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HEADER HYDROLASE 23-JUL-15 5CT9
TITLE G158E/K44E/R57E/Y49E BACILLUS SUBTILIS LIPASE A WITH 5% [BMIM][CL]
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LIPASE,LIPASE A;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: LIPA, QX56_01625;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21B
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.M.NORDWALD,J.G.PLAKS,J.R.SNELL,M.C.SOUSA,J.L.KAAR
REVDAT 1 04-NOV-15 5CT9 0
JRNL AUTH E.M.NORDWALD,J.G.PLAKS,J.R.SNELL,M.C.SOUSA,J.L.KAAR
JRNL TITL CRYSTALLOGRAPHIC INVESTIGATION OF IMIDAZOLIUM IONIC LIQUID
JRNL TITL 2 EFFECTS ON ENZYME STRUCTURE.
JRNL REF CHEMBIOCHEM 2015
JRNL REFN ESSN 1439-7633
JRNL PMID 26388426
JRNL DOI 10.1002/CBIC.201500398
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.3_928
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.91
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.490
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 34540
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.126
REMARK 3 R VALUE (WORKING SET) : 0.124
REMARK 3 FREE R VALUE : 0.154
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.790
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 27.9107 - 3.3723 0.86 2173 134 0.1915 0.2159
REMARK 3 2 3.3723 - 2.6774 1.00 2391 147 0.1493 0.1577
REMARK 3 3 2.6774 - 2.3392 1.00 2390 146 0.1342 0.1566
REMARK 3 4 2.3392 - 2.1254 1.00 2356 145 0.1072 0.1323
REMARK 3 5 2.1254 - 1.9731 1.00 2350 145 0.1067 0.1406
REMARK 3 6 1.9731 - 1.8568 1.00 2327 143 0.1021 0.1313
REMARK 3 7 1.8568 - 1.7638 1.00 2343 144 0.0986 0.1407
REMARK 3 8 1.7638 - 1.6870 1.00 2334 144 0.0936 0.1357
REMARK 3 9 1.6870 - 1.6221 1.00 2341 143 0.0892 0.1306
REMARK 3 10 1.6221 - 1.5661 1.00 2292 141 0.0852 0.1252
REMARK 3 11 1.5661 - 1.5172 1.00 2330 143 0.0905 0.1235
REMARK 3 12 1.5172 - 1.4738 1.00 2309 142 0.0923 0.1736
REMARK 3 13 1.4738 - 1.4350 1.00 2305 142 0.0976 0.1286
REMARK 3 14 1.4350 - 1.4000 1.00 2299 141 0.0945 0.1351
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 : 0.40
REMARK 3 B_SOL : 60.00
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.050
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 10.810
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) : -0.37090
REMARK 3 B22 (A**2) : -0.38280
REMARK 3 B33 (A**2) : 0.84650
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.009 1423
REMARK 3 ANGLE : 1.229 1936
REMARK 3 CHIRALITY : 0.070 215
REMARK 3 PLANARITY : 0.006 254
REMARK 3 DIHEDRAL : 12.133 517
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 5CT9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000212153.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-DEC-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9999
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34601
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 28.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 13.20
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.80
REMARK 200 R MERGE FOR SHELL (I) : 0.11900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 17.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35 % PEG 3350, 20 MM NASO4, 0.1M
REMARK 280 ETHANOLAMINE, 10MM ZNCL2, PH 9.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
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 24.07000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 32.20500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.95000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 32.20500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.07000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.95000
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: 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 GLU A 2
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 HZ1 LYS A 35 O HOH A 309 1.53
REMARK 500 O HOH A 436 O HOH A 462 1.89
REMARK 500 O HOH A 483 O HOH A 527 1.89
REMARK 500 OE1 GLU A 57 O HOH A 301 1.93
REMARK 500 OE1 GLU A 171 O HOH A 302 1.94
REMARK 500 O HOH A 376 O HOH A 442 2.01
REMARK 500 O HOH A 310 O HOH A 417 2.02
REMARK 500 N HIS A 3 O HOH A 303 2.10
REMARK 500 O HOH A 349 O HOH A 526 2.12
REMARK 500 O HOH A 548 O HOH A 549 2.15
REMARK 500 O HOH A 417 O HOH A 461 2.16
REMARK 500 OE1 GLU A 171 O HOH A 304 2.17
REMARK 500 O HOH A 494 O HOH A 542 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 107 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
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 SER A 77 -123.80 52.53
REMARK 500 SER A 77 -127.25 58.09
REMARK 500 LEU A 90 -143.95 -109.41
REMARK 500 TYR A 161 55.47 -140.22
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 547 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH A 548 DISTANCE = 7.04 ANGSTROMS
REMARK 525 HOH A 549 DISTANCE = 7.33 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BM0 A 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5CRI RELATED DB: PDB
REMARK 900 RELATED ID: 5CT4 RELATED DB: PDB
REMARK 900 RELATED ID: 5CT5 RELATED DB: PDB
REMARK 900 RELATED ID: 5CT6 RELATED DB: PDB
REMARK 900 RELATED ID: 5CT8 RELATED DB: PDB
REMARK 900 RELATED ID: 5CTA RELATED DB: PDB
DBREF 5CT9 A 2 181 UNP I6V559 I6V559_BACIU 33 212
SEQADV 5CT9 GLU A 44 UNP I6V559 LYS 75 ENGINEERED MUTATION
SEQADV 5CT9 GLU A 49 UNP I6V559 TYR 80 ENGINEERED MUTATION
SEQADV 5CT9 GLU A 57 UNP I6V559 ARG 88 ENGINEERED MUTATION
SEQADV 5CT9 GLU A 158 UNP I6V559 GLY 189 ENGINEERED MUTATION
SEQRES 1 A 180 GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY GLY
SEQRES 2 A 180 ALA SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU VAL
SEQRES 3 A 180 SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL ASP
SEQRES 4 A 180 PHE TRP ASP GLU THR GLY THR ASN GLU ASN ASN GLY PRO
SEQRES 5 A 180 VAL LEU SER GLU PHE VAL GLN LYS VAL LEU ASP GLU THR
SEQRES 6 A 180 GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET GLY
SEQRES 7 A 180 GLY ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP GLY
SEQRES 8 A 180 GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY ALA
SEQRES 9 A 180 ASN ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR ASP
SEQRES 10 A 180 PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER SER
SEQRES 11 A 180 ALA ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU ASP
SEQRES 12 A 180 GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS ILE
SEQRES 13 A 180 GLU LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE LYS
SEQRES 14 A 180 GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
HET CL A 201 1
HET BM0 A 202 25
HETNAM CL CHLORIDE ION
HETNAM BM0 1-BUTYL-3-METHYL-1H-IMIDAZOL-3-IUM
HETSYN BM0 1-BUTYL-3-METHYLIMIDAZOLIUM
FORMUL 2 CL CL 1-
FORMUL 3 BM0 C8 H15 N2 1+
FORMUL 4 HOH *249(H2 O)
HELIX 1 AA1 ALA A 15 ASN A 18 5 4
HELIX 2 AA2 PHE A 19 GLN A 29 1 11
HELIX 3 AA3 SER A 32 ASP A 34 5 3
HELIX 4 AA4 THR A 47 GLY A 67 1 21
HELIX 5 AA5 MET A 78 LEU A 90 1 13
HELIX 6 AA6 ASP A 91 ASN A 94 5 4
HELIX 7 AA7 ALA A 105 THR A 109 5 5
HELIX 8 AA8 MET A 137 ARG A 142 1 6
HELIX 9 AA9 ILE A 157 TYR A 161 5 5
HELIX 10 AB1 SER A 162 ASN A 174 1 13
SHEET 1 AA1 6 LEU A 36 ALA A 38 0
SHEET 2 AA1 6 VAL A 6 VAL A 9 1 N VAL A 6 O TYR A 37
SHEET 3 AA1 6 VAL A 71 HIS A 76 1 O ASP A 72 N VAL A 7
SHEET 4 AA1 6 VAL A 96 LEU A 102 1 O VAL A 100 N ILE A 73
SHEET 5 AA1 6 LEU A 124 SER A 130 1 O ILE A 128 N THR A 101
SHEET 6 AA1 6 ARG A 147 ILE A 151 1 O VAL A 149 N SER A 127
SITE 1 AC1 2 MET A 134 HIS A 156
SITE 1 AC2 5 ASP A 34 LEU A 36 TYR A 37 ASN A 120
SITE 2 AC2 5 GLN A 121
CRYST1 48.140 55.900 64.410 90.00 90.00 90.00 P 21 21 21 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 0.020773 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017889 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015526 0.00000
TER 2750 ASN A 181
MASTER 303 0 2 10 6 0 3 6 1611 1 25 14
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