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HEADER HYDROLASE 16-MAY-20 7C4D
TITLE MARINE MICROORGANISM ESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CARBOXYLESTERASES;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.H.ZHU,Y.K.WU,M.N.ISUPOV
REVDAT 1 26-MAY-21 7C4D 0
JRNL AUTH C.H.ZHU,Y.K.WU
JRNL TITL MARINE MICROORGANISM ESTERASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.03 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0258
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) : 2.03
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 20015
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) : 0.200
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.256
REMARK 3 FREE R VALUE TEST SET COUNT : 1052
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) : 2.03
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1315
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.3980
REMARK 3 BIN FREE R VALUE SET COUNT : 101
REMARK 3 BIN FREE R VALUE : 0.3610
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 : 17
REMARK 3 SOLVENT ATOMS : 66
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 60.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 68.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.54700
REMARK 3 B22 (A**2) : -0.54700
REMARK 3 B33 (A**2) : 1.77300
REMARK 3 B12 (A**2) : -0.27300
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): 0.193
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.184
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.169
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.692
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.904
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2187 ; 0.007 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2958 ; 1.430 ; 1.631
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 268 ; 5.828 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 106 ;36.271 ;23.491
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 405 ;18.413 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;22.927 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 293 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1638 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 954 ; 0.198 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1454 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 70 ; 0.135 ; 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): 1055 ; 5.358 ; 6.584
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1319 ; 7.387 ; 9.852
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1132 ; 6.542 ; 7.044
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1636 ; 9.295 ;10.335
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : BABINET MODEL PLUS MASK
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 7C4D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAY-20.
REMARK 100 THE DEPOSITION ID IS D_1300016988.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97892
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20051
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.030
REMARK 200 RESOLUTION RANGE LOW (A) : 58.024
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 2.13000
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: MORDA, MOLREP
REMARK 200 STARTING MODEL: 3BF8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8000, 50MM LI2SO4, 50MM
REMARK 280 NA2SO4, MES PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
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
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 41.33333
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 20.66667
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 GLN A -10
REMARK 465 GLY A -9
REMARK 465 THR A -8
REMARK 465 SER A -7
REMARK 465 SER A -6
REMARK 465 MET A -5
REMARK 465 ALA A -4
REMARK 465 ASP A -3
REMARK 465 ILE A -2
REMARK 465 GLY A -1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 170 CG CD CE NZ
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 85 -114.20 52.36
REMARK 500 HIS A 98 58.26 -142.09
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 EDO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 404
DBREF1 7C4D A 1 260 UNP A0A2S1GUX0_9BACT
DBREF2 7C4D A A0A2S1GUX0 2 261
SEQADV 7C4D GLN A -10 UNP A0A2S1GUX EXPRESSION TAG
SEQADV 7C4D GLY A -9 UNP A0A2S1GUX EXPRESSION TAG
SEQADV 7C4D THR A -8 UNP A0A2S1GUX EXPRESSION TAG
SEQADV 7C4D SER A -7 UNP A0A2S1GUX EXPRESSION TAG
SEQADV 7C4D SER A -6 UNP A0A2S1GUX EXPRESSION TAG
SEQADV 7C4D MET A -5 UNP A0A2S1GUX EXPRESSION TAG
SEQADV 7C4D ALA A -4 UNP A0A2S1GUX EXPRESSION TAG
SEQADV 7C4D ASP A -3 UNP A0A2S1GUX EXPRESSION TAG
SEQADV 7C4D ILE A -2 UNP A0A2S1GUX EXPRESSION TAG
SEQADV 7C4D GLY A -1 UNP A0A2S1GUX EXPRESSION TAG
SEQADV 7C4D SER A 0 UNP A0A2S1GUX EXPRESSION TAG
SEQRES 1 A 271 GLN GLY THR SER SER MET ALA ASP ILE GLY SER LEU GLU
SEQRES 2 A 271 LEU PHE PHE ARG LYS LYS GLY GLU SER GLY GLU PRO LEU
SEQRES 3 A 271 ILE ILE LEU HIS GLY LEU TYR GLY SER GLY ASP ASN TRP
SEQRES 4 A 271 ILE SER ILE ALA ASN GLU LEU LYS ASP TYR PHE GLN VAL
SEQRES 5 A 271 TYR LEU ILE ASP GLN ARG ASN HIS GLY ARG SER PRO HIS
SEQRES 6 A 271 ALA ASP ASP MET SER TYR GLU SER MET ALA GLU ASP LEU
SEQRES 7 A 271 HIS GLU PHE ILE LYS SER GLN ASN LEU GLU SER VAL ASN
SEQRES 8 A 271 ILE ILE GLY HIS SER MET GLY GLY LYS THR ALA MET TRP
SEQRES 9 A 271 PHE THR ALA ALA HIS PRO ASP LYS VAL LYS LYS LEU ILE
SEQRES 10 A 271 VAL ALA ASP ILE ALA PRO GLY LYS TYR ASP THR THR SER
SEQRES 11 A 271 PRO ASN VAL LYS THR HIS LYS LYS ILE ILE ALA ALA LEU
SEQRES 12 A 271 LYS SER ILE ASP PRO SER GLU ALA LYS THR ARG LYS GLU
SEQRES 13 A 271 ILE GLU THR GLN LEU SER ARG TYR ILE ASP ASN VAL GLN
SEQRES 14 A 271 LEU ARG MET PHE LEU LEU LYS ASN ILE GLU ARG LYS GLU
SEQRES 15 A 271 ASP GLY CYS TYR ARG TRP LYS ILE ASN ILE ASP SER ILE
SEQRES 16 A 271 GLU LYS ASN ILE ILE ASN ILE MET SER GLY ILE THR GLY
SEQRES 17 A 271 ILE ASP ILE PRO VAL HIS VAL PRO ALA LEU PHE LEU LYS
SEQRES 18 A 271 GLY GLU LEU SER ASP TYR ILE THR ASP LYS ASP ILE PRO
SEQRES 19 A 271 LEU ILE LYS GLU ILE PHE PRO ASP ALA LYS LEU VAL THR
SEQRES 20 A 271 ILE PRO GLY ALA GLY HIS TRP LEU HIS ALA GLN GLN PRO
SEQRES 21 A 271 LYS ILE PHE ILE GLN LYS THR LEU GLU PHE LEU
HET EDO A 401 4
HET EDO A 402 4
HET ACT A 403 4
HET SO4 A 404 5
HETNAM EDO 1,2-ETHANEDIOL
HETNAM ACT ACETATE ION
HETNAM SO4 SULFATE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO 2(C2 H6 O2)
FORMUL 4 ACT C2 H3 O2 1-
FORMUL 5 SO4 O4 S 2-
FORMUL 6 HOH *66(H2 O)
HELIX 1 AA1 SER A 24 ASN A 27 5 4
HELIX 2 AA2 TRP A 28 LYS A 36 1 9
HELIX 3 AA3 SER A 59 GLN A 74 1 16
HELIX 4 AA4 SER A 85 HIS A 98 1 14
HELIX 5 AA5 SER A 119 SER A 134 1 16
HELIX 6 AA6 ASP A 136 ALA A 140 5 5
HELIX 7 AA7 THR A 142 ILE A 154 1 13
HELIX 8 AA8 ASN A 156 LYS A 165 1 10
HELIX 9 AA9 ASN A 180 LYS A 186 1 7
HELIX 10 AB1 ASN A 187 SER A 193 1 7
HELIX 11 AB2 LYS A 220 PHE A 229 1 10
HELIX 12 AB3 TRP A 243 GLN A 248 1 6
HELIX 13 AB4 GLN A 248 LEU A 260 1 13
SHEET 1 AA1 7 PHE A 5 LYS A 8 0
SHEET 2 AA1 7 GLN A 40 ILE A 44 -1 O LEU A 43 N ARG A 6
SHEET 3 AA1 7 PRO A 14 LEU A 18 1 N LEU A 15 O TYR A 42
SHEET 4 AA1 7 VAL A 79 HIS A 84 1 O ASN A 80 N ILE A 16
SHEET 5 AA1 7 VAL A 102 ALA A 108 1 O ILE A 106 N ILE A 81
SHEET 6 AA1 7 ALA A 206 GLY A 211 1 O LEU A 207 N VAL A 107
SHEET 7 AA1 7 LYS A 233 ILE A 237 1 O LYS A 233 N PHE A 208
SHEET 1 AA2 2 ILE A 167 ARG A 169 0
SHEET 2 AA2 2 TYR A 175 TRP A 177 -1 O ARG A 176 N GLU A 168
CISPEP 1 ILE A 200 PRO A 201 0 -6.17
SITE 1 AC1 3 PRO A 99 ASP A 100 VAL A 102
SITE 1 AC2 3 HIS A 68 LYS A 72 LYS A 123
SITE 1 AC3 6 GLY A 20 LEU A 21 SER A 85 MET A 86
SITE 2 AC3 6 HIS A 125 HIS A 242
SITE 1 AC4 11 HIS A 19 GLY A 20 GLY A 23 SER A 24
SITE 2 AC4 11 ASN A 27 TRP A 28 HIS A 84 PHE A 162
SITE 3 AC4 11 TRP A 243 HIS A 245 HOH A 519
CRYST1 67.000 67.000 62.000 90.00 90.00 120.00 P 32 3
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 0.014925 0.008617 0.000000 0.00000
SCALE2 0.000000 0.017234 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016129 0.00000
TER 2122 LEU A 260
MASTER 296 0 4 13 9 0 7 6 2171 1 17 21
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