longtext: 5z95-pdb

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HEADER    HYDROLASE                               02-FEB-18   5Z95
TITLE     STRUCTURAL BASIS FOR SPECIFIC INHIBITION OF HIGHLY SENSITIVE SHHTL7
TITLE    2 RECEPTOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HYPOSENSITIVE TO LIGHT 7;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: SHHTL7;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: STRIGA HERMONTHICA;
SOURCE   3 ORGANISM_COMMON: PURPLE WITCHWEED;
SOURCE   4 ORGANISM_TAXID: 68872;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    STRIGOLACTONE RECEPTOR, HYDROLASE, STRIGA GERMINATION SIGNALING
EXPDTA    X-RAY DIFFRACTION
AUTHOR    U.S.HAMEED,S.T.AROLD
REVDAT   1   25-JUL-18 5Z95    0
JRNL        AUTH   U.S.HAMEED,I.HAIDER,M.JAMIL,B.A.KOUNTCHE,X.GUO,R.A.ZARBAN,
JRNL        AUTH 2 D.KIM,S.AL-BABILI,S.T.AROLD
JRNL        TITL   STRUCTURAL BASIS FOR SPECIFIC INHIBITION OF THE HIGHLY
JRNL        TITL 2 SENSITIVE SHHTL7 RECEPTOR
JRNL        REF    EMBO REP.                     V.  19 45619 2018
JRNL        REFN                   ISSN 1469-221X
REMARK   2
REMARK   2 RESOLUTION.    1.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.8.0189
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 80.19
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8
REMARK   3   NUMBER OF REFLECTIONS             : 115730
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 + TEST SET) : 0.130
REMARK   3   R VALUE            (WORKING SET) : 0.129
REMARK   3   FREE R VALUE                     : 0.143
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 6091
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.20
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.23
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8365
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.63
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3350
REMARK   3   BIN FREE R VALUE SET COUNT          : 440
REMARK   3   BIN FREE R VALUE                    : 0.3520
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2088
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 47
REMARK   3   SOLVENT ATOMS            : 289
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.23
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.17000
REMARK   3    B22 (A**2) : -0.17000
REMARK   3    B33 (A**2) : 0.54000
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.028
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.028
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.020
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.016
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.983
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.978
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2692 ; 0.013 ; 0.019
REMARK   3   BOND LENGTHS OTHERS               (A):  2469 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3724 ; 1.685 ; 1.990
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5787 ; 1.040 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   374 ; 6.188 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   103 ;34.173 ;24.078
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   465 ;12.990 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;18.183 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   417 ; 0.107 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3180 ; 0.009 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):   537 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1361 ; 1.016 ; 1.335
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1360 ; 1.007 ; 1.333
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1780 ; 1.441 ; 2.012
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1781 ; 1.442 ; 2.014
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1331 ; 1.961 ; 1.721
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1331 ; 1.961 ; 1.721
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1945 ; 2.565 ; 2.464
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3190 ; 3.090 ;18.271
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3120 ; 2.709 ;17.559
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  5158 ; 2.011 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   183 ;25.909 ; 5.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  5171 ;10.768 ; 5.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.70
REMARK   3   SHRINKAGE RADIUS   : 0.70
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 5Z95 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1300006672.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 27-JAN-17
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               : SOLEIL
REMARK 200  BEAMLINE                       : PROXIMA 1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9789
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 115730
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 80.190
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 9.900
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 24.5600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.24
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: MOLREP
REMARK 200 STARTING MODEL: 5CBK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 62.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M LITHIUM SULFATE, 0.1 M HEPES PH
REMARK 280  7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+1/6
REMARK 290       6555   X-Y,X,Z+5/6
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       53.50667
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       26.75333
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       40.13000
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       13.37667
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       66.88333
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     GLY A    -4
REMARK 465     PRO A    -3
REMARK 465     LEU A    -2
REMARK 465     GLY A    -1
REMARK 465     SER A     0
REMARK 465     MET A     1
REMARK 465     SER A     2
REMARK 465     HIS A   271
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     -106.35     29.42
REMARK 500    SER A  95     -112.27     59.52
REMARK 500    ARG A 123      144.18   -175.10
REMARK 500    ASP A 197       89.73   -150.10
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 A 688        DISTANCE =  6.56 ANGSTROMS
REMARK 525    HOH A 689        DISTANCE =  6.82 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     EGC A  301
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EGC A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 304
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5Z82   RELATED DB: PDB
REMARK 900 RELATED ID: 5Z89   RELATED DB: PDB
REMARK 900 RELATED ID: 5Z8P   RELATED DB: PDB
DBREF1 5Z95 A    1   271  UNP                  A0A0M3PNA2_STRHE
DBREF2 5Z95 A     A0A0M3PNA2                          1         271
SEQADV 5Z95 GLY A   -4  UNP  A0A0M3PNA           EXPRESSION TAG
SEQADV 5Z95 PRO A   -3  UNP  A0A0M3PNA           EXPRESSION TAG
SEQADV 5Z95 LEU A   -2  UNP  A0A0M3PNA           EXPRESSION TAG
SEQADV 5Z95 GLY A   -1  UNP  A0A0M3PNA           EXPRESSION TAG
SEQADV 5Z95 SER A    0  UNP  A0A0M3PNA           EXPRESSION TAG
SEQRES   1 A  276  GLY PRO LEU GLY SER MET SER SER ILE GLY LEU ALA HIS
SEQRES   2 A  276  ASN VAL THR ILE LEU GLY SER GLY GLU THR THR VAL VAL
SEQRES   3 A  276  LEU GLY HIS GLY TYR GLY THR ASP GLN SER VAL TRP LYS
SEQRES   4 A  276  LEU LEU VAL PRO TYR LEU VAL ASP ASP TYR LYS VAL LEU
SEQRES   5 A  276  LEU TYR ASP HIS MET GLY ALA GLY THR THR ASN PRO ASP
SEQRES   6 A  276  TYR PHE ASP PHE ASP ARG TYR SER SER LEU GLU GLY TYR
SEQRES   7 A  276  SER TYR ASP LEU ILE ALA ILE LEU GLU GLU PHE GLN VAL
SEQRES   8 A  276  SER LYS CYS ILE TYR VAL GLY HIS SER MET SER SER MET
SEQRES   9 A  276  ALA ALA ALA VAL ALA SER ILE PHE ARG PRO ASP LEU PHE
SEQRES  10 A  276  HIS LYS LEU VAL MET ILE SER PRO THR PRO ARG LEU ILE
SEQRES  11 A  276  ASN THR GLU GLU TYR TYR GLY GLY PHE GLU GLN LYS VAL
SEQRES  12 A  276  MET ASP GLU THR LEU ARG SER LEU ASP GLU ASN PHE LYS
SEQRES  13 A  276  SER LEU SER LEU GLY THR ALA PRO LEU LEU LEU ALA CYS
SEQRES  14 A  276  ASP LEU GLU SER ALA ALA MET GLN GLU TYR CYS ARG THR
SEQRES  15 A  276  LEU PHE ASN MET ARG PRO ASP ILE ALA CYS CYS ILE THR
SEQRES  16 A  276  ARG MET ILE CYS GLY LEU ASP LEU ARG PRO TYR LEU GLY
SEQRES  17 A  276  HIS VAL THR VAL PRO CYS HIS ILE ILE GLN SER SER ASN
SEQRES  18 A  276  ASP ILE MET VAL PRO VAL ALA VAL GLY GLU TYR LEU ARG
SEQRES  19 A  276  LYS ASN LEU GLY GLY PRO SER VAL VAL GLU VAL MET PRO
SEQRES  20 A  276  THR GLU GLY HIS LEU PRO HIS LEU SER MET PRO GLU VAL
SEQRES  21 A  276  THR ILE PRO VAL VAL LEU ARG HIS ILE ARG GLN ASP ILE
SEQRES  22 A  276  THR ASP HIS
HET    EGC  A 301      31
HET    SO4  A 302       5
HET    SO4  A 303       5
HET    GOL  A 304       6
HETNAM     EGC 2-(2-{2-[2-(2-{2-[2-(2-{2-[4-(1,1,3,3-TETRAMETHYL-
HETNAM   2 EGC  BUTYL)-PHENOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-
HETNAM   3 EGC  ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL
HETNAM     SO4 SULFATE ION
HETNAM     GOL GLYCEROL
HETSYN     EGC TRITON X-100
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2  EGC    C32 H58 O10
FORMUL   3  SO4    2(O4 S 2-)
FORMUL   5  GOL    C3 H8 O3
FORMUL   6  HOH   *289(H2 O)
HELIX    1 AA1 SER A    3  HIS A    8  1                                   6
HELIX    2 AA2 ASP A   29  LYS A   34  5                                   6
HELIX    3 AA3 LEU A   36  LEU A   40  5                                   5
HELIX    4 AA4 ASN A   58  PHE A   62  5                                   5
HELIX    5 AA5 ASP A   65  SER A   69  5                                   5
HELIX    6 AA6 LEU A   70  PHE A   84  1                                  15
HELIX    7 AA7 SER A   95  ARG A  108  1                                  14
HELIX    8 AA8 GLU A  135  SER A  145  1                                  11
HELIX    9 AA9 LEU A  146  GLU A  148  5                                   3
HELIX   10 AB1 ASN A  149  ALA A  163  1                                  15
HELIX   11 AB2 SER A  168  PHE A  179  1                                  12
HELIX   12 AB3 ARG A  182  GLY A  195  1                                  14
HELIX   13 AB4 LEU A  198  VAL A  205  5                                   8
HELIX   14 AB5 VAL A  222  LEU A  232  1                                  11
HELIX   15 AB6 LEU A  247  MET A  252  1                                   6
HELIX   16 AB7 MET A  252  GLN A  266  1                                  15
SHEET    1 AA1 7 THR A  11  GLY A  14  0
SHEET    2 AA1 7 LYS A  45  TYR A  49 -1  O  VAL A  46   N  LEU A  13
SHEET    3 AA1 7 THR A  19  GLY A  23  1  N  VAL A  20   O  LYS A  45
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  ILE A 118  1  O  VAL A 116   N  TYR A  91
SHEET    6 AA1 7 CYS A 209  ASN A 216  1  O  HIS A 210   N  MET A 117
SHEET    7 AA1 7 SER A 236  GLU A 244  1  O  VAL A 237   N  ILE A 211
SITE     1 AC1 13 ILE A 106  PHE A 107  PRO A 109  PHE A 134
SITE     2 AC1 13 VAL A 138  THR A 142  THR A 157  LEU A 160
SITE     3 AC1 13 THR A 190  MET A 219  HOH A 402  HOH A 535
SITE     4 AC1 13 HOH A 637
SITE     1 AC2  6 SER A  15  GLY A  16  LYS A  45  ARG A 229
SITE     2 AC2  6 LYS A 230  HOH A 521
SITE     1 AC3  3 THR A 127  ARG A 199  HOH A 606
SITE     1 AC4  6 TYR A 130  TYR A 131  TYR A 227  HOH A 426
SITE     2 AC4  6 HOH A 457  HOH A 516
CRYST1   92.590   92.590   80.260  90.00  90.00 120.00 P 65          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      0.010800  0.006236  0.000000        0.00000
SCALE2      0.000000  0.012471  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012460        0.00000
TER    2553      ASP A 270
MASTER      321    0    4   16    7    0    9    6 2424    1   47   22
END