longtext: 6aae-pdb

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HEADER    HYDROLASE                               18-JUL-18   6AAE
TITLE     CRYSTAL STRUCTURE OF CHLORAMPHENICOL-METABOLIZAING ENZYME ESTDL136
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ESTERASE;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 3.1.1.1;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: YES;
COMPND   7 OTHER_DETAILS: TO MAKE ESTDL136 CRYSTAL, INTERNAL RESIDUES FROM P37
COMPND   8 TO P39 WERE DELETED
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE   3 ORGANISM_TAXID: 77133;
SOURCE   4 GENE: ESTDL136;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS    CHLORAMPHENICOL, METAGENOME, HORNOME SENSITIVE LIPASE, HSL, ESTDL136,
KEYWDS   2 ESTERASE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.H.KIM,P.A.KANG,K.T.HAN,S.W.LEE,S.K.RHEE
REVDAT   1   06-FEB-19 6AAE    0
JRNL        AUTH   S.H.KIM,P.A.KANG,K.T.HAN,S.W.LEE,S.K.RHEE
JRNL        TITL   CRYSTAL STRUCTURE OF CHLORAMPHENICOL-METABOLIZING ENZYME
JRNL        TITL 2 ESTDL136 FROM A METAGENOME.
JRNL        REF    PLOS ONE                      V.  14 10298 2019
JRNL        REFN                   ESSN 1932-6203
JRNL        PMID   30645605
JRNL        DOI    10.1371/JOURNAL.PONE.0210298
REMARK   2
REMARK   2 RESOLUTION.    1.64 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX 1.9_1692
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 : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.64
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.26
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9
REMARK   3   NUMBER OF REFLECTIONS             : 99964
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190
REMARK   3   R VALUE            (WORKING SET) : 0.189
REMARK   3   FREE R VALUE                     : 0.220
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1999
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 32.2638 -  3.9529    1.00     7418   150  0.1468 0.1706
REMARK   3     2  3.9529 -  3.1384    1.00     7121   146  0.1591 0.2015
REMARK   3     3  3.1384 -  2.7419    1.00     7077   144  0.1846 0.2025
REMARK   3     4  2.7419 -  2.4913    1.00     7014   143  0.1895 0.2200
REMARK   3     5  2.4913 -  2.3128    1.00     7024   144  0.1893 0.2430
REMARK   3     6  2.3128 -  2.1765    1.00     6986   143  0.2241 0.2769
REMARK   3     7  2.1765 -  2.0675    1.00     6976   142  0.2082 0.2257
REMARK   3     8  2.0675 -  1.9775    1.00     6927   141  0.2202 0.2335
REMARK   3     9  1.9775 -  1.9014    1.00     6944   142  0.2646 0.2927
REMARK   3    10  1.9014 -  1.8358    1.00     6917   142  0.2640 0.3134
REMARK   3    11  1.8358 -  1.7784    1.00     6920   141  0.2426 0.2927
REMARK   3    12  1.7784 -  1.7276    1.00     6983   142  0.2570 0.2958
REMARK   3    13  1.7276 -  1.6821    1.00     6875   141  0.2688 0.2607
REMARK   3    14  1.6821 -  1.6410    0.98     6783   138  0.2864 0.3076
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : NULL
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)     : 0.190
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.160
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  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      :  0.007           4994
REMARK   3   ANGLE     :  1.068           6747
REMARK   3   CHIRALITY :  0.043            716
REMARK   3   PLANARITY :  0.005            882
REMARK   3   DIHEDRAL  : 15.370           1795
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 6AAE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1300008421.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 26-JUN-14
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PAL/PLS
REMARK 200  BEAMLINE                       : 7A (6B, 6C1)
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97933
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 100067
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.640
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 14.30
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 23.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.70
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 1U4N
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 58.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 500MM AMMONIUM FLUORIDE (PH6.5), 30%
REMARK 280  PEG3350, 5% GLYCEROL AND 120MM TCEP, VAPOR DIFFUSION, SITTING
REMARK 280  DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
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        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       59.47150
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       76.79300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       59.47150
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       76.79300
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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     MET A     1
REMARK 465     HIS A   310
REMARK 465     HIS A   311
REMARK 465     HIS A   312
REMARK 465     HIS A   313
REMARK 465     HIS A   314
REMARK 465     HIS A   315
REMARK 465     HIS A   316
REMARK 465     HIS A   317
REMARK 465     MET B     1
REMARK 465     HIS B   316
REMARK 465     HIS B   317
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    HOH A   661     O    HOH A   712              2.15
REMARK 500   O    HOH A   683     O    HOH A   703              2.16
REMARK 500   O1   PEG B   406     O1   PEG B   407              2.19
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    ASP A  54      109.97    -58.60
REMARK 500    SER A 153     -122.34     60.82
REMARK 500    TYR A 181       65.41     25.55
REMARK 500    TYR A 202      -74.91     77.78
REMARK 500    ALA A 227      -67.76    -92.20
REMARK 500    MET B  17     -178.20    177.02
REMARK 500    SER B 153     -121.24     61.16
REMARK 500    TYR B 181       64.70     24.37
REMARK 500    TYR B 202      -50.50     74.03
REMARK 500    ALA B 227      -61.89    -99.11
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 B 746        DISTANCE =  6.04 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 414
DBREF  6AAE A    1   307  UNP    G3CR02   G3CR02_9BACT     1    310
DBREF  6AAE B    1   307  UNP    G3CR02   G3CR02_9BACT     1    310
SEQADV 6AAE     A       UNP  G3CR02    PRO    37 DELETION
SEQADV 6AAE     A       UNP  G3CR02    MET    38 DELETION
SEQADV 6AAE     A       UNP  G3CR02    PRO    39 DELETION
SEQADV 6AAE LEU A  308  UNP  G3CR02              EXPRESSION TAG
SEQADV 6AAE GLU A  309  UNP  G3CR02              EXPRESSION TAG
SEQADV 6AAE HIS A  310  UNP  G3CR02              EXPRESSION TAG
SEQADV 6AAE HIS A  311  UNP  G3CR02              EXPRESSION TAG
SEQADV 6AAE HIS A  312  UNP  G3CR02              EXPRESSION TAG
SEQADV 6AAE HIS A  313  UNP  G3CR02              EXPRESSION TAG
SEQADV 6AAE HIS A  314  UNP  G3CR02              EXPRESSION TAG
SEQADV 6AAE HIS A  315  UNP  G3CR02              EXPRESSION TAG
SEQADV 6AAE HIS A  316  UNP  G3CR02              EXPRESSION TAG
SEQADV 6AAE HIS A  317  UNP  G3CR02              EXPRESSION TAG
SEQADV 6AAE     B       UNP  G3CR02    PRO    37 DELETION
SEQADV 6AAE     B       UNP  G3CR02    MET    38 DELETION
SEQADV 6AAE     B       UNP  G3CR02    PRO    39 DELETION
SEQADV 6AAE LEU B  308  UNP  G3CR02              EXPRESSION TAG
SEQADV 6AAE GLU B  309  UNP  G3CR02              EXPRESSION TAG
SEQADV 6AAE HIS B  310  UNP  G3CR02              EXPRESSION TAG
SEQADV 6AAE HIS B  311  UNP  G3CR02              EXPRESSION TAG
SEQADV 6AAE HIS B  312  UNP  G3CR02              EXPRESSION TAG
SEQADV 6AAE HIS B  313  UNP  G3CR02              EXPRESSION TAG
SEQADV 6AAE HIS B  314  UNP  G3CR02              EXPRESSION TAG
SEQADV 6AAE HIS B  315  UNP  G3CR02              EXPRESSION TAG
SEQADV 6AAE HIS B  316  UNP  G3CR02              EXPRESSION TAG
SEQADV 6AAE HIS B  317  UNP  G3CR02              EXPRESSION TAG
SEQRES   1 A  317  MET PRO LEU ASN PRO HIS VAL GLU ALA LEU LEU GLN MET
SEQRES   2 A  317  MET ALA GLN MET PRO ALA PRO ASP PHE SER VAL ALA ASN
SEQRES   3 A  317  PRO ALA GLU ILE ARG ALA VAL PHE ASP ASN LEU ALA ALA
SEQRES   4 A  317  PRO PRO GLN VAL ALA ARG VAL GLU ASN ILE ALA ILE SER
SEQRES   5 A  317  LEU ASP GLY ARG ASP LEU ASP ALA ARG LEU TYR VAL PRO
SEQRES   6 A  317  GLU ASP ALA ASP GLU ARG PRO ALA LEU MET VAL TYR TYR
SEQRES   7 A  317  HIS GLY GLY GLY TRP VAL ILE GLY THR LEU ASP THR HIS
SEQRES   8 A  317  ASP GLY THR CYS ARG ALA LEU ALA GLN LYS SER GLY CYS
SEQRES   9 A  317  ALA VAL LEU SER ILE ALA TYR ARG LEU ALA PRO GLU TYR
SEQRES  10 A  317  ARG TYR PRO ALA PRO ALA GLU ASP CYS TYR ASP ALA LEU
SEQRES  11 A  317  VAL TRP ALA LYS GLN ASN ALA ALA THR LEU GLY VAL ASP
SEQRES  12 A  317  GLY ASP ARG LEU ALA VAL GLY GLY ASP SER ALA GLY GLY
SEQRES  13 A  317  ASN LEU ALA ALA ALA VAL ALA ILE MET ALA ARG ASP ARG
SEQRES  14 A  317  ASN GLY PRO ALA LEU ARG HIS GLN LEU LEU ILE TYR PRO
SEQRES  15 A  317  VAL THR ASP ASN ASP PHE THR LEU ALA SER TYR ALA GLU
SEQRES  16 A  317  ASN GLY GLY GLY GLU TYR TYR LEU SER THR ASP GLY MET
SEQRES  17 A  317  ARG TRP PHE TRP GLY HIS TYR LEU GLY ASP THR ALA ALA
SEQRES  18 A  317  GLU ASN ALA PRO LEU ALA ALA VAL LEU ASN VAL ALA ASP
SEQRES  19 A  317  LEU SER GLY LEU ALA PRO ALA THR VAL ILE THR ALA GLU
SEQRES  20 A  317  TYR ASP PRO LEU ARG ASP GLU GLY ILE ALA TYR ALA LYS
SEQRES  21 A  317  LYS LEU ASP ALA ALA GLY VAL PRO VAL ASP ALA ALA THR
SEQRES  22 A  317  ALA PRO GLY MET ILE HIS GLY PHE PHE SER MET PHE GLU
SEQRES  23 A  317  ALA VAL PRO ASP SER TRP GLU TRP ILE GLU ARG GLY ALA
SEQRES  24 A  317  SER ASN LEU LYS ARG ASP LEU ALA LEU GLU HIS HIS HIS
SEQRES  25 A  317  HIS HIS HIS HIS HIS
SEQRES   1 B  317  MET PRO LEU ASN PRO HIS VAL GLU ALA LEU LEU GLN MET
SEQRES   2 B  317  MET ALA GLN MET PRO ALA PRO ASP PHE SER VAL ALA ASN
SEQRES   3 B  317  PRO ALA GLU ILE ARG ALA VAL PHE ASP ASN LEU ALA ALA
SEQRES   4 B  317  PRO PRO GLN VAL ALA ARG VAL GLU ASN ILE ALA ILE SER
SEQRES   5 B  317  LEU ASP GLY ARG ASP LEU ASP ALA ARG LEU TYR VAL PRO
SEQRES   6 B  317  GLU ASP ALA ASP GLU ARG PRO ALA LEU MET VAL TYR TYR
SEQRES   7 B  317  HIS GLY GLY GLY TRP VAL ILE GLY THR LEU ASP THR HIS
SEQRES   8 B  317  ASP GLY THR CYS ARG ALA LEU ALA GLN LYS SER GLY CYS
SEQRES   9 B  317  ALA VAL LEU SER ILE ALA TYR ARG LEU ALA PRO GLU TYR
SEQRES  10 B  317  ARG TYR PRO ALA PRO ALA GLU ASP CYS TYR ASP ALA LEU
SEQRES  11 B  317  VAL TRP ALA LYS GLN ASN ALA ALA THR LEU GLY VAL ASP
SEQRES  12 B  317  GLY ASP ARG LEU ALA VAL GLY GLY ASP SER ALA GLY GLY
SEQRES  13 B  317  ASN LEU ALA ALA ALA VAL ALA ILE MET ALA ARG ASP ARG
SEQRES  14 B  317  ASN GLY PRO ALA LEU ARG HIS GLN LEU LEU ILE TYR PRO
SEQRES  15 B  317  VAL THR ASP ASN ASP PHE THR LEU ALA SER TYR ALA GLU
SEQRES  16 B  317  ASN GLY GLY GLY GLU TYR TYR LEU SER THR ASP GLY MET
SEQRES  17 B  317  ARG TRP PHE TRP GLY HIS TYR LEU GLY ASP THR ALA ALA
SEQRES  18 B  317  GLU ASN ALA PRO LEU ALA ALA VAL LEU ASN VAL ALA ASP
SEQRES  19 B  317  LEU SER GLY LEU ALA PRO ALA THR VAL ILE THR ALA GLU
SEQRES  20 B  317  TYR ASP PRO LEU ARG ASP GLU GLY ILE ALA TYR ALA LYS
SEQRES  21 B  317  LYS LEU ASP ALA ALA GLY VAL PRO VAL ASP ALA ALA THR
SEQRES  22 B  317  ALA PRO GLY MET ILE HIS GLY PHE PHE SER MET PHE GLU
SEQRES  23 B  317  ALA VAL PRO ASP SER TRP GLU TRP ILE GLU ARG GLY ALA
SEQRES  24 B  317  SER ASN LEU LYS ARG ASP LEU ALA LEU GLU HIS HIS HIS
SEQRES  25 B  317  HIS HIS HIS HIS HIS
HET    1PE  A 401      16
HET    1PE  A 402      16
HET    PEG  A 403       7
HET    PEG  A 404       7
HET    PEG  A 405       7
HET    1PE  B 401      16
HET    1PE  B 402      16
HET    1PE  B 403      16
HET    1PE  B 404      16
HET    PEG  B 405       7
HET    PEG  B 406       7
HET    PEG  B 407       7
HET    PEG  B 408       7
HET    PEG  B 409       7
HET    PEG  B 410       7
HET    PEG  B 411       7
HET    PEG  B 412       7
HET    PEG  B 413       7
HET    PEG  B 414       7
HETNAM     1PE PENTAETHYLENE GLYCOL
HETNAM     PEG DI(HYDROXYETHYL)ETHER
HETSYN     1PE PEG400
FORMUL   3  1PE    6(C10 H22 O6)
FORMUL   5  PEG    13(C4 H10 O3)
FORMUL  22  HOH   *487(H2 O)
HELIX    1 AA1 ASN A    4  GLN A   16  1                                  13
HELIX    2 AA2 ASN A   26  ALA A   39  1                                  14
HELIX    3 AA3 HIS A   91  GLY A  103  1                                  13
HELIX    4 AA4 PRO A  120  ASN A  136  1                                  17
HELIX    5 AA5 ASN A  136  GLY A  141  1                                   6
HELIX    6 AA6 SER A  153  ARG A  169  1                                  17
HELIX    7 AA7 LEU A  190  GLY A  197  1                                   8
HELIX    8 AA8 SER A  204  GLY A  217  1                                  14
HELIX    9 AA9 ALA A  220  ALA A  224  5                                   5
HELIX   10 AB1 ALA A  228  VAL A  232  5                                   5
HELIX   11 AB2 LEU A  251  ALA A  265  1                                  15
HELIX   12 AB3 GLY A  280  PHE A  285  5                                   6
HELIX   13 AB4 ASP A  290  LEU A  306  1                                  17
HELIX   14 AB5 ASN B    4  ALA B   15  1                                  12
HELIX   15 AB6 ASN B   26  ASP B   35  1                                  10
HELIX   16 AB7 HIS B   91  GLY B  103  1                                  13
HELIX   17 AB8 PRO B  120  ASN B  136  1                                  17
HELIX   18 AB9 ASN B  136  GLY B  141  1                                   6
HELIX   19 AC1 SER B  153  ARG B  169  1                                  17
HELIX   20 AC2 LEU B  190  GLY B  197  1                                   8
HELIX   21 AC3 SER B  204  GLY B  217  1                                  14
HELIX   22 AC4 ALA B  220  ALA B  224  5                                   5
HELIX   23 AC5 ALA B  228  VAL B  232  5                                   5
HELIX   24 AC6 LEU B  251  ALA B  265  1                                  15
HELIX   25 AC7 GLY B  280  PHE B  285  5                                   6
HELIX   26 AC8 ASP B  290  LEU B  306  1                                  17
SHEET    1 AA1 8 ARG A  45  LEU A  53  0
SHEET    2 AA1 8 ARG A  56  VAL A  64 -1  O  LEU A  58   N  ILE A  51
SHEET    3 AA1 8 ALA A 105  ILE A 109 -1  O  SER A 108   N  ARG A  61
SHEET    4 AA1 8 LEU A  74  TYR A  78  1  N  MET A  75   O  LEU A 107
SHEET    5 AA1 8 LEU A 147  ASP A 152  1  O  ALA A 148   N  VAL A  76
SHEET    6 AA1 8 HIS A 176  ILE A 180  1  O  LEU A 178   N  VAL A 149
SHEET    7 AA1 8 ALA A 241  ALA A 246  1  O  THR A 242   N  LEU A 179
SHEET    8 AA1 8 VAL A 269  ALA A 274  1  O  ALA A 274   N  THR A 245
SHEET    1 AA2 8 ARG B  45  LEU B  53  0
SHEET    2 AA2 8 ARG B  56  VAL B  64 -1  O  LEU B  58   N  ILE B  51
SHEET    3 AA2 8 ALA B 105  ILE B 109 -1  O  VAL B 106   N  TYR B  63
SHEET    4 AA2 8 LEU B  74  TYR B  78  1  N  TYR B  77   O  LEU B 107
SHEET    5 AA2 8 LEU B 147  ASP B 152  1  O  ALA B 148   N  VAL B  76
SHEET    6 AA2 8 HIS B 176  ILE B 180  1  O  LEU B 178   N  VAL B 149
SHEET    7 AA2 8 ALA B 241  ALA B 246  1  O  THR B 242   N  LEU B 179
SHEET    8 AA2 8 VAL B 269  ALA B 274  1  O  ALA B 274   N  THR B 245
CISPEP   1 ALA A  114    PRO A  115          0         1.99
CISPEP   2 TYR A  119    PRO A  120          0         5.39
CISPEP   3 ALA B  114    PRO B  115          0         1.86
CISPEP   4 TYR B  119    PRO B  120          0         6.47
SITE     1 AC1  7 ASP A 152  SER A 153  TYR A 202  HIS A 279
SITE     2 AC1  7 GLY A 280  SER A 283  1PE B 402
SITE     1 AC2  6 GLU A  47  TRP A 132  THR A 139  LEU A 140
SITE     2 AC2  6 GLU B  47  THR B 139
SITE     1 AC3  2 GLU A   8  GLU B 200
SITE     1 AC4  4 GLN A 100  LYS A 101  TRP A 292  GLU A 296
SITE     1 AC5  4 ASP A 206  ARG A 209  GLY A 213  PHE B  22
SITE     1 AC6  8 MET A  14  GLY B  81  ASP B 152  SER B 153
SITE     2 AC6  8 TYR B 202  HIS B 279  HOH B 502  HOH B 656
SITE     1 AC7  7 MET A  13  1PE A 401  MET B  13  MET B  14
SITE     2 AC7  7 ALA B  38  HOH B 502  HOH B 545
SITE     1 AC8 10 ALA A  28  ASP B  67  ASP B  69  GLN B 100
SITE     2 AC8 10 LYS B 101  SER B 102  GLY B 103  LYS B 303
SITE     3 AC8 10 PEG B 406  HOH B 549
SITE     1 AC9 12 GLU B 116  ARG B 118  HIS B 214  ARG B 304
SITE     2 AC9 12 ASP B 305  ALA B 307  GLU B 309  HOH B 521
SITE     3 AC9 12 HOH B 539  HOH B 543  HOH B 663  HOH B 686
SITE     1 AD1  5 ALA A  25  PHE B 211  HOH B 504  HOH B 642
SITE     2 AD1  5 HOH B 646
SITE     1 AD2  5 GLN B 100  LYS B 101  GLU B 296  1PE B 403
SITE     2 AD2  5 PEG B 407
SITE     1 AD3  6 ASN B  36  GLN B 100  LYS B 101  TRP B 292
SITE     2 AD3  6 GLU B 296  PEG B 406
SITE     1 AD4  3 TYR B 248  HOH B 598  HOH B 600
SITE     1 AD5  4 VAL A  24  ALA A  25  ASN A  26  ASP B 270
SITE     1 AD6  5 ARG B 112  PRO B 120  ALA B 121  HOH B 529
SITE     2 AD6  5 HOH B 616
SITE     1 AD7  8 ARG B  45  VAL B  64  PRO B  65  ALA B  68
SITE     2 AD7  8 ASP B  69  GLU B  70  LEU B 140  GLY B 141
SITE     1 AD8  5 ALA B 271  ALA B 272  TRP B 294  ARG B 297
SITE     2 AD8  5 HOH B 551
SITE     1 AD9  9 VAL A  46  VAL B  46  ASN B  48  ARG B  61
SITE     2 AD9  9 HOH B 509  HOH B 577  HOH B 585  HOH B 618
SITE     3 AD9  9 HOH B 620
SITE     1 AE1  6 ALA B 166  GLY B 171  PRO B 172  LEU B 174
SITE     2 AE1  6 GLY B 237  ALA B 239
CRYST1  118.943  153.586   44.243  90.00  90.00  90.00 P 21 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      0.008407  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006511  0.000000        0.00000
SCALE3      0.000000  0.000000  0.022602        0.00000
TER    2323      GLU A 309
TER    4706      HIS B 315
MASTER      354    0   19   26   16    0   36    6 5378    2  187   50
END