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HEADER HYDROLASE 29-DEC-18 6J1R
TITLE CRYSTAL STRUCTURE OF CANDIDA ANTARCTICA LIPASE B MUTANT - RR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE B;
COMPND 3 CHAIN: B, A;
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 6J1R 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.51
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.6
REMARK 3 NUMBER OF REFLECTIONS : 65549
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3340
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 46.5286 - 4.6171 0.99 2875 152 0.1369 0.1639
REMARK 3 2 4.6171 - 3.6652 0.99 2833 141 0.1366 0.1626
REMARK 3 3 3.6652 - 3.2020 1.00 2837 147 0.1799 0.2036
REMARK 3 4 3.2020 - 2.9093 1.00 2815 166 0.2003 0.2398
REMARK 3 5 2.9093 - 2.7008 0.98 2794 160 0.1929 0.2321
REMARK 3 6 2.7008 - 2.5416 0.99 2801 156 0.1798 0.2373
REMARK 3 7 2.5416 - 2.4143 1.00 2868 126 0.1805 0.2361
REMARK 3 8 2.4143 - 2.3092 1.00 2835 152 0.1767 0.1989
REMARK 3 9 2.3092 - 2.2203 1.00 2789 163 0.1678 0.2204
REMARK 3 10 2.2203 - 2.1437 0.99 2755 179 0.1752 0.2139
REMARK 3 11 2.1437 - 2.0767 0.99 2849 122 0.1888 0.2175
REMARK 3 12 2.0767 - 2.0173 1.00 2800 151 0.1870 0.2213
REMARK 3 13 2.0173 - 1.9642 1.00 2821 156 0.1866 0.2500
REMARK 3 14 1.9642 - 1.9163 1.00 2827 158 0.1866 0.2198
REMARK 3 15 1.9163 - 1.8727 0.99 2789 137 0.1858 0.2236
REMARK 3 16 1.8727 - 1.8329 0.98 2784 155 0.1903 0.2220
REMARK 3 17 1.8329 - 1.7962 0.90 2510 110 0.1890 0.2512
REMARK 3 18 1.7962 - 1.7623 0.84 2380 134 0.2098 0.2769
REMARK 3 19 1.7623 - 1.7308 0.82 2317 122 0.2073 0.2393
REMARK 3 20 1.7308 - 1.7015 0.79 2269 119 0.2181 0.2496
REMARK 3 21 1.7015 - 1.6740 0.76 2099 122 0.1922 0.2499
REMARK 3 22 1.6740 - 1.6483 0.70 1999 107 0.1908 0.2654
REMARK 3 23 1.6483 - 1.6240 0.67 1875 98 0.1954 0.2317
REMARK 3 24 1.6240 - 1.6012 0.60 1688 107 0.2114 0.2939
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.290
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 : 0.018 4959
REMARK 3 ANGLE : 1.560 6824
REMARK 3 CHIRALITY : 0.115 787
REMARK 3 PLANARITY : 0.010 899
REMARK 3 DIHEDRAL : 17.371 1794
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): -75.1514 19.0727 106.1914
REMARK 3 T TENSOR
REMARK 3 T11: 0.1087 T22: 0.0363
REMARK 3 T33: 0.0679 T12: 0.0194
REMARK 3 T13: 0.0979 T23: -0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 0.5281 L22: 0.6301
REMARK 3 L33: 0.5152 L12: 0.3680
REMARK 3 L13: 0.4292 L23: 0.3486
REMARK 3 S TENSOR
REMARK 3 S11: 0.1306 S12: -0.0762 S13: -0.0907
REMARK 3 S21: 0.0564 S22: -0.0257 S23: -0.0732
REMARK 3 S31: 0.1138 S32: -0.0808 S33: -0.0312
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 6J1R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1300010234.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-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) : 0.97853
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 : 70816
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 (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.9770
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) : 0.66600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.636
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 (%): 41.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LITHIUM SULFATE 0.1M TRIS 7.5 30%
REMARK 280 PEG3000 3% 2-METHYL-2,4-PENTADIOL, 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 40.33500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 2
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: 210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 GLY B -3
REMARK 465 ALA B -2
REMARK 465 GLY A -3
REMARK 465 ALA A -2
REMARK 465 MET A -1
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 NH1 ARG B 249 O4 SO4 B 401 2.00
REMARK 500 O PRO B 143 OG SER B 150 2.01
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 ASP B 49 CB - CG - OD1 ANGL. DEV. = 6.5 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 B 29 78.11 -159.65
REMARK 500 ASN B 51 -93.61 -150.16
REMARK 500 ASP B 75 123.89 -38.71
REMARK 500 SER B 105 -125.18 52.90
REMARK 500 ALA B 146 -1.88 60.86
REMARK 500 ASN B 206 -0.52 71.93
REMARK 500 LEU B 278 -3.46 115.15
REMARK 500 ALA B 282 -61.45 -135.66
REMARK 500 ALA B 305 36.88 -145.51
REMARK 500 SER A 29 81.61 -153.49
REMARK 500 ASN A 51 -90.41 -148.76
REMARK 500 SER A 105 -127.12 60.13
REMARK 500 ASP A 134 73.04 -113.35
REMARK 500 PRO A 198 -9.50 -58.20
REMARK 500 ASN A 206 -0.64 74.38
REMARK 500 ALA A 305 37.67 -142.95
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 675 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH A 646 DISTANCE = 5.81 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 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405
DBREF 6J1R B 1 317 UNP P41365 LIPB_PSEA2 26 342
DBREF 6J1R A 1 317 UNP P41365 LIPB_PSEA2 26 342
SEQADV 6J1R GLY B -3 UNP P41365 EXPRESSION TAG
SEQADV 6J1R ALA B -2 UNP P41365 EXPRESSION TAG
SEQADV 6J1R MET B -1 UNP P41365 EXPRESSION TAG
SEQADV 6J1R ALA B 0 UNP P41365 EXPRESSION TAG
SEQADV 6J1R ALA B 57 UNP P41365 THR 82 ENGINEERED MUTATION
SEQADV 6J1R THR B 89 UNP P41365 ALA 114 ENGINEERED MUTATION
SEQADV 6J1R LEU B 157 UNP P41365 GLN 182 ENGINEERED MUTATION
SEQADV 6J1R ALA B 189 UNP P41365 ILE 214 ENGINEERED MUTATION
SEQADV 6J1R GLY A -3 UNP P41365 EXPRESSION TAG
SEQADV 6J1R ALA A -2 UNP P41365 EXPRESSION TAG
SEQADV 6J1R MET A -1 UNP P41365 EXPRESSION TAG
SEQADV 6J1R ALA A 0 UNP P41365 EXPRESSION TAG
SEQADV 6J1R ALA A 57 UNP P41365 THR 82 ENGINEERED MUTATION
SEQADV 6J1R THR A 89 UNP P41365 ALA 114 ENGINEERED MUTATION
SEQADV 6J1R LEU A 157 UNP P41365 GLN 182 ENGINEERED MUTATION
SEQADV 6J1R ALA A 189 UNP P41365 ILE 214 ENGINEERED MUTATION
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 LEU 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 ALA 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
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 LEU 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 ALA 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
HET SO4 B 401 5
HET EDO B 402 4
HET EDO B 403 4
HET EDO B 404 4
HET PEG B 405 7
HET SO4 A 401 5
HET SO4 A 402 5
HET SO4 A 403 5
HET EDO A 404 4
HET EDO A 405 4
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 4 EDO 5(C2 H6 O2)
FORMUL 7 PEG C4 H10 O3
FORMUL 13 HOH *321(H2 O)
HELIX 1 AA1 PRO B 12 GLY B 19 1 8
HELIX 2 AA2 THR B 43 ASP B 49 1 7
HELIX 3 AA3 ASN B 51 LEU B 59 1 9
HELIX 4 AA4 ASP B 75 SER B 94 1 20
HELIX 5 AA5 SER B 105 PHE B 118 1 14
HELIX 6 AA6 PRO B 119 ARG B 122 5 4
HELIX 7 AA7 ALA B 151 LEU B 157 1 7
HELIX 8 AA8 SER B 161 GLY B 171 1 11
HELIX 9 AA9 ALA B 212 GLY B 217 1 6
HELIX 10 AB1 ALA B 225 SER B 230 1 6
HELIX 11 AB2 SER B 230 SER B 243 1 14
HELIX 12 AB3 ARG B 249 TYR B 253 5 5
HELIX 13 AB4 GLY B 254 CYS B 258 5 5
HELIX 14 AB5 THR B 267 ALA B 276 1 10
HELIX 15 AB6 ALA B 282 ALA B 287 1 6
HELIX 16 AB7 ALA B 301 VAL B 306 5 6
HELIX 17 AB8 PRO A 12 GLY A 19 1 8
HELIX 18 AB9 THR A 43 ASP A 49 1 7
HELIX 19 AC1 ASN A 51 LEU A 59 1 9
HELIX 20 AC2 ASP A 75 SER A 94 1 20
HELIX 21 AC3 SER A 105 PHE A 118 1 14
HELIX 22 AC4 PRO A 119 SER A 123 5 5
HELIX 23 AC5 PRO A 143 LEU A 147 5 5
HELIX 24 AC6 ALA A 151 LEU A 157 1 7
HELIX 25 AC7 SER A 161 ALA A 170 1 10
HELIX 26 AC8 ALA A 212 GLY A 217 1 6
HELIX 27 AC9 ALA A 225 SER A 230 1 6
HELIX 28 AD1 SER A 230 SER A 243 1 14
HELIX 29 AD2 ARG A 249 TYR A 253 5 5
HELIX 30 AD3 GLY A 254 CYS A 258 5 5
HELIX 31 AD4 THR A 267 ALA A 276 1 10
HELIX 32 AD5 LEU A 278 GLY A 288 1 11
HELIX 33 AD6 ALA A 301 ALA A 305 5 5
SHEET 1 AA1 7 LEU B 20 CYS B 22 0
SHEET 2 AA1 7 THR B 62 ILE B 66 -1 O TRP B 65 N THR B 21
SHEET 3 AA1 7 PRO B 33 VAL B 37 1 N LEU B 36 O CYS B 64
SHEET 4 AA1 7 LEU B 99 TRP B 104 1 O LEU B 102 N LEU B 35
SHEET 5 AA1 7 VAL B 125 PHE B 131 1 O MET B 129 N VAL B 101
SHEET 6 AA1 7 THR B 179 TYR B 183 1 O THR B 180 N ALA B 130
SHEET 7 AA1 7 LYS B 208 GLN B 211 1 O VAL B 210 N ASN B 181
SHEET 1 AA2 2 ARG B 309 THR B 310 0
SHEET 2 AA2 2 GLY B 313 ILE B 314 -1 O GLY B 313 N THR B 310
SHEET 1 AA3 7 LEU A 20 CYS A 22 0
SHEET 2 AA3 7 THR A 62 ILE A 66 -1 O TRP A 65 N THR A 21
SHEET 3 AA3 7 PRO A 33 VAL A 37 1 N LEU A 36 O CYS A 64
SHEET 4 AA3 7 LEU A 99 TRP A 104 1 O LEU A 102 N LEU A 35
SHEET 5 AA3 7 VAL A 125 PHE A 131 1 O MET A 129 N VAL A 101
SHEET 6 AA3 7 THR A 179 TYR A 183 1 O THR A 180 N ALA A 130
SHEET 7 AA3 7 LYS A 208 GLN A 211 1 O VAL A 210 N ASN A 181
SHEET 1 AA4 2 ARG A 309 THR A 310 0
SHEET 2 AA4 2 GLY A 313 ILE A 314 -1 O GLY A 313 N THR A 310
SSBOND 1 CYS B 22 CYS B 64 1555 1555 2.09
SSBOND 2 CYS B 216 CYS B 258 1555 1555 2.06
SSBOND 3 CYS B 293 CYS B 311 1555 1555 2.08
SSBOND 4 CYS A 22 CYS A 64 1555 1555 2.10
SSBOND 5 CYS A 216 CYS A 258 1555 1555 2.04
SSBOND 6 CYS A 293 CYS A 311 1555 1555 2.15
CISPEP 1 PRO B 69 PRO B 70 0 -15.07
CISPEP 2 GLN B 191 PRO B 192 0 2.46
CISPEP 3 PRO A 69 PRO A 70 0 -15.36
CISPEP 4 GLN A 191 PRO A 192 0 3.24
SITE 1 AC1 5 LYS B 208 ARG B 249 SER B 250 HOH B 523
SITE 2 AC1 5 HOH B 525
SITE 1 AC2 2 ASP B 49 GLN B 270
SITE 1 AC3 5 SER A 123 HOH A 523 SER B 26 PRO B 27
SITE 2 AC3 5 HOH B 645
SITE 1 AC4 4 THR B 40 SER B 105 GLN B 106 LEU B 157
SITE 1 AC5 4 GLY A 142 VAL B 215 GLY B 217 HOH B 653
SITE 1 AC6 5 LYS A 208 ARG A 249 SER A 250 HOH A 545
SITE 2 AC6 5 HOH A 565
SITE 1 AC7 4 THR A 165 ARG A 168 LYS A 308 HOH A 535
SITE 1 AC8 6 THR A 40 SER A 105 GLN A 106 ASP A 134
SITE 2 AC8 6 LEU A 157 HIS A 224
SITE 1 AC9 4 LYS A 32 PRO B 12 LYS B 13 HOH B 624
SITE 1 AD1 6 VAL A 286 LYS A 290 VAL B 221 PRO B 260
SITE 2 AD1 6 LEU B 261 HOH B 614
CRYST1 47.023 80.670 73.646 90.00 98.48 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 0.021266 0.000000 0.003170 0.00000
SCALE2 0.000000 0.012396 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013729 0.00000
TER 2365 PRO B 317
TER 4785 PRO A 317
MASTER 365 0 10 33 18 0 15 6 5026 2 59 50
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