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HEADER HYDROLASE 28-JUN-18 6A6O
TITLE CRYSTAL STRUCTURE OF ACETYL ESTER-XYLOSIDE BIFUNCTIONAL HYDROLASE FROM
TITLE 2 CALDICELLULOSIRUPTOR LACTOACETICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE/LIPASE-LIKE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CALDICELLULOSIRUPTOR LACTOACETICUS 6A;
SOURCE 3 ORGANISM_TAXID: 632516;
SOURCE 4 GENE: CALLA_1993;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS BIFUNCTIONAL HYDROLASE; ACETYL ESTERASE ACTIVTY; 1, 4-BETA-XYLOSIDASE
KEYWDS 2 ACTIVITY, HYDROLASE., HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.CAO,Y.HUANG,L.C.SUN,X.LIU,T.F.LIU,F.Z.WANG,F.J.XIN
REVDAT 1 12-JUN-19 6A6O 0
JRNL AUTH H.CAO,L.C.SUN,Y.HUANG,X.LIU,D.YANG,T.F.LIU,X.J.JIA,B.T.WEN,
JRNL AUTH 2 T.GU,F.Z.WANG,F.J.XIN
JRNL TITL STRUCTURAL INSIGHTS INTO THE DUAL-SUBSTRATE RECOGNITION AND
JRNL TITL 2 CATALYTIC MECHANISMS OF A BIFUNCTIONAL ACETYL ESTER-XYLOSIDE
JRNL TITL 3 HYDROLASE FROM CALDICELLULOSIRUPTOR LACTOACETICUS.
JRNL REF ACS CATALYSIS V. 9 1739 2019
JRNL REFN ESSN 2155-5435
JRNL DOI 10.1021/ACSCATAL.8B03383
REMARK 2
REMARK 2 RESOLUTION. 1.80 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 31446
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 1558
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 39.7303 - 3.9999 1.00 2931 164 0.1410 0.1642
REMARK 3 2 3.9999 - 3.1753 1.00 2780 155 0.1580 0.1840
REMARK 3 3 3.1753 - 2.7740 1.00 2733 150 0.1762 0.1917
REMARK 3 4 2.7740 - 2.5204 1.00 2713 148 0.1786 0.2006
REMARK 3 5 2.5204 - 2.3398 1.00 2704 142 0.1771 0.2028
REMARK 3 6 2.3398 - 2.2019 1.00 2691 132 0.1860 0.1988
REMARK 3 7 2.2019 - 2.0916 1.00 2703 126 0.1699 0.2243
REMARK 3 8 2.0916 - 2.0006 1.00 2674 139 0.1683 0.2032
REMARK 3 9 2.0006 - 1.9235 1.00 2670 138 0.1830 0.2270
REMARK 3 10 1.9235 - 1.8572 0.99 2643 129 0.2441 0.3129
REMARK 3 11 1.8572 - 1.7991 1.00 2646 135 0.1900 0.2325
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.030
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.19
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.59
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 : 0.006 2212
REMARK 3 ANGLE : 0.822 3018
REMARK 3 CHIRALITY : 0.059 328
REMARK 3 PLANARITY : 0.006 388
REMARK 3 DIHEDRAL : 2.524 1816
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 6A6O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1300008223.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-MAY-17
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 : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97852
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31576
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 25.30
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 25.50
REMARK 200 R MERGE FOR SHELL (I) : 0.47000
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: 3HXK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8 M POTASSIUM PHOSPHATE, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 294K
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 70.08650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 34.09000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.09000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 105.12975
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.09000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 34.09000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 35.04325
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.09000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.09000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 105.12975
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 34.09000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.09000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 35.04325
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 70.08650
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 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 MET A -18
REMARK 465 GLY A -17
REMARK 465 SER A -16
REMARK 465 SER A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 SER A -8
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 54 -85.09 -119.42
REMARK 500 SER A 114 -121.11 56.57
REMARK 500 TYR A 152 60.79 30.69
REMARK 500 ILE A 155 -56.73 -129.37
REMARK 500 ALA A 158 -102.89 -98.66
REMARK 500 TYR A 245 -27.59 63.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 506 DISTANCE = 6.11 ANGSTROMS
DBREF 6A6O A 1 264 UNP G2PVG6 G2PVG6_9FIRM 1 264
SEQADV 6A6O MET A -18 UNP G2PVG6 INITIATING METHIONINE
SEQADV 6A6O GLY A -17 UNP G2PVG6 EXPRESSION TAG
SEQADV 6A6O SER A -16 UNP G2PVG6 EXPRESSION TAG
SEQADV 6A6O SER A -15 UNP G2PVG6 EXPRESSION TAG
SEQADV 6A6O HIS A -14 UNP G2PVG6 EXPRESSION TAG
SEQADV 6A6O HIS A -13 UNP G2PVG6 EXPRESSION TAG
SEQADV 6A6O HIS A -12 UNP G2PVG6 EXPRESSION TAG
SEQADV 6A6O HIS A -11 UNP G2PVG6 EXPRESSION TAG
SEQADV 6A6O HIS A -10 UNP G2PVG6 EXPRESSION TAG
SEQADV 6A6O HIS A -9 UNP G2PVG6 EXPRESSION TAG
SEQADV 6A6O SER A -8 UNP G2PVG6 EXPRESSION TAG
SEQADV 6A6O SER A -7 UNP G2PVG6 EXPRESSION TAG
SEQADV 6A6O GLY A -6 UNP G2PVG6 EXPRESSION TAG
SEQADV 6A6O LEU A -5 UNP G2PVG6 EXPRESSION TAG
SEQADV 6A6O VAL A -4 UNP G2PVG6 EXPRESSION TAG
SEQADV 6A6O PRO A -3 UNP G2PVG6 EXPRESSION TAG
SEQADV 6A6O ARG A -2 UNP G2PVG6 EXPRESSION TAG
SEQADV 6A6O GLY A -1 UNP G2PVG6 EXPRESSION TAG
SEQADV 6A6O SER A 0 UNP G2PVG6 EXPRESSION TAG
SEQRES 1 A 283 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 283 LEU VAL PRO ARG GLY SER MET ILE PRO LEU TRP GLU ASN
SEQRES 3 A 283 GLN ASN ASP ILE PRO LEU PHE ASP PRO ALA ASN PRO PHE
SEQRES 4 A 283 VAL PRO HIS LEU VAL PRO TYR ILE LEU ASP SER SER LYS
SEQRES 5 A 283 GLN LEU PRO CYS ILE ILE VAL PHE PRO GLY GLY GLY TYR
SEQRES 6 A 283 THR HIS ARG ALA GLN HIS GLU SER GLU PRO VAL CYS LEU
SEQRES 7 A 283 TRP LEU ASN SER ILE GLY ILE SER ALA PHE VAL LEU ASN
SEQRES 8 A 283 TYR ARG VAL GLN PRO TYR LYS HIS PRO ALA PRO LEU LEU
SEQRES 9 A 283 ASP ALA LYS ARG ALA ILE ARG LEU VAL ARG TYR PHE SER
SEQRES 10 A 283 LYS LYS LEU ASN ILE ASP PRO ASN ARG ILE GLY VAL LEU
SEQRES 11 A 283 GLY PHE SER ALA GLY GLY HIS LEU ALA SER LEU VAL GLY
SEQRES 12 A 283 THR HIS PHE ASP SER GLY ASP LYS LYS ASN ASP ASP PRO
SEQRES 13 A 283 VAL GLU ARG VAL SER CYS ARG PRO ASP CYS ILE VAL LEU
SEQRES 14 A 283 CYS TYR PRO VAL ILE SER LEU ALA GLU PHE ALA HIS GLU
SEQRES 15 A 283 GLY SER LYS LYS ALA LEU LEU GLY GLU ASN PRO ASP PRO
SEQRES 16 A 283 VAL LEU VAL TRP THR LEU SER SER HIS ASN MET VAL SER
SEQRES 17 A 283 SER LYS THR PRO PRO THR PHE LEU TRP HIS THR SER ASP
SEQRES 18 A 283 ASP SER SER VAL PRO VAL GLU ASN SER LEU LEU PHE ALA
SEQRES 19 A 283 MET ALA LEU LYS LYS HIS GLY VAL PRO PHE GLU LEU HIS
SEQRES 20 A 283 ILE PHE PRO HIS GLY ARG HIS GLY LEU GLY LEU ALA SER
SEQRES 21 A 283 ASP THR LEU TYR VAL LYS GLU TRP THR LYS LEU CYS GLU
SEQRES 22 A 283 LYS TRP PHE GLU SER ILE GLY PHE ILE GLY
FORMUL 2 HOH *206(H2 O)
HELIX 1 AA1 ASN A 7 ILE A 11 5 5
HELIX 2 AA2 ALA A 50 GLU A 53 5 4
HELIX 3 AA3 SER A 54 ILE A 64 1 11
HELIX 4 AA4 PRO A 81 PHE A 97 1 17
HELIX 5 AA5 PHE A 97 ASN A 102 1 6
HELIX 6 AA6 SER A 114 GLY A 124 1 11
HELIX 7 AA7 ASP A 136 VAL A 141 5 6
HELIX 8 AA8 HIS A 162 GLY A 171 1 10
HELIX 9 AA9 ASP A 175 LEU A 182 1 8
HELIX 10 AB1 SER A 183 VAL A 188 5 6
HELIX 11 AB2 VAL A 208 HIS A 221 1 14
HELIX 12 AB3 TYR A 245 LYS A 247 5 3
HELIX 13 AB4 GLU A 248 ILE A 260 1 13
SHEET 1 AA1 8 ILE A 2 PRO A 3 0
SHEET 2 AA1 8 HIS A 23 TYR A 27 -1 O LEU A 24 N ILE A 2
SHEET 3 AA1 8 SER A 67 ASN A 72 -1 O ALA A 68 N TYR A 27
SHEET 4 AA1 8 LEU A 35 PHE A 41 1 N VAL A 40 O PHE A 69
SHEET 5 AA1 8 ILE A 103 PHE A 113 1 O LEU A 111 N PHE A 41
SHEET 6 AA1 8 ILE A 148 CYS A 151 1 O CYS A 151 N GLY A 112
SHEET 7 AA1 8 THR A 195 THR A 200 1 O PHE A 196 N LEU A 150
SHEET 8 AA1 8 PHE A 225 PHE A 230 1 O GLU A 226 N LEU A 197
CISPEP 1 GLN A 76 PRO A 77 0 9.76
CISPEP 2 HIS A 80 PRO A 81 0 3.84
CRYST1 68.180 68.180 140.173 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 0.014667 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014667 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007134 0.00000
TER 2142 GLY A 264
MASTER 267 0 0 13 8 0 0 6 2340 1 0 22
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