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HEADER HYDROLASE 06-JUN-18 6A12
TITLE X-RAY STRUCTURE OF LIPASE FROM GEOBACILLUS THERMOLEOVORANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: THERMOSTABLE LIPASE;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS THERMOLEOVORANS;
SOURCE 3 ORGANISM_COMMON: BACILLUS THERMOLEOVORANS;
SOURCE 4 ORGANISM_TAXID: 33941;
SOURCE 5 GENE: LIPA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS LIPASE, GEOBACILLUS THERMOLEOVORANS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.R.MOHARANA,B.PAL,N.M.RAO
REVDAT 1 20-JUN-18 6A12 0
JRNL AUTH T.R.MOHARANA,B.PAL,N.M.RAO
JRNL TITL X-RAY STRUCTURE OF LIPASE FROM GEOBACILLUS THERMOLEOVORANS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.03
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 22456
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1100
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 45.0353 - 4.2879 1.00 2879 128 0.1492 0.1983
REMARK 3 2 4.2879 - 3.4038 1.00 2710 145 0.1473 0.1851
REMARK 3 3 3.4038 - 2.9737 1.00 2691 143 0.1850 0.2356
REMARK 3 4 2.9737 - 2.7018 1.00 2666 145 0.1958 0.2270
REMARK 3 5 2.7018 - 2.5082 1.00 2652 132 0.1889 0.2304
REMARK 3 6 2.5082 - 2.3603 1.00 2650 141 0.1907 0.2401
REMARK 3 7 2.3603 - 2.2421 0.99 2614 129 0.1821 0.2612
REMARK 3 8 2.2421 - 2.1445 0.94 2494 137 0.1952 0.2667
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.000
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 : 0.008 3127
REMARK 3 ANGLE : 1.006 4252
REMARK 3 CHIRALITY : 0.041 443
REMARK 3 PLANARITY : 0.005 559
REMARK 3 DIHEDRAL : 13.131 1112
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 6A12 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JUN-18.
REMARK 100 THE DEPOSITION ID IS D_1300007899.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22506
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.130
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 (%) : 97.3
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.13
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 47.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.29700
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: MOLREP
REMARK 200 STARTING MODEL: 1KU0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CACODYLATE BUFFER, PH
REMARK 280 6.83, 0.4M MAGNESIUM ACETATE, 15% PEG 8000, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 293K
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 24.57000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.20250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.14550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.20250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.57000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.14550
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 90 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 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 ALA A 1
REMARK 465 THR A 2
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 113 -137.49 56.55
REMARK 500 HIS A 153 72.01 -112.93
REMARK 500 ASP A 175 43.58 -106.81
REMARK 500 ILE A 203 -61.96 70.31
REMARK 500 LEU A 208 41.67 -95.64
REMARK 500 ARG A 271 46.52 -140.43
REMARK 500 ALA A 276 -71.80 -73.82
REMARK 500 ASP A 310 -159.53 -120.68
REMARK 500 ILE A 319 -43.10 -137.63
REMARK 500 LYS A 329 -43.13 -135.47
REMARK 500 ASN A 367 89.65 -161.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 61 OD1
REMARK 620 2 ASP A 61 OD2 52.9
REMARK 620 3 HIS A 81 NE2 95.2 148.1
REMARK 620 4 HIS A 87 NE2 114.9 91.0 103.9
REMARK 620 5 ASP A 238 OD2 133.1 97.3 107.9 98.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 286 O
REMARK 620 2 GLU A 360 OE2 83.4
REMARK 620 3 ASP A 365 OD2 102.4 109.0
REMARK 620 4 PRO A 366 O 169.1 89.4 87.7
REMARK 620 5 HOH A 610 O 84.5 89.3 160.9 87.2
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 402
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 386 LEU AND 387 ARG ARE FROM VARIANT OF GEOBACILLUS
REMARK 999 THERMOLEOVORANS.
DBREF 6A12 A 1 388 UNP Q8L1V2 Q8L1V2_GEOTH 29 416
SEQADV 6A12 MET A 0 UNP Q8L1V2 INITIATING METHIONINE
SEQADV 6A12 LEU A 386 UNP Q8L1V2 PHE 414 SEE SEQUENCE DETAILS
SEQADV 6A12 ARG A 387 UNP Q8L1V2 GLY 415 SEE SEQUENCE DETAILS
SEQRES 1 A 389 MET ALA THR SER ARG ALA ASN ASP ALA PRO ILE VAL LEU
SEQRES 2 A 389 LEU HIS GLY PHE THR GLY TRP GLY ARG GLU GLU MET PHE
SEQRES 3 A 389 GLY PHE LYS TYR TRP GLY GLY VAL ARG GLY ASP ILE GLU
SEQRES 4 A 389 GLN TRP LEU ASN ASP ASN GLY TYR ARG THR TYR THR LEU
SEQRES 5 A 389 ALA VAL GLY PRO LEU SER SER ASN TRP ASP ARG ALA CYS
SEQRES 6 A 389 GLU ALA TYR ALA GLN LEU VAL GLY GLY THR VAL ASP TYR
SEQRES 7 A 389 GLY ALA ALA HIS ALA ALA LYS HIS GLY HIS ALA ARG PHE
SEQRES 8 A 389 GLY ARG THR TYR PRO GLY LEU LEU PRO GLU LEU LYS ARG
SEQRES 9 A 389 GLY GLY ARG ILE HIS ILE ILE ALA HIS SER GLN GLY GLY
SEQRES 10 A 389 GLN THR ALA ARG MET LEU VAL SER LEU LEU GLU ASN GLY
SEQRES 11 A 389 SER GLN GLU GLU ARG GLU TYR ALA LYS ALA HIS ASN VAL
SEQRES 12 A 389 SER LEU SER PRO LEU PHE GLU GLY GLY HIS HIS PHE VAL
SEQRES 13 A 389 LEU SER VAL THR THR ILE ALA THR PRO HIS ASP GLY THR
SEQRES 14 A 389 THR LEU VAL ASN MET VAL ASP PHE THR ASP ARG PHE PHE
SEQRES 15 A 389 ASP LEU GLN LYS ALA VAL LEU GLU ALA ALA ALA VAL ALA
SEQRES 16 A 389 SER ASN ALA PRO TYR THR SER GLU ILE TYR ASP PHE LYS
SEQRES 17 A 389 LEU ASP GLN TRP GLY LEU ARG ARG GLU PRO GLY GLU SER
SEQRES 18 A 389 PHE ASP HIS TYR PHE GLU ARG LEU LYS ARG SER PRO VAL
SEQRES 19 A 389 TRP THR SER THR ASP THR ALA ARG TYR ASP LEU SER VAL
SEQRES 20 A 389 PRO GLY ALA GLU THR LEU ASN ARG TRP VAL LYS ALA SER
SEQRES 21 A 389 PRO ASN THR TYR TYR LEU SER PHE SER THR GLU ARG THR
SEQRES 22 A 389 TYR ARG GLY ALA LEU THR GLY ASN TYR TYR PRO GLU LEU
SEQRES 23 A 389 GLY MET ASN ALA PHE SER ALA ILE VAL CYS ALA PRO PHE
SEQRES 24 A 389 LEU GLY SER TYR ARG ASN ALA ALA LEU GLY ILE ASP SER
SEQRES 25 A 389 HIS TRP LEU GLU ASN ASP GLY ILE VAL ASN THR ILE SER
SEQRES 26 A 389 MET ASN GLY PRO LYS ARG GLY SER SER ASP ARG ILE VAL
SEQRES 27 A 389 PRO TYR ASP GLY ALA LEU LYS LYS GLY VAL TRP ASN ASP
SEQRES 28 A 389 MET GLY THR TYR ASN VAL ASP HIS LEU GLU ILE ILE GLY
SEQRES 29 A 389 VAL ASP PRO ASN PRO SER PHE ASP ILE ARG ALA PHE TYR
SEQRES 30 A 389 LEU ARG LEU ALA GLU GLN LEU ALA SER LEU ARG PRO
HET CA A 401 1
HET ZN A 402 1
HETNAM CA CALCIUM ION
HETNAM ZN ZINC ION
FORMUL 2 CA CA 2+
FORMUL 3 ZN ZN 2+
FORMUL 4 HOH *116(H2 O)
HELIX 1 AA1 GLU A 23 PHE A 27 5 5
HELIX 2 AA2 ASP A 36 ASN A 44 1 9
HELIX 3 AA3 SER A 58 GLY A 72 1 15
HELIX 4 AA4 GLY A 78 GLY A 86 1 9
HELIX 5 AA5 LEU A 98 LYS A 102 5 5
HELIX 6 AA6 GLN A 114 GLY A 129 1 16
HELIX 7 AA7 SER A 130 ASN A 141 1 12
HELIX 8 AA8 SER A 145 GLU A 149 5 5
HELIX 9 AA9 THR A 168 MET A 173 5 6
HELIX 10 AB1 ASP A 175 ALA A 191 1 17
HELIX 11 AB2 SER A 220 ARG A 230 1 11
HELIX 12 AB3 SER A 231 SER A 236 1 6
HELIX 13 AB4 THR A 239 SER A 245 1 7
HELIX 14 AB5 SER A 245 ARG A 254 1 10
HELIX 15 AB6 ASN A 288 CYS A 295 1 8
HELIX 16 AB7 CYS A 295 GLY A 300 1 6
HELIX 17 AB8 ASP A 310 LEU A 314 5 5
HELIX 18 AB9 ASN A 321 MET A 325 5 5
HELIX 19 AC1 ASP A 371 SER A 385 1 15
SHEET 1 AA1 7 THR A 48 LEU A 51 0
SHEET 2 AA1 7 ILE A 10 LEU A 13 1 N LEU A 12 O LEU A 51
SHEET 3 AA1 7 ILE A 107 HIS A 112 1 O HIS A 108 N VAL A 11
SHEET 4 AA1 7 VAL A 155 ILE A 161 1 O THR A 159 N ALA A 111
SHEET 5 AA1 7 TYR A 263 THR A 269 1 O TYR A 263 N LEU A 156
SHEET 6 AA1 7 TRP A 348 TYR A 354 1 O MET A 351 N SER A 266
SHEET 7 AA1 7 ILE A 336 PRO A 338 1 N VAL A 337 O TRP A 348
SHEET 1 AA2 2 GLY A 73 ASP A 76 0
SHEET 2 AA2 2 PHE A 90 TYR A 94 -1 O ARG A 92 N VAL A 75
SHEET 1 AA3 2 THR A 272 ARG A 274 0
SHEET 2 AA3 2 TYR A 281 PRO A 283 -1 O TYR A 282 N TYR A 273
LINK OD1 ASP A 61 ZN ZN A 402 1555 1555 2.18
LINK OD2 ASP A 61 ZN ZN A 402 1555 1555 2.64
LINK NE2 HIS A 81 ZN ZN A 402 1555 1555 2.12
LINK NE2 HIS A 87 ZN ZN A 402 1555 1555 2.29
LINK OD2 ASP A 238 ZN ZN A 402 1555 1555 2.09
LINK O GLY A 286 CA CA A 401 1555 1555 2.31
LINK OE2 GLU A 360 CA CA A 401 1555 1555 2.42
LINK OD2 ASP A 365 CA CA A 401 1555 1555 2.39
LINK O PRO A 366 CA CA A 401 1555 1555 2.36
LINK CA CA A 401 O HOH A 610 1555 1555 2.60
SITE 1 AC1 5 GLY A 286 GLU A 360 ASP A 365 PRO A 366
SITE 2 AC1 5 HOH A 610
SITE 1 AC2 4 ASP A 61 HIS A 81 HIS A 87 ASP A 238
CRYST1 49.140 72.291 112.405 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 0.020350 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013833 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008896 0.00000
TER 3043 PRO A 388
MASTER 275 0 2 19 11 0 3 6 3160 1 14 30
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