| 7yc0-pdb | HEADER HYDROLASE 30-JUN-22 7YC0
TITLE ACETYLESTERASE (LGESTI) W.T.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOCOCCUS GARVIEAE SUBSP. GARVIEAE;
SOURCE 3 ORGANISM_TAXID: 1890280;
SOURCE 4 GENE: F4V47_03290;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ESTERASE, LIPASE, HYDROLASE, PATHOGEN BACTERIA
EXPDTA X-RAY DIFFRACTION
AUTHOR H.DO,J.H.LEE
REVDAT 1 07-JUN-23 7YC0 0
JRNL AUTH H.DO,W.YOO,Y.WANG,Y.NAM,S.C.SHIN,H.W.KIM,K.K.KIM,J.H.LEE
JRNL TITL CRYSTAL STRUCTURE AND BIOCHEMICAL ANALYSIS OF ACETYLESTERASE
JRNL TITL 2 (LGESTI) FROM LACTOCOCCUS GARVIEAE.
JRNL REF PLOS ONE V. 18 80988 2023
JRNL REFN ESSN 1932-6203
JRNL PMID 36745644
JRNL DOI 10.1371/JOURNAL.PONE.0280988
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 71845
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 : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.998
REMARK 3 FREE R VALUE TEST SET COUNT : 3591
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5106
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.80
REMARK 3 BIN R VALUE (WORKING SET) : 0.3270
REMARK 3 BIN FREE R VALUE SET COUNT : 249
REMARK 3 BIN FREE R VALUE : 0.3510
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7572
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 496
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00300
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.01200
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.186
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.165
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.143
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.646
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7737 ; 0.008 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 7194 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10506 ; 1.565 ; 1.642
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16533 ; 1.319 ; 1.579
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 942 ; 7.172 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 453 ;34.683 ;23.245
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1308 ;15.459 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ;14.971 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1014 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8882 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1806 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1658 ; 0.204 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 48 ; 0.236 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3729 ; 0.162 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 488 ; 0.157 ; 0.200
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): 3779 ; 2.988 ; 4.133
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3777 ; 2.988 ; 4.131
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4716 ; 4.001 ; 6.189
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4717 ; 4.001 ; 6.190
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3958 ; 3.642 ; 4.471
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3959 ; 3.642 ; 4.471
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5790 ; 5.435 ; 6.575
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5791 ; 5.435 ; 6.575
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 7YC0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JUL-22.
REMARK 100 THE DEPOSITION ID IS D_1300030632.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-NOV-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 5C (4A)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
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
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71847
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 28.490
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.04
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.54000
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: MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, PH 7.0, 0.2M CALCIUM
REMARK 280 ACETATE HYDRATE, 20% (W/V) PEG 3000, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 1 2 1
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+1/2
REMARK 290 4555 -X+1/2,Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 14.64211
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.38500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 108.32948
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 14.64211
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 46.38500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 108.32948
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 LYS A 317
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 LYS B 317
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 LYS C 317
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 ALA A 87 45.88 99.62
REMARK 500 TRP A 89 -8.60 66.11
REMARK 500 ASN A 93 179.04 179.61
REMARK 500 SER A 159 -121.74 68.48
REMARK 500 TYR A 187 58.64 39.41
REMARK 500 ASN A 205 2.29 84.70
REMARK 500 PHE A 207 -71.49 69.50
REMARK 500 THR A 221 130.95 -177.11
REMARK 500 SER A 233 79.87 -118.43
REMARK 500 GLU B 52 115.86 -161.26
REMARK 500 HIS B 73 40.10 72.54
REMARK 500 ALA B 87 42.19 95.58
REMARK 500 TRP B 89 -11.05 69.03
REMARK 500 LYS B 147 75.65 43.27
REMARK 500 SER B 159 -119.73 61.73
REMARK 500 TYR B 187 60.07 39.96
REMARK 500 ASN B 205 1.58 89.35
REMARK 500 PHE B 207 -71.00 68.07
REMARK 500 THR B 221 130.17 -176.54
REMARK 500 SER B 233 77.57 -116.74
REMARK 500 ALA C 87 37.79 104.67
REMARK 500 TRP C 89 -4.48 69.85
REMARK 500 ASN C 93 -179.02 -174.06
REMARK 500 PRO C 126 33.98 -99.89
REMARK 500 SER C 159 -121.64 62.88
REMARK 500 TYR C 187 60.65 34.41
REMARK 500 ASN C 205 6.52 82.01
REMARK 500 PHE C 207 -72.75 69.77
REMARK 500 THR C 221 129.49 -173.04
REMARK 500 SER C 233 77.83 -117.17
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7YC0 A 1 317 UNP A0A5M9R5N4_9LACT
DBREF2 7YC0 A A0A5M9R5N4 1 317
DBREF1 7YC0 B 1 317 UNP A0A5M9R5N4_9LACT
DBREF2 7YC0 B A0A5M9R5N4 1 317
DBREF1 7YC0 C 1 317 UNP A0A5M9R5N4_9LACT
DBREF2 7YC0 C A0A5M9R5N4 1 317
SEQADV 7YC0 GLY A -2 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC0 SER A -1 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC0 HIS A 0 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC0 GLY B -2 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC0 SER B -1 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC0 HIS B 0 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC0 GLY C -2 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC0 SER C -1 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC0 HIS C 0 UNP A0A5M9R5N EXPRESSION TAG
SEQRES 1 A 320 GLY SER HIS MET VAL GLU ARG ILE SER LEU GLU LYS ALA
SEQRES 2 A 320 ALA LEU GLU PHE SER GLU ALA ASN ALA PRO HIS PRO ARG
SEQRES 3 A 320 ILE TYR GLU LEU PRO VAL GLU GLU GLY ARG SER LEU LEU
SEQRES 4 A 320 ASN GLU VAL GLN ASP SER PRO VAL VAL LYS GLU ASP VAL
SEQRES 5 A 320 ASP ILE GLU ASP ILE ALA VAL ASP THR GLY GLU TRP GLY
SEQRES 6 A 320 GLU ILE ASN VAL ARG PHE ILE ARG PRO LEU HIS GLN GLU
SEQRES 7 A 320 LYS LYS LEU PRO VAL ILE PHE TYR ILE HIS GLY ALA GLY
SEQRES 8 A 320 TRP VAL PHE GLY ASN ALA HIS THR HIS ASP LYS LEU ILE
SEQRES 9 A 320 ARG GLU LEU ALA VAL ARG THR ASN SER VAL VAL VAL PHE
SEQRES 10 A 320 SER GLU TYR SER LEU SER PRO GLU ALA LYS TYR PRO THR
SEQRES 11 A 320 ALA ILE GLU GLN ASN TYR ALA VAL LEU GLN GLN LEU LYS
SEQRES 12 A 320 ASP PHE ALA ASN ASP LYS LYS PHE ASP VAL ASN HIS LEU
SEQRES 13 A 320 THR VAL ALA GLY ASP SER VAL GLY GLY ASN MET ALA THR
SEQRES 14 A 320 VAL MET THR LEU LEU THR LYS GLN ARG GLY GLY GLN LYS
SEQRES 15 A 320 ILE GLY GLN GLN VAL LEU TYR TYR PRO VAL THR ASP ALA
SEQRES 16 A 320 ASN PHE ASP THR ASP SER TYR ASN GLU PHE ALA GLU ASN
SEQRES 17 A 320 TYR PHE LEU THR LYS GLU GLY MET ILE TRP PHE TRP ASP
SEQRES 18 A 320 GLN TYR THR THR SER GLN GLU GLU ARG HIS GLN ILE THR
SEQRES 19 A 320 ALA SER PRO LEU ARG ALA THR LYS GLU ASP LEU ALA ASP
SEQRES 20 A 320 LEU PRO ALA ALA LEU ILE ILE THR GLY GLU ALA ASP VAL
SEQRES 21 A 320 LEU ARG ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ARG
SEQRES 22 A 320 GLU ALA ASP VAL GLU VAL THR GLN VAL ARG PHE GLN ALA
SEQRES 23 A 320 ILE ILE HIS ASP PHE VAL MET VAL ASN SER MET ASN GLU
SEQRES 24 A 320 THR HIS ALA THR ARG ALA ALA MET SER LEU SER THR GLN
SEQRES 25 A 320 TRP ILE ASN GLU LYS ASN ARG LYS
SEQRES 1 B 320 GLY SER HIS MET VAL GLU ARG ILE SER LEU GLU LYS ALA
SEQRES 2 B 320 ALA LEU GLU PHE SER GLU ALA ASN ALA PRO HIS PRO ARG
SEQRES 3 B 320 ILE TYR GLU LEU PRO VAL GLU GLU GLY ARG SER LEU LEU
SEQRES 4 B 320 ASN GLU VAL GLN ASP SER PRO VAL VAL LYS GLU ASP VAL
SEQRES 5 B 320 ASP ILE GLU ASP ILE ALA VAL ASP THR GLY GLU TRP GLY
SEQRES 6 B 320 GLU ILE ASN VAL ARG PHE ILE ARG PRO LEU HIS GLN GLU
SEQRES 7 B 320 LYS LYS LEU PRO VAL ILE PHE TYR ILE HIS GLY ALA GLY
SEQRES 8 B 320 TRP VAL PHE GLY ASN ALA HIS THR HIS ASP LYS LEU ILE
SEQRES 9 B 320 ARG GLU LEU ALA VAL ARG THR ASN SER VAL VAL VAL PHE
SEQRES 10 B 320 SER GLU TYR SER LEU SER PRO GLU ALA LYS TYR PRO THR
SEQRES 11 B 320 ALA ILE GLU GLN ASN TYR ALA VAL LEU GLN GLN LEU LYS
SEQRES 12 B 320 ASP PHE ALA ASN ASP LYS LYS PHE ASP VAL ASN HIS LEU
SEQRES 13 B 320 THR VAL ALA GLY ASP SER VAL GLY GLY ASN MET ALA THR
SEQRES 14 B 320 VAL MET THR LEU LEU THR LYS GLN ARG GLY GLY GLN LYS
SEQRES 15 B 320 ILE GLY GLN GLN VAL LEU TYR TYR PRO VAL THR ASP ALA
SEQRES 16 B 320 ASN PHE ASP THR ASP SER TYR ASN GLU PHE ALA GLU ASN
SEQRES 17 B 320 TYR PHE LEU THR LYS GLU GLY MET ILE TRP PHE TRP ASP
SEQRES 18 B 320 GLN TYR THR THR SER GLN GLU GLU ARG HIS GLN ILE THR
SEQRES 19 B 320 ALA SER PRO LEU ARG ALA THR LYS GLU ASP LEU ALA ASP
SEQRES 20 B 320 LEU PRO ALA ALA LEU ILE ILE THR GLY GLU ALA ASP VAL
SEQRES 21 B 320 LEU ARG ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ARG
SEQRES 22 B 320 GLU ALA ASP VAL GLU VAL THR GLN VAL ARG PHE GLN ALA
SEQRES 23 B 320 ILE ILE HIS ASP PHE VAL MET VAL ASN SER MET ASN GLU
SEQRES 24 B 320 THR HIS ALA THR ARG ALA ALA MET SER LEU SER THR GLN
SEQRES 25 B 320 TRP ILE ASN GLU LYS ASN ARG LYS
SEQRES 1 C 320 GLY SER HIS MET VAL GLU ARG ILE SER LEU GLU LYS ALA
SEQRES 2 C 320 ALA LEU GLU PHE SER GLU ALA ASN ALA PRO HIS PRO ARG
SEQRES 3 C 320 ILE TYR GLU LEU PRO VAL GLU GLU GLY ARG SER LEU LEU
SEQRES 4 C 320 ASN GLU VAL GLN ASP SER PRO VAL VAL LYS GLU ASP VAL
SEQRES 5 C 320 ASP ILE GLU ASP ILE ALA VAL ASP THR GLY GLU TRP GLY
SEQRES 6 C 320 GLU ILE ASN VAL ARG PHE ILE ARG PRO LEU HIS GLN GLU
SEQRES 7 C 320 LYS LYS LEU PRO VAL ILE PHE TYR ILE HIS GLY ALA GLY
SEQRES 8 C 320 TRP VAL PHE GLY ASN ALA HIS THR HIS ASP LYS LEU ILE
SEQRES 9 C 320 ARG GLU LEU ALA VAL ARG THR ASN SER VAL VAL VAL PHE
SEQRES 10 C 320 SER GLU TYR SER LEU SER PRO GLU ALA LYS TYR PRO THR
SEQRES 11 C 320 ALA ILE GLU GLN ASN TYR ALA VAL LEU GLN GLN LEU LYS
SEQRES 12 C 320 ASP PHE ALA ASN ASP LYS LYS PHE ASP VAL ASN HIS LEU
SEQRES 13 C 320 THR VAL ALA GLY ASP SER VAL GLY GLY ASN MET ALA THR
SEQRES 14 C 320 VAL MET THR LEU LEU THR LYS GLN ARG GLY GLY GLN LYS
SEQRES 15 C 320 ILE GLY GLN GLN VAL LEU TYR TYR PRO VAL THR ASP ALA
SEQRES 16 C 320 ASN PHE ASP THR ASP SER TYR ASN GLU PHE ALA GLU ASN
SEQRES 17 C 320 TYR PHE LEU THR LYS GLU GLY MET ILE TRP PHE TRP ASP
SEQRES 18 C 320 GLN TYR THR THR SER GLN GLU GLU ARG HIS GLN ILE THR
SEQRES 19 C 320 ALA SER PRO LEU ARG ALA THR LYS GLU ASP LEU ALA ASP
SEQRES 20 C 320 LEU PRO ALA ALA LEU ILE ILE THR GLY GLU ALA ASP VAL
SEQRES 21 C 320 LEU ARG ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ARG
SEQRES 22 C 320 GLU ALA ASP VAL GLU VAL THR GLN VAL ARG PHE GLN ALA
SEQRES 23 C 320 ILE ILE HIS ASP PHE VAL MET VAL ASN SER MET ASN GLU
SEQRES 24 C 320 THR HIS ALA THR ARG ALA ALA MET SER LEU SER THR GLN
SEQRES 25 C 320 TRP ILE ASN GLU LYS ASN ARG LYS
HET CL A 401 1
HET ACT B 401 4
HET ACT C 401 4
HETNAM CL CHLORIDE ION
HETNAM ACT ACETATE ION
FORMUL 4 CL CL 1-
FORMUL 5 ACT 2(C2 H3 O2 1-)
FORMUL 7 HOH *496(H2 O)
HELIX 1 AA1 GLU A 8 ASN A 18 1 11
HELIX 2 AA2 ARG A 23 LEU A 27 5 5
HELIX 3 AA3 PRO A 28 GLN A 40 1 13
HELIX 4 AA4 GLY A 59 TRP A 61 5 3
HELIX 5 AA5 HIS A 97 THR A 108 1 12
HELIX 6 AA6 PRO A 126 GLN A 138 1 13
HELIX 7 AA7 GLN A 138 ALA A 143 1 6
HELIX 8 AA8 SER A 159 GLY A 176 1 18
HELIX 9 AA9 THR A 196 PHE A 202 1 7
HELIX 10 AB1 THR A 209 THR A 221 1 13
HELIX 11 AB2 SER A 223 GLN A 229 1 7
HELIX 12 AB3 SER A 233 ALA A 237 5 5
HELIX 13 AB4 THR A 238 ALA A 243 1 6
HELIX 14 AB5 LEU A 258 ALA A 272 1 15
HELIX 15 AB6 VAL A 291 ASN A 295 5 5
HELIX 16 AB7 THR A 297 ASN A 315 1 19
HELIX 17 AB8 GLU B 8 ASN B 18 1 11
HELIX 18 AB9 ARG B 23 LEU B 27 5 5
HELIX 19 AC1 PRO B 28 GLN B 40 1 13
HELIX 20 AC2 HIS B 97 ASN B 109 1 13
HELIX 21 AC3 PRO B 126 GLN B 138 1 13
HELIX 22 AC4 GLN B 138 ALA B 143 1 6
HELIX 23 AC5 SER B 159 GLY B 176 1 18
HELIX 24 AC6 THR B 196 PHE B 202 1 7
HELIX 25 AC7 THR B 209 THR B 221 1 13
HELIX 26 AC8 SER B 223 GLN B 229 1 7
HELIX 27 AC9 SER B 233 ALA B 237 5 5
HELIX 28 AD1 THR B 238 ALA B 243 1 6
HELIX 29 AD2 LEU B 258 ALA B 272 1 15
HELIX 30 AD3 VAL B 291 ASN B 295 5 5
HELIX 31 AD4 THR B 297 ASN B 315 1 19
HELIX 32 AD5 GLU C 8 ASN C 18 1 11
HELIX 33 AD6 ARG C 23 LEU C 27 5 5
HELIX 34 AD7 PRO C 28 GLN C 40 1 13
HELIX 35 AD8 GLY C 59 TRP C 61 5 3
HELIX 36 AD9 HIS C 97 ASN C 109 1 13
HELIX 37 AE1 PRO C 126 LEU C 139 1 14
HELIX 38 AE2 PHE C 142 LYS C 147 1 6
HELIX 39 AE3 SER C 159 GLY C 176 1 18
HELIX 40 AE4 THR C 196 PHE C 202 1 7
HELIX 41 AE5 THR C 209 THR C 221 1 13
HELIX 42 AE6 SER C 223 HIS C 228 1 6
HELIX 43 AE7 SER C 233 ALA C 237 5 5
HELIX 44 AE8 THR C 238 ALA C 243 1 6
HELIX 45 AE9 LEU C 258 ALA C 272 1 15
HELIX 46 AF1 VAL C 291 ASN C 295 5 5
HELIX 47 AF2 THR C 297 ASN C 315 1 19
SHEET 1 AA116 VAL A 49 ASP A 57 0
SHEET 2 AA116 GLU A 63 PRO A 71 -1 O PHE A 68 N GLU A 52
SHEET 3 AA116 VAL A 111 SER A 115 -1 O PHE A 114 N ARG A 67
SHEET 4 AA116 LEU A 78 ILE A 84 1 N TYR A 83 O VAL A 113
SHEET 5 AA116 PHE A 148 ASP A 158 1 O HIS A 152 N VAL A 80
SHEET 6 AA116 GLN A 182 TYR A 186 1 O VAL A 184 N VAL A 155
SHEET 7 AA116 ALA A 247 ALA A 255 1 O LEU A 249 N LEU A 185
SHEET 8 AA116 VAL A 276 ILE A 285 1 O THR A 277 N ILE A 250
SHEET 9 AA116 VAL B 276 ILE B 285 -1 O ARG B 280 N ARG A 280
SHEET 10 AA116 ALA B 247 ALA B 255 1 N THR B 252 O PHE B 281
SHEET 11 AA116 GLN B 182 TYR B 186 1 N LEU B 185 O LEU B 249
SHEET 12 AA116 PHE B 148 ASP B 158 1 N GLY B 157 O TYR B 186
SHEET 13 AA116 LEU B 78 ILE B 84 1 N PHE B 82 O ALA B 156
SHEET 14 AA116 VAL B 111 SER B 115 1 O VAL B 113 N TYR B 83
SHEET 15 AA116 GLU B 63 ARG B 70 -1 N ARG B 67 O PHE B 114
SHEET 16 AA116 ASP B 50 ASP B 57 -1 N ILE B 54 O VAL B 66
SHEET 1 AA2 8 VAL C 49 ASP C 57 0
SHEET 2 AA2 8 GLU C 63 PRO C 71 -1 O ILE C 64 N VAL C 56
SHEET 3 AA2 8 VAL C 111 SER C 115 -1 O PHE C 114 N ARG C 67
SHEET 4 AA2 8 LEU C 78 ILE C 84 1 N ILE C 81 O VAL C 113
SHEET 5 AA2 8 PHE C 148 ASP C 158 1 O THR C 154 N PHE C 82
SHEET 6 AA2 8 GLN C 182 TYR C 186 1 O TYR C 186 N GLY C 157
SHEET 7 AA2 8 ALA C 247 GLY C 253 1 O LEU C 249 N LEU C 185
SHEET 8 AA2 8 VAL C 276 PHE C 281 1 O THR C 277 N ILE C 250
CISPEP 1 HIS A 21 PRO A 22 0 -0.98
CISPEP 2 SER A 120 PRO A 121 0 -2.60
CISPEP 3 TYR A 125 PRO A 126 0 -1.71
CISPEP 4 HIS B 21 PRO B 22 0 1.48
CISPEP 5 SER B 120 PRO B 121 0 -5.35
CISPEP 6 TYR B 125 PRO B 126 0 4.86
CISPEP 7 HIS C 21 PRO C 22 0 3.14
CISPEP 8 SER C 120 PRO C 121 0 -0.41
CISPEP 9 TYR C 125 PRO C 126 0 -1.11
CRYST1 54.410 92.770 218.111 90.00 96.62 90.00 I 1 2 1 12
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 0.018379 0.000000 0.002131 0.00000
SCALE2 0.000000 0.010779 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004616 0.00000
TER 2525 ARG A 316
TER 5050 ARG B 316
TER 7575 ARG C 316
MASTER 315 0 3 47 24 0 0 6 8077 3 8 75
END
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