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PDBsum entry 2dqx

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Hydrolase PDB id
2dqx
Jmol
Contents
Protein chain
491 a.a.
Waters ×327
HEADER    HYDROLASE                               01-JUN-06   2DQX
TITLE     MUTANT BETA-AMYLASE (W55R) FROM SOY BEAN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: BETA-AMYLASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.2.1.2;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: GLYCINE MAX;
SOURCE   3 ORGANISM_COMMON: SOYBEAN;
SOURCE   4 ORGANISM_TAXID: 3847;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PBAMSO
KEYWDS    AMYLASE MUTANT SLIDING SOY BEAN, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.ISHIKAWA
REVDAT   2   24-FEB-09 2DQX    1       VERSN
REVDAT   1   08-MAY-07 2DQX    0
JRNL        AUTH   K.ISHIKAWA,H.NAKATANI,Y.KATSUYA,C.FUKAZAWA
JRNL        TITL   KINETIC AND STRUCTURAL ANALYSIS OF ENZYME SLIDING
JRNL        TITL 2 ON A SUBSTRATE: MULTIPLE ATTACK IN BETA-AMYLASE
JRNL        REF    BIOCHEMISTRY                  V.  46   792 2007
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   17223700
JRNL        DOI    10.1021/BI061605W
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
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) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.90
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2526968.690
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.1
REMARK   3   NUMBER OF REFLECTIONS             : 30579
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) : 0.206
REMARK   3   FREE R VALUE                     : 0.252
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900
REMARK   3   FREE R VALUE TEST SET COUNT      : 1513
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.90
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4578
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2210
REMARK   3   BIN FREE R VALUE                    : 0.2700
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.20
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 250
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3921
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 327
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 5.00
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 11.70
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 2.23000
REMARK   3    B22 (A**2) : 2.23000
REMARK   3    B33 (A**2) : -4.46000
REMARK   3    B12 (A**2) : 0.08000
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) : 0.24
REMARK   3   ESD FROM SIGMAA              (A) : 0.15
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.31
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.22
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) : 22.30
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.82
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.170 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.820 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.990 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.750 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.41
REMARK   3   BSOL        : 60.51
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  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : ION.PARAM
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP
REMARK   3  TOPOLOGY FILE  3   : ION.TOP
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2DQX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUN-06.
REMARK 100 THE RCSB ID CODE IS RCSB025738.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 12-OCT-99
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.4
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SPRING-8
REMARK 200  BEAMLINE                       : BL24XU
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.835
REMARK 200  MONOCHROMATOR                  : GRAPHITE
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR (MSC/RIGAKU)
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31087
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.950
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.07400
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) : 2.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1WDP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE (PH 5.4),  1MM
REMARK 280  EDTA, 50% AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+2/3
REMARK 290       6555   -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.36100
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       96.72200
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       96.72200
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       48.36100
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     ALA A     1
REMARK 465     THR A     2
REMARK 465     SER A     3
REMARK 465     ASP A     4
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    LYS A   214     O    HOH A   775              2.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH A   548     O    HOH A   548     4555     2.18
REMARK 500
REMARK 500 REMARK: NULL
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    PHE A  92       31.67    -92.82
REMARK 500    ALA A 184       16.39     59.23
REMARK 500    PRO A 201       49.60   -105.03
REMARK 500    HIS A 308       45.29     38.83
REMARK 500    SER A 412      143.43   -170.69
REMARK 500    ARG A 420      127.34     54.24
REMARK 500    ASP A 494       86.13    -68.74
REMARK 500
REMARK 500 REMARK: NULL
DBREF  2DQX A    1   495  UNP    Q42795   Q42795_SOYBN     2    496
SEQADV 2DQX ARG A   55  UNP  Q42795    TRP    56 ENGINEERED
SEQRES   1 A  495  ALA THR SER ASP SER ASN MET LEU LEU ASN TYR VAL PRO
SEQRES   2 A  495  VAL TYR VAL MET LEU PRO LEU GLY VAL VAL ASN VAL ASP
SEQRES   3 A  495  ASN VAL PHE GLU ASP PRO ASP GLY LEU LYS GLU GLN LEU
SEQRES   4 A  495  LEU GLN LEU ARG ALA ALA GLY VAL ASP GLY VAL MET VAL
SEQRES   5 A  495  ASP VAL ARG TRP GLY ILE ILE GLU LEU LYS GLY PRO LYS
SEQRES   6 A  495  GLN TYR ASP TRP ARG ALA TYR ARG SER LEU PHE GLN LEU
SEQRES   7 A  495  VAL GLN GLU CYS GLY LEU THR LEU GLN ALA ILE MET SER
SEQRES   8 A  495  PHE HIS GLN CYS GLY GLY ASN VAL GLY ASP ILE VAL ASN
SEQRES   9 A  495  ILE PRO ILE PRO GLN TRP VAL LEU ASP ILE GLY GLU SER
SEQRES  10 A  495  ASN HIS ASP ILE PHE TYR THR ASN ARG SER GLY THR ARG
SEQRES  11 A  495  ASN LYS GLU TYR LEU THR VAL GLY VAL ASP ASN GLU PRO
SEQRES  12 A  495  ILE PHE HIS GLY ARG THR ALA ILE GLU ILE TYR SER ASP
SEQRES  13 A  495  TYR MET LYS SER PHE ARG GLU ASN MET SER ASP PHE LEU
SEQRES  14 A  495  GLU SER GLY LEU ILE ILE ASP ILE GLU VAL GLY LEU GLY
SEQRES  15 A  495  PRO ALA GLY GLU LEU ARG TYR PRO SER TYR PRO GLN SER
SEQRES  16 A  495  GLN GLY TRP GLU PHE PRO GLY ILE GLY GLU PHE GLN CYS
SEQRES  17 A  495  TYR ASP LYS TYR LEU LYS ALA ASP PHE LYS ALA ALA VAL
SEQRES  18 A  495  ALA ARG ALA GLY HIS PRO GLU TRP GLU LEU PRO ASP ASP
SEQRES  19 A  495  ALA GLY LYS TYR ASN ASP VAL PRO GLU SER THR GLY PHE
SEQRES  20 A  495  PHE LYS SER ASN GLY THR TYR VAL THR GLU LYS GLY LYS
SEQRES  21 A  495  PHE PHE LEU THR TRP TYR SER ASN LYS LEU LEU ASN HIS
SEQRES  22 A  495  GLY ASP GLN ILE LEU ASP GLU ALA ASN LYS ALA PHE LEU
SEQRES  23 A  495  GLY CYS LYS VAL LYS LEU ALA ILE LYS VAL SER GLY ILE
SEQRES  24 A  495  HIS TRP TRP TYR LYS VAL GLU ASN HIS ALA ALA GLU LEU
SEQRES  25 A  495  THR ALA GLY TYR TYR ASN LEU ASN ASP ARG ASP GLY TYR
SEQRES  26 A  495  ARG PRO ILE ALA ARG MET LEU SER ARG HIS HIS ALA ILE
SEQRES  27 A  495  LEU ASN PHE THR CYS LEU GLU MET ARG ASP SER GLU GLN
SEQRES  28 A  495  PRO SER ASP ALA LYS SER GLY PRO GLN GLU LEU VAL GLN
SEQRES  29 A  495  GLN VAL LEU SER GLY GLY TRP ARG GLU ASP ILE ARG VAL
SEQRES  30 A  495  ALA GLY GLU ASN ALA LEU PRO ARG TYR ASP ALA THR ALA
SEQRES  31 A  495  TYR ASN GLN ILE ILE LEU ASN ALA ARG PRO GLN GLY VAL
SEQRES  32 A  495  ASN ASN ASN GLY PRO PRO LYS LEU SER MET PHE GLY VAL
SEQRES  33 A  495  THR TYR LEU ARG LEU SER ASP ASP LEU LEU GLN LYS SER
SEQRES  34 A  495  ASN PHE ASN ILE PHE LYS LYS PHE VAL LEU LYS MET HIS
SEQRES  35 A  495  ALA ASP GLN ASP TYR CYS ALA ASN PRO GLN LYS TYR ASN
SEQRES  36 A  495  HIS ALA ILE THR PRO LEU LYS PRO SER ALA PRO LYS ILE
SEQRES  37 A  495  PRO ILE GLU VAL LEU LEU GLU ALA THR LYS PRO THR LEU
SEQRES  38 A  495  PRO PHE PRO TRP LEU PRO GLU THR ASP MET LYS VAL ASP
SEQRES  39 A  495  GLY
FORMUL   2  HOH   *327(H2 O)
HELIX    1   1 ASN A    6  TYR A   11  5                                   6
HELIX    2   2 ASP A   31  ALA A   45  1                                  15
HELIX    3   3 TRP A   56  GLU A   60  1                                   5
HELIX    4   4 TRP A   69  CYS A   82  1                                  14
HELIX    5   5 PRO A  108  ASN A  118  1                                  11
HELIX    6   6 VAL A  137  ASP A  140  5                                   4
HELIX    7   7 THR A  149  MET A  165  1                                  17
HELIX    8   8 MET A  165  SER A  171  1                                   7
HELIX    9   9 GLY A  182  GLU A  186  5                                   5
HELIX   10  10 PRO A  193  GLY A  197  5                                   5
HELIX   11  11 ASP A  210  ALA A  224  1                                  15
HELIX   12  12 VAL A  241  THR A  245  5                                   5
HELIX   13  13 GLY A  252  VAL A  255  5                                   4
HELIX   14  14 THR A  256  PHE A  285  1                                  30
HELIX   15  15 HIS A  308  GLY A  315  1                                   8
HELIX   16  16 TYR A  325  ARG A  334  1                                  10
HELIX   17  17 ARG A  347  GLN A  351  5                                   5
HELIX   18  18 PRO A  352  LYS A  356  5                                   5
HELIX   19  19 GLY A  358  GLU A  373  1                                  16
HELIX   20  20 ASP A  387  ARG A  399  1                                  13
HELIX   21  21 SER A  422  GLN A  427  1                                   6
HELIX   22  22 GLN A  427  HIS A  442  1                                  16
HELIX   23  23 ASN A  450  ASN A  455  5                                   6
HELIX   24  24 PRO A  469  LEU A  474  1                                   6
HELIX   25  25 GLU A  475  LYS A  478  5                                   4
SHEET    1   A 9 VAL A  14  MET A  17  0
SHEET    2   A 9 GLY A  49  ARG A  55  1  O  GLY A  49   N  VAL A  16
SHEET    3   A 9 THR A  85  SER A  91  1  O  ILE A  89   N  VAL A  54
SHEET    4   A 9 ILE A 174  VAL A 179  1  O  ASP A 176   N  ALA A  88
SHEET    5   A 9 LYS A 291  LYS A 295  1  O  LYS A 291   N  ILE A 177
SHEET    6   A 9 ILE A 338  PHE A 341  1  O  ILE A 338   N  LEU A 292
SHEET    7   A 9 VAL A 377  GLU A 380  1  O  ALA A 378   N  PHE A 341
SHEET    8   A 9 GLY A 415  TYR A 418  1  O  THR A 417   N  GLY A 379
SHEET    9   A 9 VAL A  14  MET A  17  1  N  TYR A  15   O  TYR A 418
SHEET    1   B 2 PHE A 122  THR A 124  0
SHEET    2   B 2 ARG A 130  LEU A 135 -1  O  ASN A 131   N  TYR A 123
CISPEP   1 PHE A  200    PRO A  201          0         0.05
CRYST1   85.042   85.042  145.083  90.00  90.00 120.00 P 31 2 1      6
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      0.011759  0.006789  0.000000        0.00000
SCALE2      0.000000  0.013578  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006893        0.00000
      
PROCHECK
Go to PROCHECK summary
 References