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PDBsum entry 2aaa

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Glycosidase PDB id
2aaa
Jmol
Contents
Protein chain
476 a.a.
Metals
_CA ×2
Waters ×350
HEADER    GLYCOSIDASE                             27-FEB-91   2AAA
TITLE     CALCIUM BINDING IN ALPHA-AMYLASES: AN X-RAY DIFFRACTION STUDY AT 2.1
TITLE    2 ANGSTROMS RESOLUTION OF TWO ENZYMES FROM ASPERGILLUS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ALPHA-AMYLASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.2.1.1;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;
SOURCE   3 ORGANISM_TAXID: 5061
KEYWDS    GLYCOSIDASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    L.BRADY,A.M.BRZOZOWSKI,Z.DEREWENDA,E.J.DODSON,G.G.DODSON
REVDAT   4   17-SEP-14 2AAA    1       REMARK
REVDAT   3   24-FEB-09 2AAA    1       VERSN
REVDAT   2   01-APR-03 2AAA    1       JRNL
REVDAT   1   15-JUL-93 2AAA    0
JRNL        AUTH   E.BOEL,L.BRADY,A.M.BRZOZOWSKI,Z.DEREWENDA,G.G.DODSON,
JRNL        AUTH 2 V.J.JENSEN,S.B.PETERSEN,H.SWIFT,L.THIM,H.F.WOLDIKE
JRNL        TITL   CALCIUM BINDING IN ALPHA-AMYLASES: AN X-RAY DIFFRACTION
JRNL        TITL 2 STUDY AT 2.1-A RESOLUTION OF TWO ENZYMES FROM ASPERGILLUS.
JRNL        REF    BIOCHEMISTRY                  V.  29  6244 1990
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   2207069
JRNL        DOI    10.1021/BI00478A019
REMARK   2
REMARK   2 RESOLUTION.    2.12 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PROLSQ
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.12
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 7.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : NULL
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.169
REMARK   3   R VALUE            (WORKING SET) : NULL
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3669
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 350
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
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  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2AAA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : NULL
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 52.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   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        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       69.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       40.55000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       49.15000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       40.55000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       49.15000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       69.00000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       40.55000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       49.15000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       69.00000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       40.55000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       49.15000
REMARK 290   SMTRY3   8  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 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     GLY A   477
REMARK 465     SER A   478
REMARK 465     GLY A   479
REMARK 465     ARG A   480
REMARK 465     LEU A   481
REMARK 465     TYR A   482
REMARK 465     VAL A   483
REMARK 465     GLU A   484
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 560        DISTANCE =  5.54 ANGSTROMS
REMARK 525    HOH A 805        DISTANCE =  6.17 ANGSTROMS
REMARK 525    HOH A 814        DISTANCE =  7.48 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                              CA A 485  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 210   O
REMARK 620 2 GLU A 162   O    83.4
REMARK 620 3 HOH A 499   O    84.8  72.4
REMARK 620 4 HOH A 590   O    83.4  78.4 149.6
REMARK 620 5 ASP A 121   OD1  77.4 158.8 114.4  90.2
REMARK 620 6 ASP A 175   OD1 137.0 116.8 136.0  66.1  73.3
REMARK 620 7 ASP A 175   OD2 158.9  77.7  98.3  83.5 119.1  49.0
REMARK 620 8 HOH A 495   O   119.9 128.2  65.5 143.6  70.6  78.6  79.8
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 486  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 230   OE1
REMARK 620 2 GLU A 230   OE2  48.5
REMARK 620 3 HOH A 507   O    69.4  90.7
REMARK 620 4 HOH A 599   O   109.1  83.1 172.3
REMARK 620 5 HOH A 789   O   109.6  74.6  74.6  99.2
REMARK 620 6 HOH A 800   O   161.0 118.1 100.5  78.7  51.4
REMARK 620 7 HOH A 801   O   139.3 171.5  95.8  90.0 101.8  55.4
REMARK 620 8 ASP A 206   OD1  84.7 117.9 110.5  76.6 165.6 114.2  64.7
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 485
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 486
DBREF  2AAA A    1   484  UNP    P56271   AMYA_ASPNG       1    484
SEQRES   1 A  484  LEU SER ALA ALA SER TRP ARG THR GLN SER ILE TYR PHE
SEQRES   2 A  484  LEU LEU THR ASP ARG PHE GLY ARG THR ASP ASN SER THR
SEQRES   3 A  484  THR ALA THR CYS ASN THR GLY ASN GLU ILE TYR CYS GLY
SEQRES   4 A  484  GLY SER TRP GLN GLY ILE ILE ASP HIS LEU ASP TYR ILE
SEQRES   5 A  484  GLU GLY MET GLY PHE THR ALA ILE TRP ILE SER PRO ILE
SEQRES   6 A  484  THR GLU GLN LEU PRO GLN ASP THR ALA ASP GLY GLU ALA
SEQRES   7 A  484  TYR HIS GLY TYR TRP GLN GLN LYS ILE TYR ASP VAL ASN
SEQRES   8 A  484  SER ASN PHE GLY THR ALA ASP ASN LEU LYS SER LEU SER
SEQRES   9 A  484  ASP ALA LEU HIS ALA ARG GLY MET TYR LEU MET VAL ASP
SEQRES  10 A  484  VAL VAL PRO ASP HIS MET GLY TYR ALA GLY ASN GLY ASN
SEQRES  11 A  484  ASP VAL ASP TYR SER VAL PHE ASP PRO PHE ASP SER SER
SEQRES  12 A  484  SER TYR PHE HIS PRO TYR CYS LEU ILE THR ASP TRP ASP
SEQRES  13 A  484  ASN LEU THR MET VAL GLU ASP CYS TRP GLU GLY ASP THR
SEQRES  14 A  484  ILE VAL SER LEU PRO ASP LEU ASP THR THR GLU THR ALA
SEQRES  15 A  484  VAL ARG THR ILE TRP TYR ASP TRP VAL ALA ASP LEU VAL
SEQRES  16 A  484  SER ASN TYR SER VAL ASP GLY LEU ARG ILE ASP SER VAL
SEQRES  17 A  484  LEU GLU VAL GLN PRO ASP PHE PHE PRO GLY TYR ASN LYS
SEQRES  18 A  484  ALA SER GLY VAL TYR CYS VAL GLY GLU ILE ASP ASN GLY
SEQRES  19 A  484  ASN PRO ALA SER ASP CYS PRO TYR GLN LYS VAL LEU ASP
SEQRES  20 A  484  GLY VAL LEU ASN TYR PRO ILE TYR TRP GLN LEU LEU TYR
SEQRES  21 A  484  ALA PHE GLU SER SER SER GLY SER ILE SER ASN LEU TYR
SEQRES  22 A  484  ASN MET ILE LYS SER VAL ALA SER ASP CYS SER ASP PRO
SEQRES  23 A  484  THR LEU LEU GLY ASN PHE ILE GLU ASN HIS ASP ASN PRO
SEQRES  24 A  484  ARG PHE ALA LYS TYR THR SER ASP TYR SER GLN ALA LYS
SEQRES  25 A  484  ASN VAL LEU SER TYR ILE PHE LEU SER ASP GLY ILE PRO
SEQRES  26 A  484  ILE VAL TYR ALA GLY GLU GLU GLN HIS TYR ALA GLY GLY
SEQRES  27 A  484  LYS VAL PRO TYR ASN ARG GLU ALA THR TRP LEU SER GLY
SEQRES  28 A  484  TYR ASP THR SER ALA GLU LEU TYR THR TRP ILE ALA THR
SEQRES  29 A  484  THR ASN ALA ILE ARG LYS LEU ALA ILE ALA ALA ASP SER
SEQRES  30 A  484  ALA TYR ILE THR TYR ALA ASN ASP ALA PHE TYR THR ASP
SEQRES  31 A  484  SER ASN THR ILE ALA MET ALA LYS GLY THR SER GLY SER
SEQRES  32 A  484  GLN VAL ILE THR VAL LEU SER ASN LYS GLY SER SER GLY
SEQRES  33 A  484  SER SER TYR THR LEU THR LEU SER GLY SER GLY TYR THR
SEQRES  34 A  484  SER GLY THR LYS LEU ILE GLU ALA TYR THR CYS THR SER
SEQRES  35 A  484  VAL THR VAL ASP SER SER GLY ASP ILE PRO VAL PRO MET
SEQRES  36 A  484  ALA SER GLY LEU PRO ARG VAL LEU LEU PRO ALA SER VAL
SEQRES  37 A  484  VAL ASP SER SER SER LEU CYS GLY GLY SER GLY ARG LEU
SEQRES  38 A  484  TYR VAL GLU
HET     CA  A 485       1
HET     CA  A 486       1
HETNAM      CA CALCIUM ION
FORMUL   2   CA    2(CA 2+)
FORMUL   4  HOH   *350(H2 O)
HELIX    1   1 SER A    2  ARG A    7  1                                   6
HELIX    2   2 LEU A   15  GLY A   20  1                                   6
HELIX    3   3 ASN A   31  GLU A   35  5                                   5
HELIX    4   4 SER A   41  HIS A   48  1                                   8
HELIX    5   5 HIS A   48  GLY A   54  1                                   7
HELIX    6   6 THR A   96  ALA A  109  1                                  14
HELIX    7   7 ASN A  128  VAL A  132  5                                   5
HELIX    8   8 ASP A  133  PHE A  137  5                                   5
HELIX    9   9 SER A  142  TYR A  145  5                                   4
HELIX   10  10 ASN A  157  CYS A  164  1                                   8
HELIX   11  11 GLU A  180  SER A  199  1                                  20
HELIX   12  12 GLN A  212  ASP A  214  5                                   3
HELIX   13  13 PHE A  215  GLY A  224  1                                  10
HELIX   14  14 ASN A  235  CYS A  240  1                                   6
HELIX   15  15 PRO A  241  VAL A  245  5                                   5
HELIX   16  16 ASN A  251  GLU A  263  1                                  13
HELIX   17  17 SER A  268  CYS A  283  1                                  16
HELIX   18  18 ASP A  285  LEU A  288  5                                   4
HELIX   19  19 ARG A  300  TYR A  304  5                                   5
HELIX   20  20 ASP A  307  SER A  321  1                                  15
HELIX   21  21 ALA A  346  GLY A  351  5                                   6
HELIX   22  22 ALA A  356  ASP A  376  1                                  21
HELIX   23  23 ALA A  466  ASP A  470  1                                   5
SHEET    1   A 8 GLY A 248  VAL A 249  0
SHEET    2   A 8 TYR A 226  GLY A 229  1  O  CYS A 227   N  GLY A 248
SHEET    3   A 8 GLY A 202  ILE A 205  1  N  LEU A 203   O  TYR A 226
SHEET    4   A 8 TYR A 113  VAL A 118  1  O  LEU A 114   N  GLY A 202
SHEET    5   A 8 ALA A  59  ILE A  62  1  O  ILE A  60   N  MET A 115
SHEET    6   A 8 ILE A  11  PHE A  13  1  N  TYR A  12   O  ALA A  59
SHEET    7   A 8 ILE A 324  TYR A 328  1  O  PRO A 325   N  ILE A  11
SHEET    8   A 8 GLY A 290  ASN A 291  1  N  ASN A 291   O  ILE A 324
SHEET    1   B 2 THR A  66  GLN A  68  0
SHEET    2   B 2 GLN A  84  VAL A  90 -1  N  GLN A  85   O  GLU A  67
SHEET    1   C 2 GLU A 166  GLY A 167  0
SHEET    2   C 2 SER A 172  LEU A 173 -1  N  LEU A 173   O  GLU A 166
SHEET    1   D 6 ASP A 385  ASP A 390  0
SHEET    2   D 6 THR A 393  LYS A 398 -1  O  THR A 393   N  ASP A 390
SHEET    3   D 6 VAL A 405  SER A 410 -1  N  VAL A 405   O  LYS A 398
SHEET    4   D 6 ARG A 461  PRO A 465 -1  O  ARG A 461   N  VAL A 408
SHEET    5   D 6 LYS A 433  GLU A 436 -1  N  ILE A 435   O  LEU A 464
SHEET    6   D 6 THR A 441  THR A 444 -1  O  THR A 441   N  GLU A 436
SHEET    1   E 2 TYR A 419  LEU A 423  0
SHEET    2   E 2 ILE A 451  MET A 455 -1  N  ILE A 451   O  LEU A 423
SSBOND   1 CYS A   30    CYS A   38                          1555   1555  2.06
SSBOND   2 CYS A  150    CYS A  164                          1555   1555  2.00
SSBOND   3 CYS A  240    CYS A  283                          1555   1555  2.04
SSBOND   4 CYS A  440    CYS A  475                          1555   1555  2.04
LINK        CA    CA A 485                 O   GLU A 210     1555   1555  2.40
LINK        CA    CA A 485                 O   GLU A 162     1555   1555  2.63
LINK        CA    CA A 485                 O   HOH A 499     1555   1555  2.60
LINK        CA    CA A 485                 O   HOH A 590     1555   1555  2.58
LINK        CA    CA A 485                 OD1 ASP A 121     1555   1555  2.56
LINK        CA    CA A 485                 OD1 ASP A 175     1555   1555  2.81
LINK        CA    CA A 485                 OD2 ASP A 175     1555   1555  2.61
LINK        CA    CA A 485                 O   HOH A 495     1555   1555  2.50
LINK        CA    CA A 486                 OE1 GLU A 230     1555   1555  2.72
LINK        CA    CA A 486                 OE2 GLU A 230     1555   1555  2.86
LINK        CA    CA A 486                 O   HOH A 507     1555   1555  2.53
LINK        CA    CA A 486                 O   HOH A 599     1555   1555  2.62
LINK        CA    CA A 486                 O   HOH A 789     1555   1555  2.83
LINK        CA    CA A 486                 O   HOH A 800     1555   1555  2.83
LINK        CA    CA A 486                 O   HOH A 801     1555   1555  2.72
LINK        CA    CA A 486                 OD1 ASP A 206     1555   1555  2.62
CISPEP   1 ASP A  138    PRO A  139          0        -0.08
CISPEP   2 VAL A  340    PRO A  341          0        -1.31
SITE     1 AC1  7 ASP A 121  GLU A 162  ASP A 175  GLU A 210
SITE     2 AC1  7 HOH A 495  HOH A 499  HOH A 590
SITE     1 AC2  7 ASP A 206  GLU A 230  HOH A 507  HOH A 599
SITE     2 AC2  7 HOH A 789  HOH A 800  HOH A 801
CRYST1   81.100   98.300  138.000  90.00  90.00  90.00 C 2 2 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      0.012330  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010173  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007246        0.00000
      
PROCHECK
Go to PROCHECK summary
 References