   5  B30    6(C13 H15 CU N3 O7 S)
FORMUL  11  HOH   *574(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 ASN A   52  ALA A   54  5                                   3
HELIX    4   4 SER A  130  ALA A  135  1                                   6
HELIX    5   5 ASN A  154  LYS A  156  5                                   3
HELIX    6   6 LEU A  157  LEU A  164  1                                   8
HELIX    7   7 GLN A  165  ILE A  167  5                                   3
HELIX    8   8 ASP A  180  LEU A  185  5                                   6
HELIX    9   9 SER A  219  SER A  228  1                                  10
HELIX   10  10 GLY B   12  LEU B   19  5                                   8
HELIX   11  11 TYR B   20  GLY B   25  5                                   6
HELIX   12  12 LYS B   34  THR B   38  5                                   5
HELIX   13  13 ASN B   52  ALA B   54  5                                   3
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  SER B  228  1                                  10
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  HIS A  40  0
SHEET    2   B10 ARG A 257  ALA A 258  1  O  ALA A 258   N  LYS A  39
SHEET    3   B10 PHE A 191  GLY A 196 -1  N  THR A 193   O  ARG A 257
SHEET    4   B10 VAL A 207  CYS 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  ALA A 116   O  MET A 148
SHEET    7   B10 TYR A  88  TRP A  97 -1  N  ARG A  89   O  TRP A 123
SHEET    8   B10 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93
SHEET    9   B10 ALA A  56  ASN A  61 -1  N  GLU A  58   O  ASN A  69
SHEET   10   B10 ARG A 173  PRO A 175 -1  O  ALA A 174   N  ILE A  59
SHEET    1   C 6 ILE A  47  SER A  50  0
SHEET    2   C 6 VAL A  78  GLY A  81 -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  TRP A 123   N  ARG A  89
SHEET    5   C 6 LEU A 141  VAL A 150 -1  O  MET A 148   N  ALA A 116
SHEET    6   C 6 ILE A 216  VAL A 218  1  O  ILE A 216   N  LYS A 149
SHEET    1   D 2 ASP B  32  ILE B  33  0
SHEET    2   D 2 THR B 108  VAL B 109  1  O  THR B 108   N  ILE B  33
SHEET    1   E10 LYS B  39  HIS B  40  0
SHEET    2   E10 ARG B 257  ALA B 258  1  O  ALA B 258   N  LYS B  39
SHEET    3   E10 PHE B 191  GLY B 196 -1  N  THR B 193   O  ARG B 257
SHEET    4   E10 VAL B 207  CYS B 212 -1  O  VAL B 207   N  GLY B 196
SHEET    5   E10 LEU B 141  VAL B 150  1  N  GLY B 145   O  ILE B 210
SHEET    6   E10 ALA B 116  ASN B 124 -1  N  ALA B 116   O  MET B 148
SHEET    7   E10 TYR B  88  TRP B  97 -1  N  ARG B  89   O  TRP B 123
SHEET    8   E10 PHE B  66  PHE B  70 -1  N  PHE B  70   O  PHE B  91
SHEET    9   E10 ALA B  56  ASN B  61 -1  N  GLU B  58   O  ASN B  69
SHEET   10   E10 ARG B 173  PRO B 175 -1  O  ALA B 174   N  ILE B  59
SHEET    1   F 6 ILE B  47  SER B  50  0
SHEET    2   F 6 VAL B  78  GLY B  81 -1  O  LYS B  80   N  SER B  48
SHEET    3   F 6 TYR B  88  TRP B  97 -1  O  TYR B  88   N  LEU B  79
SHEET    4   F 6 ALA B 116  ASN B 124 -1  O  TRP B 123   N  ARG B  89
SHEET    5   F 6 LEU B 141  VAL B 150 -1  O  MET B 148   N  ALA B 116
SHEET    6   F 6 ILE B 216  VAL B 218  1  O  ILE B 216   N  LYS B 149
LINK        ZN    ZN A 301                 N1  B30 A 311     1555   1555  2.14
LINK        ZN    ZN A 301                 ND1 HIS A 119     1555   1555  2.12
LINK        ZN    ZN A 301                 NE2 HIS A  94     1555   1555  2.11
LINK        ZN    ZN A 301                 NE2 HIS A  96     1555   1555  2.11
LINK        CU   B30 A 311                 NE2 HIS A 200     1555   1555  2.43
LINK        CU   B30 A 311                 O   HOH A 958     1555   1555  2.48
LINK        CU   B30 A 313                 NE2 HIS A 243     1555   1555  2.47
LINK        CU   B30 A 315                 NE2 HIS A 103     1555   1555  2.43
LINK        ZN    ZN B 302                 N1  B30 B 312     1555   1555  2.12
LINK        ZN    ZN B 302                 ND1 HIS B 119     1555   1555  2.14
LINK        ZN    ZN B 302                 NE2 HIS B  96     1555   1555  2.10
LINK        ZN    ZN B 302                 NE2 HIS B  94     1555   1555  2.08
LINK        CU   B30 B 312                 NE2 HIS B 200     1555   1555  2.35
LINK        CU   B30 B 314                 NE2 HIS B 243     1555   1555  2.33
LINK        CU   B30 B 316                 NE2 HIS B 103     1555   1555  2.36
CISPEP   1 SER A   29    PRO A   30          0         0.16
CISPEP   2 PRO A  201    PRO A  202          0         0.74
CISPEP   3 SER B   29    PRO B   30          0         0.22
CISPEP   4 PRO B  201    PRO B  202          0         0.59
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  B30 A 311
SITE     1 AC2  4 HIS B  94  HIS B  96  HIS B 119  B30 B 312
SITE     1 AC3 13 HIS A  67  GLN A  92  HIS A  94  HIS A  96
SITE     2 AC3 13 HIS A 119  LEU A 198  THR A 199  HIS A 200
SITE     3 AC3 13 PRO A 201  TRP A 209   ZN A 301  HOH A 958
SITE     4 AC3 13 SER B 136
SITE     1 AC4 12 HIS B  67  HIS B  94  HIS B  96  HIS B 119
SITE     2 AC4 12 LEU B 198  THR B 199  HIS B 200  PRO B 201
SITE     3 AC4 12 PRO B 202  TRP B 209   ZN B 302  HOH B 861
SITE     1 AC5 12 TYR A   7  ASP A   8  ASP A   9  GLY A  63
SITE     2 AC5 12 HIS A  64  PRO A 240  MET A 241  GLN A 242
SITE     3 AC5 12 HIS A 243  HOH A 456  HOH A 839  HOH A 948
SITE     1 AC6 11 TYR B   7  ASP B   8  ASP B   9  GLY B  63
SITE     2 AC6 11 SER B 231  PRO B 240  MET B 241  GLN B 242
SITE     3 AC6 11 HIS B 243  HOH B 453  HOH B 942
SITE     1 AC7  7 GLY A  98  SER A  99  GLU A 102  HIS A 103
SITE     2 AC7  7 LYS A 113  HIS A 243  ASN A 245
SITE     1 AC8  7 GLY B  98  SER B  99  GLU B 102  HIS B 103
SITE     2 AC8  7 HIS B 243  ASN B 245  HOH B 538
CRYST1   63.219   72.608  121.949  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      0.015820  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013770  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008200        0.00000
      
PROCHECK
Go to PROCHECK summary
 References