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HEADER HYDROLASE 16-APR-13 4K6K
TITLE CRYSTAL STRUCTURE OF CALB MUTANT D223G 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 4K6K 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 (%) : 94.1
REMARK 3 NUMBER OF REFLECTIONS : 71355
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) : 0.236
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3598
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) : 4664
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.17
REMARK 3 BIN R VALUE (WORKING SET) : 0.2990
REMARK 3 BIN FREE R VALUE SET COUNT : 250
REMARK 3 BIN FREE R VALUE : 0.3470
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4571
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 246
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.37000
REMARK 3 B22 (A**2) : 1.82000
REMARK 3 B33 (A**2) : 1.56000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.00000
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.124
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.118
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.674
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4719 ; 0.008 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6461 ; 1.163 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 619 ; 5.438 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 162 ;33.695 ;24.938
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 674 ;12.593 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;18.774 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 754 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3568 ; 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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 317
REMARK 3 ORIGIN FOR THE GROUP (A): -11.5778 17.2955 -16.5919
REMARK 3 T TENSOR
REMARK 3 T11: 0.0491 T22: 0.0238
REMARK 3 T33: 0.0233 T12: 0.0197
REMARK 3 T13: 0.0066 T23: 0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 0.9574 L22: 0.4531
REMARK 3 L33: 0.3427 L12: -0.1507
REMARK 3 L13: -0.0556 L23: 0.1063
REMARK 3 S TENSOR
REMARK 3 S11: 0.0522 S12: 0.1324 S13: 0.1401
REMARK 3 S21: -0.0186 S22: -0.0329 S23: -0.0359
REMARK 3 S31: -0.0329 S32: -0.0376 S33: -0.0193
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 317
REMARK 3 ORIGIN FOR THE GROUP (A): -11.5893 24.0463 -52.1194
REMARK 3 T TENSOR
REMARK 3 T11: 0.0762 T22: 0.0169
REMARK 3 T33: 0.0504 T12: -0.0070
REMARK 3 T13: 0.0179 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 2.5745 L22: 0.8237
REMARK 3 L33: 0.4737 L12: 0.9886
REMARK 3 L13: -0.2416 L23: -0.2436
REMARK 3 S TENSOR
REMARK 3 S11: -0.1201 S12: 0.0511 S13: -0.3228
REMARK 3 S21: -0.1068 S22: 0.0774 S23: -0.1159
REMARK 3 S31: 0.1051 S32: 0.0065 S33: 0.0428
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 RESIDUAL ONLY
REMARK 4
REMARK 4 4K6K 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 RCSB078954.
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 : 71410
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 (%) : 94.2
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.7000
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) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : 0.45300
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 (%): 40.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
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 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 23.35400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.43500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.54550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.43500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.35400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.54550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: 1970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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 ALA A 0
REMARK 465 ALA A 141
REMARK 465 GLY A 142
REMARK 465 PRO A 143
REMARK 465 LEU A 144
REMARK 465 ASP A 145
REMARK 465 ALA A 146
REMARK 465 LEU A 318
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 ALA B 0
REMARK 465 ALA B 141
REMARK 465 GLY B 142
REMARK 465 PRO B 143
REMARK 465 LEU B 144
REMARK 465 ASP B 145
REMARK 465 ALA B 146
REMARK 465 GLU B 319
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 LEU B 1 N
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O1 EDO A 406 C2 EDO A 408 4555 1.37
REMARK 500 C1 EDO A 406 C2 EDO A 408 4555 1.57
REMARK 500 O1 EDO A 406 O2 EDO A 408 4555 1.64
REMARK 500 O2 EDO A 406 O1 EDO A 408 4555 2.08
REMARK 500 O1 EDO A 406 C1 EDO A 408 4555 2.16
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 83.43 -151.09
REMARK 500 ASN A 51 -91.76 -149.03
REMARK 500 SER A 105 -132.55 58.44
REMARK 500 ASP A 134 70.29 -119.19
REMARK 500 VAL A 149 69.43 -116.02
REMARK 500 ASN A 206 -1.60 76.71
REMARK 500 ALA A 305 30.41 -141.94
REMARK 500 ASN B 51 -91.50 -145.49
REMARK 500 SER B 105 -126.14 59.95
REMARK 500 ASP B 134 63.71 -110.96
REMARK 500 ASN B 206 -3.09 76.13
REMARK 500 ALA B 305 31.28 -140.02
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 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 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 B 401
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: 4K6H RELATED DB: PDB
DBREF 4K6K A 1 317 UNP P41365 LIPB_CANAR 26 342
DBREF 4K6K B 1 317 UNP P41365 LIPB_CANAR 26 342
SEQADV 4K6K ALA A 0 UNP P41365 EXPRESSION TAG
SEQADV 4K6K GLY A 223 UNP P41365 ASP 248 ENGINEERED MUTATION
SEQADV 4K6K LEU A 318 UNP P41365 EXPRESSION TAG
SEQADV 4K6K GLU A 319 UNP P41365 EXPRESSION TAG
SEQADV 4K6K HIS A 320 UNP P41365 EXPRESSION TAG
SEQADV 4K6K HIS A 321 UNP P41365 EXPRESSION TAG
SEQADV 4K6K HIS A 322 UNP P41365 EXPRESSION TAG
SEQADV 4K6K HIS A 323 UNP P41365 EXPRESSION TAG
SEQADV 4K6K HIS A 324 UNP P41365 EXPRESSION TAG
SEQADV 4K6K HIS A 325 UNP P41365 EXPRESSION TAG
SEQADV 4K6K ALA B 0 UNP P41365 EXPRESSION TAG
SEQADV 4K6K GLY B 223 UNP P41365 ASP 248 ENGINEERED MUTATION
SEQADV 4K6K LEU B 318 UNP P41365 EXPRESSION TAG
SEQADV 4K6K GLU B 319 UNP P41365 EXPRESSION TAG
SEQADV 4K6K HIS B 320 UNP P41365 EXPRESSION TAG
SEQADV 4K6K HIS B 321 UNP P41365 EXPRESSION TAG
SEQADV 4K6K HIS B 322 UNP P41365 EXPRESSION TAG
SEQADV 4K6K HIS B 323 UNP P41365 EXPRESSION TAG
SEQADV 4K6K HIS B 324 UNP P41365 EXPRESSION TAG
SEQADV 4K6K 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 GLY 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 LEU 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 GLY 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 LEU 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 A 404 4
HET EDO A 405 4
HET EDO A 406 4
HET EDO A 407 4
HET EDO A 408 4
HET EDO B 401 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 9(C2 H6 O2)
FORMUL 12 HOH *246(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 ALA A 151 GLN A 157 1 7
HELIX 8 8 SER A 161 ALA A 170 1 10
HELIX 9 9 ALA A 212 GLY A 217 1 6
HELIX 10 10 ALA A 225 SER A 230 1 6
HELIX 11 11 SER A 230 SER A 243 1 14
HELIX 12 12 ARG A 249 TYR A 253 5 5
HELIX 13 13 GLY A 254 CYS A 258 5 5
HELIX 14 14 THR A 267 ALA A 276 1 10
HELIX 15 15 LEU A 278 GLY A 288 1 11
HELIX 16 16 ALA A 301 ALA A 305 5 5
HELIX 17 17 PRO B 12 GLY B 19 1 8
HELIX 18 18 THR B 43 ASP B 49 1 7
HELIX 19 19 ASN B 51 LEU B 59 1 9
HELIX 20 20 ASP B 75 SER B 94 1 20
HELIX 21 21 SER B 105 PHE B 118 1 14
HELIX 22 22 PRO B 119 SER B 123 5 5
HELIX 23 23 ALA B 151 GLN B 157 1 7
HELIX 24 24 SER B 161 ALA B 170 1 10
HELIX 25 25 ALA B 212 GLY B 217 1 6
HELIX 26 26 ALA B 225 SER B 230 1 6
HELIX 27 27 SER B 230 SER B 243 1 14
HELIX 28 28 ARG B 249 TYR B 253 5 5
HELIX 29 29 GLY B 254 CYS B 258 5 5
HELIX 30 30 THR B 267 ALA B 276 1 10
HELIX 31 31 LEU B 277 ALA B 287 1 11
HELIX 32 32 ALA B 301 VAL B 306 5 6
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 ILE A 34 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 2.06
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 2.04
SSBOND 5 CYS B 216 CYS B 258 1555 1555 2.02
SSBOND 6 CYS B 293 CYS B 311 1555 1555 2.03
CISPEP 1 PRO A 69 PRO A 70 0 -9.63
CISPEP 2 GLN A 191 PRO A 192 0 0.66
CISPEP 3 PRO B 69 PRO B 70 0 -10.30
CISPEP 4 GLN B 191 PRO B 192 0 5.75
SITE 1 AC1 6 ALA A 18 EDO A 402 EDO A 404 HOH A 577
SITE 2 AC1 6 HOH A 626 EDO B 401
SITE 1 AC2 3 EDO A 401 EDO A 407 EDO A 408
SITE 1 AC3 5 TYR A 203 GLY A 207 LYS A 208 ASN A 209
SITE 2 AC3 5 HOH A 578
SITE 1 AC4 6 TYR A 203 PHE A 205 EDO A 401 HOH A 554
SITE 2 AC4 6 THR B 316 EDO B 401
SITE 1 AC5 4 TYR A 91 ASN A 96 EDO A 408 HOH A 635
SITE 1 AC6 1 EDO A 408
SITE 1 AC7 2 ALA A 18 EDO A 402
SITE 1 AC8 3 EDO A 402 EDO A 405 EDO A 406
SITE 1 AC9 6 EDO A 401 EDO A 404 HOH A 589 PRO B 317
SITE 2 AC9 6 LEU B 318 HOH B 561
CRYST1 46.708 87.091 138.870 90.00 90.00 90.00 P 21 21 21 8
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 0.021410 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011482 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007201 0.00000
TER 2283 PRO A 317
TER 4573 LEU B 318
MASTER 411 0 9 32 18 0 13 6 4853 2 48 52
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