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PDBsum entry 1fsr

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Lyase PDB id
1fsr
Jmol
Contents
Protein chain
258 a.a. *
Metals
_CU ×2
Waters ×94
* Residue conservation analysis
HEADER    LYASE                                   11-SEP-00   1FSR
TITLE     X-RAY CRYSTAL STRUCTURE OF COPPER-BOUND F93S/F95L/W97M
TITLE    2 CARBONIC ANHYDRASE (CAII) VARIANT
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE II;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 4.2.1.1;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    CARBONIC ANHYDRASE, METAL BINDING, METAL SPECIFICITY,
KEYWDS   2 COPPER, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.D.COX,J.A.HUNT,K.M.COMPHER,C.A.FIERKE,D.W.CHRISTIANSON
REVDAT   2   24-FEB-09 1FSR    1       VERSN
REVDAT   1   17-JAN-01 1FSR    0
JRNL        AUTH   J.D.COX,J.A.HUNT,K.M.COMPHER,C.A.FIERKE,
JRNL        AUTH 2 D.W.CHRISTIANSON
JRNL        TITL   STRUCTURAL INFLUENCE OF HYDROPHOBIC CORE RESIDUES
JRNL        TITL 2 ON METAL BINDING AND SPECIFICITY IN CARBONIC
JRNL        TITL 3 ANHYDRASE II.
JRNL        REF    BIOCHEMISTRY                  V.  39 13687 2000
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   11076507
JRNL        DOI    10.1021/BI001649J
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.851
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 22180
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.240
REMARK   3   FREE R VALUE                     : 0.297
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1105
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) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
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            : 4090
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 94
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 24.50
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED 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) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.50
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
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  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 1FSR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-SEP-00.
REMARK 100 THE RCSB ID CODE IS RCSB011870.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 06-JAN-00
REMARK 200  TEMPERATURE           (KELVIN) : 130
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22676
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 71.5
REMARK 200  DATA REDUNDANCY                : 1.400
REMARK 200  R MERGE                    (I) : 0.08500
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 4.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07
REMARK 200  COMPLETENESS FOR SHELL     (%) : 60.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.20
REMARK 200  R MERGE FOR SHELL          (I) : 0.37100
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: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, PEG 1500, PH 7.0, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER
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     MET A     1
REMARK 465     SER A     2
REMARK 465     MET B     1
REMARK 465     SER B     2
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    ASN A  11       10.24   -147.31
REMARK 500    GLU A  14        5.05    -68.08
REMARK 500    VAL A  49       72.67   -109.86
REMARK 500    ASP A  52      -76.46    -52.59
REMARK 500    LEU A  57      -64.06   -120.98
REMARK 500    LYS A 111       -7.14     77.51
REMARK 500    THR A 125        0.43    -63.91
REMARK 500    ILE A 167       35.00   -145.97
REMARK 500    ASN A 244       59.37    -97.80
REMARK 500    LYS A 252     -125.27     59.06
REMARK 500    ASN B  11       10.21   -147.33
REMARK 500    GLU B  14        5.08    -68.08
REMARK 500    VAL B  49       72.66   -109.87
REMARK 500    ASP B  52      -76.41    -52.58
REMARK 500    LEU B  57      -64.09   -120.97
REMARK 500    LYS B 111       -7.14     77.48
REMARK 500    THR B 125        0.43    -63.88
REMARK 500    ILE B 167       35.02   -145.96
REMARK 500    ASN B 244       59.37    -97.79
REMARK 500    LYS B 252     -125.24     59.07
REMARK 500
REMARK 500 REMARK: NULL
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 262  CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 119   ND1
REMARK 620 2 HIS A  94   NE2 122.5
REMARK 620 3 HIS A  96   NE2  81.5  94.9
REMARK 620 4 HOH A 301   O   136.2  98.5  80.3
REMARK 620 5 HOH A 302   O   104.1  92.4 166.5  87.4
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CU B 263  CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 119   ND1
REMARK 620 2 HIS B  96   NE2  81.5
REMARK 620 3 HIS B  94   NE2 122.5  94.9
REMARK 620 4 HOH B 353   O   136.2  80.3  98.5
REMARK 620 5 HOH B 354   O   104.1 166.5  92.4  87.3
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 262
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 263
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FSQ   RELATED DB: PDB
REMARK 900 COBALT-BOUND CARBONIC ANHYDRASE II (F93S/F95L/W97M) VARIANT.
REMARK 900 RELATED ID: 1FSN   RELATED DB: PDB
REMARK 900 METAL-FREE CARBONIC ANHYDRASE II (F93S/F95L/W97M) VARIANT.
REMARK 900 RELATED ID: 1FR7   RELATED DB: PDB
REMARK 900 ZINC-BOUND CARBONIC ANHYDRASE II (F93I/F95M/W97V) VARIANT.
REMARK 900 RELATED ID: 1FR4   RELATED DB: PDB
REMARK 900 COPPER-BOUND CARBONIC ANHYDRASE II (F93I/F95M/W97V) VARIANT.
REMARK 900 RELATED ID: 1FQL   RELATED DB: PDB
REMARK 900 ZINC-BOUND CARBONIC ANHYDRASE II (F95M/W97V) VARIANT.
REMARK 900 RELATED ID: 1FQM   RELATED DB: PDB
REMARK 900 ZINC-BOUND CARBONIC ANHYDRASE II (F93I/F95M/W97V) VARIANT.
REMARK 900 RELATED ID: 1FQN   RELATED DB: PDB
REMARK 900 METAL-FREE CARBONIC ANHYDRASE II (F93I/F95M/W97V) VARIANT.
REMARK 900 RELATED ID: 1FQR   RELATED DB: PDB
REMARK 900 COBALT-BOUND CARBONIC ANHYDRASE II (F93I/F95M/W97V) VARIANT.
DBREF  1FSR A    1   261  UNP    P00918   CAH2_HUMAN       1    260
DBREF  1FSR B    1   261  UNP    P00918   CAH2_HUMAN       1    260
SEQADV 1FSR SER A   93  UNP  P00918    PHE    92 ENGINEERED
SEQADV 1FSR LEU A   95  UNP  P00918    PHE    94 ENGINEERED
SEQADV 1FSR MET A   97  UNP  P00918    TRP    96 ENGINEERED
SEQADV 1FSR SER B   93  UNP  P00918    PHE    92 ENGINEERED
SEQADV 1FSR LEU B   95  UNP  P00918    PHE    94 ENGINEERED
SEQADV 1FSR MET B   97  UNP  P00918    TRP    96 ENGINEERED
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 SER HIS LEU HIS MET 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
SEQRES   1 B  260  MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO
SEQRES   2 B  260  GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU
SEQRES   3 B  260  ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS
SEQRES   4 B  260  TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP
SEQRES   5 B  260  GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA
SEQRES   6 B  260  PHE ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL
SEQRES   7 B  260  LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE
SEQRES   8 B  260  GLN SER HIS LEU HIS MET GLY SER LEU ASP GLY GLN GLY
SEQRES   9 B  260  SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU
SEQRES  10 B  260  LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE
SEQRES  11 B  260  GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU
SEQRES  12 B  260  GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU
SEQRES  13 B  260  GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS
SEQRES  14 B  260  GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY
SEQRES  15 B  260  LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY
SEQRES  16 B  260  SER LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP
SEQRES  17 B  260  ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN
SEQRES  18 B  260  VAL LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES  19 B  260  GLU PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA
SEQRES  20 B  260  GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET     CU  A 262       1
HET     CU  B 263       1
HETNAM      CU COPPER (II) ION
FORMUL   3   CU    2(CU 2+)
FORMUL   5  HOH   *94(H2 O)
HELIX    1   1 GLY A   12  HIS A   17  1                                   6
HELIX    2   2 LYS A   18  ASP A   19  5                                   2
HELIX    3   3 PHE A   20  GLY A   25  5                                   6
HELIX    4   4 LYS A  127  GLY A  129  5                                   3
HELIX    5   5 ASP A  130  VAL A  135  1                                   6
HELIX    6   6 LYS A  154  ASP A  162  1                                   9
HELIX    7   7 VAL A  163  LYS A  168  5                                   6
HELIX    8   8 ASP A  180  LEU A  185  5                                   6
HELIX    9   9 SER A  219  ARG A  227  1                                   9
HELIX   10  10 GLY B   12  HIS B   17  1                                   6
HELIX   11  11 LYS B   18  ASP B   19  5                                   2
HELIX   12  12 PHE B   20  GLY B   25  5                                   6
HELIX   13  13 LYS B  127  GLY B  129  5                                   3
HELIX   14  14 ASP B  130  VAL B  135  1                                   6
HELIX   15  15 LYS B  154  ASP B  162  1                                   9
HELIX   16  16 VAL B  163  LYS B  168  5                                   6
HELIX   17  17 ASP B  180  LEU B  185  5                                   6
HELIX   18  18 SER B  219  ARG B  227  1                                   9
SHEET    1  A1 2 ASP A  32  ILE A  33  0
SHEET    2  A1 2 THR A 108  VAL A 109  1  O  THR A 108   N  ILE A  33
SHEET    1  A216 SER A 173  ASP A 175  0
SHEET    2  A216 SER A  56  ASN A  61 -1  O  ILE A  59   N  ALA A 174
SHEET    3  A216 PHE A  66  PHE A  70 -1  N  ASN A  67   O  LEU A  60
SHEET    4  A216 TYR A  88  MET A  97 -1  O  ILE A  91   N  PHE A  70
SHEET    5  A216 VAL A  78  GLY A  81 -1  O  LEU A  79   N  TYR A  88
SHEET    6  A216 LEU A  47  SER A  48 -1  N  SER A  48   O  LYS A  80
SHEET    7  A216 VAL A  78  GLY A  81 -1  O  LYS A  80   N  SER A  48
SHEET    8  A216 TYR A  88  MET A  97 -1  N  TYR A  88   O  LEU A  79
SHEET    9  A216 ALA A 116  ASN A 124 -1  O  GLU A 117   N  HIS A  96
SHEET   10  A216 LEU A 141  VAL A 150 -1  O  ALA A 142   N  HIS A 122
SHEET   11  A216 ILE A 216  VAL A 218  1  O  ILE A 216   N  LYS A 149
SHEET   12  A216 LEU A 141  VAL A 150  1  O  PHE A 147   N  ILE A 216
SHEET   13  A216 VAL A 207  LEU A 212  1  O  THR A 208   N  VAL A 143
SHEET   14  A216 TYR A 191  GLY A 196 -1  O  TRP A 192   N  VAL A 211
SHEET   15  A216 LYS A 257  ALA A 258 -1  N  LYS A 257   O  THR A 193
SHEET   16  A216 LYS A  39  TYR A  40  1  O  LYS A  39   N  ALA A 258
SHEET    1  A3 2 ASP B  32  ILE B  33  0
SHEET    2  A3 2 THR B 108  VAL B 109  1  O  THR B 108   N  ILE B  33
SHEET    1  A416 SER B 173  ASP B 175  0
SHEET    2  A416 SER B  56  ASN B  61 -1  O  ILE B  59   N  ALA B 174
SHEET    3  A416 PHE B  66  PHE B  70 -1  N  ASN B  67   O  LEU B  60
SHEET    4  A416 TYR B  88  MET B  97 -1  O  ILE B  91   N  PHE B  70
SHEET    5  A416 VAL B  78  GLY B  81 -1  O  LEU B  79   N  TYR B  88
SHEET    6  A416 LEU B  47  SER B  48 -1  N  SER B  48   O  LYS B  80
SHEET    7  A416 VAL B  78  GLY B  81 -1  O  LYS B  80   N  SER B  48
SHEET    8  A416 TYR B  88  MET B  97 -1  N  TYR B  88   O  LEU B  79
SHEET    9  A416 ALA B 116  ASN B 124 -1  O  GLU B 117   N  HIS B  96
SHEET   10  A416 LEU B 141  VAL B 150 -1  O  ALA B 142   N  HIS B 122
SHEET   11  A416 ILE B 216  VAL B 218  1  O  ILE B 216   N  LYS B 149
SHEET   12  A416 LEU B 141  VAL B 150  1  O  PHE B 147   N  ILE B 216
SHEET   13  A416 VAL B 207  LEU B 212  1  O  THR B 208   N  VAL B 143
SHEET   14  A416 TYR B 191  GLY B 196 -1  O  TRP B 192   N  VAL B 211
SHEET   15  A416 LYS B 257  ALA B 258 -1  N  LYS B 257   O  THR B 193
SHEET   16  A416 LYS B  39  TYR B  40  1  O  LYS B  39   N  ALA B 258
LINK        CU    CU A 262                 ND1 HIS A 119     1555   1555  2.08
LINK        CU    CU A 262                 NE2 HIS A  94     1555   1555  2.04
LINK        CU    CU A 262                 NE2 HIS A  96     1555   1555  2.17
LINK        CU    CU B 263                 ND1 HIS B 119     1555   1555  2.08
LINK        CU    CU B 263                 NE2 HIS B  96     1555   1555  2.17
LINK        CU    CU B 263                 NE2 HIS B  94     1555   1555  2.04
LINK        CU    CU A 262                 O   HOH A 301     1555   1555  2.43
LINK        CU    CU A 262                 O   HOH A 302     1555   1555  2.38
LINK        CU    CU B 263                 O   HOH B 353     1555   1555  2.43
LINK        CU    CU B 263                 O   HOH B 354     1555   1555  2.38
CISPEP   1 SER A   29    PRO A   30          0         0.09
CISPEP   2 PRO A  201    PRO A  202          0         0.32
CISPEP   3 SER B   29    PRO B   30          0         0.02
CISPEP   4 PRO B  201    PRO B  202          0         0.28
SITE     1 AC1  6 HIS A  94  HIS A  96  HIS A 119  THR A 199
SITE     2 AC1  6 HOH A 301  HOH A 302
SITE     1 AC2  6 HIS B  94  HIS B  96  HIS B 119  THR B 199
SITE     2 AC2  6 HOH B 353  HOH B 354
CRYST1   42.300   43.800   67.600  86.70  90.00  75.60 P 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      0.023641 -0.006070  0.000361        0.00000
SCALE2      0.000000  0.023572 -0.001403        0.00000
SCALE3      0.000000  0.000000  0.014819        0.00000
      
PROCHECK
Go to PROCHECK summary
 References