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HEADER HYDROLASE 10-FEB-17 5N4F
TITLE PROLYL OLIGOPEPTIDASE B FROM GALERINA MARGINATA - APO PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL OLIGOPEPTIDASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALERINA MARGINATA;
SOURCE 3 ORGANISM_TAXID: 109633;
SOURCE 4 GENE: POPB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS AMANITIN BIOSYNTHESIS, PROLYL OLIGOPEPTIDASE, MACROCYCLASE,
KEYWDS 2 PEPTIDASE, BETA-PROPELLER, OPEN FORM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.M.CZEKSTER,S.A.MCMAHON,H.LUDEWIG,J.H.NAISMITH
REVDAT 1 01-NOV-17 5N4F 0
JRNL AUTH C.M.CZEKSTER,H.LUDEWIG,S.A.MCMAHON,J.H.NAISMITH
JRNL TITL CHARACTERIZATION OF A DUAL FUNCTION MACROCYCLASE ENABLES
JRNL TITL 2 DESIGN AND USE OF EFFICIENT MACROCYCLIZATION SUBSTRATES
JRNL REF NAT COMMUN 2017
JRNL REFN ESSN 2041-1723
JRNL DOI 10.1038/S41467-017-00862-4
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 3 NUMBER OF REFLECTIONS : 29853
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1584
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1767
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 76.73
REMARK 3 BIN R VALUE (WORKING SET) : 0.3220
REMARK 3 BIN FREE R VALUE SET COUNT : 89
REMARK 3 BIN FREE R VALUE : 0.3820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5578
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 187
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.95000
REMARK 3 B22 (A**2) : 2.03000
REMARK 3 B33 (A**2) : -3.97000
REMARK 3 B12 (A**2) : 0.00000
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): 0.497
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.278
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.227
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.051
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5739 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5144 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7789 ; 1.171 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11952 ; 0.870 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 699 ; 6.328 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 276 ;33.590 ;24.239
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 913 ;12.342 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;10.303 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 826 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6438 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1229 ; 0.001 ; 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): 2808 ; 1.141 ; 2.132
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2807 ; 1.141 ; 2.132
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3503 ; 2.003 ; 3.190
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3504 ; 2.003 ; 3.190
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2931 ; 0.998 ; 2.236
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2931 ; 0.998 ; 2.236
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4287 ; 1.701 ; 3.298
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6305 ;10.323 ;24.765
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6305 ;10.324 ;24.764
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 7 A 726
REMARK 3 ORIGIN FOR THE GROUP (A): 71.7980 25.8110 73.0170
REMARK 3 T TENSOR
REMARK 3 T11: 0.0016 T22: 0.0471
REMARK 3 T33: 0.4502 T12: -0.0045
REMARK 3 T13: 0.0073 T23: -0.0341
REMARK 3 L TENSOR
REMARK 3 L11: 0.5018 L22: 0.6757
REMARK 3 L33: 1.2462 L12: -0.1263
REMARK 3 L13: 0.0691 L23: -0.5219
REMARK 3 S TENSOR
REMARK 3 S11: 0.0026 S12: 0.1188 S13: -0.0688
REMARK 3 S21: 0.0047 S22: -0.0121 S23: 0.0552
REMARK 3 S31: 0.0090 S32: -0.0388 S33: 0.0095
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 1.00
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5N4F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1200003501.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-OCT-15
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 : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31438
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 54.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG4000 AND 100 MM MES BUFFER, PH
REMARK 280 6.5., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K
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 45.44500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.81000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.44500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.81000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 MET A 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 VAL A 4
REMARK 465 THR A 5
REMARK 465 TRP A 6
REMARK 465 GLU A 223
REMARK 465 ARG A 224
REMARK 465 HIS A 225
REMARK 465 GLU A 226
REMARK 465 GLY A 227
REMARK 465 THR A 228
REMARK 465 ARG A 229
REMARK 465 GLU A 294
REMARK 465 ASP A 295
REMARK 465 LEU A 696
REMARK 465 GLY A 697
REMARK 465 HIS A 698
REMARK 465 GLY A 699
REMARK 465 MET A 700
REMARK 465 GLY A 701
REMARK 465 LYS A 702
REMARK 465 PRO A 703
REMARK 465 LYS A 727
REMARK 465 THR A 728
REMARK 465 VAL A 729
REMARK 465 GLU A 730
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 LEU A 103 -62.08 -105.41
REMARK 500 LEU A 147 145.36 -170.77
REMARK 500 GLU A 309 136.94 78.11
REMARK 500 THR A 318 -177.09 -170.90
REMARK 500 ALA A 332 82.38 -166.76
REMARK 500 ASN A 368 48.46 39.91
REMARK 500 GLU A 369 -57.23 59.84
REMARK 500 TYR A 496 -64.03 -125.18
REMARK 500 ARG A 543 -110.62 44.17
REMARK 500 SER A 577 -111.48 61.21
REMARK 500 ALA A 605 -39.03 -148.78
REMARK 500 THR A 614 119.67 -37.99
REMARK 500 ARG A 663 -88.19 1.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 802
DBREF 5N4F A 1 730 UNP H2E7Q8 H2E7Q8_9AGAR 1 730
SEQRES 1 A 730 MET SER SER VAL THR TRP ALA PRO GLY ASN TYR PRO SER
SEQRES 2 A 730 THR ARG ARG SER ASP HIS VAL ASP THR TYR GLN SER ALA
SEQRES 3 A 730 SER LYS GLY GLU VAL PRO VAL PRO ASP PRO TYR GLN TRP
SEQRES 4 A 730 LEU GLU GLU SER THR ASP GLU VAL ASP LYS TRP THR THR
SEQRES 5 A 730 ALA GLN ALA ASP LEU ALA GLN SER TYR LEU ASP GLN ASN
SEQRES 6 A 730 ALA ASP ILE GLN LYS LEU ALA GLU LYS PHE ARG ALA SER
SEQRES 7 A 730 ARG ASN TYR ALA LYS PHE SER ALA PRO THR LEU LEU ASP
SEQRES 8 A 730 ASP GLY HIS TRP TYR TRP PHE TYR ASN ARG GLY LEU GLN
SEQRES 9 A 730 SER GLN SER VAL LEU TYR ARG SER LYS GLU PRO ALA LEU
SEQRES 10 A 730 PRO ASP PHE SER LYS GLY ASP ASP ASN VAL GLY ASP VAL
SEQRES 11 A 730 PHE PHE ASP PRO ASN VAL LEU ALA ALA ASP GLY SER ALA
SEQRES 12 A 730 GLY MET VAL LEU CYS LYS PHE SER PRO ASP GLY LYS PHE
SEQRES 13 A 730 PHE ALA TYR ALA VAL SER HIS LEU GLY GLY ASP TYR SER
SEQRES 14 A 730 THR ILE TYR VAL ARG SER THR SER SER PRO LEU SER GLN
SEQRES 15 A 730 ALA SER VAL ALA GLN GLY VAL ASP GLY ARG LEU SER ASP
SEQRES 16 A 730 GLU VAL LYS TRP PHE LYS PHE SER THR ILE ILE TRP THR
SEQRES 17 A 730 LYS ASP SER LYS GLY PHE LEU TYR GLN ARG TYR PRO ALA
SEQRES 18 A 730 ARG GLU ARG HIS GLU GLY THR ARG SER ASP ARG ASN ALA
SEQRES 19 A 730 MET MET CYS TYR HIS LYS VAL GLY THR THR GLN GLU GLU
SEQRES 20 A 730 ASP ILE ILE VAL TYR GLN ASP ASN GLU HIS PRO GLU TRP
SEQRES 21 A 730 ILE TYR GLY ALA ASP THR SER GLU ASP GLY LYS TYR LEU
SEQRES 22 A 730 TYR LEU TYR GLN PHE LYS ASP THR SER LYS LYS ASN LEU
SEQRES 23 A 730 LEU TRP VAL ALA GLU LEU ASP GLU ASP GLY VAL LYS SER
SEQRES 24 A 730 GLY ILE HIS TRP ARG LYS VAL VAL ASN GLU TYR ALA ALA
SEQRES 25 A 730 ASP TYR ASN ILE ILE THR ASN HIS GLY SER LEU VAL TYR
SEQRES 26 A 730 ILE LYS THR ASN LEU ASN ALA PRO GLN TYR LYS VAL ILE
SEQRES 27 A 730 THR ILE ASP LEU SER LYS ASP GLU PRO GLU ILE ARG ASP
SEQRES 28 A 730 PHE ILE PRO GLU GLU LYS ASP ALA LYS LEU ALA GLN VAL
SEQRES 29 A 730 ASN CYS ALA ASN GLU GLU TYR PHE VAL ALA ILE TYR LYS
SEQRES 30 A 730 ARG ASN VAL LYS ASP GLU ILE TYR LEU TYR SER LYS ALA
SEQRES 31 A 730 GLY VAL GLN LEU THR ARG LEU ALA PRO ASP PHE VAL GLY
SEQRES 32 A 730 ALA ALA SER ILE ALA ASN ARG GLN LYS GLN THR HIS PHE
SEQRES 33 A 730 PHE LEU THR LEU SER GLY PHE ASN THR PRO GLY THR ILE
SEQRES 34 A 730 ALA ARG TYR ASP PHE THR ALA PRO GLU THR GLN ARG PHE
SEQRES 35 A 730 SER ILE LEU ARG THR THR LYS VAL ASN GLU LEU ASP PRO
SEQRES 36 A 730 ASP ASP PHE GLU SER THR GLN VAL TRP TYR GLU SER LYS
SEQRES 37 A 730 ASP GLY THR LYS ILE PRO MET PHE ILE VAL ARG HIS LYS
SEQRES 38 A 730 SER THR LYS PHE ASP GLY THR ALA ALA ALA ILE GLN TYR
SEQRES 39 A 730 GLY TYR GLY GLY PHE ALA THR SER ALA ASP PRO PHE PHE
SEQRES 40 A 730 SER PRO ILE ILE LEU THR PHE LEU GLN THR TYR GLY ALA
SEQRES 41 A 730 ILE PHE ALA VAL PRO SER ILE ARG GLY GLY GLY GLU PHE
SEQRES 42 A 730 GLY GLU GLU TRP HIS LYS GLY GLY ARG ARG GLU THR LYS
SEQRES 43 A 730 VAL ASN THR PHE ASP ASP PHE ILE ALA ALA ALA GLN PHE
SEQRES 44 A 730 LEU VAL LYS ASN LYS TYR ALA ALA PRO GLY LYS VAL ALA
SEQRES 45 A 730 ILE ASN GLY ALA SER ASN GLY GLY LEU LEU VAL MET GLY
SEQRES 46 A 730 SER ILE VAL ARG ALA PRO GLU GLY THR PHE GLY ALA ALA
SEQRES 47 A 730 VAL PRO GLU GLY GLY VAL ALA ASP LEU LEU LYS PHE HIS
SEQRES 48 A 730 LYS PHE THR GLY GLY GLN ALA TRP ILE SER GLU TYR GLY
SEQRES 49 A 730 ASN PRO SER ILE PRO GLU GLU PHE ASP TYR ILE TYR PRO
SEQRES 50 A 730 LEU SER PRO VAL HIS ASN VAL ARG THR ASP LYS VAL MET
SEQRES 51 A 730 PRO ALA THR LEU ILE THR VAL ASN ILE GLY ASP GLY ARG
SEQRES 52 A 730 VAL VAL PRO MET HIS SER PHE LYS PHE ILE ALA THR LEU
SEQRES 53 A 730 GLN HIS ASN VAL PRO GLN ASN PRO HIS PRO LEU LEU ILE
SEQRES 54 A 730 LYS ILE ASP LYS SER TRP LEU GLY HIS GLY MET GLY LYS
SEQRES 55 A 730 PRO THR ASP LYS ASN VAL LYS ASP ALA ALA ASP LYS TRP
SEQRES 56 A 730 GLY PHE ILE ALA ARG ALA LEU GLY LEU GLU LEU LYS THR
SEQRES 57 A 730 VAL GLU
HET GOL A 801 6
HET GOL A 802 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 2(C3 H8 O3)
FORMUL 4 HOH *187(H2 O)
HELIX 1 AA1 TYR A 37 GLU A 42 5 6
HELIX 2 AA2 THR A 44 GLN A 64 1 21
HELIX 3 AA3 ALA A 66 ARG A 79 1 14
HELIX 4 AA4 GLY A 123 VAL A 127 1 5
HELIX 5 AA5 ASP A 133 LEU A 137 5 5
HELIX 6 AA6 SER A 181 GLY A 188 1 8
HELIX 7 AA7 THR A 244 ASP A 248 5 5
HELIX 8 AA8 PRO A 437 GLN A 440 5 4
HELIX 9 AA9 ASP A 454 ASP A 456 5 3
HELIX 10 AB1 SER A 508 GLY A 519 1 12
HELIX 11 AB2 PHE A 533 GLY A 540 1 8
HELIX 12 AB3 GLY A 541 THR A 545 5 5
HELIX 13 AB4 LYS A 546 ASN A 563 1 18
HELIX 14 AB5 SER A 577 ALA A 590 1 14
HELIX 15 AB6 LYS A 609 PHE A 613 5 5
HELIX 16 AB7 GLY A 616 ALA A 618 5 3
HELIX 17 AB8 TRP A 619 GLY A 624 1 6
HELIX 18 AB9 ILE A 628 TYR A 636 1 9
HELIX 19 AC1 PRO A 637 ASN A 643 5 7
HELIX 20 AC2 PRO A 666 VAL A 680 1 15
HELIX 21 AC3 VAL A 708 LEU A 722 1 15
SHEET 1 AA1 2 VAL A 20 SER A 25 0
SHEET 2 AA1 2 GLY A 29 PRO A 34 -1 O GLY A 29 N SER A 25
SHEET 1 AA2 3 LYS A 83 PHE A 84 0
SHEET 2 AA2 3 TRP A 95 ASN A 100 -1 O ASN A 100 N LYS A 83
SHEET 3 AA2 3 THR A 88 LEU A 89 -1 N THR A 88 O TYR A 96
SHEET 1 AA3 4 LYS A 83 PHE A 84 0
SHEET 2 AA3 4 TRP A 95 ASN A 100 -1 O ASN A 100 N LYS A 83
SHEET 3 AA3 4 VAL A 108 SER A 112 -1 O TYR A 110 N TRP A 97
SHEET 4 AA3 4 GLY A 128 PHE A 132 -1 O PHE A 132 N LEU A 109
SHEET 1 AA4 4 ALA A 143 PHE A 150 0
SHEET 2 AA4 4 PHE A 156 HIS A 163 -1 O ALA A 160 N LEU A 147
SHEET 3 AA4 4 SER A 169 SER A 175 -1 O THR A 170 N VAL A 161
SHEET 4 AA4 4 VAL A 197 PHE A 200 -1 O VAL A 197 N ILE A 171
SHEET 1 AA5 4 ILE A 206 TRP A 207 0
SHEET 2 AA5 4 GLY A 213 ARG A 218 -1 O LEU A 215 N ILE A 206
SHEET 3 AA5 4 MET A 235 LYS A 240 -1 O CYS A 237 N TYR A 216
SHEET 4 AA5 4 ILE A 249 GLN A 253 -1 O ILE A 249 N TYR A 238
SHEET 1 AA6 4 ILE A 261 THR A 266 0
SHEET 2 AA6 4 TYR A 272 PHE A 278 -1 O TYR A 274 N ASP A 265
SHEET 3 AA6 4 LEU A 286 GLU A 291 -1 O TRP A 288 N LEU A 275
SHEET 4 AA6 4 ARG A 304 VAL A 307 -1 O ARG A 304 N VAL A 289
SHEET 1 AA7 4 TYR A 314 HIS A 320 0
SHEET 2 AA7 4 LEU A 323 THR A 328 -1 O TYR A 325 N THR A 318
SHEET 3 AA7 4 LYS A 336 ASP A 341 -1 O ILE A 340 N VAL A 324
SHEET 4 AA7 4 GLU A 348 ILE A 353 -1 O ARG A 350 N THR A 339
SHEET 1 AA8 4 LYS A 360 ALA A 367 0
SHEET 2 AA8 4 TYR A 371 LYS A 377 -1 O VAL A 373 N ASN A 365
SHEET 3 AA8 4 ASP A 382 SER A 388 -1 O TYR A 387 N PHE A 372
SHEET 4 AA8 4 GLN A 393 LEU A 397 -1 O THR A 395 N LEU A 386
SHEET 1 AA9 4 ALA A 404 ALA A 408 0
SHEET 2 AA9 4 HIS A 415 SER A 421 -1 O SER A 421 N ALA A 404
SHEET 3 AA9 4 THR A 428 ASP A 433 -1 O THR A 428 N LEU A 420
SHEET 4 AA9 4 PHE A 442 THR A 447 -1 O SER A 443 N ARG A 431
SHEET 1 AB1 8 PHE A 458 GLU A 466 0
SHEET 2 AB1 8 LYS A 472 HIS A 480 -1 O ILE A 477 N THR A 461
SHEET 3 AB1 8 ILE A 521 PRO A 525 -1 O VAL A 524 N PHE A 476
SHEET 4 AB1 8 ALA A 491 TYR A 494 1 N ILE A 492 O ALA A 523
SHEET 5 AB1 8 VAL A 571 ALA A 576 1 O ALA A 572 N GLN A 493
SHEET 6 AB1 8 ALA A 597 GLU A 601 1 O VAL A 599 N ILE A 573
SHEET 7 AB1 8 ALA A 652 VAL A 657 1 O THR A 656 N PRO A 600
SHEET 8 AB1 8 LEU A 687 ILE A 691 1 O LEU A 688 N THR A 653
SITE 1 AC1 7 VAL A 337 ILE A 353 LEU A 361 ALA A 374
SITE 2 AC1 7 ILE A 375 TYR A 376 TYR A 387
SITE 1 AC2 7 ASP A 400 PHE A 401 VAL A 402 ASN A 424
SITE 2 AC2 7 PHE A 458 GLU A 459 SER A 460
CRYST1 90.890 105.620 86.960 90.00 90.00 90.00 P 21 21 2 4
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 0.011002 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009468 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011500 0.00000
TER 5579 LEU A 726
MASTER 328 0 2 21 41 0 4 6 5777 1 12 57
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