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HEADER HYDROLASE 12-FEB-22 7WWH
TITLE CRYSTAL STRUCTURE OF THE GEOBACILLUS THERMOGLUCOSIDASIUS FERULOYL
TITLE 2 ESTERASE GTHFAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PARAGEOBACILLUS THERMOGLUCOSIDASIUS;
SOURCE 3 ORGANISM_TAXID: 1426;
SOURCE 4 GENE: DV712_01095;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ALPHA/BETA HYDROLASE, FERULOYL ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.YANG,Y.WU
REVDAT 1 09-MAR-22 7WWH 0
JRNL AUTH W.YANG,L.SUN,P.DONG,Y.CHEN,H.ZHANG,X.HUANG,L.WU,L.CHEN,
JRNL AUTH 2 D.JING,Y.WU
JRNL TITL STRUCTURE-GUIDED RATIONAL DESIGN OF THE GEOBACILLUS
JRNL TITL 2 THERMOGLUCOSIDASIUS FERULOYL ESTERASE GTHFAE TO IMPROVE ITS
JRNL TITL 3 THERMOSTABILITY.
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 600 117 2022
JRNL REFN ESSN 1090-2104
JRNL PMID 35219099
JRNL DOI 10.1016/J.BBRC.2022.02.074
REMARK 2
REMARK 2 RESOLUTION. 1.92 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18.2_3874
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) : 1.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.29
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.410
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 41098
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 2035
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 26.2900 - 4.7200 0.99 2717 129 0.1761 0.1916
REMARK 3 2 4.7200 - 3.7500 1.00 2675 131 0.1466 0.1580
REMARK 3 3 3.7500 - 3.2800 0.97 2568 139 0.1653 0.1664
REMARK 3 4 3.2800 - 2.9800 0.99 2674 140 0.1789 0.2273
REMARK 3 5 2.9800 - 2.7700 1.00 2628 146 0.1753 0.2264
REMARK 3 6 2.7700 - 2.6000 1.00 2624 145 0.1866 0.1997
REMARK 3 7 2.6000 - 2.4700 1.00 2639 139 0.1851 0.2262
REMARK 3 8 2.4700 - 2.3600 0.98 2639 134 0.1776 0.2421
REMARK 3 9 2.3600 - 2.2700 0.99 2622 125 0.1791 0.2158
REMARK 3 10 2.2700 - 2.2000 1.00 2601 154 0.1778 0.2112
REMARK 3 11 2.2000 - 2.1300 1.00 2653 138 0.1760 0.2267
REMARK 3 12 2.1300 - 2.0700 0.99 2623 140 0.1906 0.2593
REMARK 3 13 2.0700 - 2.0100 0.98 2595 128 0.2006 0.2504
REMARK 3 14 2.0100 - 1.9600 0.97 2580 128 0.2067 0.2539
REMARK 3 15 1.9600 - 1.9200 0.86 2225 119 0.2099 0.2557
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.290
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.64
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 7WWH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-FEB-22.
REMARK 100 THE DEPOSITION ID IS D_1300027644.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAY-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 : SSRF
REMARK 200 BEAMLINE : BL17B1
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41148
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.910
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 (%) : 98.7
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : 0.50500
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: 3PF8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH 7.0, 20% PEG 1000,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 43.70500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 0
REMARK 465 MET B 0
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 GLU A 43 167.03 64.26
REMARK 500 SER A 113 -108.69 57.36
REMARK 500 ASN A 141 40.89 -94.26
REMARK 500 GLU B 43 169.29 65.51
REMARK 500 SER B 113 -110.94 51.45
REMARK 500 ALA B 139 78.83 -108.90
REMARK 500 ASN B 141 58.89 -98.79
REMARK 500 GLN B 152 -74.26 -102.61
REMARK 500 ASN B 154 76.78 57.13
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7WWH A 0 251 UNP A0A369WTY0_PARTM
DBREF2 7WWH A A0A369WTY0 1 252
DBREF1 7WWH B 0 251 UNP A0A369WTY0_PARTM
DBREF2 7WWH B A0A369WTY0 1 252
SEQRES 1 A 252 MET GLN LYS ALA ILE THR LEU THR HIS ARG GLY MET THR
SEQRES 2 A 252 LEU ARG GLY MET GLU HIS ILE PRO GLU LYS SER LEU ASP
SEQRES 3 A 252 GLU LYS VAL PRO ALA VAL ILE LEU PHE HIS GLY PHE THR
SEQRES 4 A 252 GLY THR LYS LEU GLU PRO HIS ARG LEU PHE LEU LYS ILE
SEQRES 5 A 252 SER ARG ALA LEU GLU LYS GLN GLY ILE ALA SER PHE ARG
SEQRES 6 A 252 PHE ASP PHE LEU GLY SER GLY GLU SER ASP GLY ASP PHE
SEQRES 7 A 252 GLU GLU MET THR VAL SER LYS GLU ILE GLU GLU ALA HIS
SEQRES 8 A 252 ALA ILE VAL ASP PHE VAL LYS ARG ASP GLY ARG ILE ASP
SEQRES 9 A 252 PRO SER HIS ILE TYR LEU LEU GLY LEU SER MET GLY GLY
SEQRES 10 A 252 LEU VAL ALA SER VAL VAL ALA GLY GLU ARG PRO ASN ASP
SEQRES 11 A 252 VAL ALA LYS LEU ILE LEU MET ALA PRO ALA GLY ASN MET
SEQRES 12 A 252 TYR GLU LEU ILE THR GLU THR ILE ARG GLN GLU ASN ILE
SEQRES 13 A 252 ASP VAL THR ALA PRO TYR PHE ASP HIS GLY GLY ASN LEU
SEQRES 14 A 252 VAL GLY ARG SER PHE LEU GLU ASP LEU GLN THR ILE ASN
SEQRES 15 A 252 VAL PHE GLU ARG ALA LYS PRO TYR ASP GLY PRO VAL LEU
SEQRES 16 A 252 LEU ILE HIS GLY THR GLU ASP ASP VAL VAL PRO HIS ARG
SEQRES 17 A 252 VAL SER HIS LEU TYR GLU GLN LEU CYS TYR GLY SER ARG
SEQRES 18 A 252 ALA THR VAL HIS LEU ILE GLU GLY ALA ASN HIS THR PHE
SEQRES 19 A 252 ASP GLY HIS ARG TRP GLU THR GLU VAL ILE LYS THR ILE
SEQRES 20 A 252 LEU GLY PHE VAL SER
SEQRES 1 B 252 MET GLN LYS ALA ILE THR LEU THR HIS ARG GLY MET THR
SEQRES 2 B 252 LEU ARG GLY MET GLU HIS ILE PRO GLU LYS SER LEU ASP
SEQRES 3 B 252 GLU LYS VAL PRO ALA VAL ILE LEU PHE HIS GLY PHE THR
SEQRES 4 B 252 GLY THR LYS LEU GLU PRO HIS ARG LEU PHE LEU LYS ILE
SEQRES 5 B 252 SER ARG ALA LEU GLU LYS GLN GLY ILE ALA SER PHE ARG
SEQRES 6 B 252 PHE ASP PHE LEU GLY SER GLY GLU SER ASP GLY ASP PHE
SEQRES 7 B 252 GLU GLU MET THR VAL SER LYS GLU ILE GLU GLU ALA HIS
SEQRES 8 B 252 ALA ILE VAL ASP PHE VAL LYS ARG ASP GLY ARG ILE ASP
SEQRES 9 B 252 PRO SER HIS ILE TYR LEU LEU GLY LEU SER MET GLY GLY
SEQRES 10 B 252 LEU VAL ALA SER VAL VAL ALA GLY GLU ARG PRO ASN ASP
SEQRES 11 B 252 VAL ALA LYS LEU ILE LEU MET ALA PRO ALA GLY ASN MET
SEQRES 12 B 252 TYR GLU LEU ILE THR GLU THR ILE ARG GLN GLU ASN ILE
SEQRES 13 B 252 ASP VAL THR ALA PRO TYR PHE ASP HIS GLY GLY ASN LEU
SEQRES 14 B 252 VAL GLY ARG SER PHE LEU GLU ASP LEU GLN THR ILE ASN
SEQRES 15 B 252 VAL PHE GLU ARG ALA LYS PRO TYR ASP GLY PRO VAL LEU
SEQRES 16 B 252 LEU ILE HIS GLY THR GLU ASP ASP VAL VAL PRO HIS ARG
SEQRES 17 B 252 VAL SER HIS LEU TYR GLU GLN LEU CYS TYR GLY SER ARG
SEQRES 18 B 252 ALA THR VAL HIS LEU ILE GLU GLY ALA ASN HIS THR PHE
SEQRES 19 B 252 ASP GLY HIS ARG TRP GLU THR GLU VAL ILE LYS THR ILE
SEQRES 20 B 252 LEU GLY PHE VAL SER
FORMUL 3 HOH *417(H2 O)
HELIX 1 AA1 PRO A 20 ASP A 25 5 6
HELIX 2 AA2 GLU A 43 HIS A 45 5 3
HELIX 3 AA3 ARG A 46 GLN A 58 1 13
HELIX 4 AA4 ASP A 76 MET A 80 5 5
HELIX 5 AA5 THR A 81 ARG A 98 1 18
HELIX 6 AA6 SER A 113 ARG A 126 1 14
HELIX 7 AA7 PRO A 127 VAL A 130 5 4
HELIX 8 AA8 ASN A 141 GLU A 153 1 13
HELIX 9 AA9 ARG A 171 THR A 179 1 9
HELIX 10 AB1 ASN A 181 LYS A 187 1 7
HELIX 11 AB2 HIS A 206 CYS A 216 1 11
HELIX 12 AB3 TYR A 217 SER A 219 5 3
HELIX 13 AB4 GLY A 235 SER A 251 1 17
HELIX 14 AB5 PRO B 20 ASP B 25 5 6
HELIX 15 AB6 GLU B 43 HIS B 45 5 3
HELIX 16 AB7 ARG B 46 GLN B 58 1 13
HELIX 17 AB8 ASP B 76 MET B 80 5 5
HELIX 18 AB9 THR B 81 ARG B 98 1 18
HELIX 19 AC1 SER B 113 ARG B 126 1 14
HELIX 20 AC2 PRO B 127 VAL B 130 5 4
HELIX 21 AC3 TYR B 143 GLU B 148 1 6
HELIX 22 AC4 ARG B 171 THR B 179 1 9
HELIX 23 AC5 ASN B 181 LYS B 187 1 7
HELIX 24 AC6 ARG B 207 CYS B 216 1 10
HELIX 25 AC7 TYR B 217 SER B 219 5 3
HELIX 26 AC8 GLY B 235 SER B 251 1 17
SHEET 1 AA1 8 LYS A 2 HIS A 8 0
SHEET 2 AA1 8 MET A 11 HIS A 18 -1 O LEU A 13 N LEU A 6
SHEET 3 AA1 8 ALA A 61 PHE A 65 -1 O SER A 62 N HIS A 18
SHEET 4 AA1 8 VAL A 28 PHE A 34 1 N PRO A 29 O ALA A 61
SHEET 5 AA1 8 ILE A 102 LEU A 112 1 O TYR A 108 N ALA A 30
SHEET 6 AA1 8 LYS A 132 MET A 136 1 O ILE A 134 N LEU A 109
SHEET 7 AA1 8 VAL A 193 GLY A 198 1 O LEU A 194 N LEU A 135
SHEET 8 AA1 8 ALA A 221 ILE A 226 1 O HIS A 224 N LEU A 195
SHEET 1 AA2 2 TYR A 161 HIS A 164 0
SHEET 2 AA2 2 ASN A 167 GLY A 170 -1 O VAL A 169 N PHE A 162
SHEET 1 AA3 8 LYS B 2 HIS B 8 0
SHEET 2 AA3 8 MET B 11 HIS B 18 -1 O MET B 11 N HIS B 8
SHEET 3 AA3 8 ALA B 61 PHE B 65 -1 O SER B 62 N HIS B 18
SHEET 4 AA3 8 VAL B 28 PHE B 34 1 N PRO B 29 O ALA B 61
SHEET 5 AA3 8 ILE B 102 LEU B 112 1 O TYR B 108 N ALA B 30
SHEET 6 AA3 8 LYS B 132 MET B 136 1 O MET B 136 N GLY B 111
SHEET 7 AA3 8 VAL B 193 GLY B 198 1 O LEU B 194 N LEU B 135
SHEET 8 AA3 8 ALA B 221 ILE B 226 1 O HIS B 224 N LEU B 195
SHEET 1 AA4 2 TYR B 161 HIS B 164 0
SHEET 2 AA4 2 ASN B 167 GLY B 170 -1 O VAL B 169 N PHE B 162
CRYST1 46.038 87.410 69.456 90.00 95.97 90.00 P 1 21 1 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 0.021721 0.000000 0.002270 0.00000
SCALE2 0.000000 0.011440 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014476 0.00000
TER 1975 SER A 251
TER 3950 SER B 251
MASTER 235 0 0 26 20 0 0 6 4365 2 0 40
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