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HEADER HYDROLASE 09-DEC-14 4X7B
TITLE CRYSTAL STRUCTURE OF LIPASE FROM GEOBACILLUS STEAROTHERMOPHILUS T6
TITLE 2 METHANOL STABLE VARIANT H86Y/A269T
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 34-418;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS T6;
SOURCE 3 ORGANISM_TAXID: 646309;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET9A
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KANTEEV,A.DROR,S.GIHAZ,A.FISHMAN
REVDAT 1 10-JUN-15 4X7B 0
JRNL AUTH A.DROR,M.KANTEEV,I.KAGAN,S.GIHAZ,A.SHAHAR,A.FISHMAN
JRNL TITL STRUCTURAL INSIGHTS INTO METHANOL-STABLE VARIANTS OF LIPASE
JRNL TITL 2 T6 FROM GEOBACILLUS STEAROTHERMOPHILUS.
JRNL REF APPL.MICROBIOL.BIOTECHNOL. 2015
JRNL REFN ESSN 1432-0614
JRNL PMID 26026940
JRNL DOI 10.1007/S00253-015-6700-4
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 16078
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 811
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 30.2745 - 4.3575 0.93 2598 128 0.1751 0.1906
REMARK 3 2 4.3575 - 3.4603 0.94 2513 120 0.1672 0.1998
REMARK 3 3 3.4603 - 3.0233 0.98 2556 138 0.2121 0.2615
REMARK 3 4 3.0233 - 2.7471 0.98 2543 142 0.2378 0.2823
REMARK 3 5 2.7471 - 2.5503 0.99 2526 154 0.2512 0.3158
REMARK 3 6 2.5503 - 2.4000 0.99 2531 129 0.2669 0.3513
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 20.85
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.340
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.99
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.44110
REMARK 3 B22 (A**2) : -9.72660
REMARK 3 B33 (A**2) : 15.13750
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 : 0.005 3205
REMARK 3 ANGLE : 0.723 4366
REMARK 3 CHIRALITY : 0.051 451
REMARK 3 PLANARITY : 0.003 570
REMARK 3 DIHEDRAL : 11.109 1133
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 4X7B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1000205205.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-APR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.56
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16204
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 60.778
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07500
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) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.17800
REMARK 200 R SYM FOR SHELL (I) : 0.17800
REMARK 200 FOR SHELL : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.3.0
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM CITRATE, 25% PEG3350,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 24.90500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.18000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.87500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.18000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.90500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.87500
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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: 15560 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 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 114 -131.15 57.34
REMARK 500 HIS A 154 65.86 -116.68
REMARK 500 ASP A 176 40.85 -109.07
REMARK 500 LEU A 209 47.96 -95.26
REMARK 500 ARG A 272 43.71 -149.14
REMARK 500 ASP A 311 -163.13 -102.22
REMARK 500 LYS A 330 -45.77 -130.79
REMARK 500 ASP A 351 98.88 -68.94
REMARK 500 ASN A 368 89.58 -161.23
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 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 62 OD1
REMARK 620 2 ASP A 62 OD2 63.0
REMARK 620 3 HIS A 82 NE2 89.4 152.3
REMARK 620 4 HIS A 88 NE2 112.6 95.3 98.3
REMARK 620 5 ASP A 239 OD1 98.0 101.4 78.5 149.3
REMARK 620 6 ASP A 239 OD2 144.7 89.8 114.0 90.7 63.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 287 O
REMARK 620 2 GLU A 361 OE2 83.7
REMARK 620 3 ASP A 366 OD2 108.1 102.4
REMARK 620 4 PRO A 367 O 163.7 101.2 86.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4X6U RELATED DB: PDB
DBREF 4X7B A 5 389 UNP Q93A71 Q93A71_GEOSE 34 418
SEQADV 4X7B TYR A 86 UNP Q93A71 HIS 115 ENGINEERED MUTATION
SEQADV 4X7B THR A 269 UNP Q93A71 ALA 298 ENGINEERED MUTATION
SEQADV 4X7B ALA A 323 UNP Q93A71 THR 352 CONFLICT
SEQADV 4X7B HIS A 390 UNP Q93A71 EXPRESSION TAG
SEQADV 4X7B HIS A 391 UNP Q93A71 EXPRESSION TAG
SEQADV 4X7B HIS A 392 UNP Q93A71 EXPRESSION TAG
SEQADV 4X7B HIS A 393 UNP Q93A71 EXPRESSION TAG
SEQADV 4X7B HIS A 394 UNP Q93A71 EXPRESSION TAG
SEQADV 4X7B HIS A 395 UNP Q93A71 EXPRESSION TAG
SEQRES 1 A 391 ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU HIS GLY PHE
SEQRES 2 A 391 THR GLY TRP GLY ARG GLU GLU MET PHE GLY PHE LYS TYR
SEQRES 3 A 391 TRP GLY GLY VAL ARG GLY ASP ILE GLU GLN TRP LEU ASN
SEQRES 4 A 391 ASP ASN GLY TYR ARG THR TYR THR LEU ALA VAL GLY PRO
SEQRES 5 A 391 LEU SER SER ASN TRP ASP ARG ALA CYS GLU ALA TYR ALA
SEQRES 6 A 391 GLN LEU VAL GLY GLY THR VAL ASP TYR GLY ALA ALA HIS
SEQRES 7 A 391 ALA ALA LYS TYR GLY HIS ALA ARG PHE GLY ARG THR TYR
SEQRES 8 A 391 PRO GLY LEU LEU PRO GLU LEU LYS ARG GLY GLY ARG ILE
SEQRES 9 A 391 HIS ILE ILE ALA HIS SER GLN GLY GLY GLN THR ALA ARG
SEQRES 10 A 391 MET LEU VAL SER LEU LEU GLU ASN GLY SER GLN GLU GLU
SEQRES 11 A 391 ARG GLU TYR ALA LYS ALA HIS ASN VAL SER LEU SER PRO
SEQRES 12 A 391 LEU PHE GLU GLY GLY HIS HIS PHE VAL LEU SER VAL THR
SEQRES 13 A 391 THR ILE ALA THR PRO HIS ASP GLY THR THR LEU VAL ASN
SEQRES 14 A 391 MET VAL ASP PHE THR ASP ARG PHE PHE ASP LEU GLN LYS
SEQRES 15 A 391 ALA VAL LEU LYS ALA ALA ALA VAL ALA SER ASN VAL PRO
SEQRES 16 A 391 TYR THR SER GLN VAL TYR ASP PHE LYS LEU ASP GLN TRP
SEQRES 17 A 391 GLY LEU ARG ARG GLN PRO GLY GLU SER PHE ASP GLN TYR
SEQRES 18 A 391 PHE GLU ARG LEU LYS ARG SER PRO VAL TRP THR SER THR
SEQRES 19 A 391 ASP THR ALA ARG TYR ASP LEU SER VAL PRO GLY ALA GLU
SEQRES 20 A 391 LYS LEU ASN GLN TRP VAL LYS ALA SER PRO ASN THR TYR
SEQRES 21 A 391 TYR LEU SER PHE THR THR GLU ARG THR TYR ARG GLY ALA
SEQRES 22 A 391 LEU THR GLY ASN TYR TYR PRO GLU LEU GLY MET ASN ALA
SEQRES 23 A 391 PHE SER ALA VAL VAL CYS ALA PRO PHE LEU GLY SER TYR
SEQRES 24 A 391 ARG ASN ALA THR LEU GLY ILE ASP ASP ARG TRP LEU GLU
SEQRES 25 A 391 ASN ASP GLY ILE VAL ASN ALA PHE SER MET ASN GLY PRO
SEQRES 26 A 391 LYS ARG GLY SER THR ASP ARG ILE VAL PRO TYR ASP GLY
SEQRES 27 A 391 THR ILE LYS LYS GLY VAL TRP ASN ASP MET GLY THR TYR
SEQRES 28 A 391 ASN VAL ASP HIS LEU GLU VAL ILE GLY VAL ASP PRO ASN
SEQRES 29 A 391 PRO LEU PHE ASP ILE ARG ALA PHE TYR LEU ARG LEU ALA
SEQRES 30 A 391 GLU GLN LEU ALA SER LEU GLN PRO HIS HIS HIS HIS HIS
SEQRES 31 A 391 HIS
HET ZN A 401 1
HET CA A 402 1
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
FORMUL 2 ZN ZN 2+
FORMUL 3 CA CA 2+
FORMUL 4 HOH *176(H2 O)
HELIX 1 AA1 GLU A 24 PHE A 28 5 5
HELIX 2 AA2 ASP A 37 ASN A 45 1 9
HELIX 3 AA3 SER A 59 GLY A 73 1 15
HELIX 4 AA4 GLY A 79 GLY A 87 1 9
HELIX 5 AA5 LEU A 99 LYS A 103 5 5
HELIX 6 AA6 GLN A 115 GLY A 130 1 16
HELIX 7 AA7 SER A 131 ASN A 142 1 12
HELIX 8 AA8 SER A 146 GLU A 150 5 5
HELIX 9 AA9 THR A 169 MET A 174 5 6
HELIX 10 AB1 ASP A 176 ALA A 192 1 17
HELIX 11 AB2 SER A 221 ARG A 231 1 11
HELIX 12 AB3 SER A 232 SER A 237 1 6
HELIX 13 AB4 THR A 240 SER A 246 1 7
HELIX 14 AB5 SER A 246 GLN A 255 1 10
HELIX 15 AB6 ASN A 289 VAL A 295 1 7
HELIX 16 AB7 CYS A 296 GLY A 301 1 6
HELIX 17 AB8 ASN A 322 MET A 326 5 5
HELIX 18 AB9 ASP A 372 SER A 386 1 15
SHEET 1 AA1 7 THR A 49 LEU A 52 0
SHEET 2 AA1 7 ILE A 11 LEU A 14 1 N ILE A 11 O TYR A 50
SHEET 3 AA1 7 ILE A 108 HIS A 113 1 O HIS A 109 N VAL A 12
SHEET 4 AA1 7 VAL A 156 ILE A 162 1 O THR A 160 N ALA A 112
SHEET 5 AA1 7 TYR A 264 THR A 270 1 O LEU A 266 N THR A 161
SHEET 6 AA1 7 TRP A 349 TYR A 355 1 O TYR A 355 N THR A 269
SHEET 7 AA1 7 ILE A 337 PRO A 339 1 N VAL A 338 O ASP A 351
SHEET 1 AA2 2 GLY A 74 ASP A 77 0
SHEET 2 AA2 2 PHE A 91 TYR A 95 -1 O ARG A 93 N VAL A 76
SHEET 1 AA3 2 THR A 273 ARG A 275 0
SHEET 2 AA3 2 TYR A 282 PRO A 284 -1 O TYR A 283 N TYR A 274
LINK OD1 ASP A 62 ZN ZN A 401 1555 1555 2.04
LINK OD2 ASP A 62 ZN ZN A 401 1555 1555 2.09
LINK NE2 HIS A 82 ZN ZN A 401 1555 1555 2.04
LINK NE2 HIS A 88 ZN ZN A 401 1555 1555 2.10
LINK OD1 ASP A 239 ZN ZN A 401 1555 1555 2.12
LINK OD2 ASP A 239 ZN ZN A 401 1555 1555 1.99
LINK O GLY A 287 CA CA A 402 1555 1555 2.39
LINK OE2 GLU A 361 CA CA A 402 1555 1555 2.35
LINK OD2 ASP A 366 CA CA A 402 1555 1555 2.38
LINK O PRO A 367 CA CA A 402 1555 1555 2.35
SITE 1 AC1 4 ASP A 62 HIS A 82 HIS A 88 ASP A 239
SITE 1 AC2 4 GLY A 287 GLU A 361 ASP A 366 PRO A 367
CRYST1 49.810 71.750 114.360 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 0.020076 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013937 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008744 0.00000
TER 3106 HIS A 395
MASTER 260 0 2 18 11 0 2 6 3283 1 13 31
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