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PDBsum entry 1b0i

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Hydrolase PDB id
1b0i
Jmol
Contents
Protein chain
448 a.a. *
Metals
_CL
_CA
Waters ×303
* Residue conservation analysis
HEADER    HYDROLASE                               10-NOV-98   1B0I
TITLE     ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN (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: PSEUDOALTEROMONAS HALOPLANKTIS;
SOURCE   3 ORGANISM_TAXID: 228;
SOURCE   4 STRAIN: ALTEROMONAS HALOPLANCTIS A23;
SOURCE   5 GENE: AMY;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    ALPHA-AMYLASE, ALPHA-1, 4-GLUCAN-4-GLUCANOHYDROLASE, BETA-
KEYWDS   2 ALPHA-EIGHT BARREL, PSYCHROPHILIC ENZYME
EXPDTA    X-RAY DIFFRACTION
AUTHOR    N.AGHAJARI,R.HASER
REVDAT   3   24-FEB-09 1B0I    1       VERSN
REVDAT   2   01-APR-03 1B0I    1       JRNL
REVDAT   1   17-NOV-99 1B0I    0
JRNL        AUTH   N.AGHAJARI,G.FELLER,C.GERDAY,R.HASER
JRNL        TITL   STRUCTURES OF THE PSYCHROPHILIC ALTEROMONAS
JRNL        TITL 2 HALOPLANCTIS ALPHA-AMYLASE GIVE INSIGHTS INTO COLD
JRNL        TITL 3 ADAPTATION AT A MOLECULAR LEVEL.
JRNL        REF    STRUCTURE                     V.   6  1503 1998
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   9862804
JRNL        DOI    10.1016/S0969-2126(98)00149-X
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   N.AGHAJARI,G.FELLER,C.H.GERDAY,R.HASER
REMARK   1  TITL   CRYSTAL STRUCTURES OF THE PSYCHROPHILIC
REMARK   1  TITL 2 ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS IN ITS
REMARK   1  TITL 3 NATIVE FORM AND COMPLEXED WITH AN INHIBITOR
REMARK   1  REF    PROTEIN SCI.                  V.   7   564 1998
REMARK   1  REFN                   ISSN 0961-8368
REMARK   2
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.843
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.7
REMARK   3   NUMBER OF REFLECTIONS             : 21666
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.180
REMARK   3   FREE R VALUE                     : 0.217
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 8
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.53
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.00
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2216
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2740
REMARK   3   BIN FREE R VALUE                    : 0.3160
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 : 0.020
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4213
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 303
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  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) : 0.010
REMARK   3   BOND ANGLES            (DEGREES) : 1.65
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.40
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  : PARHCSDX.PRO
REMARK   3  PARAMETER FILE  2  : PARAM3_MOD.CHO
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT REFINEMENT HAS BEEN
REMARK   3  APPLIED THROUGHOUT THE REFINEMENT PROCESS
REMARK   4
REMARK   4 1B0I COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-NOV-98.
REMARK 100 THE RCSB ID CODE IS RCSB000053.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 288.0
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 RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE
REMARK 200  OPTICS                         : COLLIMATOR
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (AGROVATA, ROTAVATA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21666
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0
REMARK 200  DATA REDUNDANCY                : 5.900
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.17700
REMARK 200   FOR THE DATA SET  : 4.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.68200
REMARK 200   FOR SHELL         : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: WILDTYPE AHA (1AQH)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 56.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0
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       28.40000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.05000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.15000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.05000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.40000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.15000
REMARK 290   SMTRY3   4  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     THR A   449
REMARK 465     SER A   450
REMARK 465     SER A   451
REMARK 465     ALA A   452
REMARK 465     SER A   453
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     HIS A 269    CA   C    O    CB   CG   ND1  CD2
REMARK 470     HIS A 269    CE1  NE2
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    THR A   3      -13.45   -140.98
REMARK 500    TYR A  23      -63.19   -138.80
REMARK 500    ASN A 323       73.55     58.28
REMARK 500    GLU A 327       57.19    -90.82
REMARK 500    PHE A 329       -9.63     71.45
REMARK 500    ALA A 330     -125.89   -104.18
REMARK 500    ASN A 332     -105.96   -107.27
REMARK 500    ASN A 355       93.28   -162.59
REMARK 500    THR A 365       -4.56     70.26
REMARK 500    ASN A 366     -114.96   -124.86
REMARK 500    LYS A 383       39.33    -99.36
REMARK 500    ALA A 445       48.13   -141.62
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                              CA A 800  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 144   OD1
REMARK 620 2 ASP A 144   OD2  52.5
REMARK 620 3 GLN A 135   O   123.1  77.6
REMARK 620 4 ASN A  88   OD1  75.8 127.7 149.3
REMARK 620 5 HIS A 178   O   136.8 150.2  76.6  73.9
REMARK 620 6 HOH A1091   O    78.3  87.3 129.9  74.2 120.8
REMARK 620 7 HOH A1107   O    75.9  82.8  72.0  92.4  75.4 153.2
REMARK 620 8 HOH A1108   O   138.9 101.8  68.9 114.6  82.4  68.0 138.5
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE
REMARK 800 SITE_IDENTIFIER: CLB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CHLORIDE BINDING SITE
REMARK 800 SITE_IDENTIFIER: CAB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 900
DBREF  1B0I A    1   453  UNP    P29957   AMY_ALTHA       25    477
SEQRES   1 A  453  THR PRO THR THR PHE VAL HIS LEU PHE GLU TRP ASN TRP
SEQRES   2 A  453  GLN ASP VAL ALA GLN GLU CYS GLU GLN TYR LEU GLY PRO
SEQRES   3 A  453  LYS GLY TYR ALA ALA VAL GLN VAL SER PRO PRO ASN GLU
SEQRES   4 A  453  HIS ILE THR GLY SER GLN TRP TRP THR ARG TYR GLN PRO
SEQRES   5 A  453  VAL SER TYR GLU LEU GLN SER ARG GLY GLY ASN ARG ALA
SEQRES   6 A  453  GLN PHE ILE ASP MET VAL ASN ARG CYS SER ALA ALA GLY
SEQRES   7 A  453  VAL ASP ILE TYR VAL ASP THR LEU ILE ASN HIS MET ALA
SEQRES   8 A  453  ALA GLY SER GLY THR GLY THR ALA GLY ASN SER PHE GLY
SEQRES   9 A  453  ASN LYS SER PHE PRO ILE TYR SER PRO GLN ASP PHE HIS
SEQRES  10 A  453  GLU SER CYS THR ILE ASN ASN SER ASP TYR GLY ASN ASP
SEQRES  11 A  453  ARG TYR ARG VAL GLN ASN CYS GLU LEU VAL GLY LEU ALA
SEQRES  12 A  453  ASP LEU ASP THR ALA SER ASN TYR VAL GLN ASN THR ILE
SEQRES  13 A  453  ALA ALA TYR ILE ASN ASP LEU GLN ALA ILE GLY VAL LYS
SEQRES  14 A  453  GLY PHE ARG PHE ASP ALA SER LYS HIS VAL ALA ALA SER
SEQRES  15 A  453  ASP ILE GLN SER LEU MET ALA LYS VAL ASN GLY SER PRO
SEQRES  16 A  453  VAL VAL PHE GLN GLU VAL ILE ASP GLN GLY GLY GLU ALA
SEQRES  17 A  453  VAL GLY ALA SER GLU TYR LEU SER THR GLY LEU VAL THR
SEQRES  18 A  453  GLU PHE LYS TYR SER THR GLU LEU GLY ASN THR PHE ARG
SEQRES  19 A  453  ASN GLY SER LEU ALA TRP LEU SER ASN PHE GLY GLU GLY
SEQRES  20 A  453  TRP GLY PHE MET PRO SER SER SER ALA VAL VAL PHE VAL
SEQRES  21 A  453  ASP ASN HIS ASP ASN GLN ARG GLY HIS GLY GLY ALA GLY
SEQRES  22 A  453  ASN VAL ILE THR PHE GLU ASP GLY ARG LEU TYR ASP LEU
SEQRES  23 A  453  ALA ASN VAL PHE MET LEU ALA TYR PRO TYR GLY TYR PRO
SEQRES  24 A  453  LYS VAL MET SER SER TYR ASP PHE HIS GLY ASP THR ASP
SEQRES  25 A  453  ALA GLY GLY PRO ASN VAL PRO VAL HIS ASN ASN GLY ASN
SEQRES  26 A  453  LEU GLU CYS PHE ALA SER ASN TRP LYS CYS GLU HIS ARG
SEQRES  27 A  453  TRP SER TYR ILE ALA GLY GLY VAL ASP PHE ARG ASN ASN
SEQRES  28 A  453  THR ALA ASP ASN TRP ALA VAL THR ASN TRP TRP ASP ASN
SEQRES  29 A  453  THR ASN ASN GLN ILE SER PHE GLY ARG GLY SER SER GLY
SEQRES  30 A  453  HIS MET ALA ILE ASN LYS GLU ASP SER THR LEU THR ALA
SEQRES  31 A  453  THR VAL GLN THR ASP MET ALA SER GLY GLN TYR CYS ASN
SEQRES  32 A  453  VAL LEU LYS GLY GLU LEU SER ALA ASP ALA LYS SER CYS
SEQRES  33 A  453  SER GLY GLU VAL ILE THR VAL ASN SER ASP GLY THR ILE
SEQRES  34 A  453  ASN LEU ASN ILE GLY ALA TRP ASP ALA MET ALA ILE HIS
SEQRES  35 A  453  LYS ASN ALA LYS LEU ASN THR SER SER ALA SER
HET     CA  A 800       1
HET     CL  A 900       1
HETNAM      CA CALCIUM ION
HETNAM      CL CHLORIDE ION
FORMUL   2   CA    CA 2+
FORMUL   3   CL    CL 1-
FORMUL   4  HOH   *101(H2 O)
HELIX    1   1 TRP A   13  GLN A   22  1                                  10
HELIX    2   2 LEU A   24  LYS A   27  1                                   4
HELIX    3   3 TRP A   46  TYR A   50  5                                   5
HELIX    4   4 ARG A   64  ALA A   76  1                                  13
HELIX    5   5 PRO A  113  ASP A  115  5                                   3
HELIX    6   6 ASP A  126  ASN A  129  1                                   4
HELIX    7   7 ARG A  131  ASN A  136  1                                   6
HELIX    8   8 LEU A  139  GLY A  141  5                                   3
HELIX    9   9 ASN A  150  ILE A  166  1                                  17
HELIX   10  10 SER A  176  HIS A  178  5                                   3
HELIX   11  11 ALA A  181  LYS A  190  1                                  10
HELIX   12  12 ALA A  211  THR A  217  5                                   7
HELIX   13  13 PHE A  223  ASN A  235  1                                  13
HELIX   14  14 LEU A  238  ASN A  243  5                                   6
HELIX   15  15 GLU A  246  TRP A  248  5                                   3
HELIX   16  16 SER A  253  SER A  255  5                                   3
HELIX   17  17 PHE A  278  ALA A  293  5                                  16
HELIX   18  18 GLU A  336  ARG A  338  5                                   3
HELIX   19  19 SER A  340  ASN A  351  1                                  12
SHEET    1   A 6 LYS A 300  SER A 303  0
SHEET    2   A 6 PHE A   5  LEU A   8  1  N  PHE A   5   O  VAL A 301
SHEET    3   A 6 ALA A  31  VAL A  34  1  N  ALA A  31   O  VAL A   6
SHEET    4   A 6 ASP A  80  LEU A  86  1  N  ASP A  80   O  VAL A  32
SHEET    5   A 6 GLY A 170  ASP A 174  1  N  GLY A 170   O  VAL A  83
SHEET    6   A 6 VAL A 196  GLN A 199  1  N  VAL A 196   O  PHE A 171
SHEET    1   B 3 GLN A 368  GLY A 372  0
SHEET    2   B 3 GLY A 377  ASN A 382 -1  N  ILE A 381   O  ILE A 369
SHEET    3   B 3 ASP A 437  HIS A 442 -1  N  ILE A 441   O  HIS A 378
SHEET    1   C 2 THR A 391  GLN A 393  0
SHEET    2   C 2 THR A 428  ASN A 430 -1  N  ILE A 429   O  VAL A 392
SHEET    1   D 2 GLY A 399  CYS A 402  0
SHEET    2   D 2 VAL A 420  VAL A 423 -1  N  VAL A 423   O  GLY A 399
SSBOND   1 CYS A   20    CYS A   74                          1555   1555  2.03
SSBOND   2 CYS A  120    CYS A  137                          1555   1555  2.04
SSBOND   3 CYS A  328    CYS A  335                          1555   1555  2.03
SSBOND   4 CYS A  402    CYS A  416                          1555   1555  2.03
LINK        CA    CA A 800                 OD1 ASP A 144     1555   1555  2.46
LINK        CA    CA A 800                 OD2 ASP A 144     1555   1555  2.48
LINK        CA    CA A 800                 O   GLN A 135     1555   1555  2.68
LINK        CA    CA A 800                 OD1 ASN A  88     1555   1555  2.41
LINK        CA    CA A 800                 O   HIS A 178     1555   1555  2.46
LINK        CA    CA A 800                 O   HOH A1091     1555   1555  2.44
LINK        CA    CA A 800                 O   HOH A1107     1555   1555  2.34
LINK        CA    CA A 800                 O   HOH A1108     1555   1555  2.57
SITE     1 ACT  3 ASP A 174  GLU A 200  ASP A 264
SITE     1 CLB  4 ARG A 172  LYS A 300  ASN A 262  HOH A1003
SITE     1 CAB  7 ASN A  88  ASP A 144  GLN A 135  HIS A 178
SITE     2 CAB  7 HOH A1108  HOH A1091  HOH A1107
SITE     1 AC1  7 ASN A  88  GLN A 135  ASP A 144  HIS A 178
SITE     2 AC1  7 HOH A1091  HOH A1107  HOH A1108
SITE     1 AC2  2 ARG A 172  LYS A 300
CRYST1   56.800   80.300  120.100  90.00  90.00  90.00 P 21 21 21    4
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      0.017606  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012453  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008326        0.00000
      
PROCHECK
Go to PROCHECK summary
 References