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PDBsum entry 1fsn

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Lyase PDB id
1fsn
Jmol
Contents
Protein chain
257 a.a. *
Waters ×247
* Residue conservation analysis
HEADER    LYASE                                   11-SEP-00   1FSN
TITLE     X-RAY CRYSTAL STRUCTURE OF METAL-FREE 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, 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 1FSN    1       VERSN
REVDAT   1   17-JAN-01 1FSN    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             : 28153
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) : 0.244
REMARK   3   FREE R VALUE                     : 0.291
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1375
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            : 4070
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 247
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 21.60
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) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.30
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 1FSN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-SEP-00.
REMARK 100 THE RCSB ID CODE IS RCSB011867.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 04-JUL-99
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   : 29335
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     (%) : 93.8
REMARK 200  DATA REDUNDANCY                : 3.400
REMARK 200  R MERGE                    (I) : 0.05400
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 8.8000
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     (%) : 78.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20
REMARK 200  R MERGE FOR SHELL          (I) : 0.23700
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   (%): 40.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
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     HIS A     3
REMARK 465     MET B     1
REMARK 465     SER B     2
REMARK 465     HIS 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    PRO A  21      -19.20    -48.88
REMARK 500    LYS A 111       -4.63     71.05
REMARK 500    PHE A 176       94.83   -165.49
REMARK 500    ASN A 244       55.61    -96.59
REMARK 500    PRO B  21      -19.19    -48.88
REMARK 500    LYS B 111       -4.65     71.11
REMARK 500    PHE B 176       94.85   -165.48
REMARK 500    ASN B 244       55.64    -96.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
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.
REMARK 900 RELATED ID: 1FR4   RELATED DB: PDB
REMARK 900 COPPER-BOUND CARBONIC ANHYDRASE II (F93I/F95M/W97V) VARIANT.
REMARK 900 RELATED ID: 1FR7   RELATED DB: PDB
REMARK 900 ZINC-BOUND CARBONIC ANHYDRASE II (F93I/F95M/W97V) VARIANT.
REMARK 900 RELATED ID: 1FSQ   RELATED DB: PDB
REMARK 900 COBALT-BOUND CARBONIC ANHYDRASE II (F93S/F95L/W97M) VARIANT.
REMARK 900 RELATED ID: 1FSR   RELATED DB: PDB
REMARK 900 COPPER-BOUND CARBONIC ANHYDRASE II (F93S/F95L/W97M) VARIANT.
DBREF  1FSN A    1   261  UNP    P00918   CAH2_HUMAN       1    260
DBREF  1FSN B    1   261  UNP    P00918   CAH2_HUMAN       1    260
SEQADV 1FSN SER A   93  UNP  P00918    PHE    92 ENGINEERED
SEQADV 1FSN LEU A   95  UNP  P00918    PHE    94 ENGINEERED
SEQADV 1FSN MET A   97  UNP  P00918    TRP    96 ENGINEERED
SEQADV 1FSN SER B   93  UNP  P00918    PHE    92 ENGINEERED
SEQADV 1FSN LEU B   95  UNP  P00918    PHE    94 ENGINEERED
SEQADV 1FSN 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
FORMUL   3  HOH   *247(H2 O)
HELIX    1   1 HIS A   15  PHE A   20  1                                   6
HELIX    2   2 PRO A   21  GLY A   25  5                                   5
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  VAL A  163  1                                   7
HELIX    7   7 LEU A  164  LYS A  168  5                                   5
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 HIS B   15  PHE B   20  1                                   6
HELIX   11  11 PRO B   21  GLY B   25  5                                   5
HELIX   12  12 LYS B  127  GLY B  129  5                                   3
HELIX   13  13 ASP B  130  VAL B  135  1                                   6
HELIX   14  14 LYS B  154  GLY B  156  5                                   3
HELIX   15  15 LEU B  157  VAL B  163  1                                   7
HELIX   16  16 LEU B  164  LYS B  168  5                                   5
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 LYS A 172  ASP A 175  0
SHEET    2  A216 SER A  56  ASN A  61 -1  N  ILE A  59   O  ALA A 174
SHEET    3  A216 PHE A  66  PHE A  70 -1  O  ASN A  67   N  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  82 -1  N  LEU A  79   O  TYR A  88
SHEET    6  A216 LYS A  45  SER A  50 -1  N  LYS A  45   O  GLY A  82
SHEET    7  A216 VAL A  78  GLY A  82 -1  O  VAL A  78   N  SER A  50
SHEET    8  A216 TYR A  88  MET A  97 -1  O  TYR A  88   N  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  N  ILE A 216   O  PHE A 147
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  N  THR A 208   O  LEU A 141
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 LYS B 172  ASP B 175  0
SHEET    2  A416 SER B  56  ASN B  61 -1  N  ILE B  59   O  ALA B 174
SHEET    3  A416 PHE B  66  PHE B  70 -1  O  ASN B  67   N  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  82 -1  N  LEU B  79   O  TYR B  88
SHEET    6  A416 LYS B  45  SER B  50 -1  N  LYS B  45   O  GLY B  82
SHEET    7  A416 VAL B  78  GLY B  82 -1  O  VAL B  78   N  SER B  50
SHEET    8  A416 TYR B  88  MET B  97 -1  O  TYR B  88   N  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  N  ILE B 216   O  PHE B 147
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  N  THR B 208   O  LEU B 141
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
CISPEP   1 SER A   29    PRO A   30          0         0.10
CISPEP   2 PRO A  201    PRO A  202          0         0.76
CISPEP   3 SER B   29    PRO B   30          0         0.17
CISPEP   4 PRO B  201    PRO B  202          0         0.75
CRYST1   42.240   43.870   66.630  87.01  89.90  75.96 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      0.023674 -0.005920  0.000275        0.00000
SCALE2      0.000000  0.023497 -0.001255        0.00000
SCALE3      0.000000  0.000000  0.015030        0.00000
      
PROCHECK
Go to PROCHECK summary
 References