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HEADER HYDROLASE 10-MAY-22 7XRH
TITLE FERULOYL ESTERASE FROM LACTOBACILLUS ACIDOPHILUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CINNAMOYL ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: SEVERAL PARTS OF THE STRUCTURE WHICH SHOWED A WEAK
COMPND 7 ELECTRON DENSITY MAP WERE DELETED.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS ACIDOPHILUS;
SOURCE 3 ORGANISM_TAXID: 1579;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FERULOYL ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.HWANG,C.W.LEE,J.H.LEE,H.DO
REVDAT 1 17-MAY-23 7XRH 0
JRNL AUTH J.HWANG,C.W.LEE,J.H.LEE,H.DO
JRNL TITL FERULOYL ESTERASE FROM LACTOBACILLUS ACIDOPHILUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14_3260
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 : CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.06
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 20110
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.950
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 41.0600 - 5.5300 1.00 1458 161 0.2148 0.2246
REMARK 3 2 5.5300 - 4.3900 0.91 1253 139 0.2019 0.2783
REMARK 3 3 4.3900 - 3.8400 0.92 1243 137 0.1939 0.2534
REMARK 3 4 3.8400 - 3.4900 0.81 1090 120 0.2118 0.2510
REMARK 3 5 3.4900 - 3.2400 1.00 1335 147 0.2157 0.2765
REMARK 3 6 3.2400 - 3.0500 1.00 1347 149 0.2398 0.3072
REMARK 3 7 3.0500 - 2.8900 1.00 1314 146 0.2453 0.3291
REMARK 3 8 2.8900 - 2.7700 1.00 1330 146 0.2439 0.2945
REMARK 3 9 2.7700 - 2.6600 1.00 1341 149 0.2667 0.3319
REMARK 3 10 2.6600 - 2.5700 1.00 1313 144 0.2589 0.3092
REMARK 3 11 2.5700 - 2.4900 1.00 1324 146 0.2657 0.3086
REMARK 3 12 2.4900 - 2.4200 1.00 1312 145 0.2724 0.3528
REMARK 3 13 2.4200 - 2.3500 1.00 1333 148 0.2718 0.3280
REMARK 3 14 2.3500 - 2.3000 0.84 1117 123 0.2824 0.3670
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.302
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.320
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.02
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 : 0.012 3697
REMARK 3 ANGLE : 1.324 5018
REMARK 3 CHIRALITY : 0.078 563
REMARK 3 PLANARITY : 0.008 664
REMARK 3 DIHEDRAL : 22.752 1357
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 7XRH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-MAY-22.
REMARK 100 THE DEPOSITION ID IS D_1300029445.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-20
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 : 5C (4A)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20175
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 97.2
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.0500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
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 : 4.620
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: 3PF8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % (W/V) PEG MME 5000, 0.1 M BIS
REMARK 280 -TRIS-HCL (PH 6.5), VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 24.59400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.68350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.29500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.68350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.59400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.29500
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: 2000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 SER A 0
REMARK 465 MET A 1
REMARK 465 GLN A 145
REMARK 465 GLY A 146
REMARK 465 LEU A 246
REMARK 465 PHE A 247
REMARK 465 ASP B 143
REMARK 465 THR B 144
REMARK 465 GLN B 145
REMARK 465 GLY B 146
REMARK 465 ALA B 147
REMARK 465 THR B 148
REMARK 465 TYR B 149
REMARK 465 ASN B 150
REMARK 465 PRO B 151
REMARK 465 GLU B 152
REMARK 465 HIS B 153
REMARK 465 ILE B 154
REMARK 465 PRO B 155
REMARK 465 ALA B 156
REMARK 465 ALA B 157
REMARK 465 ILE B 158
REMARK 465 PRO B 159
REMARK 465 PHE B 160
REMARK 465 HIS B 161
REMARK 465 GLY B 162
REMARK 465 LYS B 163
REMARK 465 LYS B 164
REMARK 465 LEU B 246
REMARK 465 PHE B 247
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 PHE A 21 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE B 21 CG CD1 CD2 CE1 CE2 CZ
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 36 -159.73 -95.84
REMARK 500 ASN A 54 32.89 74.84
REMARK 500 ARG A 98 -70.81 -111.04
REMARK 500 SER A 106 -123.03 54.10
REMARK 500 TYR A 149 -165.39 -171.00
REMARK 500 ALA A 157 147.78 -172.56
REMARK 500 PHE A 160 -89.70 -129.50
REMARK 500 ASP A 222 -3.79 74.44
REMARK 500 THR B 35 -5.61 79.70
REMARK 500 ARG B 98 -78.46 -95.54
REMARK 500 SER B 106 -121.25 58.02
REMARK 500 ALA B 132 47.70 -81.37
REMARK 500 ASN B 214 75.28 -152.17
REMARK 500 ASP B 222 -3.52 78.11
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7XRH A 1 247 UNP A0A060IN49_LACAI
DBREF2 7XRH A A0A060IN49 1 247
DBREF1 7XRH B 1 247 UNP A0A060IN49_LACAI
DBREF2 7XRH B A0A060IN49 1 247
SEQADV 7XRH SER A 0 UNP A0A060IN4 EXPRESSION TAG
SEQADV 7XRH SER B 0 UNP A0A060IN4 EXPRESSION TAG
SEQRES 1 A 248 SER MET SER ARG ILE THR ILE GLU ARG ASP GLY LEU THR
SEQRES 2 A 248 LEU VAL GLY ASP ARG GLU GLU PRO PHE GLY GLU ILE TYR
SEQRES 3 A 248 ASP MET ALA ILE LEU MET HIS GLY PHE THR ALA ASN ARG
SEQRES 4 A 248 ASN THR PRO LEU LEU ARG GLN ILE ALA ASP ASN LEU ARG
SEQRES 5 A 248 ASP GLU ASN VAL ALA SER VAL ARG PHE ASP PHE ASN GLY
SEQRES 6 A 248 HIS GLY GLU SER ASP GLY ALA PHE GLU ASP MET THR VAL
SEQRES 7 A 248 CYS ASN GLU ILE ALA ASP ALA GLN LYS ILE LEU GLU TYR
SEQRES 8 A 248 VAL ARG THR ASP PRO HIS VAL ARG ASN ILE PHE LEU VAL
SEQRES 9 A 248 GLY HIS SER GLN GLY GLY VAL VAL ALA SER MET LEU ALA
SEQRES 10 A 248 GLY LEU TYR PRO ASP ILE VAL LYS LYS VAL VAL LEU LEU
SEQRES 11 A 248 ALA PRO ALA ALA GLN LEU LYS ASP ASP ALA LEU ASN GLY
SEQRES 12 A 248 ASP THR GLN GLY ALA THR TYR ASN PRO GLU HIS ILE PRO
SEQRES 13 A 248 ALA ALA ILE PRO PHE HIS GLY LYS LYS LEU GLY GLY PHE
SEQRES 14 A 248 TYR LEU ARG THR ALA GLN VAL LEU PRO ILE TYR GLU ILE
SEQRES 15 A 248 ALA LYS HIS TYR THR ASN PRO VAL SER ILE ILE VAL GLY
SEQRES 16 A 248 SER ASN ASP GLN VAL VAL ALA PRO LYS TYR SER LYS LYS
SEQRES 17 A 248 TYR ASP GLU VAL TYR GLU ASN SER GLU LEU HIS MET VAL
SEQRES 18 A 248 PRO ASP ALA ASP HIS SER PHE THR GLY GLN TYR LYS ASP
SEQRES 19 A 248 SER ALA VAL ASP LEU THR ALA GLU PHE LEU LYS PRO LEU
SEQRES 20 A 248 PHE
SEQRES 1 B 248 SER MET SER ARG ILE THR ILE GLU ARG ASP GLY LEU THR
SEQRES 2 B 248 LEU VAL GLY ASP ARG GLU GLU PRO PHE GLY GLU ILE TYR
SEQRES 3 B 248 ASP MET ALA ILE LEU MET HIS GLY PHE THR ALA ASN ARG
SEQRES 4 B 248 ASN THR PRO LEU LEU ARG GLN ILE ALA ASP ASN LEU ARG
SEQRES 5 B 248 ASP GLU ASN VAL ALA SER VAL ARG PHE ASP PHE ASN GLY
SEQRES 6 B 248 HIS GLY GLU SER ASP GLY ALA PHE GLU ASP MET THR VAL
SEQRES 7 B 248 CYS ASN GLU ILE ALA ASP ALA GLN LYS ILE LEU GLU TYR
SEQRES 8 B 248 VAL ARG THR ASP PRO HIS VAL ARG ASN ILE PHE LEU VAL
SEQRES 9 B 248 GLY HIS SER GLN GLY GLY VAL VAL ALA SER MET LEU ALA
SEQRES 10 B 248 GLY LEU TYR PRO ASP ILE VAL LYS LYS VAL VAL LEU LEU
SEQRES 11 B 248 ALA PRO ALA ALA GLN LEU LYS ASP ASP ALA LEU ASN GLY
SEQRES 12 B 248 ASP THR GLN GLY ALA THR TYR ASN PRO GLU HIS ILE PRO
SEQRES 13 B 248 ALA ALA ILE PRO PHE HIS GLY LYS LYS LEU GLY GLY PHE
SEQRES 14 B 248 TYR LEU ARG THR ALA GLN VAL LEU PRO ILE TYR GLU ILE
SEQRES 15 B 248 ALA LYS HIS TYR THR ASN PRO VAL SER ILE ILE VAL GLY
SEQRES 16 B 248 SER ASN ASP GLN VAL VAL ALA PRO LYS TYR SER LYS LYS
SEQRES 17 B 248 TYR ASP GLU VAL TYR GLU ASN SER GLU LEU HIS MET VAL
SEQRES 18 B 248 PRO ASP ALA ASP HIS SER PHE THR GLY GLN TYR LYS ASP
SEQRES 19 B 248 SER ALA VAL ASP LEU THR ALA GLU PHE LEU LYS PRO LEU
SEQRES 20 B 248 PHE
FORMUL 3 HOH *66(H2 O)
HELIX 1 AA1 THR A 40 GLU A 53 1 14
HELIX 2 AA2 ALA A 71 MET A 75 5 5
HELIX 3 AA3 THR A 76 THR A 93 1 18
HELIX 4 AA4 SER A 106 TYR A 119 1 14
HELIX 5 AA5 ALA A 133 GLY A 142 1 10
HELIX 6 AA6 GLY A 167 VAL A 175 1 9
HELIX 7 AA7 PRO A 177 LYS A 183 1 7
HELIX 8 AA8 ALA A 201 TYR A 212 1 12
HELIX 9 AA9 GLN A 230 LEU A 243 1 14
HELIX 10 AB1 THR B 40 ASP B 52 1 13
HELIX 11 AB2 ALA B 71 MET B 75 5 5
HELIX 12 AB3 THR B 76 THR B 93 1 18
HELIX 13 AB4 GLN B 107 TYR B 119 1 13
HELIX 14 AB5 GLN B 134 GLY B 142 1 9
HELIX 15 AB6 GLY B 166 GLN B 174 1 9
HELIX 16 AB7 PRO B 177 HIS B 184 1 8
HELIX 17 AB8 PRO B 202 TYR B 212 1 11
HELIX 18 AB9 THR B 228 LYS B 244 1 17
SHEET 1 AA1 8 ARG A 3 ARG A 8 0
SHEET 2 AA1 8 LEU A 11 GLU A 18 -1 O LEU A 13 N ILE A 6
SHEET 3 AA1 8 VAL A 55 PHE A 60 -1 O SER A 57 N GLU A 18
SHEET 4 AA1 8 TYR A 25 MET A 31 1 N LEU A 30 O VAL A 58
SHEET 5 AA1 8 VAL A 97 HIS A 105 1 O VAL A 103 N MET A 31
SHEET 6 AA1 8 VAL A 123 LEU A 129 1 O LEU A 129 N GLY A 104
SHEET 7 AA1 8 VAL A 189 GLY A 194 1 O ILE A 192 N LEU A 128
SHEET 8 AA1 8 SER A 215 VAL A 220 1 O HIS A 218 N ILE A 191
SHEET 1 AA2 2 ALA A 157 ILE A 158 0
SHEET 2 AA2 2 LEU A 165 GLY A 166 -1 O LEU A 165 N ILE A 158
SHEET 1 AA3 8 MET B 1 ARG B 8 0
SHEET 2 AA3 8 LEU B 11 GLU B 18 -1 O LEU B 13 N ILE B 6
SHEET 3 AA3 8 VAL B 55 PHE B 60 -1 O SER B 57 N GLU B 18
SHEET 4 AA3 8 TYR B 25 MET B 31 1 N ASP B 26 O ALA B 56
SHEET 5 AA3 8 VAL B 97 HIS B 105 1 O PHE B 101 N MET B 27
SHEET 6 AA3 8 VAL B 123 LEU B 129 1 O LYS B 124 N ILE B 100
SHEET 7 AA3 8 VAL B 189 GLY B 194 1 O SER B 190 N VAL B 126
SHEET 8 AA3 8 SER B 215 VAL B 220 1 O VAL B 220 N VAL B 193
CRYST1 49.188 74.590 123.367 90.00 90.00 90.00 P 21 21 21 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 0.020330 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013407 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008106 0.00000
TER 1884 PRO A 245
TER 3626 PRO B 245
MASTER 282 0 0 18 18 0 0 6 3690 2 0 40
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