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HEADER HYDROLASE 29-NOV-19 6TKX
TITLE CARBOHYDRATE ESTERASE FROM GUT MICROBIOTA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOHYDRATE ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METAGENOME;
SOURCE 3 ORGANISM_TAXID: 256318;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CARBOHYDRATE ESTERASE, ALPHA/BETA HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.PENTTINEN,N.HAKULINEN,R.E.MASTER
REVDAT 1 16-DEC-20 6TKX 0
JRNL AUTH L.PENTTINEN,L.HAMELEERS,N.HAKULINEN,E.JURAK,R.E.MASTER
JRNL TITL CRYSTAL STRUCTURE AND CHARACTERIZATION OF AN ACETYL XYLAN
JRNL TITL 2 ESTERASE FROM BEAVER GUT METAGENOMICS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.06 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.14_3260: 000)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.06
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 17055
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880
REMARK 3 FREE R VALUE TEST SET COUNT : 832
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 41.3990 - 3.7426 1.00 2876 133 0.1679 0.1895
REMARK 3 2 3.7426 - 2.9708 1.00 2713 153 0.1963 0.3079
REMARK 3 3 2.9708 - 2.5954 1.00 2677 145 0.2387 0.3123
REMARK 3 4 2.5954 - 2.3581 1.00 2639 139 0.2453 0.3406
REMARK 3 5 2.3581 - 2.1891 1.00 2680 121 0.2716 0.3408
REMARK 3 6 2.1891 - 2.0600 1.00 2638 141 0.2984 0.3673
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.070
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 2279
REMARK 3 ANGLE : 1.156 3107
REMARK 3 CHIRALITY : 0.058 342
REMARK 3 PLANARITY : 0.008 406
REMARK 3 DIHEDRAL : 12.580 1345
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 6TKX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-NOV-19.
REMARK 100 THE DEPOSITION ID IS D_1292105516.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAY-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17093
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.060
REMARK 200 RESOLUTION RANGE LOW (A) : 41.399
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.06
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
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 : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: ROSETTA
REMARK 200 STARTING MODEL: 3HXK, 4N5H, 5AO9, 2WTM, 3BXP, 3BJR, 4V2I, 2C7B,
REMARK 200 4E15, 4Q3K, 3PFB, 3ZWQ, 5L2P, 3QH4, 5G5C, 5JD4, 4ZI5, 3F67, 5CML,
REMARK 200 4WY8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 25% PEG MME
REMARK 280 5000, 0.1 M MES PH 6.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 22.39500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 54.23000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 54.23000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 33.59250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 54.23000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 54.23000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 11.19750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 54.23000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.23000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 33.59250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 54.23000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.23000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 11.19750
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 22.39500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 604 LIES ON A SPECIAL POSITION.
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 LEU A 293
REMARK 465 GLU A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG SER A 128 O HOH A 501 2.00
REMARK 500 OE1 GLU A 156 OG SER A 167 2.10
REMARK 500 OD2 ASP A 226 O HOH A 502 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 41 101.92 -54.86
REMARK 500 SER A 55 16.61 -174.97
REMARK 500 ASN A 61 22.12 -155.69
REMARK 500 SER A 128 -128.32 62.69
REMARK 500 PHE A 176 57.40 31.48
REMARK 500 ASN A 186 18.38 54.70
REMARK 500 PHE A 274 43.36 -86.23
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 401
DBREF 6TKX A 1 300 PDB 6TKX 6TKX 1 300
SEQRES 1 A 300 MET GLN ASP PHE GLN MET PRO LYS GLY PRO ALA GLU ASP
SEQRES 2 A 300 THR TYR SER THR SER TRP THR ASN VAL ASN TYR ALA SER
SEQRES 3 A 300 ASP SER LEU GLU SER HIS ASN LEU ASP ILE TYR LEU PRO
SEQRES 4 A 300 LYS GLU GLN LYS THR ALA TYR LYS ALA ILE ILE ILE ILE
SEQRES 5 A 300 TYR GLY SER ALA TRP PHE ALA ASN ASN ALA LYS ALA MET
SEQRES 6 A 300 ALA SER ALA SER ILE GLY ALA PRO LEU LEU LYS ALA GLY
SEQRES 7 A 300 PHE ALA VAL ILE SER ILE ASN HIS ARG SER SER MET GLU
SEQRES 8 A 300 ALA ILE TRP PRO ALA GLN ILE GLN ASP VAL LYS ALA ALA
SEQRES 9 A 300 ILE ARG TYR VAL ARG SER ASN ALA ALA LYS TYR ASN ILE
SEQRES 10 A 300 ASP PRO SER PHE ILE GLY ILE THR GLY PHE SER SER GLY
SEQRES 11 A 300 GLY HIS LEU SER ALA PHE ALA GLY VAL THR ASN GLY VAL
SEQRES 12 A 300 LYS THR LEU THR SER GLY ASP LEU THR VAL ASP ILE GLU
SEQRES 13 A 300 GLY SER LEU GLY ASN TYR LEU SER THR GLY SER HIS VAL
SEQRES 14 A 300 ASP ALA VAL VAL ASP TRP PHE GLY PRO VAL ASP MET ALA
SEQRES 15 A 300 HIS MET SER ASN CYS VAL ALA PRO ASN ASP ALA SER THR
SEQRES 16 A 300 PRO GLU ALA VAL LEU ILE GLY LYS LYS ASP PRO ARG GLU
SEQRES 17 A 300 GLU PRO ASP TRP VAL LYS LEU ILE SER PRO ILE ASN PHE
SEQRES 18 A 300 VAL ASP LYS ASP ASP PRO ASP ILE LEU ILE ILE HIS GLY
SEQRES 19 A 300 ASP ALA ASP ASN VAL VAL PRO HIS CYS GLN SER VAL ASN
SEQRES 20 A 300 LEU LYS ASN VAL TYR ASP ASN ALA GLY ALA LYS ALA THR
SEQRES 21 A 300 PHE ILE SER VAL PRO GLY GLY GLY HIS GLY PRO GLY CYS
SEQRES 22 A 300 PHE ASP THR GLN TYR PHE LYS ASP MET THR ASP PHE PHE
SEQRES 23 A 300 THR GLU GLN SER THR LYS LEU GLU HIS HIS HIS HIS HIS
SEQRES 24 A 300 HIS
HET SO4 A 401 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 O4 S 2-
FORMUL 3 HOH *114(H2 O)
HELIX 1 AA1 ALA A 11 ASP A 13 5 3
HELIX 2 AA2 LEU A 29 SER A 31 5 3
HELIX 3 AA3 ALA A 62 GLY A 78 1 17
HELIX 4 AA4 PRO A 95 ASN A 111 1 17
HELIX 5 AA5 ALA A 112 TYR A 115 5 4
HELIX 6 AA6 SER A 128 VAL A 139 1 12
HELIX 7 AA7 ASP A 180 VAL A 188 5 9
HELIX 8 AA8 THR A 195 ILE A 201 1 7
HELIX 9 AA9 ASP A 205 GLU A 208 5 4
HELIX 10 AB1 GLU A 209 ILE A 216 1 8
HELIX 11 AB2 SER A 217 VAL A 222 5 6
HELIX 12 AB3 HIS A 242 GLY A 256 1 15
SHEET 1 AA1 8 TYR A 15 ASN A 23 0
SHEET 2 AA1 8 ASN A 33 PRO A 39 -1 O LEU A 34 N VAL A 22
SHEET 3 AA1 8 ALA A 80 ILE A 84 -1 O VAL A 81 N TYR A 37
SHEET 4 AA1 8 TYR A 46 ILE A 52 1 N ILE A 51 O ILE A 82
SHEET 5 AA1 8 ILE A 117 PHE A 127 1 O GLY A 123 N ILE A 50
SHEET 6 AA1 8 VAL A 172 TRP A 175 1 O TRP A 175 N GLY A 126
SHEET 7 AA1 8 ILE A 229 GLY A 234 1 O LEU A 230 N ASP A 174
SHEET 8 AA1 8 ALA A 259 VAL A 264 1 O ILE A 262 N ILE A 231
SHEET 1 AA2 2 THR A 145 SER A 148 0
SHEET 2 AA2 2 LEU A 151 ASP A 154 -1 O VAL A 153 N LEU A 146
SSBOND 1 CYS A 187 CYS A 243 1555 1555 2.06
CISPEP 1 TRP A 94 PRO A 95 0 7.74
SITE 1 AC1 9 GLY A 54 SER A 55 SER A 128 HIS A 183
SITE 2 AC1 9 VAL A 188 HIS A 269 HOH A 501 HOH A 507
SITE 3 AC1 9 HOH A 534
CRYST1 108.460 108.460 44.790 90.00 90.00 90.00 P 43 21 2 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 0.009220 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009220 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022326 0.00000
TER 4277 LYS A 292
MASTER 280 0 1 12 10 0 3 6 2326 1 7 24
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