longtext: 7w1k-pdb

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HEADER    HYDROLASE                               19-NOV-21   7W1K
TITLE     CRYSTAL STRUCTURE OF CARBOXYLESTERASE FROM THERMOBIFIDA FUSCA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBOXYLESTERASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.1.1.1;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOBIFIDA FUSCA;
SOURCE   3 ORGANISM_COMMON: THERMOMONOSPORA FUSCA;
SOURCE   4 ORGANISM_TAXID: 2021;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-28A
KEYWDS    PLASTIC DEGRADATION, HYDROLASE, CATALYSIS
EXPDTA    X-RAY DIFFRACTION
AUTHOR    X.HAN,H.GERLIS,Z.LI,J.GAO,R.WEI,W.LIU
REVDAT   1   23-NOV-22 7W1K    0
JRNL        AUTH   X.HAN,H.GERLIS,Z.LI,J.GAO,R.WEI,W.LIU
JRNL        TITL   CRYSTAL STRUCTURE OF CARBOXYLESTERASE MUTANT FROM
JRNL        TITL 2 THERMOBIFIDA FUSCA WITH C8X AND C9C
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.39 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX 1.19.2_4158
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.39
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.89
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.370
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8
REMARK   3   NUMBER OF REFLECTIONS             : 103747
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.168
REMARK   3   R VALUE            (WORKING SET) : 0.167
REMARK   3   FREE R VALUE                     : 0.184
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 5188
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 24.8900 -  3.0000    1.00    10035   528  0.1493 0.1664
REMARK   3     2  3.0000 -  2.3800    0.99     9907   522  0.1691 0.1875
REMARK   3     3  2.3800 -  2.0800    1.00    10005   527  0.1623 0.1832
REMARK   3     4  2.0800 -  1.8900    0.99     9837   518  0.1701 0.1808
REMARK   3     5  1.8900 -  1.7600    1.00     9913   521  0.1725 0.1812
REMARK   3     6  1.7600 -  1.6500    1.00     9928   523  0.1810 0.1915
REMARK   3     7  1.6500 -  1.5700    1.00     9881   520  0.1812 0.2013
REMARK   3     8  1.5700 -  1.5000    0.98     9805   516  0.1857 0.2161
REMARK   3     9  1.5000 -  1.4400    0.99     9858   519  0.2013 0.2202
REMARK   3    10  1.4400 -  1.3900    0.94     9390   494  0.2228 0.2475
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : NULL
REMARK   3   B_SOL              : NULL
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.140
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.850
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 13.79
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.37
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  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :   NULL           NULL
REMARK   3   ANGLE     :   NULL           NULL
REMARK   3   CHIRALITY :   NULL           NULL
REMARK   3   PLANARITY :   NULL           NULL
REMARK   3   DIHEDRAL  :   NULL           NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 7W1K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-NOV-21.
REMARK 100 THE DEPOSITION ID IS D_1300025799.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-JUL-21
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRF
REMARK 200  BEAMLINE                       : BL10U2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : GRAPHITE
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 103778
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.390
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4
REMARK 200  DATA REDUNDANCY                : 6.600
REMARK 200  R MERGE                    (I) : 0.06300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 6.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.45
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.56300
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: PHASER
REMARK 200 STARTING MODEL: 2OGT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 51.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% W/V POLY(ACRYLIC ACID SODIUM SALT)
REMARK 280  5100 0.02 M MGCL2 0.1 M HEPES PH 7.5, 10% GLYCEROL, VAPOR
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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       56.48050
REMARK 290   SMTRY3   2  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     LEU A   497
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   7     -152.29   -106.00
REMARK 500    ASN A  18       62.64     64.87
REMARK 500    ALA A  58      151.51    -46.03
REMARK 500    ASP A  92      118.52   -167.61
REMARK 500    SER A 185     -122.72     55.71
REMARK 500    ALA A 213     -147.17   -134.15
REMARK 500    ALA A 416       -7.73     81.81
REMARK 500    ASP A 483       66.51     29.59
REMARK 500
REMARK 500 REMARK: NULL
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 A1224        DISTANCE =  5.83 ANGSTROMS
REMARK 525    HOH A1225        DISTANCE =  5.86 ANGSTROMS
REMARK 525    HOH A1226        DISTANCE =  5.95 ANGSTROMS
REMARK 525    HOH A1227        DISTANCE =  6.02 ANGSTROMS
REMARK 525    HOH A1228        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A1229        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A1230        DISTANCE =  6.98 ANGSTROMS
DBREF  7W1K A    1   497  UNP    P86325   EST1_THEFU       1    497
SEQRES   1 A  497  MET GLU ILE VAL ILE ARG THR GLY SER GLY ASP VAL ARG
SEQRES   2 A  497  GLY SER LYS GLU ASN GLY ILE ALA VAL PHE ARG GLY ILE
SEQRES   3 A  497  PRO TYR ALA GLU PRO PRO VAL GLY ALA HIS ARG PHE THR
SEQRES   4 A  497  ALA PRO ARG PRO PRO ARG PRO TRP ASP GLY VAL ARG ASP
SEQRES   5 A  497  ALA THR GLU PHE SER ALA THR ALA PRO ARG PRO PRO TYR
SEQRES   6 A  497  PRO GLU ALA ILE GLY ALA LEU LEU ILE GLU ARG PHE ILE
SEQRES   7 A  497  PRO GLY ASP ASP TYR LEU THR LEU ASN VAL TRP THR PRO
SEQRES   8 A  497  ASP PRO ASN ALA VAL GLY LEU PRO VAL MET VAL TRP ILE
SEQRES   9 A  497  HIS GLY GLY ALA PHE THR ASN GLY SER GLY SER GLU PRO
SEQRES  10 A  497  VAL TYR ASP GLY ALA ALA PHE ALA ARG ASP GLY VAL VAL
SEQRES  11 A  497  PHE VAL SER PHE ASN TYR ARG LEU GLY ILE ILE GLY PHE
SEQRES  12 A  497  ALA ASP LEU PRO ASP ALA PRO SER ASN ARG GLY LEU LEU
SEQRES  13 A  497  ASP GLN ILE ALA ALA LEU GLU TRP VAL ARG ASP ASN ILE
SEQRES  14 A  497  ALA ARG PHE GLY GLY ASP PRO GLY ASN VAL THR VAL PHE
SEQRES  15 A  497  GLY GLU SER ALA GLY ALA MET SER VAL CYS THR LEU MET
SEQRES  16 A  497  ALA THR PRO ARG ALA ARG GLY LEU PHE ARG ARG ALA ILE
SEQRES  17 A  497  LEU GLN SER GLY ALA GLY ASN MET ALA VAL ALA ALA GLU
SEQRES  18 A  497  ASP ALA THR THR ILE ALA ALA VAL ILE ALA HIS ARG LEU
SEQRES  19 A  497  GLY VAL GLU PRO THR ALA ALA ALA LEU ALA HIS VAL PRO
SEQRES  20 A  497  VAL ALA GLN LEU LEU ASP VAL GLN GLN GLN VAL ALA GLN
SEQRES  21 A  497  GLU ILE GLN GLY ALA PRO ASP PRO ALA VAL TRP GLY GLU
SEQRES  22 A  497  ARG ILE ALA GLY GLY SER VAL LEU LEU PRO PHE ALA PRO
SEQRES  23 A  497  VAL ILE ASP GLY GLU LEU LEU SER GLN ARG PRO ALA GLU
SEQRES  24 A  497  ALA ILE ALA GLY GLY ALA GLY HIS ASP VAL ASP LEU LEU
SEQRES  25 A  497  PHE GLY THR THR THR ASP GLU TYR ARG LEU PHE LEU ALA
SEQRES  26 A  497  PRO THR GLY LEU LEU PRO PHE ILE THR SER ASP TYR VAL
SEQRES  27 A  497  THR ALA HIS LEU ALA LYS SER GLY LEU ASP ALA ASP ALA
SEQRES  28 A  497  ALA LYS ALA TYR THR ALA GLU GLY ARG GLY GLU GLU PRO
SEQRES  29 A  497  GLY ASP ILE LEU ALA SER ILE ILE THR ASP GLN VAL PHE
SEQRES  30 A  497  ARG ILE PRO ALA LEU ARG ILE ALA GLU SER ARG VAL ASP
SEQRES  31 A  497  ALA PRO ALA ARG THR PHE GLY TYR GLU PHE ALA TRP ARG
SEQRES  32 A  497  THR PRO GLN LEU ASP GLY ILE LEU GLY ALA CYS HIS ALA
SEQRES  33 A  497  VAL GLU LEU PRO PHE VAL PHE ARG THR LEU ASP ARG ALA
SEQRES  34 A  497  ALA SER LEU VAL GLY THR ASN PRO PRO GLU GLU LEU ALA
SEQRES  35 A  497  GLU THR VAL HIS ASN ALA TRP VAL ARG PHE ALA THR SER
SEQRES  36 A  497  GLY ASP PRO GLY TRP PRO ALA TRP ASN PRO GLU THR ARG
SEQRES  37 A  497  SER VAL MET ARG PHE ASP HIS PRO VAL SER GLU MET VAL
SEQRES  38 A  497  THR ASP PRO TYR PRO ALA THR ARG ALA LEU TRP ASP GLY
SEQRES  39 A  497  VAL PRO LEU
FORMUL   2  HOH   *730(H2 O)
HELIX    1 AA1 VAL A   33  PHE A   38  5                                   6
HELIX    2 AA2 PRO A   66  LEU A   73  1                                   8
HELIX    3 AA3 GLU A  116  ASP A  120  5                                   5
HELIX    4 AA4 GLY A  121  ASP A  127  1                                   7
HELIX    5 AA5 LEU A  138  ALA A  144  1                                   7
HELIX    6 AA6 ASN A  152  ILE A  169  1                                  18
HELIX    7 AA7 ALA A  170  PHE A  172  5                                   3
HELIX    8 AA8 SER A  185  ALA A  196  1                                  12
HELIX    9 AA9 THR A  197  ARG A  201  5                                   5
HELIX   10 AB1 ALA A  220  GLY A  235  1                                  16
HELIX   11 AB2 THR A  239  ALA A  244  1                                   6
HELIX   12 AB3 PRO A  247  GLY A  264  1                                  18
HELIX   13 AB4 ASP A  267  GLY A  277  1                                  11
HELIX   14 AB5 ARG A  296  GLY A  303  1                                   8
HELIX   15 AB6 TYR A  320  ALA A  325  1                                   6
HELIX   16 AB7 LEU A  329  ILE A  333  5                                   5
HELIX   17 AB8 THR A  334  SER A  345  1                                  12
HELIX   18 AB9 ASP A  350  GLU A  358  1                                   9
HELIX   19 AC1 GLU A  363  PHE A  377  1                                  15
HELIX   20 AC2 PHE A  377  ARG A  388  1                                  12
HELIX   21 AC3 PRO A  405  ILE A  410  5                                   6
HELIX   22 AC4 GLU A  418  ARG A  424  1                                   7
HELIX   23 AC5 THR A  425  ARG A  428  5                                   4
HELIX   24 AC6 ALA A  429  GLY A  434  1                                   6
HELIX   25 AC7 PRO A  438  GLY A  456  1                                  19
HELIX   26 AC8 TYR A  485  LEU A  491  1                                   7
SHEET    1 AA1 3 GLU A   2  ARG A   6  0
SHEET    2 AA1 3 ASP A  11  LYS A  16 -1  O  GLY A  14   N  ILE A   3
SHEET    3 AA1 3 VAL A  50  ASP A  52  1  O  ARG A  51   N  ASP A  11
SHEET    1 AA212 GLU A   2  ARG A   6  0
SHEET    2 AA212 ASP A  11  LYS A  16 -1  O  GLY A  14   N  ILE A   3
SHEET    3 AA212 ALA A  21  PRO A  27 -1  O  VAL A  22   N  SER A  15
SHEET    4 AA212 THR A  85  THR A  90 -1  O  THR A  90   N  ALA A  21
SHEET    5 AA212 VAL A 130  PHE A 134 -1  O  SER A 133   N  ASN A  87
SHEET    6 AA212 LEU A  98  ILE A 104  1  N  TRP A 103   O  VAL A 132
SHEET    7 AA212 GLY A 174  GLU A 184  1  O  THR A 180   N  VAL A 100
SHEET    8 AA212 ARG A 206  GLN A 210  1  O  GLN A 210   N  GLY A 183
SHEET    9 AA212 ASP A 310  THR A 316  1  O  LEU A 312   N  LEU A 209
SHEET   10 AA212 THR A 395  PHE A 400  1  O  PHE A 400   N  THR A 315
SHEET   11 AA212 SER A 469  PHE A 473  1  O  MET A 471   N  GLU A 399
SHEET   12 AA212 GLU A 479  THR A 482 -1  O  GLU A 479   N  ARG A 472
SHEET    1 AA3 2 VAL A 218  ALA A 219  0
SHEET    2 AA3 2 VAL A 287  ILE A 288  1  O  ILE A 288   N  VAL A 218
CISPEP   1 HIS A  475    PRO A  476          0        10.03
CRYST1   45.277  112.961   54.780  90.00 106.04  90.00 P 1 21 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      0.022086  0.000000  0.006349        0.00000
SCALE2      0.000000  0.008853  0.000000        0.00000
SCALE3      0.000000  0.000000  0.018994        0.00000
TER    3736      PRO A 496
MASTER      241    0    0   26   17    0    0    6 4465    1    0   39
END