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HEADER HYDROLASE 29-DEC-18 6J1P
TITLE CRYSTAL STRUCTURE OF CANDIDA ANTARCTICA LIPASE B MUTANT - SR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE B;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CALB;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOZYMA ANTARCTICA;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 84753;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS CALB, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.X.CEN,J.H.ZHOU,Q.WU
REVDAT 1 01-JAN-20 6J1P 0
JRNL AUTH J.XU,Y.CEN,W.SINGH,J.FAN,L.WU,X.LIN,J.ZHOU,M.HUANG,
JRNL AUTH 2 M.T.REETZ,Q.WU
JRNL TITL STEREODIVERGENT PROTEIN ENGINEERING OF A LIPASE TO ACCESS
JRNL TITL 2 ALL POSSIBLE STEREOISOMERS OF CHIRAL ESTERS WITH TWO
JRNL TITL 3 STEREOCENTERS.
JRNL REF J.AM.CHEM.SOC. V. 141 7934 2019
JRNL REFN ESSN 1520-5126
JRNL PMID 31023008
JRNL DOI 10.1021/JACS.9B02709
REMARK 2
REMARK 2 RESOLUTION. 1.76 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 1.76
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 3 NUMBER OF REFLECTIONS : 49330
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2517
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 36.8235 - 4.6080 1.00 2831 153 0.1521 0.1434
REMARK 3 2 4.6080 - 3.6586 1.00 2787 147 0.1362 0.1604
REMARK 3 3 3.6586 - 3.1964 1.00 2768 163 0.1630 0.1745
REMARK 3 4 3.1964 - 2.9043 1.00 2754 149 0.1830 0.2154
REMARK 3 5 2.9043 - 2.6962 1.00 2773 155 0.1886 0.2483
REMARK 3 6 2.6962 - 2.5373 1.00 2779 147 0.1876 0.2147
REMARK 3 7 2.5373 - 2.4102 1.00 2753 134 0.1879 0.2342
REMARK 3 8 2.4102 - 2.3053 1.00 2758 133 0.1919 0.2352
REMARK 3 9 2.3053 - 2.2166 1.00 2764 146 0.1900 0.2448
REMARK 3 10 2.2166 - 2.1401 1.00 2782 144 0.1960 0.2330
REMARK 3 11 2.1401 - 2.0732 1.00 2740 154 0.2045 0.2540
REMARK 3 12 2.0732 - 2.0139 0.98 2671 158 0.2074 0.2317
REMARK 3 13 2.0139 - 1.9609 0.96 2664 120 0.2199 0.2430
REMARK 3 14 1.9609 - 1.9131 0.93 2574 140 0.2202 0.2372
REMARK 3 15 1.9131 - 1.8696 0.88 2395 136 0.2187 0.2675
REMARK 3 16 1.8696 - 1.8298 0.83 2276 130 0.2305 0.2808
REMARK 3 17 1.8298 - 1.7932 0.73 2021 104 0.2471 0.2679
REMARK 3 18 1.7932 - 1.7594 0.63 1723 104 0.2648 0.3437
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.040
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 : 0.004 4921
REMARK 3 ANGLE : 0.824 6726
REMARK 3 CHIRALITY : 0.047 770
REMARK 3 PLANARITY : 0.007 871
REMARK 3 DIHEDRAL : 13.450 2926
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 76.0672 -2.9662 33.0967
REMARK 3 T TENSOR
REMARK 3 T11: 0.1293 T22: 0.1379
REMARK 3 T33: 0.1626 T12: 0.0251
REMARK 3 T13: 0.0191 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.5649 L22: 0.7207
REMARK 3 L33: 1.4834 L12: 0.6989
REMARK 3 L13: 0.8237 L23: 0.8761
REMARK 3 S TENSOR
REMARK 3 S11: 0.1657 S12: -0.0655 S13: -0.1179
REMARK 3 S21: 0.1463 S22: 0.0342 S23: -0.1335
REMARK 3 S31: 0.1703 S32: -0.0679 S33: -0.1358
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 6J1P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1300010232.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JAN-18
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 : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97854
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52265
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.759
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 24.0620
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.83400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 1TCA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE 32% PEG 4000
REMARK 280 0.1 M SODIUM ACETATE PH 5.6, VAPOR DIFFUSION, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 40.00650
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 GLY A -3
REMARK 465 ALA A -2
REMARK 465 MET A -1
REMARK 465 GLY B -3
REMARK 465 ALA B -2
REMARK 465 MET B -1
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 29 86.17 -155.99
REMARK 500 ASN A 51 -90.98 -147.47
REMARK 500 ASP A 75 119.34 -28.32
REMARK 500 SER A 105 -126.24 55.84
REMARK 500 ASP A 134 67.68 -109.90
REMARK 500 ALA A 146 -3.02 64.83
REMARK 500 LEU A 147 139.04 -172.00
REMARK 500 LEU A 278 -42.34 126.69
REMARK 500 VAL A 282 -40.53 -131.17
REMARK 500 THR A 310 -167.32 -127.52
REMARK 500 ASN B 51 -90.75 -147.07
REMARK 500 ASP B 75 119.14 -29.90
REMARK 500 SER B 105 -127.93 58.85
REMARK 500 ASP B 134 67.73 -110.73
REMARK 500 ALA B 276 48.73 -101.81
REMARK 500 LEU B 278 15.88 104.88
REMARK 500 THR B 310 -167.54 -121.38
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
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 419
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 417
DBREF 6J1P A 1 317 UNP P41365 LIPB_PSEA2 26 342
DBREF 6J1P B 1 317 UNP P41365 LIPB_PSEA2 26 342
SEQADV 6J1P GLY A -3 UNP P41365 EXPRESSION TAG
SEQADV 6J1P ALA A -2 UNP P41365 EXPRESSION TAG
SEQADV 6J1P MET A -1 UNP P41365 EXPRESSION TAG
SEQADV 6J1P ALA A 0 UNP P41365 EXPRESSION TAG
SEQADV 6J1P ALA A 57 UNP P41365 THR 82 ENGINEERED MUTATION
SEQADV 6J1P THR A 89 UNP P41365 ALA 114 ENGINEERED MUTATION
SEQADV 6J1P CYS A 190 UNP P41365 VAL 215 ENGINEERED MUTATION
SEQADV 6J1P GLY A 281 UNP P41365 ALA 306 ENGINEERED MUTATION
SEQADV 6J1P VAL A 282 UNP P41365 ALA 307 ENGINEERED MUTATION
SEQADV 6J1P GLY B -3 UNP P41365 EXPRESSION TAG
SEQADV 6J1P ALA B -2 UNP P41365 EXPRESSION TAG
SEQADV 6J1P MET B -1 UNP P41365 EXPRESSION TAG
SEQADV 6J1P ALA B 0 UNP P41365 EXPRESSION TAG
SEQADV 6J1P ALA B 57 UNP P41365 THR 82 ENGINEERED MUTATION
SEQADV 6J1P THR B 89 UNP P41365 ALA 114 ENGINEERED MUTATION
SEQADV 6J1P CYS B 190 UNP P41365 VAL 215 ENGINEERED MUTATION
SEQADV 6J1P GLY B 281 UNP P41365 ALA 306 ENGINEERED MUTATION
SEQADV 6J1P VAL B 282 UNP P41365 ALA 307 ENGINEERED MUTATION
SEQRES 1 A 321 GLY ALA MET ALA LEU PRO SER GLY SER ASP PRO ALA PHE
SEQRES 2 A 321 SER GLN PRO LYS SER VAL LEU ASP ALA GLY LEU THR CYS
SEQRES 3 A 321 GLN GLY ALA SER PRO SER SER VAL SER LYS PRO ILE LEU
SEQRES 4 A 321 LEU VAL PRO GLY THR GLY THR THR GLY PRO GLN SER PHE
SEQRES 5 A 321 ASP SER ASN TRP ILE PRO LEU SER ALA GLN LEU GLY TYR
SEQRES 6 A 321 THR PRO CYS TRP ILE SER PRO PRO PRO PHE MET LEU ASN
SEQRES 7 A 321 ASP THR GLN VAL ASN THR GLU TYR MET VAL ASN ALA ILE
SEQRES 8 A 321 THR THR LEU TYR ALA GLY SER GLY ASN ASN LYS LEU PRO
SEQRES 9 A 321 VAL LEU THR TRP SER GLN GLY GLY LEU VAL ALA GLN TRP
SEQRES 10 A 321 GLY LEU THR PHE PHE PRO SER ILE ARG SER LYS VAL ASP
SEQRES 11 A 321 ARG LEU MET ALA PHE ALA PRO ASP TYR LYS GLY THR VAL
SEQRES 12 A 321 LEU ALA GLY PRO LEU ASP ALA LEU ALA VAL SER ALA PRO
SEQRES 13 A 321 SER VAL TRP GLN GLN THR THR GLY SER ALA LEU THR THR
SEQRES 14 A 321 ALA LEU ARG ASN ALA GLY GLY LEU THR GLN ILE VAL PRO
SEQRES 15 A 321 THR THR ASN LEU TYR SER ALA THR ASP GLU ILE CYS GLN
SEQRES 16 A 321 PRO GLN VAL SER ASN SER PRO LEU ASP SER SER TYR LEU
SEQRES 17 A 321 PHE ASN GLY LYS ASN VAL GLN ALA GLN ALA VAL CYS GLY
SEQRES 18 A 321 PRO LEU PHE VAL ILE ASP HIS ALA GLY SER LEU THR SER
SEQRES 19 A 321 GLN PHE SER TYR VAL VAL GLY ARG SER ALA LEU ARG SER
SEQRES 20 A 321 THR THR GLY GLN ALA ARG SER ALA ASP TYR GLY ILE THR
SEQRES 21 A 321 ASP CYS ASN PRO LEU PRO ALA ASN ASP LEU THR PRO GLU
SEQRES 22 A 321 GLN LYS VAL ALA ALA ALA ALA LEU LEU ALA PRO GLY VAL
SEQRES 23 A 321 ALA ALA ILE VAL ALA GLY PRO LYS GLN ASN CYS GLU PRO
SEQRES 24 A 321 ASP LEU MET PRO TYR ALA ARG PRO PHE ALA VAL GLY LYS
SEQRES 25 A 321 ARG THR CYS SER GLY ILE VAL THR PRO
SEQRES 1 B 321 GLY ALA MET ALA LEU PRO SER GLY SER ASP PRO ALA PHE
SEQRES 2 B 321 SER GLN PRO LYS SER VAL LEU ASP ALA GLY LEU THR CYS
SEQRES 3 B 321 GLN GLY ALA SER PRO SER SER VAL SER LYS PRO ILE LEU
SEQRES 4 B 321 LEU VAL PRO GLY THR GLY THR THR GLY PRO GLN SER PHE
SEQRES 5 B 321 ASP SER ASN TRP ILE PRO LEU SER ALA GLN LEU GLY TYR
SEQRES 6 B 321 THR PRO CYS TRP ILE SER PRO PRO PRO PHE MET LEU ASN
SEQRES 7 B 321 ASP THR GLN VAL ASN THR GLU TYR MET VAL ASN ALA ILE
SEQRES 8 B 321 THR THR LEU TYR ALA GLY SER GLY ASN ASN LYS LEU PRO
SEQRES 9 B 321 VAL LEU THR TRP SER GLN GLY GLY LEU VAL ALA GLN TRP
SEQRES 10 B 321 GLY LEU THR PHE PHE PRO SER ILE ARG SER LYS VAL ASP
SEQRES 11 B 321 ARG LEU MET ALA PHE ALA PRO ASP TYR LYS GLY THR VAL
SEQRES 12 B 321 LEU ALA GLY PRO LEU ASP ALA LEU ALA VAL SER ALA PRO
SEQRES 13 B 321 SER VAL TRP GLN GLN THR THR GLY SER ALA LEU THR THR
SEQRES 14 B 321 ALA LEU ARG ASN ALA GLY GLY LEU THR GLN ILE VAL PRO
SEQRES 15 B 321 THR THR ASN LEU TYR SER ALA THR ASP GLU ILE CYS GLN
SEQRES 16 B 321 PRO GLN VAL SER ASN SER PRO LEU ASP SER SER TYR LEU
SEQRES 17 B 321 PHE ASN GLY LYS ASN VAL GLN ALA GLN ALA VAL CYS GLY
SEQRES 18 B 321 PRO LEU PHE VAL ILE ASP HIS ALA GLY SER LEU THR SER
SEQRES 19 B 321 GLN PHE SER TYR VAL VAL GLY ARG SER ALA LEU ARG SER
SEQRES 20 B 321 THR THR GLY GLN ALA ARG SER ALA ASP TYR GLY ILE THR
SEQRES 21 B 321 ASP CYS ASN PRO LEU PRO ALA ASN ASP LEU THR PRO GLU
SEQRES 22 B 321 GLN LYS VAL ALA ALA ALA ALA LEU LEU ALA PRO GLY VAL
SEQRES 23 B 321 ALA ALA ILE VAL ALA GLY PRO LYS GLN ASN CYS GLU PRO
SEQRES 24 B 321 ASP LEU MET PRO TYR ALA ARG PRO PHE ALA VAL GLY LYS
SEQRES 25 B 321 ARG THR CYS SER GLY ILE VAL THR PRO
HET SO4 A 401 5
HET SO4 A 402 5
HET SO4 A 403 5
HET SO4 A 404 5
HET SO4 A 405 5
HET SO4 A 406 5
HET EDO A 407 4
HET EDO A 408 4
HET EDO A 409 4
HET EDO A 410 4
HET EDO A 411 4
HET EDO A 412 4
HET ACT A 413 4
HET CL A 414 1
HET CL A 415 1
HET CL A 416 1
HET CL A 417 1
HET CL A 418 1
HET CL A 419 1
HET SO4 B 401 5
HET SO4 B 402 5
HET SO4 B 403 5
HET SO4 B 404 5
HET EDO B 405 8
HET EDO B 406 4
HET EDO B 407 4
HET EDO B 408 4
HET EDO B 409 4
HET EDO B 410 4
HET EDO B 411 4
HET EDO B 412 4
HET EDO B 413 4
HET EDO B 414 4
HET CL B 415 1
HET CL B 416 1
HET PGE B 417 10
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM ACT ACETATE ION
HETNAM CL CHLORIDE ION
HETNAM PGE TRIETHYLENE GLYCOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 SO4 10(O4 S 2-)
FORMUL 9 EDO 16(C2 H6 O2)
FORMUL 15 ACT C2 H3 O2 1-
FORMUL 16 CL 8(CL 1-)
FORMUL 38 PGE C6 H14 O4
FORMUL 39 HOH *333(H2 O)
HELIX 1 AA1 PRO A 12 GLY A 19 1 8
HELIX 2 AA2 THR A 43 ASP A 49 1 7
HELIX 3 AA3 ASN A 51 LEU A 59 1 9
HELIX 4 AA4 ASP A 75 SER A 94 1 20
HELIX 5 AA5 SER A 105 PHE A 118 1 14
HELIX 6 AA6 PRO A 119 ARG A 122 5 4
HELIX 7 AA7 ALA A 151 GLN A 157 1 7
HELIX 8 AA8 SER A 161 ALA A 170 1 10
HELIX 9 AA9 ALA A 212 GLY A 217 1 6
HELIX 10 AB1 ALA A 225 SER A 230 1 6
HELIX 11 AB2 SER A 230 SER A 243 1 14
HELIX 12 AB3 ARG A 249 TYR A 253 5 5
HELIX 13 AB4 GLY A 254 CYS A 258 5 5
HELIX 14 AB5 THR A 267 ALA A 276 1 10
HELIX 15 AB6 ALA A 279 GLY A 288 1 10
HELIX 16 AB7 ALA A 301 VAL A 306 5 6
HELIX 17 AB8 PRO B 12 GLY B 19 1 8
HELIX 18 AB9 THR B 43 ASP B 49 1 7
HELIX 19 AC1 ASN B 51 LEU B 59 1 9
HELIX 20 AC2 ASP B 75 SER B 94 1 20
HELIX 21 AC3 SER B 105 PHE B 118 1 14
HELIX 22 AC4 PRO B 119 SER B 123 5 5
HELIX 23 AC5 PRO B 143 LEU B 147 5 5
HELIX 24 AC6 ALA B 151 GLN B 157 1 7
HELIX 25 AC7 SER B 161 ALA B 170 1 10
HELIX 26 AC8 ALA B 212 CYS B 216 1 5
HELIX 27 AC9 ALA B 225 SER B 230 1 6
HELIX 28 AD1 SER B 230 SER B 243 1 14
HELIX 29 AD2 ARG B 249 TYR B 253 5 5
HELIX 30 AD3 GLY B 254 CYS B 258 5 5
HELIX 31 AD4 THR B 267 ALA B 276 1 10
HELIX 32 AD5 ALA B 279 GLY B 288 1 10
HELIX 33 AD6 ALA B 301 VAL B 306 5 6
SHEET 1 AA1 7 LEU A 20 CYS A 22 0
SHEET 2 AA1 7 THR A 62 ILE A 66 -1 O TRP A 65 N THR A 21
SHEET 3 AA1 7 PRO A 33 VAL A 37 1 N LEU A 36 O CYS A 64
SHEET 4 AA1 7 LEU A 99 TRP A 104 1 O LEU A 102 N LEU A 35
SHEET 5 AA1 7 VAL A 125 PHE A 131 1 O MET A 129 N VAL A 101
SHEET 6 AA1 7 THR A 179 TYR A 183 1 O THR A 180 N ALA A 130
SHEET 7 AA1 7 LYS A 208 GLN A 211 1 O VAL A 210 N ASN A 181
SHEET 1 AA2 2 ARG A 309 THR A 310 0
SHEET 2 AA2 2 GLY A 313 ILE A 314 -1 O GLY A 313 N THR A 310
SHEET 1 AA3 7 LEU B 20 CYS B 22 0
SHEET 2 AA3 7 THR B 62 ILE B 66 -1 O TRP B 65 N THR B 21
SHEET 3 AA3 7 PRO B 33 VAL B 37 1 N LEU B 36 O CYS B 64
SHEET 4 AA3 7 LEU B 99 TRP B 104 1 O LEU B 102 N LEU B 35
SHEET 5 AA3 7 VAL B 125 PHE B 131 1 O MET B 129 N VAL B 101
SHEET 6 AA3 7 THR B 179 TYR B 183 1 O THR B 180 N ALA B 130
SHEET 7 AA3 7 LYS B 208 GLN B 211 1 O VAL B 210 N ASN B 181
SHEET 1 AA4 2 ARG B 309 THR B 310 0
SHEET 2 AA4 2 GLY B 313 ILE B 314 -1 O GLY B 313 N THR B 310
SSBOND 1 CYS A 22 CYS A 64 1555 1555 2.05
SSBOND 2 CYS A 216 CYS A 258 1555 1555 2.03
SSBOND 3 CYS A 293 CYS A 311 1555 1555 2.03
SSBOND 4 CYS B 22 CYS B 64 1555 1555 2.04
SSBOND 5 CYS B 216 CYS B 258 1555 1555 1.93
SSBOND 6 CYS B 293 CYS B 311 1555 1555 2.04
CISPEP 1 PRO A 69 PRO A 70 0 -11.63
CISPEP 2 GLN A 191 PRO A 192 0 3.69
CISPEP 3 PRO B 69 PRO B 70 0 -10.12
CISPEP 4 GLN B 191 PRO B 192 0 4.79
SITE 1 AC1 4 LYS A 208 ARG A 249 SER A 250 HOH A 501
SITE 1 AC2 4 SER A 26 PRO A 27 HOH A 591 SER B 123
SITE 1 AC3 1 ARG A 168
SITE 1 AC4 5 ARG A 302 ILE A 314 VAL A 315 THR A 316
SITE 2 AC4 5 HOH A 569
SITE 1 AC5 4 VAL A 30 GLY A 93 HOH A 534 HOH A 544
SITE 1 AC6 1 PRO A 299
SITE 1 AC7 6 THR A 43 SER A 67 PRO A 69 PRO A 70
SITE 2 AC7 6 PHE A 71 HOH A 512
SITE 1 AC8 7 TYR A 203 GLY A 207 LYS A 208 ASN A 209
SITE 2 AC8 7 ACT A 413 HOH A 503 HOH A 592
SITE 1 AC9 4 PRO A 12 LYS A 13 SER A 14 CL A 417
SITE 1 AD1 3 ASP A 49 TRP A 65 HOH A 502
SITE 1 AD2 3 LEU A 144 ALA A 148 ASN A 292
SITE 1 AD3 3 ALA A 214 VAL A 215 GLY A 217
SITE 1 AD4 4 ASN A 206 GLY A 207 GLN A 247 EDO A 408
SITE 1 AD5 3 PRO A 45 SER A 67 HOH A 640
SITE 1 AD6 2 GLU A 294 ARG A 309
SITE 1 AD7 2 ARG A 238 HOH A 533
SITE 1 AD8 3 PRO A 12 LYS A 13 EDO A 409
SITE 1 AD9 1 GLY A 24
SITE 1 AE1 5 ASN B 206 GLY B 207 LYS B 208 GLN B 247
SITE 2 AE1 5 EDO B 406
SITE 1 AE2 5 LYS B 208 ARG B 249 SER B 250 HOH B 503
SITE 2 AE2 5 HOH B 582
SITE 1 AE3 6 ASN B 292 CYS B 293 GLU B 294 ARG B 309
SITE 2 AE3 6 THR B 310 PGE B 417
SITE 1 AE4 4 GLN B 11 VAL B 15 PRO B 69 TYR B 82
SITE 1 AE5 7 ARG B 302 THR B 310 SER B 312 GLY B 313
SITE 2 AE5 7 ILE B 314 VAL B 315 HOH B 550
SITE 1 AE6 8 LYS A 124 THR B 245 GLN B 247 ARG B 249
SITE 2 AE6 8 SO4 B 401 HOH B 503 HOH B 508 HOH B 518
SITE 1 AE7 5 ASP B 296 LEU B 297 MET B 298 HOH B 526
SITE 2 AE7 5 HOH B 590
SITE 1 AE8 7 LYS B 32 PRO B 33 SER B 94 ASN B 97
SITE 2 AE8 7 LYS B 98 LEU B 99 PRO B 100
SITE 1 AE9 5 THR B 43 SER B 67 PRO B 69 PHE B 71
SITE 2 AE9 5 HOH B 510
SITE 1 AF1 7 THR B 165 ASN B 169 PHE B 304 ALA B 305
SITE 2 AF1 7 VAL B 306 LYS B 308 HOH B 573
SITE 1 AF2 4 THR B 40 SER B 105 ASP B 134 GLN B 157
SITE 1 AF3 3 ILE B 222 ASP B 223 PRO B 260
SITE 1 AF4 3 PRO B 54 ASP B 265 GLN B 270
SITE 1 AF5 3 GLN A 175 ILE A 176 ALA B 92
SITE 1 AF6 3 TYR B 203 ASN B 206 HOH B 607
SITE 1 AF7 5 ASN B 292 ARG B 309 CYS B 311 GLY B 313
SITE 2 AF7 5 SO4 B 403
CRYST1 46.403 80.013 72.968 90.00 97.96 90.00 P 1 21 1 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 0.021550 0.000000 0.003013 0.00000
SCALE2 0.000000 0.012498 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013838 0.00000
TER 2338 PRO A 317
TER 4687 PRO B 317
MASTER 402 0 36 33 18 0 47 6 5127 2 144 50
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