| content |
HEADER HYDROLASE 29-DEC-18 6J1Q
TITLE CRYSTAL STRUCTURE OF CANDIDA ANTARCTICA LIPASE B MUTANT - RS
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 6J1Q 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. 1.60 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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 68591
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.173
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 3456
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 46.1445 - 4.6767 0.99 2701 154 0.1562 0.1562
REMARK 3 2 4.6767 - 3.7126 1.00 2680 151 0.1227 0.1361
REMARK 3 3 3.7126 - 3.2434 1.00 2647 165 0.1363 0.1713
REMARK 3 4 3.2434 - 2.9469 1.00 2668 151 0.1526 0.1765
REMARK 3 5 2.9469 - 2.7357 1.00 2640 141 0.1521 0.1812
REMARK 3 6 2.7357 - 2.5744 1.00 2643 148 0.1454 0.1734
REMARK 3 7 2.5744 - 2.4455 1.00 2674 120 0.1434 0.1519
REMARK 3 8 2.4455 - 2.3391 1.00 2654 154 0.1436 0.1687
REMARK 3 9 2.3391 - 2.2490 1.00 2660 134 0.1373 0.1685
REMARK 3 10 2.2490 - 2.1714 1.00 2628 146 0.1387 0.1690
REMARK 3 11 2.1714 - 2.1035 1.00 2676 126 0.1402 0.1602
REMARK 3 12 2.1035 - 2.0434 1.00 2643 140 0.1441 0.1742
REMARK 3 13 2.0434 - 1.9896 1.00 2660 133 0.1451 0.1908
REMARK 3 14 1.9896 - 1.9411 1.00 2629 135 0.1486 0.1689
REMARK 3 15 1.9411 - 1.8969 1.00 2648 130 0.1493 0.1829
REMARK 3 16 1.8969 - 1.8566 1.00 2633 163 0.1554 0.1920
REMARK 3 17 1.8566 - 1.8194 1.00 2638 141 0.1610 0.1937
REMARK 3 18 1.8194 - 1.7851 1.00 2647 129 0.1647 0.1988
REMARK 3 19 1.7851 - 1.7532 1.00 2632 160 0.1655 0.2064
REMARK 3 20 1.7532 - 1.7235 1.00 2600 141 0.1835 0.2300
REMARK 3 21 1.7235 - 1.6957 0.99 2680 135 0.1874 0.2237
REMARK 3 22 1.6957 - 1.6696 0.97 2568 133 0.1886 0.2113
REMARK 3 23 1.6696 - 1.6450 0.93 2458 118 0.1950 0.2111
REMARK 3 24 1.6450 - 1.6219 0.87 2325 120 0.1935 0.2145
REMARK 3 25 1.6219 - 1.5999 0.79 2103 88 0.1979 0.2333
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.810
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) : 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 : 0.007 4964
REMARK 3 ANGLE : 1.026 6798
REMARK 3 CHIRALITY : 0.056 780
REMARK 3 PLANARITY : 0.007 886
REMARK 3 DIHEDRAL : 12.200 3001
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): 34.9718 0.4834 2.9038
REMARK 3 T TENSOR
REMARK 3 T11: 0.0742 T22: 0.0851
REMARK 3 T33: 0.0933 T12: -0.0051
REMARK 3 T13: 0.0219 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.4057 L22: 0.2821
REMARK 3 L33: 0.7260 L12: -0.2208
REMARK 3 L13: 0.4713 L23: -0.2949
REMARK 3 S TENSOR
REMARK 3 S11: 0.0408 S12: 0.0563 S13: -0.0221
REMARK 3 S21: -0.0312 S22: -0.0102 S23: 0.0455
REMARK 3 S31: 0.0405 S32: 0.0647 S33: -0.0270
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 6J1Q 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_1300010233.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUN-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) : 0.97775
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 : 69637
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 29.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.48000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.800
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 (%): 39.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE 0.1 M HEPES 7.0
REMARK 280 16% PEG 4000 10% ISOPROPANOL, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 40.22450
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 465 ALA B 0
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 73.88 -157.26
REMARK 500 ASN A 51 -93.01 -152.17
REMARK 500 ASP A 75 120.80 -30.20
REMARK 500 SER A 105 -112.13 34.83
REMARK 500 ASP A 134 68.06 -113.02
REMARK 500 ALA A 146 -125.95 58.65
REMARK 500 ALA A 305 39.90 -141.92
REMARK 500 SER B 29 72.01 -155.11
REMARK 500 ASN B 51 -91.47 -150.64
REMARK 500 ASP B 75 121.55 -30.20
REMARK 500 SER B 105 -112.70 35.59
REMARK 500 ASP B 134 68.88 -115.05
REMARK 500 ALA B 305 35.71 -142.78
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 B 798 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH B 799 DISTANCE = 6.82 ANGSTROMS
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 EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO 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 EPE A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE B 409
DBREF 6J1Q A 1 317 UNP P41365 LIPB_PSEA2 26 342
DBREF 6J1Q B 1 317 UNP P41365 LIPB_PSEA2 26 342
SEQADV 6J1Q GLY A -3 UNP P41365 EXPRESSION TAG
SEQADV 6J1Q ALA A -2 UNP P41365 EXPRESSION TAG
SEQADV 6J1Q MET A -1 UNP P41365 EXPRESSION TAG
SEQADV 6J1Q ALA A 0 UNP P41365 EXPRESSION TAG
SEQADV 6J1Q ALA A 57 UNP P41365 THR 82 ENGINEERED MUTATION
SEQADV 6J1Q THR A 89 UNP P41365 ALA 114 ENGINEERED MUTATION
SEQADV 6J1Q ALA A 104 UNP P41365 TRP 129 ENGINEERED MUTATION
SEQADV 6J1Q VAL A 189 UNP P41365 ILE 214 ENGINEERED MUTATION
SEQADV 6J1Q GLY B -3 UNP P41365 EXPRESSION TAG
SEQADV 6J1Q ALA B -2 UNP P41365 EXPRESSION TAG
SEQADV 6J1Q MET B -1 UNP P41365 EXPRESSION TAG
SEQADV 6J1Q ALA B 0 UNP P41365 EXPRESSION TAG
SEQADV 6J1Q ALA B 57 UNP P41365 THR 82 ENGINEERED MUTATION
SEQADV 6J1Q THR B 89 UNP P41365 ALA 114 ENGINEERED MUTATION
SEQADV 6J1Q ALA B 104 UNP P41365 TRP 129 ENGINEERED MUTATION
SEQADV 6J1Q VAL B 189 UNP P41365 ILE 214 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 ALA 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 VAL VAL 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 ALA ALA
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 ALA 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 VAL VAL 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 ALA ALA
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 EDO A 405 4
HET EDO A 406 4
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 EPE A 412 15
HET EPE A 413 15
HET PEG A 414 7
HET PEG A 415 7
HET SO4 B 401 5
HET SO4 B 402 5
HET EDO B 403 4
HET EDO B 404 4
HET EDO B 405 4
HET PEG B 406 7
HET PEG B 407 7
HET CL B 408 1
HET 1PE B 409 16
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM CL CHLORIDE ION
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN EDO ETHYLENE GLYCOL
HETSYN EPE HEPES
HETSYN 1PE PEG400
FORMUL 3 SO4 6(O4 S 2-)
FORMUL 7 EDO 10(C2 H6 O2)
FORMUL 14 EPE 2(C8 H18 N2 O4 S)
FORMUL 16 PEG 4(C4 H10 O3)
FORMUL 25 CL CL 1-
FORMUL 26 1PE C10 H22 O6
FORMUL 27 HOH *569(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 ASP A 223 SER A 230 1 8
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 LEU A 278 GLY A 288 1 11
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 GLY B 217 1 6
HELIX 27 AC9 ASP B 223 SER B 230 1 8
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 LEU B 278 GLY B 288 1 11
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 ALA 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 ALA 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 2.06
SSBOND 2 CYS A 216 CYS A 258 1555 1555 2.03
SSBOND 3 CYS A 293 CYS A 311 1555 1555 2.02
SSBOND 4 CYS B 22 CYS B 64 1555 1555 2.06
SSBOND 5 CYS B 216 CYS B 258 1555 1555 2.03
SSBOND 6 CYS B 293 CYS B 311 1555 1555 2.02
CISPEP 1 PRO A 69 PRO A 70 0 -13.61
CISPEP 2 GLN A 191 PRO A 192 0 2.29
CISPEP 3 PRO B 69 PRO B 70 0 -12.82
CISPEP 4 GLN B 191 PRO B 192 0 1.34
SITE 1 AC1 5 LYS A 208 ARG A 249 SER A 250 HOH A 531
SITE 2 AC1 5 HOH A 536
SITE 1 AC2 6 SER A 26 PRO A 27 HOH A 522 HOH A 660
SITE 2 AC2 6 HOH A 690 SER B 123
SITE 1 AC3 10 SER A 120 LYS A 124 EPE A 413 HOH A 516
SITE 2 AC3 10 HOH A 588 HOH A 617 HOH A 662 THR B 245
SITE 3 AC3 10 GLN B 247 HOH B 537
SITE 1 AC4 4 TYR A 203 PHE A 205 ASN A 206 HOH A 525
SITE 1 AC5 7 THR A 21 PRO A 45 TRP A 65 SER A 67
SITE 2 AC5 7 EDO A 407 HOH A 544 HOH A 582
SITE 1 AC6 1 ARG A 242
SITE 1 AC7 5 THR A 43 PRO A 45 GLN A 46 EDO A 405
SITE 2 AC7 5 HOH A 653
SITE 1 AC8 1 EDO A 409
SITE 1 AC9 7 THR A 40 SER A 105 GLN A 106 GLN A 157
SITE 2 AC9 7 VAL A 189 EDO A 408 HOH A 549
SITE 1 AD1 6 GLN A 231 TYR A 234 ARG A 238 ASP A 265
SITE 2 AD1 6 EPE A 412 HOH A 501
SITE 1 AD2 4 ALA A 8 PRO A 299 TYR A 300 HOH A 686
SITE 1 AD3 9 ARG A 238 ASP A 252 GLY A 254 ILE A 255
SITE 2 AD3 9 THR A 256 ASP A 257 EDO A 410 HOH A 501
SITE 3 AD3 9 HOH A 503
SITE 1 AD4 11 GLY A 4 PRO A 119 SER A 120 ARG A 122
SITE 2 AD4 11 SO4 A 403 HOH A 532 HOH A 562 HOH A 622
SITE 3 AD4 11 ALA B 25 SER B 26 SO4 B 401
SITE 1 AD5 4 CYS A 258 LEU B 147 VAL B 149 HOH B 633
SITE 1 AD6 5 ALA A 214 VAL A 215 GLY A 217 HOH A 665
SITE 2 AD6 5 GLY B 142
SITE 1 AD7 6 EPE A 413 LYS B 208 ARG B 249 SER B 250
SITE 2 AD7 6 HOH B 537 HOH B 588
SITE 1 AD8 3 THR B 165 ARG B 168 LYS B 308
SITE 1 AD9 5 PRO B 7 ALA B 8 PRO B 299 TYR B 300
SITE 2 AD9 5 HOH B 505
SITE 1 AE1 4 ASN B 169 PHE B 304 HOH B 514 HOH B 709
SITE 1 AE2 5 GLU A 188 HOH A 715 ALA B 283 HOH B 557
SITE 2 AE2 5 HOH B 626
SITE 1 AE3 4 ALA B 287 GLY B 288 PRO B 289 HOH B 515
SITE 1 AE4 5 HOH A 736 THR B 138 VAL B 154 HOH B 512
SITE 2 AE4 5 HOH B 621
SITE 1 AE5 4 PRO B 45 SER B 67 HOH B 698 HOH B 781
SITE 1 AE6 8 LEU B 144 ASN B 292 ARG B 309 THR B 310
SITE 2 AE6 8 CYS B 311 GLY B 313 HOH B 503 HOH B 731
CRYST1 46.530 80.449 72.588 90.00 97.56 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 0.021492 0.000000 0.002853 0.00000
SCALE2 0.000000 0.012430 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013897 0.00000
TER 2367 PRO A 317
TER 4717 PRO B 317
MASTER 381 0 24 33 18 0 42 6 5347 2 156 50
END |