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HEADER HYDROLASE 02-APR-13 3W9B
TITLE CRYSTAL STRUCTURE OF CANDIDA ANTARCTICA LIPASE B WITH ANION-TAG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE B;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 26-342;
COMPND 5 SYNONYM: CALB;
COMPND 6 EC: 3.1.1.3;
COMPND 7 ENGINEERED: 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
KEYWDS LIPASE (CARBOXYLIC ESTERASE), HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.K.KIM,H.H.LEE,Y.C.PARK,S.T.JEON,S.H.SON,W.K.MIN,J.H.SEO
REVDAT 1 02-APR-14 3W9B 0
JRNL AUTH S.K.KIM,H.H.LEE,Y.C.PARK,S.T.JEON,S.H.SON,W.K.MIN,J.H.SEO
JRNL TITL ANION TAGS IMPROVE EXTRACELLULAR PRODUCTION OF CANDIDA
JRNL TITL 2 ANTARCTICA LIPASE B IN ESCHERICHIA COLI
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.90 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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 34806
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) : 0.234
REMARK 3 R VALUE (WORKING SET) : 0.232
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1834
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2490
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.3160
REMARK 3 BIN FREE R VALUE SET COUNT : 117
REMARK 3 BIN FREE R VALUE : 0.3440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9292
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 88
REMARK 3 SOLVENT ATOMS : 364
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -0.00000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.415
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.306
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.377
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.901
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.856
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9628 ; 0.007 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13200 ; 1.057 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1264 ; 5.363 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 332 ;35.358 ;25.060
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1360 ;15.418 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;15.929 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1532 ; 0.058 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7304 ; 0.006 ; 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 : 4
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): 12.4732 30.1162 -7.8780
REMARK 3 T TENSOR
REMARK 3 T11: 0.1011 T22: 0.1398
REMARK 3 T33: 0.1179 T12: 0.0944
REMARK 3 T13: 0.0227 T23: -0.0238
REMARK 3 L TENSOR
REMARK 3 L11: 0.1160 L22: 0.3505
REMARK 3 L33: 0.5430 L12: -0.1094
REMARK 3 L13: 0.1134 L23: 0.1519
REMARK 3 S TENSOR
REMARK 3 S11: -0.0794 S12: -0.0831 S13: -0.0417
REMARK 3 S21: -0.0064 S22: 0.0390 S23: 0.0161
REMARK 3 S31: -0.1429 S32: -0.1640 S33: 0.0404
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): 44.0946 47.7876 -3.9966
REMARK 3 T TENSOR
REMARK 3 T11: 0.3034 T22: 0.0907
REMARK 3 T33: 0.0894 T12: -0.0958
REMARK 3 T13: -0.0778 T23: -0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 0.6024 L22: 0.0694
REMARK 3 L33: 0.2295 L12: -0.0321
REMARK 3 L13: 0.2264 L23: 0.0569
REMARK 3 S TENSOR
REMARK 3 S11: -0.1822 S12: 0.0110 S13: -0.0067
REMARK 3 S21: -0.0183 S22: 0.0851 S23: 0.0083
REMARK 3 S31: -0.2278 S32: 0.0881 S33: 0.0971
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 317
REMARK 3 ORIGIN FOR THE GROUP (A): 32.3300 -4.2540 -24.1160
REMARK 3 T TENSOR
REMARK 3 T11: 0.2103 T22: 0.0307
REMARK 3 T33: 0.1197 T12: 0.0291
REMARK 3 T13: 0.0103 T23: -0.0347
REMARK 3 L TENSOR
REMARK 3 L11: 0.1674 L22: 0.2608
REMARK 3 L33: 0.5651 L12: -0.1300
REMARK 3 L13: -0.1602 L23: -0.0918
REMARK 3 S TENSOR
REMARK 3 S11: -0.0310 S12: -0.0375 S13: 0.0028
REMARK 3 S21: -0.1114 S22: -0.0051 S23: 0.0386
REMARK 3 S31: 0.2164 S32: 0.0406 S33: 0.0361
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 317
REMARK 3 ORIGIN FOR THE GROUP (A): 63.4331 14.3082 -27.9764
REMARK 3 T TENSOR
REMARK 3 T11: 0.0718 T22: 0.3329
REMARK 3 T33: 0.0969 T12: 0.0482
REMARK 3 T13: 0.0372 T23: 0.0744
REMARK 3 L TENSOR
REMARK 3 L11: 0.2104 L22: 0.3457
REMARK 3 L33: 0.2007 L12: 0.1987
REMARK 3 L13: -0.1632 L23: -0.1312
REMARK 3 S TENSOR
REMARK 3 S11: 0.0178 S12: -0.1455 S13: -0.0099
REMARK 3 S21: -0.0944 S22: -0.1232 S23: 0.0132
REMARK 3 S31: 0.0295 S32: 0.2250 S33: 0.1054
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
REMARK 4
REMARK 4 3W9B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-APR-13.
REMARK 100 THE RCSB ID CODE IS RCSB096048.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : OTHER
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36843
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHASER
REMARK 200 STARTING MODEL: 1TCA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M PHOSPHATE-CITRATE, 40% PEG600, PH
REMARK 280 4.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 127.90133
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 63.95067
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 95.92600
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 31.97533
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 159.87667
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 3950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 MET A -6
REMARK 465 ALA A -5
REMARK 465 ASP A -4
REMARK 465 ASP A -3
REMARK 465 ASP A -2
REMARK 465 ASP A -1
REMARK 465 ASP A 0
REMARK 465 ILE A 318
REMARK 465 GLU A 319
REMARK 465 GLY A 320
REMARK 465 ARG A 321
REMARK 465 MET B -6
REMARK 465 ALA B -5
REMARK 465 ASP B -4
REMARK 465 ASP B -3
REMARK 465 ASP B -2
REMARK 465 ASP B -1
REMARK 465 ASP B 0
REMARK 465 ILE B 318
REMARK 465 GLU B 319
REMARK 465 GLY B 320
REMARK 465 ARG B 321
REMARK 465 MET C -6
REMARK 465 ALA C -5
REMARK 465 ASP C -4
REMARK 465 ASP C -3
REMARK 465 ASP C -2
REMARK 465 ASP C -1
REMARK 465 ASP C 0
REMARK 465 ILE C 318
REMARK 465 GLU C 319
REMARK 465 GLY C 320
REMARK 465 ARG C 321
REMARK 465 MET D -6
REMARK 465 ALA D -5
REMARK 465 ASP D -4
REMARK 465 ASP D -3
REMARK 465 ASP D -2
REMARK 465 ASP D -1
REMARK 465 ASP D 0
REMARK 465 ILE D 318
REMARK 465 GLU D 319
REMARK 465 GLY D 320
REMARK 465 ARG D 321
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 65.94 -164.13
REMARK 500 ASN A 51 -79.56 -139.88
REMARK 500 GLN A 58 -8.12 -58.65
REMARK 500 ASP A 75 125.48 -32.60
REMARK 500 ASN A 96 44.08 36.99
REMARK 500 SER A 105 -120.20 49.94
REMARK 500 ASP A 134 62.53 -115.05
REMARK 500 SER B 3 -157.35 -159.11
REMARK 500 ASN B 51 -68.53 -144.84
REMARK 500 ASP B 75 125.69 -34.21
REMARK 500 SER B 105 -130.08 49.77
REMARK 500 ALA B 132 49.80 35.39
REMARK 500 ASN B 206 -0.54 76.28
REMARK 500 VAL B 215 -36.07 -141.01
REMARK 500 PRO B 218 44.61 -77.34
REMARK 500 SER B 250 -15.01 -48.90
REMARK 500 SER C 29 73.76 -165.01
REMARK 500 ASN C 51 -82.95 -148.43
REMARK 500 ASP C 75 122.06 -32.78
REMARK 500 ASN C 96 43.05 37.32
REMARK 500 SER C 105 -119.48 48.28
REMARK 500 ASP C 134 62.47 -118.67
REMARK 500 LEU C 199 0.33 -69.68
REMARK 500 SER C 243 154.46 -48.08
REMARK 500 SER D 3 -153.66 -144.16
REMARK 500 ALA D 25 -105.58 -121.48
REMARK 500 ASN D 51 -80.27 -148.95
REMARK 500 ASP D 75 123.59 -32.35
REMARK 500 SER D 105 -128.24 50.79
REMARK 500 ALA D 132 49.56 34.82
REMARK 500 ASP D 134 67.85 -119.64
REMARK 500 VAL D 215 -53.90 -127.94
REMARK 500 PRO D 218 49.31 -83.17
REMARK 500 LEU D 219 -0.12 -144.66
REMARK 500 THR D 310 -164.35 -122.85
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 A1082 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH A1092 DISTANCE = 7.76 ANGSTROMS
REMARK 525 HOH A1093 DISTANCE = 5.56 ANGSTROMS
REMARK 525 HOH B1073 DISTANCE = 5.04 ANGSTROMS
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 PE8 B 901
REMARK 610 PE8 D 901
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE8 A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE8 B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE8 C 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE8 D 901
DBREF 3W9B A 1 317 UNP P41365 LIPB_CANAR 26 342
DBREF 3W9B B 1 317 UNP P41365 LIPB_CANAR 26 342
DBREF 3W9B C 1 317 UNP P41365 LIPB_CANAR 26 342
DBREF 3W9B D 1 317 UNP P41365 LIPB_CANAR 26 342
SEQADV 3W9B MET A -6 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ALA A -5 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ASP A -4 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ASP A -3 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ASP A -2 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ASP A -1 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ASP A 0 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ILE A 318 UNP P41365 EXPRESSION TAG
SEQADV 3W9B GLU A 319 UNP P41365 EXPRESSION TAG
SEQADV 3W9B GLY A 320 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ARG A 321 UNP P41365 EXPRESSION TAG
SEQADV 3W9B MET B -6 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ALA B -5 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ASP B -4 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ASP B -3 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ASP B -2 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ASP B -1 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ASP B 0 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ILE B 318 UNP P41365 EXPRESSION TAG
SEQADV 3W9B GLU B 319 UNP P41365 EXPRESSION TAG
SEQADV 3W9B GLY B 320 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ARG B 321 UNP P41365 EXPRESSION TAG
SEQADV 3W9B MET C -6 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ALA C -5 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ASP C -4 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ASP C -3 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ASP C -2 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ASP C -1 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ASP C 0 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ILE C 318 UNP P41365 EXPRESSION TAG
SEQADV 3W9B GLU C 319 UNP P41365 EXPRESSION TAG
SEQADV 3W9B GLY C 320 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ARG C 321 UNP P41365 EXPRESSION TAG
SEQADV 3W9B MET D -6 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ALA D -5 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ASP D -4 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ASP D -3 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ASP D -2 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ASP D -1 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ASP D 0 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ILE D 318 UNP P41365 EXPRESSION TAG
SEQADV 3W9B GLU D 319 UNP P41365 EXPRESSION TAG
SEQADV 3W9B GLY D 320 UNP P41365 EXPRESSION TAG
SEQADV 3W9B ARG D 321 UNP P41365 EXPRESSION TAG
SEQRES 1 A 328 MET ALA ASP ASP ASP ASP ASP LEU PRO SER GLY SER ASP
SEQRES 2 A 328 PRO ALA PHE SER GLN PRO LYS SER VAL LEU ASP ALA GLY
SEQRES 3 A 328 LEU THR CYS GLN GLY ALA SER PRO SER SER VAL SER LYS
SEQRES 4 A 328 PRO ILE LEU LEU VAL PRO GLY THR GLY THR THR GLY PRO
SEQRES 5 A 328 GLN SER PHE ASP SER ASN TRP ILE PRO LEU SER THR GLN
SEQRES 6 A 328 LEU GLY TYR THR PRO CYS TRP ILE SER PRO PRO PRO PHE
SEQRES 7 A 328 MET LEU ASN ASP THR GLN VAL ASN THR GLU TYR MET VAL
SEQRES 8 A 328 ASN ALA ILE THR ALA LEU TYR ALA GLY SER GLY ASN ASN
SEQRES 9 A 328 LYS LEU PRO VAL LEU THR TRP SER GLN GLY GLY LEU VAL
SEQRES 10 A 328 ALA GLN TRP GLY LEU THR PHE PHE PRO SER ILE ARG SER
SEQRES 11 A 328 LYS VAL ASP ARG LEU MET ALA PHE ALA PRO ASP TYR LYS
SEQRES 12 A 328 GLY THR VAL LEU ALA GLY PRO LEU ASP ALA LEU ALA VAL
SEQRES 13 A 328 SER ALA PRO SER VAL TRP GLN GLN THR THR GLY SER ALA
SEQRES 14 A 328 LEU THR THR ALA LEU ARG ASN ALA GLY GLY LEU THR GLN
SEQRES 15 A 328 ILE VAL PRO THR THR ASN LEU TYR SER ALA THR ASP GLU
SEQRES 16 A 328 ILE VAL GLN PRO GLN VAL SER ASN SER PRO LEU ASP SER
SEQRES 17 A 328 SER TYR LEU PHE ASN GLY LYS ASN VAL GLN ALA GLN ALA
SEQRES 18 A 328 VAL CYS GLY PRO LEU PHE VAL ILE ASP HIS ALA GLY SER
SEQRES 19 A 328 LEU THR SER GLN PHE SER TYR VAL VAL GLY ARG SER ALA
SEQRES 20 A 328 LEU ARG SER THR THR GLY GLN ALA ARG SER ALA ASP TYR
SEQRES 21 A 328 GLY ILE THR ASP CYS ASN PRO LEU PRO ALA ASN ASP LEU
SEQRES 22 A 328 THR PRO GLU GLN LYS VAL ALA ALA ALA ALA LEU LEU ALA
SEQRES 23 A 328 PRO ALA ALA ALA ALA ILE VAL ALA GLY PRO LYS GLN ASN
SEQRES 24 A 328 CYS GLU PRO ASP LEU MET PRO TYR ALA ARG PRO PHE ALA
SEQRES 25 A 328 VAL GLY LYS ARG THR CYS SER GLY ILE VAL THR PRO ILE
SEQRES 26 A 328 GLU GLY ARG
SEQRES 1 B 328 MET ALA ASP ASP ASP ASP ASP LEU PRO SER GLY SER ASP
SEQRES 2 B 328 PRO ALA PHE SER GLN PRO LYS SER VAL LEU ASP ALA GLY
SEQRES 3 B 328 LEU THR CYS GLN GLY ALA SER PRO SER SER VAL SER LYS
SEQRES 4 B 328 PRO ILE LEU LEU VAL PRO GLY THR GLY THR THR GLY PRO
SEQRES 5 B 328 GLN SER PHE ASP SER ASN TRP ILE PRO LEU SER THR GLN
SEQRES 6 B 328 LEU GLY TYR THR PRO CYS TRP ILE SER PRO PRO PRO PHE
SEQRES 7 B 328 MET LEU ASN ASP THR GLN VAL ASN THR GLU TYR MET VAL
SEQRES 8 B 328 ASN ALA ILE THR ALA LEU TYR ALA GLY SER GLY ASN ASN
SEQRES 9 B 328 LYS LEU PRO VAL LEU THR TRP SER GLN GLY GLY LEU VAL
SEQRES 10 B 328 ALA GLN TRP GLY LEU THR PHE PHE PRO SER ILE ARG SER
SEQRES 11 B 328 LYS VAL ASP ARG LEU MET ALA PHE ALA PRO ASP TYR LYS
SEQRES 12 B 328 GLY THR VAL LEU ALA GLY PRO LEU ASP ALA LEU ALA VAL
SEQRES 13 B 328 SER ALA PRO SER VAL TRP GLN GLN THR THR GLY SER ALA
SEQRES 14 B 328 LEU THR THR ALA LEU ARG ASN ALA GLY GLY LEU THR GLN
SEQRES 15 B 328 ILE VAL PRO THR THR ASN LEU TYR SER ALA THR ASP GLU
SEQRES 16 B 328 ILE VAL GLN PRO GLN VAL SER ASN SER PRO LEU ASP SER
SEQRES 17 B 328 SER TYR LEU PHE ASN GLY LYS ASN VAL GLN ALA GLN ALA
SEQRES 18 B 328 VAL CYS GLY PRO LEU PHE VAL ILE ASP HIS ALA GLY SER
SEQRES 19 B 328 LEU THR SER GLN PHE SER TYR VAL VAL GLY ARG SER ALA
SEQRES 20 B 328 LEU ARG SER THR THR GLY GLN ALA ARG SER ALA ASP TYR
SEQRES 21 B 328 GLY ILE THR ASP CYS ASN PRO LEU PRO ALA ASN ASP LEU
SEQRES 22 B 328 THR PRO GLU GLN LYS VAL ALA ALA ALA ALA LEU LEU ALA
SEQRES 23 B 328 PRO ALA ALA ALA ALA ILE VAL ALA GLY PRO LYS GLN ASN
SEQRES 24 B 328 CYS GLU PRO ASP LEU MET PRO TYR ALA ARG PRO PHE ALA
SEQRES 25 B 328 VAL GLY LYS ARG THR CYS SER GLY ILE VAL THR PRO ILE
SEQRES 26 B 328 GLU GLY ARG
SEQRES 1 C 328 MET ALA ASP ASP ASP ASP ASP LEU PRO SER GLY SER ASP
SEQRES 2 C 328 PRO ALA PHE SER GLN PRO LYS SER VAL LEU ASP ALA GLY
SEQRES 3 C 328 LEU THR CYS GLN GLY ALA SER PRO SER SER VAL SER LYS
SEQRES 4 C 328 PRO ILE LEU LEU VAL PRO GLY THR GLY THR THR GLY PRO
SEQRES 5 C 328 GLN SER PHE ASP SER ASN TRP ILE PRO LEU SER THR GLN
SEQRES 6 C 328 LEU GLY TYR THR PRO CYS TRP ILE SER PRO PRO PRO PHE
SEQRES 7 C 328 MET LEU ASN ASP THR GLN VAL ASN THR GLU TYR MET VAL
SEQRES 8 C 328 ASN ALA ILE THR ALA LEU TYR ALA GLY SER GLY ASN ASN
SEQRES 9 C 328 LYS LEU PRO VAL LEU THR TRP SER GLN GLY GLY LEU VAL
SEQRES 10 C 328 ALA GLN TRP GLY LEU THR PHE PHE PRO SER ILE ARG SER
SEQRES 11 C 328 LYS VAL ASP ARG LEU MET ALA PHE ALA PRO ASP TYR LYS
SEQRES 12 C 328 GLY THR VAL LEU ALA GLY PRO LEU ASP ALA LEU ALA VAL
SEQRES 13 C 328 SER ALA PRO SER VAL TRP GLN GLN THR THR GLY SER ALA
SEQRES 14 C 328 LEU THR THR ALA LEU ARG ASN ALA GLY GLY LEU THR GLN
SEQRES 15 C 328 ILE VAL PRO THR THR ASN LEU TYR SER ALA THR ASP GLU
SEQRES 16 C 328 ILE VAL GLN PRO GLN VAL SER ASN SER PRO LEU ASP SER
SEQRES 17 C 328 SER TYR LEU PHE ASN GLY LYS ASN VAL GLN ALA GLN ALA
SEQRES 18 C 328 VAL CYS GLY PRO LEU PHE VAL ILE ASP HIS ALA GLY SER
SEQRES 19 C 328 LEU THR SER GLN PHE SER TYR VAL VAL GLY ARG SER ALA
SEQRES 20 C 328 LEU ARG SER THR THR GLY GLN ALA ARG SER ALA ASP TYR
SEQRES 21 C 328 GLY ILE THR ASP CYS ASN PRO LEU PRO ALA ASN ASP LEU
SEQRES 22 C 328 THR PRO GLU GLN LYS VAL ALA ALA ALA ALA LEU LEU ALA
SEQRES 23 C 328 PRO ALA ALA ALA ALA ILE VAL ALA GLY PRO LYS GLN ASN
SEQRES 24 C 328 CYS GLU PRO ASP LEU MET PRO TYR ALA ARG PRO PHE ALA
SEQRES 25 C 328 VAL GLY LYS ARG THR CYS SER GLY ILE VAL THR PRO ILE
SEQRES 26 C 328 GLU GLY ARG
SEQRES 1 D 328 MET ALA ASP ASP ASP ASP ASP LEU PRO SER GLY SER ASP
SEQRES 2 D 328 PRO ALA PHE SER GLN PRO LYS SER VAL LEU ASP ALA GLY
SEQRES 3 D 328 LEU THR CYS GLN GLY ALA SER PRO SER SER VAL SER LYS
SEQRES 4 D 328 PRO ILE LEU LEU VAL PRO GLY THR GLY THR THR GLY PRO
SEQRES 5 D 328 GLN SER PHE ASP SER ASN TRP ILE PRO LEU SER THR GLN
SEQRES 6 D 328 LEU GLY TYR THR PRO CYS TRP ILE SER PRO PRO PRO PHE
SEQRES 7 D 328 MET LEU ASN ASP THR GLN VAL ASN THR GLU TYR MET VAL
SEQRES 8 D 328 ASN ALA ILE THR ALA LEU TYR ALA GLY SER GLY ASN ASN
SEQRES 9 D 328 LYS LEU PRO VAL LEU THR TRP SER GLN GLY GLY LEU VAL
SEQRES 10 D 328 ALA GLN TRP GLY LEU THR PHE PHE PRO SER ILE ARG SER
SEQRES 11 D 328 LYS VAL ASP ARG LEU MET ALA PHE ALA PRO ASP TYR LYS
SEQRES 12 D 328 GLY THR VAL LEU ALA GLY PRO LEU ASP ALA LEU ALA VAL
SEQRES 13 D 328 SER ALA PRO SER VAL TRP GLN GLN THR THR GLY SER ALA
SEQRES 14 D 328 LEU THR THR ALA LEU ARG ASN ALA GLY GLY LEU THR GLN
SEQRES 15 D 328 ILE VAL PRO THR THR ASN LEU TYR SER ALA THR ASP GLU
SEQRES 16 D 328 ILE VAL GLN PRO GLN VAL SER ASN SER PRO LEU ASP SER
SEQRES 17 D 328 SER TYR LEU PHE ASN GLY LYS ASN VAL GLN ALA GLN ALA
SEQRES 18 D 328 VAL CYS GLY PRO LEU PHE VAL ILE ASP HIS ALA GLY SER
SEQRES 19 D 328 LEU THR SER GLN PHE SER TYR VAL VAL GLY ARG SER ALA
SEQRES 20 D 328 LEU ARG SER THR THR GLY GLN ALA ARG SER ALA ASP TYR
SEQRES 21 D 328 GLY ILE THR ASP CYS ASN PRO LEU PRO ALA ASN ASP LEU
SEQRES 22 D 328 THR PRO GLU GLN LYS VAL ALA ALA ALA ALA LEU LEU ALA
SEQRES 23 D 328 PRO ALA ALA ALA ALA ILE VAL ALA GLY PRO LYS GLN ASN
SEQRES 24 D 328 CYS GLU PRO ASP LEU MET PRO TYR ALA ARG PRO PHE ALA
SEQRES 25 D 328 VAL GLY LYS ARG THR CYS SER GLY ILE VAL THR PRO ILE
SEQRES 26 D 328 GLU GLY ARG
HET PE8 A 901 25
HET PE8 B 901 19
HET PE8 C 901 25
HET PE8 D 901 19
HETNAM PE8 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL
FORMUL 5 PE8 4(C16 H34 O9)
FORMUL 9 HOH *364(H2 O)
HELIX 1 1 PRO A 12 ALA A 18 1 7
HELIX 2 2 THR A 43 ASP A 49 1 7
HELIX 3 3 ASN A 51 GLN A 58 1 8
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 THR A 138 LEU A 140 5 3
HELIX 8 8 ALA A 141 LEU A 147 1 7
HELIX 9 9 ALA A 151 GLN A 157 1 7
HELIX 10 10 SER A 161 ALA A 170 1 10
HELIX 11 11 GLN A 213 VAL A 215 5 3
HELIX 12 12 ALA A 225 SER A 230 1 6
HELIX 13 13 SER A 230 SER A 243 1 14
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 LEU A 277 GLY A 288 1 12
HELIX 17 17 ALA A 301 VAL A 306 5 6
HELIX 18 18 PRO B 12 ALA B 18 1 7
HELIX 19 19 THR B 43 ASP B 49 1 7
HELIX 20 20 ASN B 51 GLY B 60 1 10
HELIX 21 21 ASP B 75 GLY B 93 1 19
HELIX 22 22 SER B 105 PHE B 118 1 14
HELIX 23 23 PRO B 119 SER B 123 5 5
HELIX 24 24 ALA B 141 LEU B 147 1 7
HELIX 25 25 ALA B 151 GLN B 157 1 7
HELIX 26 26 SER B 161 ALA B 170 1 10
HELIX 27 27 ALA B 212 GLY B 217 1 6
HELIX 28 28 ALA B 225 SER B 230 1 6
HELIX 29 29 SER B 230 SER B 243 1 14
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 VAL B 306 5 6
HELIX 34 34 PRO C 12 ALA C 18 1 7
HELIX 35 35 THR C 43 ASP C 49 1 7
HELIX 36 36 ASN C 51 GLN C 58 1 8
HELIX 37 37 ASP C 75 SER C 94 1 20
HELIX 38 38 SER C 105 PHE C 118 1 14
HELIX 39 39 PRO C 119 ARG C 122 5 4
HELIX 40 40 THR C 138 LEU C 140 5 3
HELIX 41 41 ALA C 141 LEU C 147 1 7
HELIX 42 42 ALA C 151 GLN C 157 1 7
HELIX 43 43 SER C 161 ALA C 170 1 10
HELIX 44 44 GLN C 213 VAL C 215 5 3
HELIX 45 45 ALA C 225 SER C 230 1 6
HELIX 46 46 SER C 230 SER C 243 1 14
HELIX 47 47 ARG C 249 TYR C 253 5 5
HELIX 48 48 GLY C 254 CYS C 258 5 5
HELIX 49 49 THR C 267 ALA C 275 1 9
HELIX 50 50 LEU C 277 GLY C 288 1 12
HELIX 51 51 ALA C 301 VAL C 306 5 6
HELIX 52 52 PRO D 12 GLY D 19 1 8
HELIX 53 53 THR D 43 ASP D 49 1 7
HELIX 54 54 ILE D 53 GLN D 58 1 6
HELIX 55 55 ASP D 75 GLY D 93 1 19
HELIX 56 56 SER D 105 PHE D 118 1 14
HELIX 57 57 PRO D 119 SER D 123 5 5
HELIX 58 58 ALA D 141 LEU D 147 1 7
HELIX 59 59 ALA D 151 GLN D 157 1 7
HELIX 60 60 SER D 161 ALA D 170 1 10
HELIX 61 61 ALA D 212 GLY D 217 1 6
HELIX 62 62 SER D 230 SER D 243 1 14
HELIX 63 63 ARG D 249 TYR D 253 5 5
HELIX 64 64 GLY D 254 CYS D 258 5 5
HELIX 65 65 THR D 267 ALA D 276 1 10
HELIX 66 66 LEU D 277 GLY D 288 1 12
HELIX 67 67 ALA D 301 VAL D 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 LYS A 208 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 ILE B 34 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 LEU B 128
SHEET 7 C 7 LYS B 208 GLN B 211 1 O LYS B 208 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
SHEET 1 E 7 LEU C 20 CYS C 22 0
SHEET 2 E 7 THR C 62 ILE C 66 -1 O TRP C 65 N THR C 21
SHEET 3 E 7 PRO C 33 VAL C 37 1 N ILE C 34 O CYS C 64
SHEET 4 E 7 LEU C 99 TRP C 104 1 O LEU C 102 N LEU C 35
SHEET 5 E 7 VAL C 125 PHE C 131 1 O MET C 129 N VAL C 101
SHEET 6 E 7 THR C 179 TYR C 183 1 O THR C 180 N ALA C 130
SHEET 7 E 7 LYS C 208 GLN C 211 1 O LYS C 208 N ASN C 181
SHEET 1 F 2 ARG C 309 THR C 310 0
SHEET 2 F 2 GLY C 313 ILE C 314 -1 O GLY C 313 N THR C 310
SHEET 1 G 7 LEU D 20 CYS D 22 0
SHEET 2 G 7 THR D 62 ILE D 66 -1 O TRP D 65 N THR D 21
SHEET 3 G 7 PRO D 33 VAL D 37 1 N ILE D 34 O CYS D 64
SHEET 4 G 7 LEU D 99 TRP D 104 1 O LEU D 102 N LEU D 35
SHEET 5 G 7 VAL D 125 PHE D 131 1 O MET D 129 N VAL D 101
SHEET 6 G 7 THR D 179 TYR D 183 1 O THR D 180 N LEU D 128
SHEET 7 G 7 LYS D 208 GLN D 211 1 O LYS D 208 N ASN D 181
SHEET 1 H 2 ARG D 309 THR D 310 0
SHEET 2 H 2 GLY D 313 ILE D 314 -1 O GLY D 313 N THR D 310
SSBOND 1 CYS A 22 CYS A 64 1555 1555 2.04
SSBOND 2 CYS A 216 CYS A 258 1555 1555 2.04
SSBOND 3 CYS A 293 CYS A 311 1555 1555 2.05
SSBOND 4 CYS B 22 CYS B 64 1555 1555 2.04
SSBOND 5 CYS B 216 CYS B 258 1555 1555 2.04
SSBOND 6 CYS B 293 CYS B 311 1555 1555 2.06
SSBOND 7 CYS C 22 CYS C 64 1555 1555 2.04
SSBOND 8 CYS C 216 CYS C 258 1555 1555 2.04
SSBOND 9 CYS C 293 CYS C 311 1555 1555 2.05
SSBOND 10 CYS D 22 CYS D 64 1555 1555 2.04
SSBOND 11 CYS D 216 CYS D 258 1555 1555 2.04
SSBOND 12 CYS D 293 CYS D 311 1555 1555 2.05
CISPEP 1 PRO A 69 PRO A 70 0 -0.16
CISPEP 2 GLN A 191 PRO A 192 0 4.35
CISPEP 3 PRO B 69 PRO B 70 0 -9.66
CISPEP 4 GLN B 191 PRO B 192 0 6.34
CISPEP 5 PRO C 69 PRO C 70 0 -0.83
CISPEP 6 GLN C 191 PRO C 192 0 6.13
CISPEP 7 LEU D 1 PRO D 2 0 -16.10
CISPEP 8 PRO D 69 PRO D 70 0 -11.14
CISPEP 9 GLN D 191 PRO D 192 0 5.83
SITE 1 AC1 8 GLN A 157 ILE A 189 THR B 40 GLN B 157
SITE 2 AC1 8 GLU B 188 ILE B 189 ALA B 282 PE8 B 901
SITE 1 AC2 9 THR A 40 SER A 105 ALA A 282 ILE A 285
SITE 2 AC2 9 PE8 A 901 THR B 40 SER B 105 ALA B 282
SITE 3 AC2 9 ILE B 285
SITE 1 AC3 9 THR C 40 GLN C 157 ILE C 189 THR D 40
SITE 2 AC3 9 SER D 105 GLN D 157 GLU D 188 ILE D 189
SITE 3 AC3 9 PE8 D 901
SITE 1 AC4 9 THR C 40 SER C 105 ALA C 282 ILE C 285
SITE 2 AC4 9 PE8 C 901 THR D 40 SER D 105 ALA D 282
SITE 3 AC4 9 ILE D 285
CRYST1 123.659 123.659 191.852 90.00 90.00 120.00 P 65 24
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 0.008087 0.004669 0.000000 0.00000
SCALE2 0.000000 0.009338 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005212 0.00000
TER 2324 PRO A 317
TER 4648 PRO B 317
TER 6972 PRO C 317
TER 9296 PRO D 317
MASTER 474 0 4 67 36 0 11 6 9744 4 112 104
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