longtext: 7ukb-pdb

content
HEADER    HYDROLASE                               01-APR-22   7UKB
TITLE     ANCESTRAL RECONSTRUCTION OF A PLANT ALPHA/BETA-HYDROLASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ALPHA/BETA-HYDROLASE;
COMPND   3 CHAIN: A;
COMPND   4 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE   3 ORGANISM_TAXID: 32630;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    ANCESTRAL RECONSTRUCTION, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.C.MARSHALL,E.ROTHZERG,A.TUCKEY,C.S.BOND,M.T.WATERS,T.A.BENNETT
REVDAT   1   05-APR-23 7UKB    0
JRNL        AUTH   A.TUCKEY
JRNL        TITL   ANCESTRAL RECONSTRUCTION OF A PLANT ALPHA/BETA-HYDROLASE
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX 1.19.1
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) : 1.95
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.80
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8
REMARK   3   NUMBER OF REFLECTIONS             : 19558
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.187
REMARK   3   R VALUE            (WORKING SET) : 0.184
REMARK   3   FREE R VALUE                     : 0.233
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050
REMARK   3   FREE R VALUE TEST SET COUNT      : 988
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 45.8000 -  3.7200    1.00     2851   155  0.1605 0.1819
REMARK   3     2  3.7200 -  2.9600    1.00     2680   142  0.1645 0.2329
REMARK   3     3  2.9600 -  2.5800    1.00     2642   146  0.2014 0.2757
REMARK   3     4  2.5800 -  2.3500    1.00     2601   158  0.2086 0.2687
REMARK   3     5  2.3500 -  2.1800    1.00     2619   128  0.2072 0.2737
REMARK   3     6  2.1800 -  2.0500    1.00     2600   131  0.2270 0.2630
REMARK   3     7  2.0500 -  1.9500    0.99     2577   128  0.2591 0.3143
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)     : 0.200
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.790
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 29.40
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.16
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  : 3
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 148 )
REMARK   3    ORIGIN FOR THE GROUP (A):  18.8971  -3.5174   8.6032
REMARK   3    T TENSOR
REMARK   3      T11:   0.2200 T22:   0.2043
REMARK   3      T33:   0.2096 T12:  -0.0298
REMARK   3      T13:  -0.0185 T23:   0.0298
REMARK   3    L TENSOR
REMARK   3      L11:   2.7406 L22:   1.0265
REMARK   3      L33:   1.2513 L12:  -0.5074
REMARK   3      L13:  -0.5611 L23:   0.0334
REMARK   3    S TENSOR
REMARK   3      S11:   0.0015 S12:   0.1024 S13:   0.2213
REMARK   3      S21:   0.0460 S22:  -0.0123 S23:  -0.0228
REMARK   3      S31:  -0.1354 S32:   0.0491 S33:   0.0043
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 149 THROUGH 193 )
REMARK   3    ORIGIN FOR THE GROUP (A):  12.3664  -6.4153  23.0260
REMARK   3    T TENSOR
REMARK   3      T11:   0.2308 T22:   0.2753
REMARK   3      T33:   0.2043 T12:  -0.0031
REMARK   3      T13:   0.0053 T23:  -0.0164
REMARK   3    L TENSOR
REMARK   3      L11:   1.5628 L22:   1.4092
REMARK   3      L33:   2.2445 L12:   0.4042
REMARK   3      L13:  -0.3894 L23:  -0.4009
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0403 S12:  -0.1975 S13:   0.0443
REMARK   3      S21:   0.0238 S22:   0.0002 S23:  -0.0094
REMARK   3      S31:  -0.1351 S32:  -0.0007 S33:   0.0412
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 194 THROUGH 265 )
REMARK   3    ORIGIN FOR THE GROUP (A):  11.5965 -14.6052   3.2105
REMARK   3    T TENSOR
REMARK   3      T11:   0.2603 T22:   0.3334
REMARK   3      T33:   0.2586 T12:  -0.0332
REMARK   3      T13:  -0.0114 T23:  -0.0530
REMARK   3    L TENSOR
REMARK   3      L11:   2.2866 L22:   1.6708
REMARK   3      L33:   1.9085 L12:  -0.3128
REMARK   3      L13:   0.8716 L23:  -1.1241
REMARK   3    S TENSOR
REMARK   3      S11:   0.0223 S12:   0.4064 S13:  -0.1988
REMARK   3      S21:  -0.2053 S22:   0.0185 S23:   0.0207
REMARK   3      S31:   0.2283 S32:  -0.0845 S33:  -0.0767
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 7UKB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-22.
REMARK 100 THE DEPOSITION ID IS D_1000264328.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 19-MAR-22
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               : AUSTRALIAN SYNCHROTRON
REMARK 200  BEAMLINE                       : MX1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95372
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 9M
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.7.4
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19665
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.690
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 26.00
REMARK 200  R MERGE                    (I) : 0.23600
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.99
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 25.60
REMARK 200  R MERGE FOR SHELL          (I) : 3.13400
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 2.8.3
REMARK 200 STARTING MODEL: 4HTA
REMARK 200
REMARK 200 REMARK: SQUARE BIPYRAMIDAL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 36.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% W/V PEG 1500, PH 7.5, VAPOR
REMARK 280  DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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   -Y+1/2,X+1/2,Z+3/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z+1/2
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       73.03400
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       29.39600
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       29.39600
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      109.55100
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       29.39600
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       29.39600
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       36.51700
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       29.39600
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       29.39600
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      109.55100
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       29.39600
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       29.39600
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       36.51700
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       73.03400
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH A 605  LIES ON A SPECIAL POSITION.
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 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     ASP A  60    OD1  OD2
REMARK 470     GLU A  87    CD   OE1  OE2
REMARK 470     ASP A 129    OD1  OD2
REMARK 470     GLU A 147    CD   OE1  OE2
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    SER A  95     -116.97     54.33
REMARK 500
REMARK 500 REMARK: NULL
DBREF  7UKB A    1   265  PDB    7UKB     7UKB             1    265
SEQRES   1 A  265  MET SER GLY LEU LEU GLU ALA LEU ASN VAL ARG VAL VAL
SEQRES   2 A  265  GLY SER GLY GLU ARG ILE LEU VAL LEU SER HIS GLY PHE
SEQRES   3 A  265  GLY THR ASP GLN SER VAL TRP GLN ARG ILE LEU PRO TYR
SEQRES   4 A  265  PHE LEU ARG ASP PHE LYS VAL VAL LEU TYR ASP LEU VAL
SEQRES   5 A  265  CYS ALA GLY SER VAL ASN PRO ASP ASN PHE ASP PHE ASN
SEQRES   6 A  265  ARG TYR SER SER LEU ASP ALA TYR VAL ASP ASP LEU LEU
SEQRES   7 A  265  ALA ILE LEU ASP GLU LEU ASN ILE GLU LYS CYS VAL TYR
SEQRES   8 A  265  VAL GLY HIS SER VAL SER ALA MET ILE GLY CYS LEU ALA
SEQRES   9 A  265  SER ILE ARG ARG PRO ALA LEU PHE GLN LYS LEU ILE LEU
SEQRES  10 A  265  LEU GLY ALA SER PRO ARG TYR LEU ASN ASP GLY ASP TYR
SEQRES  11 A  265  GLU GLY GLY PHE GLU GLN GLU ASP ILE ASP GLN VAL PHE
SEQRES  12 A  265  SER ALA MET GLU SER ASN TYR ALA ALA TRP VAL SER GLY
SEQRES  13 A  265  PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL PRO ALA ALA
SEQRES  14 A  265  VAL ARG GLU PHE SER ARG THR LEU PHE ASN MET ARG PRO
SEQRES  15 A  265  ASP ILE ALA LEU PHE VAL ALA ARG THR VAL PHE GLU SER
SEQRES  16 A  265  ASP LEU ARG GLY ILE LEU GLY GLN VAL LYS VAL PRO CYS
SEQRES  17 A  265  HIS ILE ILE GLN THR LYS LYS ASP VAL ALA VAL PRO LEU
SEQRES  18 A  265  SER VAL ALA ASP TYR LEU CYS ARG HIS LEU GLY GLY LYS
SEQRES  19 A  265  THR THR VAL GLU ILE LEU GLN THR GLU GLY HIS LEU PRO
SEQRES  20 A  265  GLN LEU SER ALA PRO ALA LEU VAL ILE GLN LEU LEU ARG
SEQRES  21 A  265  ARG ALA LEU SER SER
HET     CL  A 301       1
HETNAM      CL CHLORIDE ION
FORMUL   2   CL    CL 1-
FORMUL   3  HOH   *237(H2 O)
HELIX    1 AA1 GLY A    3  LEU A    8  1                                   6
HELIX    2 AA2 ASP A   29  GLN A   34  5                                   6
HELIX    3 AA3 ILE A   36  LEU A   41  5                                   6
HELIX    4 AA4 ASN A   58  PHE A   62  5                                   5
HELIX    5 AA5 ASN A   65  SER A   68  5                                   4
HELIX    6 AA6 SER A   69  LEU A   84  1                                  16
HELIX    7 AA7 SER A   95  ARG A  108  1                                  14
HELIX    8 AA8 GLU A  135  ASN A  149  1                                  15
HELIX    9 AA9 ASN A  149  GLY A  163  1                                  15
HELIX   10 AB1 VAL A  166  ASN A  179  1                                  14
HELIX   11 AB2 ARG A  181  GLU A  194  1                                  14
HELIX   12 AB3 LEU A  197  VAL A  204  5                                   8
HELIX   13 AB4 PRO A  220  LEU A  231  1                                  12
HELIX   14 AB5 LEU A  246  ALA A  251  1                                   6
HELIX   15 AB6 ALA A  251  LEU A  263  1                                  13
SHEET    1 AA1 7 ARG A  11  VAL A  13  0
SHEET    2 AA1 7 PHE A  44  LEU A  48 -1  O  LEU A  48   N  ARG A  11
SHEET    3 AA1 7 ARG A  18  SER A  23  1  N  LEU A  20   O  VAL A  47
SHEET    4 AA1 7 CYS A  89  HIS A  94  1  O  VAL A  92   N  VAL A  21
SHEET    5 AA1 7 PHE A 112  LEU A 118  1  O  ILE A 116   N  TYR A  91
SHEET    6 AA1 7 CYS A 208  LYS A 215  1  O  ILE A 211   N  LEU A 117
SHEET    7 AA1 7 THR A 235  GLU A 243  1  O  LEU A 240   N  GLN A 212
CRYST1   58.792   58.792  146.068  90.00  90.00  90.00 P 43 21 2     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      0.017009  0.000000  0.000000        0.00000
SCALE2      0.000000  0.017009  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006846        0.00000
TER    2056      SER A 265
MASTER      299    0    1   15    7    0    0    6 2268    1    0   21
END