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HEADER HYDROLASE 10-MAR-21 7EBO
TITLE CRYSTAL STRUCTURE OF A FERULOYL ESTERASE LP_0796 FROM LACTOBACILLUS
TITLE 2 PLANTARUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTIPLANTIBACILLUS PLANTARUM WCFS1;
SOURCE 3 ORGANISM_TAXID: 220668;
SOURCE 4 STRAIN: ATCC BAA-793 / NCIMB 8826 / WCFS1;
SOURCE 5 GENE: LP_0796;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS FERULOYL ESTERASE, LACTOBACILLUS PLANTARUM, CARBOXYLESTERASE,
KEYWDS 2 CATALYTIC TRIAD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.W.ZHANG,Y.L.WANG,F.J.XIN
REVDAT 1 03-AUG-22 7EBO 0
JRNL AUTH H.ZHANG,B.WEN,Y.LIU,G.DU,X.WEI,K.M.S.U.IMAM,H.ZHOU,S.FAN,
JRNL AUTH 2 F.WANG,Y.WANG,F.XIN
JRNL TITL A REVERSE CATALYTIC TRIAD ASP CONTAINING LOOP SHAPING A WIDE
JRNL TITL 2 SUBSTRATE BINDING POCKET OF A FERULOYL ESTERASE FROM
JRNL TITL 3 LACTOBACILLUS PLANTARUM.
JRNL REF INT.J.BIOL.MACROMOL. V. 184 92 2021
JRNL REFN ISSN 0141-8130
JRNL PMID 34116094
JRNL DOI 10.1016/J.IJBIOMAC.2021.06.033
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.18
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 16162
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.190
REMARK 3 FREE R VALUE TEST SET COUNT : 839
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 4.5420 - 3.6055 1.00 2599 128 0.1745 0.1961
REMARK 3 2 3.6055 - 3.1498 1.00 2553 147 0.1983 0.2283
REMARK 3 3 3.1498 - 2.8619 1.00 2553 112 0.2269 0.2982
REMARK 3 4 2.8619 - 2.6567 1.00 2516 143 0.2249 0.2781
REMARK 3 5 2.6567 - 2.5001 0.97 2405 153 0.2268 0.3082
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.88
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.07
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 : 0.003 3875
REMARK 3 ANGLE : 0.725 5282
REMARK 3 CHIRALITY : 0.043 591
REMARK 3 PLANARITY : 0.004 693
REMARK 3 DIHEDRAL : 22.965 1348
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 7EBO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-MAR-21.
REMARK 100 THE DEPOSITION ID IS D_1300021111.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-NOV-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21091
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
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 (%) : 96.2
REMARK 200 DATA REDUNDANCY : 10.60
REMARK 200 R MERGE (I) : 0.11200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.60
REMARK 200 R MERGE FOR SHELL (I) : 0.48600
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: 1TQH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M MES PH
REMARK 280 6.5 AND 25% POLYETHYLENE GLYCOL 8000, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
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 27.44550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.36300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.16950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.36300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.44550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.16950
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: 3280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 MET A 1
REMARK 465 MET A 2
REMARK 465 LEU A 3
REMARK 465 LYS A 4
REMARK 465 GLN A 5
REMARK 465 PRO A 6
REMARK 465 LYS A 249
REMARK 465 MET B 1
REMARK 465 MET B 2
REMARK 465 LEU B 3
REMARK 465 ASN B 124
REMARK 465 ARG B 125
REMARK 465 TYR B 248
REMARK 465 LYS B 249
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 GLU A 7 CG CD OE1 OE2
REMARK 470 ASP A 56 CG OD1 OD2
REMARK 470 MET A 131 CG SD CE
REMARK 470 ARG A 163 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 4 CG CD CE NZ
REMARK 470 GLN B 82 CG CD OE1 NE2
REMARK 470 HIS B 142 CG ND1 CD2 CE1 NE2
REMARK 470 SER B 143 OG
REMARK 470 GLN B 144 CG CD OE1 NE2
REMARK 470 ARG B 204 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 205 CG CD OE1 NE2
REMARK 470 GLN B 238 CG CD OE1 NE2
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 HIS A 13 -79.00 -138.08
REMARK 500 SER A 94 -113.14 51.66
REMARK 500 HIS B 13 -79.90 -140.80
REMARK 500 SER B 94 -113.81 51.68
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 SO4 A 300
DBREF 7EBO A 1 249 UNP F9UM18 F9UM18_LACPL 1 249
DBREF 7EBO B 1 249 UNP F9UM18 F9UM18_LACPL 1 249
SEQRES 1 A 249 MET MET LEU LYS GLN PRO GLU PRO PHE PHE PHE GLU HIS
SEQRES 2 A 249 GLY GLN HIS ALA VAL ILE LEU LEU HIS ALA TYR ALA GLY
SEQRES 3 A 249 SER ALA ASN ASP VAL ARG MET LEU ALA ARG ALA LEU GLU
SEQRES 4 A 249 ARG GLU ASP TYR THR VAL TYR GLY PRO GLN PHE SER GLY
SEQRES 5 A 249 HIS ALA THR ASP ASP PRO ARG ASP ILE LEU ALA GLN THR
SEQRES 6 A 249 PRO ALA GLN TRP TRP GLN ASP THR GLN GLN ALA ILE SER
SEQRES 7 A 249 PHE MET ARG GLN LYS GLY TYR THR LYS ILE SER ILE PHE
SEQRES 8 A 249 GLY LEU SER LEU GLY GLY ILE PHE ALA THR ALA ALA LEU
SEQRES 9 A 249 GLU ARG ASP PRO GLN LEU LEU GLY GLY GLY THR PHE SER
SEQRES 10 A 249 SER PRO LEU PHE ALA GLY ASN ARG SER ASP VAL ALA GLU
SEQRES 11 A 249 MET PHE ILE THR LEU SER HIS HIS GLN LEU ALA HIS SER
SEQRES 12 A 249 GLN PHE SER ILE ALA GLU ARG GLU GLN ILE LEU MET THR
SEQRES 13 A 249 LEU PRO GLU LEU VAL GLN ARG GLN LEU GLN ALA VAL ASN
SEQRES 14 A 249 THR PHE THR THR THR GLU VAL THR SER HIS LEU SER ALA
SEQRES 15 A 249 VAL THR GLN PRO PHE PHE ILE GLY GLN GLY GLY GLN ASP
SEQRES 16 A 249 GLU LEU ILE ASP ALA THR VAL ALA ARG GLN LEU ARG ASP
SEQRES 17 A 249 GLN LEU PRO GLN VAL PRO VAL ASP PHE HIS TRP TYR ALA
SEQRES 18 A 249 ASP ALA GLY HIS VAL ILE THR VAL ASN SER ALA HIS HIS
SEQRES 19 A 249 GLN LEU GLU GLN ASP VAL LEU THR TYR LEU LYS THR ILE
SEQRES 20 A 249 TYR LYS
SEQRES 1 B 249 MET MET LEU LYS GLN PRO GLU PRO PHE PHE PHE GLU HIS
SEQRES 2 B 249 GLY GLN HIS ALA VAL ILE LEU LEU HIS ALA TYR ALA GLY
SEQRES 3 B 249 SER ALA ASN ASP VAL ARG MET LEU ALA ARG ALA LEU GLU
SEQRES 4 B 249 ARG GLU ASP TYR THR VAL TYR GLY PRO GLN PHE SER GLY
SEQRES 5 B 249 HIS ALA THR ASP ASP PRO ARG ASP ILE LEU ALA GLN THR
SEQRES 6 B 249 PRO ALA GLN TRP TRP GLN ASP THR GLN GLN ALA ILE SER
SEQRES 7 B 249 PHE MET ARG GLN LYS GLY TYR THR LYS ILE SER ILE PHE
SEQRES 8 B 249 GLY LEU SER LEU GLY GLY ILE PHE ALA THR ALA ALA LEU
SEQRES 9 B 249 GLU ARG ASP PRO GLN LEU LEU GLY GLY GLY THR PHE SER
SEQRES 10 B 249 SER PRO LEU PHE ALA GLY ASN ARG SER ASP VAL ALA GLU
SEQRES 11 B 249 MET PHE ILE THR LEU SER HIS HIS GLN LEU ALA HIS SER
SEQRES 12 B 249 GLN PHE SER ILE ALA GLU ARG GLU GLN ILE LEU MET THR
SEQRES 13 B 249 LEU PRO GLU LEU VAL GLN ARG GLN LEU GLN ALA VAL ASN
SEQRES 14 B 249 THR PHE THR THR THR GLU VAL THR SER HIS LEU SER ALA
SEQRES 15 B 249 VAL THR GLN PRO PHE PHE ILE GLY GLN GLY GLY GLN ASP
SEQRES 16 B 249 GLU LEU ILE ASP ALA THR VAL ALA ARG GLN LEU ARG ASP
SEQRES 17 B 249 GLN LEU PRO GLN VAL PRO VAL ASP PHE HIS TRP TYR ALA
SEQRES 18 B 249 ASP ALA GLY HIS VAL ILE THR VAL ASN SER ALA HIS HIS
SEQRES 19 B 249 GLN LEU GLU GLN ASP VAL LEU THR TYR LEU LYS THR ILE
SEQRES 20 B 249 TYR LYS
HET SO4 A 300 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 O4 S 2-
FORMUL 4 HOH *96(H2 O)
HELIX 1 AA1 SER A 27 ASP A 30 5 4
HELIX 2 AA2 VAL A 31 GLU A 41 1 11
HELIX 3 AA3 PRO A 58 GLN A 64 1 7
HELIX 4 AA4 THR A 65 LYS A 83 1 19
HELIX 5 AA5 SER A 94 ASP A 107 1 14
HELIX 6 AA6 ARG A 125 ALA A 141 1 17
HELIX 7 AA7 SER A 146 VAL A 176 1 31
HELIX 8 AA8 THR A 177 VAL A 183 5 7
HELIX 9 AA9 ILE A 198 GLN A 209 1 12
HELIX 10 AB1 ALA A 232 TYR A 248 1 17
HELIX 11 AB2 SER B 27 ASP B 30 5 4
HELIX 12 AB3 VAL B 31 GLU B 41 1 11
HELIX 13 AB4 ASP B 57 GLN B 64 1 8
HELIX 14 AB5 THR B 65 LYS B 83 1 19
HELIX 15 AB6 SER B 94 ASP B 107 1 14
HELIX 16 AB7 ASP B 127 HIS B 142 1 16
HELIX 17 AB8 SER B 146 MET B 155 1 10
HELIX 18 AB9 THR B 156 VAL B 176 1 21
HELIX 19 AC1 THR B 177 VAL B 183 5 7
HELIX 20 AC2 THR B 201 GLN B 209 1 9
HELIX 21 AC3 ALA B 232 ILE B 247 1 16
SHEET 1 AA1 7 PHE A 9 PHE A 11 0
SHEET 2 AA1 7 THR A 44 GLY A 47 -1 O VAL A 45 N PHE A 11
SHEET 3 AA1 7 HIS A 16 LEU A 21 1 N VAL A 18 O THR A 44
SHEET 4 AA1 7 LYS A 87 LEU A 93 1 O SER A 89 N ILE A 19
SHEET 5 AA1 7 GLY A 112 PHE A 116 1 O PHE A 116 N GLY A 92
SHEET 6 AA1 7 PHE A 187 GLY A 192 1 O PHE A 188 N GLY A 113
SHEET 7 AA1 7 VAL A 215 TYR A 220 1 O ASP A 216 N PHE A 187
SHEET 1 AA2 7 PHE B 9 PHE B 11 0
SHEET 2 AA2 7 THR B 44 GLY B 47 -1 O VAL B 45 N PHE B 11
SHEET 3 AA2 7 ALA B 17 LEU B 21 1 N VAL B 18 O THR B 44
SHEET 4 AA2 7 ILE B 88 LEU B 93 1 O PHE B 91 N ILE B 19
SHEET 5 AA2 7 GLY B 112 PHE B 116 1 O PHE B 116 N GLY B 92
SHEET 6 AA2 7 PHE B 187 GLY B 192 1 O PHE B 188 N GLY B 113
SHEET 7 AA2 7 VAL B 215 TYR B 220 1 O TYR B 220 N GLN B 191
SITE 1 AC1 3 ARG A 40 ARG B 32 ARG B 36
CRYST1 54.891 74.339 110.726 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 0.018218 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013452 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009031 0.00000
TER 1900 TYR A 248
TER 3778 ILE B 247
MASTER 262 0 1 21 14 0 1 6 3877 2 5 40
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