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HEADER HYDROLASE 15-APR-13 4K6H
TITLE CRYSTAL STRUCTURE OF CALB MUTANT L278M FROM CANDIDA ANTARCTICA
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: CANDIDA ANTARCTICA;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 34362;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA AODE3AI;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.AN,Y.XIE,Y.FENG,G.WU
REVDAT 1 29-JAN-14 4K6H 0
JRNL AUTH Y.XIE,J.AN,G.YANG,G.WU,Y.ZHANG,L.CUI,Y.FENG
JRNL TITL ENHANCED ENZYME KINETIC STABILITY BY INCREASING RIGIDITY
JRNL TITL 2 WITHIN THE ACTIVE SITE
JRNL REF J.BIOL.CHEM. 2014
JRNL REFN ESSN 1083-351X
JRNL DOI 10.1074/JBC.M113.536045
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 70785
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3585
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4720
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2000
REMARK 3 BIN FREE R VALUE SET COUNT : 249
REMARK 3 BIN FREE R VALUE : 0.2290
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4676
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 319
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.82000
REMARK 3 B22 (A**2) : 0.73000
REMARK 3 B33 (A**2) : 0.09000
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -0.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.105
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.098
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.597
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4822 ; 0.006 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6611 ; 1.134 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 637 ; 5.493 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 166 ;34.659 ;25.060
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 686 ;12.536 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;19.385 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 771 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3664 ; 0.005 ; 0.022
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4K6H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-MAY-13.
REMARK 100 THE RCSB ID CODE IS RCSB078951.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70860
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 (%) : 99.3
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.5000
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) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.34600
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350,0.2M NAAC, 0.1M TRIS-BIS
REMARK 280 PH6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 287K
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 40.64150
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 GLU A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS B 320
REMARK 465 HIS B 321
REMARK 465 HIS B 322
REMARK 465 HIS B 323
REMARK 465 HIS B 324
REMARK 465 HIS B 325
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ALA B 0 N
REMARK 470 GLU B 319 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 TYR B 135 CE1 TYR B 135 CZ -0.085
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 A 29 84.76 -154.40
REMARK 500 ASN A 51 -97.41 -147.43
REMARK 500 SER A 105 -127.95 55.90
REMARK 500 ASP A 134 64.33 -107.86
REMARK 500 ASN A 206 -4.37 77.63
REMARK 500 ASN B 51 -92.94 -150.58
REMARK 500 SER B 105 -125.28 60.05
REMARK 500 ALA B 146 -132.47 58.39
REMARK 500 ALA B 148 21.82 -72.09
REMARK 500 ASN B 206 -6.25 79.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 EDO B 401
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4K5Q RELATED DB: PDB
REMARK 900 RELATED ID: 4K6G RELATED DB: PDB
REMARK 900 RELATED ID: 4K6K RELATED DB: PDB
DBREF 4K6H A 1 317 UNP P41365 LIPB_CANAR 26 342
DBREF 4K6H B 1 317 UNP P41365 LIPB_CANAR 26 342
SEQADV 4K6H ALA A 0 UNP P41365 EXPRESSION TAG
SEQADV 4K6H MET A 278 UNP P41365 LEU 303 ENGINEERED MUTATION
SEQADV 4K6H LEU A 318 UNP P41365 EXPRESSION TAG
SEQADV 4K6H GLU A 319 UNP P41365 EXPRESSION TAG
SEQADV 4K6H HIS A 320 UNP P41365 EXPRESSION TAG
SEQADV 4K6H HIS A 321 UNP P41365 EXPRESSION TAG
SEQADV 4K6H HIS A 322 UNP P41365 EXPRESSION TAG
SEQADV 4K6H HIS A 323 UNP P41365 EXPRESSION TAG
SEQADV 4K6H HIS A 324 UNP P41365 EXPRESSION TAG
SEQADV 4K6H HIS A 325 UNP P41365 EXPRESSION TAG
SEQADV 4K6H ALA B 0 UNP P41365 EXPRESSION TAG
SEQADV 4K6H MET B 278 UNP P41365 LEU 303 ENGINEERED MUTATION
SEQADV 4K6H LEU B 318 UNP P41365 EXPRESSION TAG
SEQADV 4K6H GLU B 319 UNP P41365 EXPRESSION TAG
SEQADV 4K6H HIS B 320 UNP P41365 EXPRESSION TAG
SEQADV 4K6H HIS B 321 UNP P41365 EXPRESSION TAG
SEQADV 4K6H HIS B 322 UNP P41365 EXPRESSION TAG
SEQADV 4K6H HIS B 323 UNP P41365 EXPRESSION TAG
SEQADV 4K6H HIS B 324 UNP P41365 EXPRESSION TAG
SEQADV 4K6H HIS B 325 UNP P41365 EXPRESSION TAG
SEQRES 1 A 326 ALA LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO
SEQRES 2 A 326 LYS SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA
SEQRES 3 A 326 SER PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO
SEQRES 4 A 326 GLY THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN
SEQRES 5 A 326 TRP ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS
SEQRES 6 A 326 TRP ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN
SEQRES 7 A 326 VAL ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU
SEQRES 8 A 326 TYR ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR
SEQRES 9 A 326 TRP SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR
SEQRES 10 A 326 PHE PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET
SEQRES 11 A 326 ALA PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY
SEQRES 12 A 326 PRO LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP
SEQRES 13 A 326 GLN GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG
SEQRES 14 A 326 ASN ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN
SEQRES 15 A 326 LEU TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL
SEQRES 16 A 326 SER ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY
SEQRES 17 A 326 LYS ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE
SEQRES 18 A 326 VAL ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER
SEQRES 19 A 326 TYR VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY
SEQRES 20 A 326 GLN ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN
SEQRES 21 A 326 PRO LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL
SEQRES 22 A 326 ALA ALA ALA ALA LEU MET ALA PRO ALA ALA ALA ALA ILE
SEQRES 23 A 326 VAL ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET
SEQRES 24 A 326 PRO TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS
SEQRES 25 A 326 SER GLY ILE VAL THR PRO LEU GLU HIS HIS HIS HIS HIS
SEQRES 26 A 326 HIS
SEQRES 1 B 326 ALA LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO
SEQRES 2 B 326 LYS SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA
SEQRES 3 B 326 SER PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO
SEQRES 4 B 326 GLY THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN
SEQRES 5 B 326 TRP ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS
SEQRES 6 B 326 TRP ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN
SEQRES 7 B 326 VAL ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU
SEQRES 8 B 326 TYR ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR
SEQRES 9 B 326 TRP SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR
SEQRES 10 B 326 PHE PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET
SEQRES 11 B 326 ALA PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY
SEQRES 12 B 326 PRO LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP
SEQRES 13 B 326 GLN GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG
SEQRES 14 B 326 ASN ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN
SEQRES 15 B 326 LEU TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL
SEQRES 16 B 326 SER ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY
SEQRES 17 B 326 LYS ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE
SEQRES 18 B 326 VAL ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER
SEQRES 19 B 326 TYR VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY
SEQRES 20 B 326 GLN ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN
SEQRES 21 B 326 PRO LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL
SEQRES 22 B 326 ALA ALA ALA ALA LEU MET ALA PRO ALA ALA ALA ALA ILE
SEQRES 23 B 326 VAL ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET
SEQRES 24 B 326 PRO TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS
SEQRES 25 B 326 SER GLY ILE VAL THR PRO LEU GLU HIS HIS HIS HIS HIS
SEQRES 26 B 326 HIS
HET EDO A 401 4
HET EDO A 402 4
HET EDO A 403 4
HET EDO B 401 3
HET EDO B 402 4
HET EDO B 403 4
HET EDO B 404 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 7(C2 H6 O2)
FORMUL 10 HOH *319(H2 O)
HELIX 1 1 PRO A 12 GLY A 19 1 8
HELIX 2 2 THR A 43 ASP A 49 1 7
HELIX 3 3 ASN A 51 LEU A 59 1 9
HELIX 4 4 ASP A 75 SER A 94 1 20
HELIX 5 5 SER A 105 PHE A 118 1 14
HELIX 6 6 PRO A 119 ARG A 122 5 4
HELIX 7 7 PRO A 143 LEU A 147 5 5
HELIX 8 8 ALA A 151 GLN A 157 1 7
HELIX 9 9 SER A 161 ALA A 170 1 10
HELIX 10 10 ALA A 212 GLY A 217 1 6
HELIX 11 11 ALA A 225 SER A 230 1 6
HELIX 12 12 SER A 230 SER A 243 1 14
HELIX 13 13 ARG A 249 TYR A 253 5 5
HELIX 14 14 GLY A 254 CYS A 258 5 5
HELIX 15 15 THR A 267 ALA A 276 1 10
HELIX 16 16 MET A 278 GLY A 288 1 11
HELIX 17 17 ALA A 301 ALA A 305 5 5
HELIX 18 18 PRO B 12 GLY B 19 1 8
HELIX 19 19 THR B 43 ASP B 49 1 7
HELIX 20 20 ASN B 51 LEU B 59 1 9
HELIX 21 21 ASP B 75 SER B 94 1 20
HELIX 22 22 SER B 105 PHE B 118 1 14
HELIX 23 23 PRO B 119 ARG B 122 5 4
HELIX 24 24 ALA B 151 GLN B 157 1 7
HELIX 25 25 SER B 161 ALA B 170 1 10
HELIX 26 26 ALA B 212 GLY B 217 1 6
HELIX 27 27 ALA B 225 SER B 230 1 6
HELIX 28 28 SER B 230 SER B 243 1 14
HELIX 29 29 ARG B 249 TYR B 253 5 5
HELIX 30 30 GLY B 254 CYS B 258 5 5
HELIX 31 31 THR B 267 ALA B 276 1 10
HELIX 32 32 LEU B 277 GLY B 288 1 12
HELIX 33 33 ALA B 301 ALA B 305 5 5
SHEET 1 A 7 LEU A 20 CYS A 22 0
SHEET 2 A 7 THR A 62 ILE A 66 -1 O TRP A 65 N THR A 21
SHEET 3 A 7 PRO A 33 VAL A 37 1 N LEU A 36 O CYS A 64
SHEET 4 A 7 LEU A 99 TRP A 104 1 O LEU A 102 N LEU A 35
SHEET 5 A 7 VAL A 125 PHE A 131 1 O MET A 129 N VAL A 101
SHEET 6 A 7 THR A 179 TYR A 183 1 O THR A 180 N ALA A 130
SHEET 7 A 7 LYS A 208 GLN A 211 1 O VAL A 210 N ASN A 181
SHEET 1 B 2 ARG A 309 THR A 310 0
SHEET 2 B 2 GLY A 313 ILE A 314 -1 O GLY A 313 N THR A 310
SHEET 1 C 7 LEU B 20 CYS B 22 0
SHEET 2 C 7 THR B 62 ILE B 66 -1 O TRP B 65 N THR B 21
SHEET 3 C 7 PRO B 33 VAL B 37 1 N LEU B 36 O CYS B 64
SHEET 4 C 7 LEU B 99 TRP B 104 1 O LEU B 102 N LEU B 35
SHEET 5 C 7 VAL B 125 PHE B 131 1 O MET B 129 N VAL B 101
SHEET 6 C 7 THR B 179 TYR B 183 1 O THR B 180 N ALA B 130
SHEET 7 C 7 LYS B 208 GLN B 211 1 O VAL B 210 N ASN B 181
SHEET 1 D 2 ARG B 309 THR B 310 0
SHEET 2 D 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 2.06
SSBOND 5 CYS B 216 CYS B 258 1555 1555 2.03
SSBOND 6 CYS B 293 CYS B 311 1555 1555 2.04
CISPEP 1 PRO A 69 PRO A 70 0 -12.23
CISPEP 2 GLN A 191 PRO A 192 0 0.70
CISPEP 3 PRO B 69 PRO B 70 0 -11.10
CISPEP 4 GLN B 191 PRO B 192 0 1.82
SITE 1 AC1 1 ILE A 314
SITE 1 AC2 6 GLY A 39 THR A 40 TRP A 104 SER A 105
SITE 2 AC2 6 MET A 278 ALA A 281
SITE 1 AC3 4 LYS A 13 ASP B 126 ARG B 127 THR B 244
SITE 1 AC4 4 SER B 67 PRO B 69 PRO B 70 PHE B 71
SITE 1 AC5 5 ASN B 169 PRO B 303 PHE B 304 ALA B 305
SITE 2 AC5 5 VAL B 306
SITE 1 AC6 3 THR B 40 TRP B 104 SER B 105
SITE 1 AC7 1 PRO B 198
CRYST1 47.710 81.283 71.556 90.00 95.83 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 0.020960 0.000000 0.002139 0.00000
SCALE2 0.000000 0.012303 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014048 0.00000
TER 2337 LEU A 318
TER 4678 GLU B 319
MASTER 345 0 7 33 18 0 9 6 5022 2 39 52
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